242:
219:
116:
141:
500:
493:
248:
147:
1498:
1459:
in adult male mice, but this is not found in all strains of mice. The obesity and infertility in the Cpe mice develop with age; young mice (<8 weeks of age) are fertile and have normal body weight. Peptide processing in Cpe mice is impaired, with a large accumulation of peptides with C-terminal
1173:
Carboxypeptidase E is found in all species of vertebrates that have been examined, and is also present in many other organisms that have been studied (nematode, sea slug). Carboxypeptidase E is not found in the fruit fly (Drosophila), and another enzyme (presumably carboxypeptidase D) fills in for
1137:
cut the precursor at specific sites to generate intermediates containing C-terminal basic residues (lysine and/or arginine). These intermediates are then cleaved by CPE to remove the basic residues. For some peptides, additional processing steps, such as C-terminal amidation, are subsequently
1460:
lysine and/or arginine extensions. Levels of the mature forms of peptides are generally reduced in these mice, but not eliminated. It is thought that a related enzyme (carboxypeptidase D) also contributes to neuropeptide processing and gives rise to the mature peptides in the Cpe mice.
2130:
Naggert JK, Fricker LD, Varlamov O, Nishina PM, Rouille Y, Steiner DF, Carroll RJ, Paigen BJ, Leiter EH (June 1995). "Hyperproinsulinaemia in obese fat/fat mice associated with a carboxypeptidase E mutation which reduces enzyme activity".
1817:
Naggert JK, Fricker LD, Varlamov O, Nishina PM, Rouille Y, Steiner DF, Carroll RJ, Paigen BJ, Leiter EH (June 1995). "Hyperproinsulinaemia in obese fat/fat mice associated with a carboxypeptidase E mutation which reduces enzyme activity".
2306:
Alcalde L, Tonacchera M, Costagliola S, Jaraquemada D, Pujol-Borrell R, Ludgate M (August 1996). "Cloning of candidate autoantigen carboxypeptidase H from a human islet library: sequence identity with human brain CPH".
1486:). However, because CPE is not a rate-limiting enzyme for the production of most neuropeptides and peptide hormones, it is not clear how relatively modest decreases in CPE activity can cause physiological effects.
2410:"Cholecystokinin (CCK) levels are greatly reduced in the brains but not the duodenums of Cpe(fat)/Cpe(fat) mice: a regional difference in the involvement of carboxypeptidase E (Cpe) in pro-CCK processing"
2569:"Immunohistochemical localization and comparison of carboxypeptidases D, E, and Z, alpha-MSH, ACTH, and MIB-1 between human anterior and corticotroph cell "basophil invasion" of the posterior pituitary"
1467:
gene are not common within the human population, but have been identified. One patient with extreme obesity (Body Mass Index >50) was found to have a mutation that deleted nearly the entire
1861:
Alsters SI, Goldstone AP, Buxton JL, Zekavati A, Sosinsky A, Yiorkas AM, Holder S, Klaber RE, Bridges N, van Haelst MM, le Roux CW, Walley AJ, Walters RG, Mueller M, Blakemore AI (Jun 2015).
1863:"Truncating Homozygous Mutation of Carboxypeptidase E (CPE) in a Morbidly Obese Female with Type 2 Diabetes Mellitus, Intellectual Disability and Hypogonadotrophic Hypogonadism"
2234:
Guest PC, Arden SD, Rutherford NG, Hutton JC (August 1995). "The post-translational processing and intracellular sorting of carboxypeptidase H in the islets of
Langerhans".
2602:
Friis-Hansen L, Lacourse KA, Samuelson LC, Holst JJ (June 2001). "Attenuated processing of proglucagon and glucagon-like peptide-1 in carboxypeptidase E-deficient mice".
1435:. However, this role for carboxypeptidase E remains controversial, and evidence shows that this enzyme is not necessary for the sorting of regulated secretory proteins.
1138:
required to generate the bioactive peptide, although for many peptides the action of the proprotein convertases and CPE is sufficient to produce the bioactive peptide.
1352:
255:
154:
1133:. The production of neuropeptides and peptide hormones typically requires two sets of enzymes that cleave the peptide precursors, which are small proteins. First,
1371:
2044:"Enkephalin convertase: purification and characterization of a specific enkephalin-synthesizing carboxypeptidase localized to adrenal chromaffin granules"
1474:
In obesity, high levels of circulating free fatty acids have been reported to cause a decrease in the amount of carboxypeptidase E protein in pancreatic
2379:
Maeda K, Okubo K, Shimomura I, Mizuno K, Matsuzawa Y, Matsubara K (May 1997). "Analysis of an expression profile of genes in the human adipose tissue".
1471:
gene. This patient had intellectual disability (inability to read or write) and had abnormal glucose homeostasis, similar to mice lacking CPE activity.
818:
77:
799:
1984:
Goodge KA, Hutton JC (August 2000). "Translational regulation of proinsulin biosynthesis and proinsulin conversion in the pancreatic beta-cell".
1157:. Within cells, carboxypeptidase E is present in the secretory granules along with its peptide substrates and products. Carboxypeptidase E is a
1396:. It does that by cleaving off basic C-terminal amino acids, producing the active form of the peptide. Products of carboxypeptidase E include
1683:
1596:
1578:
3413:
2338:"Carboxypeptidase E is a regulated secretory pathway sorting receptor: genetic obliteration leads to endocrine disorders in Cpe(fat) mice"
1770:"Carboxypeptidase E is a regulated secretory pathway sorting receptor: genetic obliteration leads to endocrine disorders in Cpe(fat) mice"
3060:
2690:
1018:
241:
3134:
1025:
2499:"Organization of the human carboxypeptidase E gene and molecular scanning for mutations in Japanese subjects with NIDDM or obesity"
218:
1364:
3045:
1721:"Human carboxypeptidase E. Isolation and characterization of the cDNA, sequence conservation, expression and processing in vitro"
1617:
1565:
1544:
1315:
1291:
3290:
2205:
Hall C, Manser E, Spurr NK, Lim L (February 1993). "Assignment of the human carboxypeptidase E (CPE) gene to chromosome 4".
