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CUB domain

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323:. Spermadhesins are 110–133 amino acid polypeptides. The binding activity of spermadhesins, e.g. heparin and carbohydrate binding, enables their central role in promoting attachment of the spermatozoa to carbohydrate groups on the glycoproteins found on the surface of oocytes. The spermadhesins from pigs, bulls and stallions show 40–98% similarity in their amino acid sequences and all possess a disulphide bond between adjacent cysteine residues. The porcine spermadhesin polypeptides are coded by five closely linked genes. Bovine spermadhesin relies on a significantly lower number of genes with only two being associated with expression of this protein in bovine seminal fluid. Redundant genetic coding for spermadhesins have been observed in chimpanzees, dogs, and humans. The region correlating to spermadhesin genes in rat and mice DNA is void of any spermadhesin code. These variations in expression and genetic coding of spermadhesins are seen to result from evolutionary adjustments in genes as a consequence of mutations and deletions in genetic material. 218:. The CUB domain (for complement C1r/C1s, Uegf, Bmp1) is a structural motif of approximately 110 residues found almost exclusively in extracellular and plasma membrane-associated proteins, many of which are developmentally regulated. These proteins are involved in a diverse range of functions, including complement activation, developmental patterning, tissue repair, axon guidance and angiogenesis, cell signalling, fertilisation, haemostasis, inflammation, neurotransmission, receptor-mediated endocytosis, and tumour suppression. Many CUB-containing proteins are peptidases belonging to MEROPS peptidase families M12A (astacin) and S1A (chymotrypsin). 326:
Some CUB domains appear to be involved in oligomerisation and/or recognition of substrates and binding partners. For example, in the complement proteases, the CUB domains mediate dimerisation and binding to collagen-like regions of target proteins (e.g. C1q for C1r/C1s). The structure of CUB domains
826:"Insights into how CUB domains can exert specific functions while sharing a common fold: conserved and specific features of the CUB1 domain contribute to the molecular basis of procollagen C-proteinase enhancer-1 activity" 331:. Almost all CUB domains contain four conserved cysteines that probably form two disulphide bridges (C1-C2, C3-C4). The CUB1 domains of C1s and Map19 have calcium-binding sites. 140: 230:
Mammalian complement subcomponents C1s/C1r, which form the calcium-dependent complex C1, the first component of the classical pathway of the complement system.
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Haase B, Schlötterer C, Hundrieser ME, Kuiper H, Distl O, Töpfer-Petersen E, Leeb T., Evolution of the spermadhesin gene family, Gene. (2005) 352, P-20-29
709:"Crystallization and preliminary X-ray diffraction analysis of boar seminal plasma spermadhesin PSP-I/PSP-II, a heterodimer of two CUB domains" 76: 611:"Complement components C1r/C1s, bone morphogenic protein 1 and Xenopus laevis developmentally regulated protein UVS.2 share common repeats" 241:
Mammalian complement-activating component of Ra-reactive factor (RARF), a protease that cleaves the C4 component of complement.
309:
Several of the above proteins consist of a catalytic domain together with several CUB domains interspersed by calcium-binding
279:(A5 antigen), a calcium-independent cell adhesion molecule that functions during the formation of certain neuronal circuits. 160: 287: 346: 259: 238:(Hamster) serine protease Casp, which degrades type I and IV collagen and fibronectin in the presence of calcium. 96: 889: 249: 148: 574:
Bork P, Beckmann G (May 1993). "The CUB domain. A widespread module in developmentally regulated proteins".
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Töpfer-Petersen E, Romero A, Varela PF, Ekhlasi-Hundrieser M, Dostàlovà Z, Sanz L, Calvete JJ (1998).
89: 262:), a protein which induces cartilage and bone formation and expresses metalloendopeptidase activity. 234: 101: 884: 797: 748: 689: 640: 282: 294:
Mammalian hyaluronate-binding protein TSG-6 (or PS4), a serum and growth factor induced protein.
847: 789: 740: 681: 632: 591: 167: 135: 546: 418: 837: 779: 730: 720: 671: 622: 583: 528: 516: 512: 390: 342: 660:"Expression of the CUB domain containing protein 1 (CDCP1) gene in colorectal tumour cells" 502: 496: 474: 470: 456: 438: 428: 376: 364: 127: 442: 402: 356: 328: 310: 255:), a type II membrane protein of the intestinal brush border, which activates trypsinogen. 245: 824:
Blanc G, Font B, Eichenberger D, Moreau C, Ricard-Blum S, Hulmes DJ, Moali C (Jun 2007).
784: 767: 319:
is a subdivision of the CUB domain family and forms a major component of the mammalian
301: 215: 878: 725: 708: 658:
Perry SE, Robinson P, Melcher A, Quirke P, Bühring HJ, Cook GP, Blair GE (Mar 2007).