2097:"Brief report: impaired processing of prohormones associated with abnormalities of glucose homeostasis and adrenal function"
1561:
2168:
Song L, Fricker L (July 1995). "Processing of procarboxypeptidase E into carboxypeptidase E occurs in secretory vesicles".
140:
115:
2976:
2891:
1540:
2909:
1920:
Jeffrey KD, Alejandro EU, Luciani DS, Kalynyak TB, Hu X, Li H, Lin Y, Townsend RR, Polonsky KS, Johnson JD (June 2008).
57:
1388:
Carboxypeptidase E functions in the production of nearly all neuropeptides and peptide hormones. The enzyme acts as an
2444:
254:
153:
3275:
3391:
3378:
3365:
3352:
3339:
3326:
3313:
3092:
3008:
2931:
2901:
2883:
2836:
2801:
2729:
2716:
1309:
3285:
247:
146:
3239:
3182:
2871:
2707:
2662:
1202:
863:
65:
3050:
2095:
O'Rahilly S, Gray H, Humphreys PJ, Krook A, Polonsky KS, White A, Gibson S, Taylor K, Carr C (November 1995).
1296:
2013:
Beinfeld MC (January 2003). "Biosynthesis and processing of pro CCK: recent progress and future challenges".
3187:
3040:
2866:
2767:
2757:
2683:
844:
2854:
2742:
2611:
1376:
1284:
3208:
3127:
2861:
2762:
2534:"Immunohistochemical localization of carboxypeptidases E and D in the human placenta and umbilical cord"
2273:"Impaired processing of brain proneurotensin and promelanin-concentrating hormone in obese fat/fat mice"
1134:
3280:
1219:
3035:
2844:
2055:
1933:
1874:
129:
2616:
1312:
44:
3428:
3244:
2994:
2956:
2940:
1456:
1236:
1214:
3423:
3177:
3030:
2961:
2951:
2676:
2485:
2367:
2259:
2193:
2156:
1843:
1799:
1693:
1516:
1147:
89:
1001:
980:
954:
933:
3418:
3025:
2918:
2658:
2629:
2590:
2555:
2520:
2477:
2431:
2396:
2359:
2324:
2294:
2251:
2222:
2185:
2148:
2118:
2083:
2030:
2001:
1961:
1902:
1835:
1791:
1750:
1679:
1648:
1416:
1303:
37:
1161:
that exists in both membrane-associated and soluble forms. The membrane-binding is due to an
1146:
Carboxypeptidase E is found in brain and throughout the neuroendocrine system, including the
3223:
3218:
3192:
3120:
3075:
3070:
2946:
2621:
2580:
2545:
2510:
2469:
2459:
2421:
2388:
2349:
2316:
2284:
2243:
2214:
2177:
2140:
2108:
2073:
2063:
2022:
1993:
1951:
1941:
1892:
1882:
1827:
1781:
1740:
1732:
1671:
1640:
1511:
1272:
334:
265:
209:
164:
2653:
499:
492:
3270:
3254:
3167:
3080:
3065:
3020:
1705:
1420:
1248:
1154:
1130:
309:
1327:
1207:
85:
2181:
2059:
1937:
1878:
1644:
3308:
3249:
3101:
2737:
1956:
1921:
1897:
1862:
1745:
1720:
1503:
1347:
2464:
2392:
2354:
2337:
2078:
2043:
2026:
1786:
1769:
1675:
1668:
Neuropeptides and Other
Bioactive Peptides: From Discovery to Function (Color Version)
733:
728:
723:
718:
713:
708:
703:
698:
693:
688:
683:
667:
662:
657:
652:
647:
642:
637:
632:
627:
622:
617:
612:
607:
602:
586:
581:
576:
571:
566:
561:
556:
551:
546:
541:
3407:
3213:
3172:
3012:
2814:
2247:
1322:
1151:
528:
2371:
2263:
2160:
1847:
1803:
3162:
2720:
2489:
2197:
1432:
1393:
1389:
1331:
1158:
1126:
327:
106:
69:
1922:"Carboxypeptidase E mediates palmitate-induced beta-cell ER stress and apoptosis"
1887:
1478:, leading to beta-cell dysfunction (hyperproinsulinemia) and increased beta-cell
93:
3386:
3321:
3157:
2966:
2913:
2849:
2809:
2668:
2336:
Cool DR, Normant E, Shen F, Chen HC, Pannell L, Zhang Y, Loh YP (January 1997).
2113:
2096:
1768:
Cool DR, Normant E, Shen F, Chen HC, Pannell L, Zhang Y, Loh YP (January 1997).
1601:
National Center for
Biotechnology Information, U.S. National Library of Medicine
1583:
National Center for
Biotechnology Information, U.S. National Library of Medicine
1452:
1405:
1162:
1119:
2585:
2568:
2550:
2533:
2289:
2272:
2048:
Proceedings of the
National Academy of Sciences of the United States of America
1926:
Proceedings of the
National Academy of Sciences of the United States of America
1497:
410:
1719:
Manser E, Fernandez D, Loo L, Goh PY, Monfries C, Hall C, Lim L (April 1990).
1493:
1475:
1401:
1108:
226:
123:
73:
3360:
3334:
2699:
2497:
Utsunomiya N, Ohagi S, Sanke T, Tatsuta H, Hanabusa T, Nanjo K (June 1998).
2426:
2409:
2068:
1946:
1483:
1479:
1444:
1424:
763:
470:
348:
293:
280:
192:
179:
81:
2633:
2594:
2320:
2218:
2034:
2005:
1997:
1965:
1906:
1415:
It has been proposed that membrane-associated carboxypeptidase E acts as a
2625:
2559:
2524:
2515:
2498:
2481:
2473:
2445:"Disturbed progastrin processing in carboxypeptidase E-deficient fat mice"
2435:
2400:
2363:
2328:
2298:
2255:
2226:
2189:
2152:
2122:
2087:
1839:
1795:
1754:
1652:
1065:
1060:
2703:
1409:
1260:
1111:
1049:
908:
889:
2144:
1831:
1448:
1428:
1397:
1279:
875:
830:
2443:
Lacourse KA, Friis-Hansen L, Rehfeld JF, Samuelson LC (October 1997).
1736:
1174:
carboxypeptidase E in this organism. In humans, CPE is encoded by the
3373:
3143:
2789:
2782:
2777:
2649:
1359:
1255:
1243:
1231:
1115:
1097:
1033:
785:
1412:, and most other neuroendocrine peptide hormones and neuropeptides.
1670:. Vol. 1. Morgan & Claypool Life Sciences. pp. 1–92.
1427:
and in secretory granules; regulated secretory proteins are mostly
3347:
2824:
2819:
2752:
2747:
748:
744:
1267:
1178:
1104:
61:
3116:
2672:
508:
2532:
Reznik SE, Salafia CM, Lage JM, Fricker LD (December 1998).
3112:
1455:. In some strains of mice, the fat mutation also causes
317:
2652:
online database for peptidases and their inhibitors:
1666:
Fricker LD (2012). "Chapter 3.5 Carboxypeptidase E".
1165:α-helix within the C-terminal region of the protein.
482:
3299:
3263:
3232:
3201:
3150:
3091:
3007:
2987:
2930:
2900:
2882:
2835:
2800:
2728:
2715:
2271:Rovere C, Viale A, Nahon J, Kitabgi P (July 1996).
1370:
1358:
1346:
1341:
1321:
1302:
1290:
1278:
1266:
1254:
1242:
1230:
1225:
1213:
1201:
1196:
1191:
994:
973:
947:
926:
1557:
1555:
1553:
1536:
1534:
1532:
1443:Mice with mutant carboxypeptidase E, Cpe, display
264:
163:
2573:The Journal of Histochemistry and Cytochemistry
2538:The Journal of Histochemistry and Cytochemistry
2408:Cain BM, Wang W, Beinfeld MC (September 1997).
1562:GRCm38: Ensembl release 89: ENSMUSG00000037852
3128:
2684:
8:
1986:Seminars in Cell & Developmental Biology
1125:CPE is involved in the biosynthesis of most
1541:GRCh38: Ensembl release 89: ENSG00000109472
3135:
3121:
3113:
2725:
2691:
2677:
2669:
1338:
759:
524:
305:
204:
101:
2661:at the U.S. National Library of Medicine
2615:
2584:
2567:Fan X, Olson SJ, Johnson MD (June 2001).
2549:
2514:
2463:
2425:
2353:
2288:
2112:
2077:
2067:
1955:
1945:
1896:
1886:
1785:
1744:
1631:Fricker LD (1988). "Carboxypeptidase E".
734:protein localization to secretory granule
1612:
1610:
1419:for regulated secretory proteins in the
1528:
1107:. This enzyme catalyzes the release of
453:paraventricular nucleus of hypothalamus
1701:
1691:
1188:
48:, CPH, carboxypeptidase E, IDDHH, BDVS
18:
1618:"Entrez Gene: CPE carboxypeptidase E"
587:serine-type carboxypeptidase activity
269:
230:
225:
168:
127:
122:
7:
2236:Molecular and Cellular Endocrinology
694:cardiac left ventricle morphogenesis
3061:Amyloid precursor protein secretase
2182:10.1046/j.1471-4159.1995.65010444.x
2101:The New England Journal of Medicine
2042:Fricker LD, Snyder SH (June 1982).
1645:10.1146/annurev.ph.50.030188.001521
991:
970:
944:
923:
899:
880:
854:
835:
809:
790:
487:
405:
343:
322:
14:
1676:10.4199/C00056ED1V01Y201204NPE002
1100:that in humans is encoded by the
3046:Proteasome endopeptidase complex
1496:
684:protein localization to membrane
582:metallocarboxypeptidase activity
498:
491:
253:
246:
240:
217:
152:
145:
139:
114:
552:neurexin family protein binding
714:neuropeptide signaling pathway
577:cell adhesion molecule binding
509:More reference expression data
471:More reference expression data
391:dorsolateral prefrontal cortex
1:
2910:Serine type carboxypeptidases
2892:Angiotensin-converting enzyme
2465:10.1016/S0014-5793(97)01164-2
2393:10.1016/S0378-1119(96)00730-5
2355:10.1016/S0092-8674(00)81860-7
2027:10.1016/S0024-3205(02)02330-5
1787:10.1016/S0092-8674(00)81860-7
238:
137:
2604:The Journal of Endocrinology
2248:10.1016/0303-7207(95)03619-I
1888:10.1371/journal.pone.0131417
3414:Genes on human chromosome 4
2114:10.1056/NEJM199511233332104
1633:Annual Review of Physiology
437:nucleus of stria terminalis
367:paraflocculus of cerebellum
3445:
2586:10.1177/002215540104900612
2551:10.1177/002215549804601204
2290:10.1210/endo.137.7.8770919
628:transport vesicle membrane
613:secretory granule membrane
3291:Michaelis–Menten kinetics
2170:Journal of Neurochemistry
1597:"Mouse PubMed Reference:"
1579:"Human PubMed Reference:"
1337:
1064:
1059:
1055:
1048:
1032:
1013:
998:
977:
966:
951:
930:
919:
906:
902:
887:
883:
874:
861:
857:
842:
838:
829:
816:
812:
797:
793:
784:
769:
762:
758:
742:
729:peptide hormone secretion
719:peptide metabolic process
572:metallopeptidase activity
562:carboxypeptidase activity
527:
523:
506:
490:
481:
468:
457:medial geniculate nucleus
417:
408:
355:
346:
316:
308:
304:
287:
274:
237:
216:
207:
203:
186:
173:
136:
113:
104:
100:
55:
52:
42:
35:
30:
26:
21:
3183:Diffusion-limited enzyme
2872:Tripeptidyl peptidase II
2663:Medical Subject Headings
1019:Chr 4: 165.36 – 165.5 Mb
421:anterior amygdaloid area
383:external globus pallidus
3041:Threonine endopeptidase
2867:Tripeptidyl peptidase I
2427:10.1210/endo.138.9.5490
2309:Journal of Autoimmunity
2069:10.1073/pnas.79.12.3886
1947:10.1073/pnas.0711232105
1725:The Biochemical Journal
1026:Chr 8: 65.05 – 65.15 Mb
3031:Aspartic acid protease
2855:Dipeptidyl peptidase-4
2321:10.1006/jaut.1996.0070
2219:10.1006/geno.1993.1093
1998:10.1006/scdb.2000.0172
1135:proprotein convertases
433:ventral tegmental area
429:lateral septal nucleus
16:Enzyme found in humans
3276:Eadie–Hofstee diagram
3209:Allosteric regulation
2862:Tripeptidyl peptidase
2626:10.1677/joe.0.1690595
2516:10.1007/s001250050971
1439:Clinical significance
1094:enkephalin convertase
699:Wnt signaling pathway
648:extracellular exosome
271:8 B3.1|8 32.3 cM
3286:Lineweaver–Burk plot
3036:Metalloendopeptidase
2941:Metalloexopeptidases
2845:Dipeptidyl peptidase
1482:(via an increase in
1169:Species distribution
638:extracellular region
232:Chromosome 8 (mouse)
130:Chromosome 4 (human)
3051:HslU—HslV peptidase
2995:Metalloexopeptidase
2060:1982PNAS...79.3886F
1938:2008PNAS..105.8452J
1879:2015PLoSO..1031417A
1457:hyperproinsulinemia
1421:trans-Golgi network
1142:Tissue distribution
663:extracellular space
653:cytoplasmic vesicle
3245:Enzyme superfamily
3178:Enzyme promiscuity
2659:Carboxypeptidase+E
2145:10.1038/ng0695-135
1832:10.1038/ng0695-135
1517:Carboxypeptidase A
1192:Carboxypeptidase E
1148:endocrine pancreas
1086:carboxypeptidase H
1078:Carboxypeptidase E
864:ENSMUSG00000037852
724:protein processing
689:insulin processing
677:Biological process
643:neuronal cell body
596:Cellular component
567:hydrolase activity
557:peptidase activity
535:Molecular function
3401:
3400:
3110:
3109:
3059:Other/ungrouped:
3026:Cysteine protease
3003:
3002:
2921:
1737:10.1042/bj2670517
1685:978-1-61504-521-1
1463:Mutations in the
1386:
1385:
1382:
1381:
1285:metabolic pathway
1150:, pituitary, and
1084:), also known as
1075:
1074:
1071:
1070:
1044:
1043:
1009:
1008:
988:
987:
962:
961:
941:
940:
915:
914:
896:
895:
870:
869:
851:
850:
825:
824:
806:
805:
754:
753:
668:transport vesicle
633:secretory granule
603:synaptic membrane
547:metal ion binding
519:
518:
515:
514:
477:
476:
464:
463:
445:nucleus accumbens
402:
401:
395:cerebellar vermis
387:prefrontal cortex
371:nucleus accumbens
300:
299:
199:
198:
3436:
3281:Hanes–Woolf plot
3224:Enzyme activator
3219:Enzyme inhibitor
3193:Enzyme catalysis
3137:
3130:
3123:
3114:
3076:Beta-secretase 2
3071:Beta-secretase 1
2947:Carboxypeptidase
2943:
2919:
2726:
2693:
2686:
2679:
2670:
2637:
2619:
2598:
2588:
2563:
2553:
2528:
2518:
2493:
2467:
2449:
2439:
2429:
2404:
2375:
2357:
2332:
2302:
2292:
2267:
2230:
2201:
2164:
2126:
2116:
2091:
2081:
2071:
2038:
2009:
1970:
1969:
1959:
1949:
1917:
1911:
1910:
1900:
1890:
1858:
1852:
1851:
1814:
1808:
1807:
1789:
1765:
1759:
1758:
1748:
1716:
1710:
1709:
1703:
1699:
1697:
1689:
1663:
1657:
1656:
1628:
1622:
1621:
1614:
1605:
1604:
1593:
1587:
1586:
1575:
1569:
1559:
1548:
1538:
1512:Carboxypeptidase
1506:
1501:
1500:
1339:
1189:
1155:chromaffin cells
1131:peptide hormones
1057:
1056:
1028:
1021:
1004:
992:
983:
971:
967:RefSeq (protein)
957:
945:
936:
924:
900:
881:
855:
836:
810:
791:
760:
542:zinc ion binding
525:
511:
502:
495:
488:
473:
413:
411:Top expressed in
406:
351:
349:Top expressed in
344:
323:
306:
296:
283:
272:
257:
250:
244:
233:
221:
205:
195:
182:
171:
156:
149:
143:
132:
118:
102:
96:
47:
40:
19:
3444:
3443:
3439:
3438:
3437:
3435:
3434:
3433:
3404:
3403:
3402:
3397:
3309:Oxidoreductases
3295:
3271:Enzyme kinetics
3259:
3255:List of enzymes
3228:
3197:
3168:Catalytic triad
3146:
3141:
3111:
3106:
3087:
3081:Gamma secretase
3066:Alpha secretase
3021:Serine protease
2999:
2988:Other/ungrouped
2983:
2939:
2926:
2922:-Transpeptidase
2896:
2878:
2831:
2796:
2711:
2697:
2645:
2640:
2617:10.1.1.521.1042
2601:
2566:
2544:(12): 1359–68.
2531:
2496:
2447:
2442:
2407:
2378:
2335:
2305:
2270:
2233:
2204:
2167:
2133:Nature Genetics
2129:
2107:(21): 1386–90.
2094:
2054:(12): 3886–90.
2041:
2012:
1983:
1979:
1977:Further reading
1974:
1973:
1919:
1918:
1914:
1873:(6): e0131417.