627: 610: 320: 81: 801: 752: 693: 644: 45: 460: 123: 676: 659: 870: 57: 276: 305:
embryonic protein UVS.2, which is expressed during dorsoanterior development.
851: 842: 825: 685: 587: 793: 744: 636: 595: 85: 866: 768:"Spermadhesins: a new protein family. Facts, hypotheses and perspectives" 52: 735: 252: 707:
Romero A, Varela PF, Sanz L, Töpfer-Petersen E, Calvete JJ (Mar 1996).
550: 484: 414: 69: 64: 555: 508: 480: 408: 394: 155: 197: 191: 185: 179: 173: 524: 492: 488: 452: 424: 398: 384: 372: 368: 862: 542: 538: 532: 520: 464: 446: 432: 380: 338: 117: 40: 360: 352: 334:
Human genes encoding proteins containing this domain include:
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This article incorporates text from the public domain
166: 154: 134: 116: 111: 95: 75: 63: 51: 39: 31: 26: 21: 8: 265:Sea urchin blastula proteins BP10 and SpAN. 273:hypothetical proteins F42A10.8 and R151.5. 226:Proteins containing a CUB domain include: 108: 841: 783: 734: 724: 675: 626: 566: 258:Vertebrate bone morphogenic protein 1 ( 18: 7: 830:The Journal of Biological Chemistry 327:consists of a beta-sandwich with a 895:Single-pass transmembrane proteins 785:10.1111/j.1439-0272.1998.tb01163.x 14: 214:is an evolutionarily conserved 1: 677:10.1016/j.febslet.2007.02.025 288:Strongylocentrotus purpuratus 112:Available protein structures: 726:10.1016/0014-5793(96)00133-0 628:10.1016/0014-5793(91)80433-4 576:Journal of Molecular Biology 911: 860: 107: 297:Mammalian spermadhesins. 843:10.1074/jbc.M701610200 588:10.1006/jmbi.1993.1305 291:(Purple sea urchin). 609:Bork P (Apr 1991). 209: 208: 205: 204: 161:structure summary 902: 856: 855: 845: 836:(23): 16924–33. 821: 815: 812: 806: 805: 787: 763: 757: 756: 738: 728: 704: 698: 697: 679: 655: 649: 648: 630: 606: 600: 599: 571: 200: 194: 188: 182: 176: 109: 19: 910: 909: 905: 904: 903: 901: 900: 899: 890:Protein domains 875: 874: 873: 859: 823: 822: 818: 813: 809: 778:(4–5): 217–24. 765: 764: 760: 706: 705: 701: 657: 656: 652: 608: 607: 603: 573: 572: 568: 564: 329:jelly-roll fold 285:I and III from 246:enteropeptidase 224: 196: 190: 184: 178: 172: 17: 12: 11: 5: 908: 906: 898: 897: 892: 887: 877: 876: 858: 857: 816: 807: 758: 699: 670:(6): 1137–42. 650: 601: 565: 563: 560: 559: 558: 553: 536: 506: 500: 478: 468: 450: 436: 422: 412: 406: 388: 350: 307: 306: 302:Xenopus laevis 298: 295: 292: 280: 274: 266: 263: 256: 242: 239: 235:Cricetidae sp. 231: 223: 220: 216:protein domain 207: 206: 203: 202: 170: 164: 163: 158: 152: 151: 138: 132: 131: 121: 114: 113: 105: 104: 99: 93: 92: 79: 73: 72: 67: 61: 60: 55: 49: 48: 43: 37: 36: 33: 29: 28: 24: 23: 16:Protein domain 15: 13: 10: 9: 6: 4: 3: 2: 907: 896: 893: 891: 888: 886: 883: 882: 880: 872: 868: 864: 853: 849: 844: 839: 835: 831: 827: 820: 817: 811: 808: 803: 799: 795: 791: 786: 781: 777: 773: 769: 762: 759: 754: 750: 746: 742: 737: 732: 727: 722: 719:(1–2): 15–7. 718: 714: 710: 703: 700: 695: 691: 687: 683: 678: 673: 669: 665: 661: 654: 651: 646: 642: 638: 634: 629: 624: 620: 616: 612: 605: 602: 597: 593: 589: 585: 582:(2): 539–45. 