1860:
1859:
1855:
1820:Nature Genetics
1816:
1815:
1811:
1767:
1766:
1762:
1718:
1717:
1713:
1700:
1690:
1686:
1665:
1664:
1660:
1630:
1629:
1625:
1616:
1615:
1608:
1595:
1594:
1590:
1577:
1576:
1572:
1560:
1551:
1539:
1530:
1525:
1502:
1495:
1492:
1447:disorders like
1441:
1187:
1171:
1144:
1066:View/Edit Mouse
1061:View/Edit Human
1024:
1017:
1014:Location (UCSC)
1000:
979:
953:
932:
845:ENSG00000109472
738:
672:
623:plasma membrane
608:Golgi apparatus
591:
507:
497:
496:
469:
460:
455:
451:
447:
443:
439:
435:
431:
427:
425:cingulate gyrus
423:
409:
398:
393:
389:
385:
381:
377:
373:
369:
365:
363:caudate nucleus
361:
347:
291:
278:
270:
260:
259:
258:
251:
231:
208:Gene location (
190:
177:
169:
159:
158:
157:
150:
128:
105:Gene location (
94:CPE - orthologs
56:
43:
36:
17:
12:
11:
5:
3442:
3440:
3432:
3431:
3426:
3421:
3416:
3406:
3405:
3399:
3398:
3396:
3395:
3382:
3369:
3356:
3343:
3330:
3317:
3303:
3301:
3297:
3296:
3294:
3293:
3288:
3283:
3278:
3273:
3267:
3265:
3261:
3260:
3258:
3257:
3252:
3247:
3242:
3236:
3234:
3233:Classification
3230:
3229:
3227:
3226:
3221:
3216:
3211:
3205:
3203:
3199:
3198:
3196:
3195:
3190:
3185:
3180:
3175:
3170:
3165:
3160:
3154:
3152:
3148:
3147:
3142:
3140:
3139:
3132:
3125:
3117:
3108:
3107:
3105:
3104:
3102:Staphylokinase
3098:
3096:
3089:
3088:
3086:
3085:
3084:
3083:
3078:
3073:
3068:
3056:
3055:
3054:
3053:
3048:
3038:
3033:
3028:
3023:
3017:
3015:
3005:
3004:
3001:
3000:
2998:
2997:
2991:
2989:
2985:
2984:
2982:
2981:
2980:
2979:
2974:
2969:
2964:
2959:
2954:
2944:
2936:
2934:
2928:
2927:
2925:
2924:
2916:
2906:
2904:
2898:
2897:
2895:
2894:
2888:
2886:
2880:
2879:
2877:
2876:
2875:
2874:
2869:
2859:
2858:
2857:
2852:
2841:
2839:
2833:
2832:
2830:
2829:
2828:
2827:
2822:
2817:
2806:
2804:
2798:
2797:
2795:
2794:
2793:
2792:
2787:
2786:
2785:
2780:
2770:
2765:
2760:
2755:
2750:
2745:
2738:Aminopeptidase
2734:
2732:
2723:
2713:
2712:
2698:
2696:
2695:
2688:
2681:
2673:
2667:
2666:
2656:
2644:
2643:External links
2641:
2639:
2638:
2610:(3): 595–602.
2599:
2564:
2529:
2494:
2474:2027.42/116303
2440:
2405:
2376:
2333:
2303:
2268:
2231:
2202:
2165:
2127:
2092:
2039:
2010:
1980:
1978:
1975:
1972:
1971:
1932:(24): 8452–7.
1912:
1853:
1809:
1760:
1711:
1702:|journal=
1684:
1658:
1623:
1606:
1588:
1570:
1549:
1527:
1526:
1524:
1521:
1520:
1519:
1514:
1508:
1507:
1504:Biology portal
1491:
1488:
1440:
1437:
1417:sorting signal
1384:
1383:
1380:
1379:
1374:
1368:
1367:
1362:
1356:
1355:
1350:
1344:
1343:
1335:
1334:
1325:
1319:
1318:
1307:
1300:
1299:
1294:
1288:
1287:
1282:
1276:
1275:
1270:
1264:
1263:
1258:
1252:
1251:
1246:
1240:
1239:
1234:
1228:
1227:
1223:
1222:
1217:
1211:
1210:
1205:
1199:
1198:
1194:
1193:
1186:
1183:
1170:
1167:
1143:
1140:
1118:residues from
1073:
1072:
1069:
1068:
1063:
1053:
1052:
1046:
1045:
1042:
1041:
1039:
1037:
1030:
1029:
1022:
1015:
1011:
1010:
1007:
1006:
996:
995:
989:
986:
985:
975:
974:
968:
964:
963:
960:
959:
949:
948:
942:
939:
938:
928:
927:
921:
917:
916:
913:
912:
904:
903:
897:
894:
893:
885:
884:
878:
872:
871:
868:
867:
859:
858:
852:
849:
848:
840:
839:
833:
827:
826:
823:
822:
814:
813:
807:
804:
803:
795:
794:
788:
782:
781:
776:
771:
767:
766:
756:
755:
752:
751:
740:
739:
737:
736:
731:
726:
721:
716:
711:
706:
701:
696:
691:
686:
680:
678:
674:
673:
671:
670:
665:
660:
655:
650:
645:
640:
635:
630:
625:
620:
615:
610:
605:
599:
597:
593:
592:
590:
589:
584:
579:
574:
569:
564:
559:
554:
549:
544:
538:
536:
532:
531:
521:
520:
517:
516:
513:
512:
504:
503:
485:
479:
478:
475:
474:
466:
465:
462:
461:
459:
458:
454:
450:
446:
442:
438:
434:
430:
426:
422:
418:
415:
414:
403:
400:
399:
397:
396:
392:
388:
384:
380:
376:
372:
368:
364:
360:
356:
353:
352:
340:
339:
331:
320:
314:
313:
310:RNA expression
302:
301:
298:
297:
289:
285:
284:
276:
273:
268:
262:
261:
252:
245:
239:
235:
234:
229:
223:
222:
214:
213:
201:
200:
197:
196:
188:
184:
183:
175:
172:
167:
161:
160:
151:
144:
138:
134:
133:
126:
120:
119:
111:
110:
98:
97:
54:
50:
49:
41:
33:
32:
28:
27:
24:
23:
15:
13:
10:
9:
6:
4:
3:
2:
3441:
3430:
3427:
3425:
3422:
3420:
3417:
3415:
3412:
3411:
3409:
3393:
3389:
3388:
3383:
3380:
3376:
3375:
3370:
3367:
3363:
3362:
3357:
3354:
3350:
3349:
3344:
3341:
3337:
3336:
3331:
3328:
3324:
3323:
3318:
3315:
3311:
3310:
3305:
3304:
3302:
3298:
3292:
3289:
3287:
3284:
3282:
3279:
3277:
3274:
3272:
3269:
3268:
3266:
3262:
3256:
3253:
3251:
3250:Enzyme family
3248:
3246:
3243:
3241:
3238:
3237:
3235:
3231:
3225:
3222:
3220:
3217:
3215:
3214:Cooperativity
3212:
3210:
3207:
3206:
3204:
3200:
3194:
3191:
3189:
3186:
3184:
3181:
3179:
3176:
3174:
3173:Oxyanion hole
3171:
3169:
3166:
3164:
3161:
3159:
3156:
3155:
3153:
3149:
3145:
3138:
3133:
3131:
3126:
3124:
3119:
3118:
3115:
3103:
3100:
3099:
3097:
3094:
3090:
3082:
3079:
3077:
3074:
3072:
3069:
3067:
3064:
3063:
3062:
3058:
3057:
3052:
3049:
3047:
3044:
3043:
3042:
3039:
3037:
3034:
3032:
3029:
3027:
3024:
3022:
3019:
3018:
3016:
3014:
3013:Endopeptidase
3010:
3006:
2996:
2993:
2992:
2990:
2986:
2978:
2975:
2973:
2970:
2968:
2965:
2963:
2960:
2958:
2955:
2953:
2950:
2949:
2948:
2945:
2942:
2938:
2937:
2935:
2933:
2929:
2923:
2917:
2915:
2911:
2908:
2907:
2905:
2903:
2899:
2893:
2890:
2889:
2887:
2885:
2881:
2873:
2870:
2868:
2865:
2864:
2863:
2860:
2856:
2853:
2851:
2848:
2847:
2846:
2843:
2842:
2840:
2838:
2834:
2826:
2823:
2821:
2818:
2816:
2813:
2812:
2811:
2808:
2807:
2805:
2803:
2799:
2791:
2788:
2784:
2781:
2779:
2776:
2775:
2774:
2771:
2769:
2766:
2764:
2761:
2759:
2756:
2754:
2751:
2749:
2746:
2744:
2741:
2740:
2739:
2736:
2735:
2733:
2731:
2727:
2724:
2722:
2718:
2714:
2709:
2705:
2701:
2694:
2689:
2687:
2682:
2680:
2675:
2674:
2671:
2664:
2660:
2657:
2655:
2651:
2647:
2646:
2642:
2635:
2631:
2627:
2623:
2618:
2613:
2609:
2605:
2600:
2596:
2592:
2587:
2582:
2579:(6): 783–90.
2578:
2574:
2570:
2565:
2561:
2557:
2552:
2547:
2543:
2539:
2535:
2530:
2526:
2522:
2517:
2512:
2508:
2504:
2500:
2495:
2491:
2487:
2483:
2479:
2475:
2471:
2466:
2461:
2457:
2453:
2446:
2441:
2437:
2433:
2428:
2423:
2420:(9): 4034–7.
2419:
2415:
2414:Endocrinology
2411:
2406:
2402:
2398:
2394:
2390:
2387:(2): 227–35.
2386:
2382:
2377:
2373:
2369:
2365:
2361:
2356:
2351:
2347:
2343:
2339:
2334:
2330:
2326:
2322:
2318:
2314:
2310:
2304:
2300:
2296:
2291:
2286:
2283:(7): 2954–8.
2282:
2278:
2277:Endocrinology
2274:
2269:
2265:
2261:
2257:
2253:
2249:
2245:
2242:(1): 99–108.
2241:
2237:
2232:
2228:
2224:
2220:
2216:
2212:
2208:
2203:
2199:
2195:
2191:
2187:
2183:
2179:
2176:(1): 444–53.
2175:
2171:
2166:
2162:
2158:
2154:
2150:
2146:
2142:
2139:(2): 135–42.
2138:
2134:
2128:
2124:
2120:
2115:
2110:
2106:
2102:
2098:
2093:
2089:
2085:
2080:
2075:
2070:
2065:
2061:
2057:
2053:
2049:
2045:
2040:
2036:
2032:
2028:
2024:
2021:(7): 747–57.
2020:
2016:
2015:Life Sciences
2011:
2007:
2003:
1999:
1995:
1992:(4): 235–42.
1991:
1987:
1982:
1981:
1976:
1967:
1963:
1958:
1953:
1948:
1943:
1939:
1935:
1931:
1927:
1923:
1916:
1913:
1908:
1904:
1899:
1894:
1889:
1884:
1880:
1876:
1872:
1868:
1864:
1857:
1854:
1849:
1845:
1841:
1837:
1833:
1829:
1826:(2): 135–42.
1825:
1821:
1813:
1810:
1805:
1801:
1797:
1793:
1788:
1783:
1779:
1775:
1771:
1764:
1761:
1756:
1752:
1747:
1742:
1738:
1734:
1731:(2): 517–25.
1730:
1726:
1722:
1715:
1712:
1707:
1695:
1687:
1681:
1677:
1673:
1669:
1662:
1659:
1654:
1650:
1646:
1642:
1638:
1634:
1627:
1624:
1619:
1613:
1611:
1607:
1602:
1598:
1592:
1589:
1584:
1580:
1574:
1571:
1567:
1563:
1558:
1556:
1554:
1550:
1546:
1542:
1537:
1535:
1533:
1529:
1522:
1518:
1515:
1513:
1510:
1509:
1505:
1499:
1494:
1489:
1487:
1485:
1481:
1477:
1472:
1470:
1466:
1461:
1458:
1454:
1450:
1446:
1438:
1436:
1434:
1433:neuropeptides
1430:
1426:
1422:
1418:
1413:
1411:
1407:
1403:
1399:
1395:
1394:neuropeptides
1391:
1378:
1375:
1373:
1369:
1366:
1363:
1361:
1357:
1354:
1351:
1349:
1345:
1340:
1336:
1333:
1329:
1326:
1324:
1323:Gene Ontology
1320:
1317:
1314:
1311:
1308:
1305:
1301:
1298:
1295:
1293:
1289:
1286:
1283:
1281:
1277:
1274:
1271:
1269:
1265:
1262:
1261:NiceZyme view
1259:
1257:
1253:
1250:
1247:
1245:
1241:
1238:
1235:
1233:
1229:
1224:
1221:
1218:
1216:
1212:
1209:
1206:
1204:
1200:
1195:
1190:
1184:
1182:
1180:
1177:
1168:
1166:
1164:
1160:
1156:
1153:
1152:adrenal gland
1149:
1141:
1139:
1136:
1132:
1128:
1127:neuropeptides
1123:
1121:
1117:
1113:
1110:
1106:
1103:
1099:
1095:
1091:
1087:
1083:
1079:
1067:
1062:
1058:
1054:
1051:
1047:
1040:
1038:
1035:
1031:
1027:
1023:
1020:
1016:
1012:
1005:
1003:
997:
993:
990:
984:
982:
976:
972:
969:
965:
958:
956:
950:
946:
943:
937:
935:
929:
925:
922:
920:RefSeq (mRNA)
918:
911:
910:
905:
901:
898:
892:
891:
886:
882:
879:
877:
873:
866:
865:
860:
856:
853:
847:
846:
841:
837:
834:
832:
828:
821:
820:
815:
811:
808:
802:
801:
796:
792:
789:
787:
783:
780:
777:
775:
772:
768:
765:
761:
757:
750:
746:
741:
735:
732:
730:
727:
725:
722:
720:
717:
715:
712:
710:
707:
705:
702:
700:
697:
695:
692:
690:
687:
685:
682:
681:
679:
676:
675:
669:
666:
664:
661:
659:
656:
654:
651:
649:
646:
644:
641:
639:
636:
634:
631:
629:
626:
624:
621:
619:
616:
614:
611:
609:
606:
604:
601:
600:
598:
595:
594:
588:
585:
583:
580:
578:
575:
573:
570:
568:
565:
563:
560:
558:
555:
553:
550:
548:
545:
543:
540:
539:
537:
534:
533:
530:
529:Gene ontology
526:
522:
510:
505:
501:
494:
489:
486:
484:
480:
472:
467:
456:
452:
448:
444:
440:
436:
432:
428:
424:
420:
419:
416:
412:
407:
404:
394:
390:
386:
382:
378:
374:
370:
366:
362:
358:
357:
354:
350:
345:
342:
341:
338:
336:
332:
330:
329:
325:
324:
321:
319:
315:
311:
307:
303:
295:
290:
286:
282:
277:
267:
263:
256:
249:
243:
236:
228:
224:
220:
215:
211:
206:
202:
194:
189:
185:
181:
176:
166:
162:
155:
148:
142:
135:
131:
125:
121:
117:
112:
108:
103:
99:
95:
91:
87:
83:
79:
75:
71:
67:
63:
59:
51:
46:
39:
34:
29:
25:
20:
3387:Translocases
3384:
3371:
3358:
3345:
3332:
3322:Transferases
3319:
3306:
3163:Binding site
2977:Glutamate II
2971:
2772:
2721:Exopeptidase
2607:
2603:
2576:
2572:
2541:
2537:
2509:(6): 701–5.
2506:
2503:Diabetologia
2502:
2458:(1): 45–50.
2455:
2452:FEBS Letters
2451:
2417:
2413:
2384:
2380:
2348:(1): 73–83.
2345:
2341:
2315:(4): 525–8.
2312:
2308:
2280:
2276:
2239:
2235:
2213:(2): 461–3.
2210:
2206:
2173:
2169:
2136:
2132:
2104:
2100:
2051:
2047:
2018:
2014:
1989:
1985:
1929:
1925:
1915:
1870:
1866:
1856:
1823:
1819:
1812:
1780:(1): 73–83.
1777:
1773:
1763:
1728:
1724:
1714:
1667:
1661:
1636:
1632:
1626:
1600:
1591:
1582:
1573:
1473:
1468:
1464:
1462:
1442:
1414:
1392:to activate
1390:exopeptidase
1387:
1249:BRENDA entry
1175:
1172:
1159:glycoprotein
1145:
1124:
1120:polypeptides
1101:
1093:
1089:
1085:
1081:
1077:
1076:
999:
978:
952:
931:
907:
888:
862:
843:
817:
798:
778:
773:
333:
326:
191:165,498,547
178:165,361,194
53:External IDs
3158:Active site
2914:Cathepsin A
2850:Cathepsin C
2810:Dipeptidase
1453:infertility
1406:vasopressin
1402:enkephalins
1237:IntEnz view
1220:81876-95-1
1197:Identifiers
1163:amphiphilic
704:proteolysis
292:65,146,088
279:65,045,576
31:Identifiers
3429:Metabolism
3408:Categories
3361:Isomerases
3335:Hydrolases
3202:Regulation
1639:: 309–21.
1568:, May 2017
1547:, May 2017
1523:References
1476:beta-cells
1306:structures
1273:KEGG entry
1109:C-terminal
709:metabolism
337:(ortholog)
74:HomoloGene
3424:EC 3.4.17
3240:EC number
3095:: Unknown
2773:Methionyl
2704:proteases
2700:Hydrolase
2612:CiteSeerX
1704:ignored (
1694:cite book
1484:ER stress
1480:apoptosis
1445:endocrine
1425:pituitary
1226:Databases
1208:3.4.17.10
1002:NP_038522
981:NP_001864
955:NM_013494
934:NM_001873
764:Orthologs
441:subiculum
359:beta cell
82:GeneCards
3419:Proteins
3264:Kinetics
3188:Cofactor
3151:Activity
2768:Glutamyl
2758:Cystinyl
2753:Aspartyl
2634:11375130
2595:11373325
2372:18629145
2264:25659964
2207:Genomics
2161:19798125
2035:12479974
2006:10966857
1966:18550819
1907:26120850
1867:PLOS ONE
1848:19798125
1804:18629145
1564:–
1543:–
1490:See also
1429:hormones
1410:oxytocin
1377:proteins
1365:articles
1353:articles
1310:RCSB PDB
1185:Function
1112:arginine
1096:, is an
1050:Wikidata
743:Sources:
618:membrane
449:habenula
375:amygdala
3374:Ligases
3144:Enzymes
2748:Arginyl
2743:Alanine
2654:M14.005
2560:9815277
2525:9662053
2490:9680236
2482:9369230
2436:9275097
2401:9197538
2364:9019408
2329:8864828
2299:8770919
2256:8674818
2227:8449522
2198:6650995
2190:7790890
2153:7663508
2123:7477119
2088:6808517
2056:Bibcode
1957:2448857
1934:Bibcode
1898:4485893
1875:Bibcode
1840:7663508
1796:9019408
1755:2334405
1746:1131319
1653:2897826
1566:Ensembl
1545:Ensembl
1449:obesity
1423:of the
1398:insulin
1332:QuickGO
1297:profile
1280:MetaCyc
1215:CAS no.
876:UniProt
831:Ensembl
770:Species
749:QuickGO
658:nucleus
379:putamen
312:pattern
38:Aliases
3348:Lyases
3093:3.4.99
3009:3.4.21
2932:3.4.17
2902:3.4.16
2884:3.4.15
2837:3.4.14
2802:3.4.13
2763:Leucyl
2730:3.4.11
2717:3.4.11
2665:(MeSH)
2650:MEROPS
2632:
2614:
2593:
2558:
2523:
2488:
2480:
2434:
2399:
2370:
2362:
2327:
2297:
2262:
2254:
2225:
2196:
2188:
2159:
2151:
2121:
2086:
2079:346533
2076:
2033:
2004:
1964:
1954:
1905:
1895:
1846:
1838:
1802:
1794:
1753:
1743:
1682:
1651:
1400:, the
1360:PubMed
1342:Search
1328:AmiGO
1316:PDBsum
1256:ExPASy
1244:BRENDA
1232:IntEnz
1203:EC no.
1116:lysine
1098:enzyme
1092:) and
1036:search
1034:PubMed
909:Q00493
890:P16870
786:Entrez
483:BioGPS
170:4q32.3
70:101932
62:114855
3300:Types
3011:-25:
2719:-19:
2486:S2CID
2448:(PDF)
2368:S2CID
2260:S2CID
2194:S2CID
2157:S2CID
1844:S2CID
1800:S2CID
1292:PRIAM
819:12876
779:Mouse
774:Human
745:Amigo
335:Mouse
328:Human
275:Start
210:Mouse
174:Start
107:Human
78:48052
3392:list
3385:EC7
3379:list
3372:EC6
3366:list
3359:EC5
3353:list
3346:EC4
3340:list
3333:EC3
3327:list
3320:EC2
3314:list
3307:EC1
2710:3.4)
2648:The
2630:PMID
2591:PMID
2556:PMID
2521:PMID
2478:PMID
2432:PMID
2397:PMID
2381:Gene
2360:PMID
2342:Cell
2325:PMID
2295:PMID
2252:PMID
2223:PMID
2186:PMID
2149:PMID
2119:PMID
2084:PMID
2031:PMID
2002:PMID
1962:PMID
1903:PMID
1836:PMID
1792:PMID
1774:Cell
1751:PMID
1706:help
1680:ISBN
1649:PMID
1451:and
1431:and
1372:NCBI
1313:PDBe
1268:KEGG
1179:gene
1129:and
1105:gene
800:1363
318:Bgee
266:Band
227:Chr.
165:Band
124:Chr.
58:OMIM
2622:doi
2608:169
2581:doi
2546:doi
2511:doi
2470:hdl
2460:doi
2456:416
2422:doi
2418:138
2389:doi
2385:190
2350:doi
2317:doi
2285:doi
2281:137
2244:doi
2240:113
2215:doi
2178:doi
2141:doi
2109:doi
2105:333
2074:PMC
2064:doi
2023:doi
1994:doi
1952:PMC
1942:doi
1930:105
1893:PMC
1883:doi
1828:doi
1782:doi
1741:PMC
1733:doi
1729:267
1672:doi
1641:doi
1469:CPE
1465:CPE
1348:PMC
1304:PDB
1176:CPE
1114:or
1102:CPE
1090:CPH
1082:CPE
288:End
187:End
90:OMA
86:CPE
66:MGI
45:CPE
22:CPE
3410::
2957:A2
2920:DD
2912::
2708:EC
2702::
2628:.
2620:.
2606:.
2589:.
2577:49
2575:.
2571:.
2554:.
2542:46
2540:.
2536:.
2519:.
2507:41
2505:.
2501:.
2484:.
2476:.
2468:.
2454:.
2450:.
2430:.
2416:.
2412:.
2395:.
2383:.
2366:.
2358:.
2346:88
2344:.
2340:.
2323:.
2311:.
2293:.
2279:.
2275:.
2258:.
2250:.
2238:.
2221:.
2211:15
2209:.
2192:.
2184:.
2174:65
2172:.
2155:.
2147:.
2137:10
2135:.
2117:.
2103:.
2099:.
2082:.
2072:.
2062:.
2052:79
2050:.
2046:.
2029:.
2019:72
2017:.
2000:.
1990:11
1988:.
1960:.
1950:.
1940:.
1928:.
1924:.
1901:.
1891:.
1881:.
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1834:.
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1798:.
1790:.
1778:88
1776:.
1772:.
1749:.
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1727:.
1723:.
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1696:}}
1692:{{
1678:.
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1637:50
1635:.
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1599:.
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1404:,
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1181:.
1122:.
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294:bp
281:bp
193:bp
180:bp
88:;
84::
80:;
76::
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68::
64:;
60::
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3390:(
3381:)
3377:(
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3364:(
3355:)
3351:(
3342:)
3338:(
3329:)
3325:(
3316:)
3312:(
3136:e
3129:t
3122:v
2972:E
2967:C
2962:B
2952:A
2825:3
2820:2
2815:1
2790:O
2783:2
2778:1
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2636:.
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2090:.
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2037:.
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2008:.
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1968:.
1944::
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