581: 577: 570: 567: 561: 557: 554: 552: 548: 544: 540: 537: 534: 530: 526: 522: 518: 514: 510: 507: 504: 501: 498: 494: 490: 486: 482: 479: 476: 472: 469: 466: 462: 458: 454: 451: 448: 444: 440: 437: 434: 430: 426: 423: 420: 416: 413: 410: 407: 404: 400: 396: 392: 389: 386: 382: 378: 374: 370: 366: 362: 358: 354: 351: 348: 344: 340: 337: 336: 335: 332: 330: 324: 322: 321:seminal fluid 318: 314: 312: 304: 303: 299: 296: 293: 290: 289: 284: 281: 278: 275: 272: 271: 267: 264: 261: 257: 254: 251: 247: 243: 240: 237: 236: 232: 229: 228: 227: 221: 219: 217: 213: 199: 193: 189:B:28-134 187: 181: 175: 171: 169: 165: 162: 159: 157: 153: 150: 146: 142: 139: 137: 133: 129: 125: 122: 119: 115: 110: 106: 103: 100: 98: 94: 91: 87: 83: 80: 78: 74: 71: 68: 66: 62: 59: 56: 54: 50: 47: 44: 42: 38: 34: 30: 25: 20: 833: 829: 819: 810: 775: 771: 761: 736:10261/246550 716: 713:FEBS Letters 712: 702: 667: 664:FEBS Letters 663: 653: 618: 615:FEBS Letters 614: 604: 579: 575: 569: 333: 325: 317:Spermadhesin 316: 315: 308: 300: 286: 283:Fibropellins 268: 233: 225: 211: 210: 195:B:30-128 183:A:28-134 177:A:18-127 621:(1): 9–12. 311:EGF domains 244:Vertebrate 212:CUB domain 27:Identifiers 885:CUB domain 879:Categories 772:Andrologia 562:References 277:Neuropilin 270:C. elegans 124:structures 22:CUB domain 871:IPR000858 70:PDOC00758 58:IPR000859 867:InterPro 852:17446170 802:24941844 753:37515421 694:30701692 686:17335815 645:33375087 253:3.4.21.9 222:Examples 141:RCSB PDB 53:InterPro 794:9739418 745:8612739 637:2026272 596:8510165 551:TNFAIP6 547:TMPRSS7 485:PCOLCE2 419:KREMEN2 415:KREMEN1 201::30-127 102:cd00041 65:PROSITE 46:PF00431 850:  800:  792:  751:  743:  692:  684:  643:  635:  594:  529:SEZ6L2 517:SCUBE3 513:SCUBE2 509:SCUBE1 481:PCOLCE 409:GPR126 395:DCBLD2 391:DCBLD1 343:ATRNL1 156:PDBsum 130:  120:  90:SUPFAM 32:Symbol 798:S2CID 749:S2CID 690:S2CID 641:S2CID 556:psk-2 525:SEZ6L 497:PRSS7 493:PDGFD 489:PDGFC 475:OVCH2 471:OVCH1 457:NETO2 453:NETO1 443:MASP2 439:MASP1 429:LRP12 425:LRP10 399:DMBT1 385:CUZD1 377:CSMD3 373:CSMD2 369:CSMD1 365:CDCP2 260:BMP-1 86:SCOPe 77:SCOP2 865:and 863:Pfam 848:PMID 790:PMID 741:PMID 682:PMID 633:PMID 592:PMID 543:TLL2 539:TLL1 533:ST14 521:SEZ6 503:RAMP 465:NRP2 461:NRP1 447:MFRP 433:LRP3 403:DREG 381:CUBN 357:C1RL 347:BMP1 339:ATRN 198:1sfp 192:1spp 186:1szb 180:1nt0 174:1nzi 149:PDBj 145:PDBe 128:ECOD 118:Pfam 82:1sfp 41:Pfam 838:doi 834:282 780:doi 731:hdl 721:doi 717:382 672:doi 668:581 623:doi 619:282 584:doi 580:231 361:C1S 353:C1R 168:PDB 136:PDB 97:CDD 35:CUB 881:: 869:: 846:. 832:. 828:. 796:. 788:. 776:30 774:. 770:. 747:. 739:. 729:. 715:. 711:. 688:. 680:. 666:. 662:. 639:. 631:. 617:. 613:. 590:. 578:. 549:, 545:, 541:, 531:, 527:, 523:, 519:, 515:, 511:, 495:, 491:, 487:, 483:, 473:, 463:, 459:, 455:, 445:, 441:, 431:, 427:, 417:, 401:, 397:, 393:, 383:, 379:, 375:, 371:, 367:, 363:, 359:, 355:, 345:, 341:, 313:. 250:EC 147:; 143:; 126:/ 88:/ 84:/ 854:. 840:: 804:. 782:: 755:. 733:: 723:: 696:. 674:: 647:. 625:: 598:. 586:: 535:, 505:, 499:, 477:, 467:, 449:, 435:, 421:, 411:, 405:, 387:, 349:, 248:(

Index

Pfam
PF00431
InterPro
IPR000859
PROSITE
PDOC00758
SCOP2
1sfp
SCOPe
SUPFAM
CDD
cd00041
Pfam
structures
ECOD
PDB
RCSB PDB
PDBe
PDBj
PDBsum
structure summary
PDB
1nzi
1nt0
1szb
1spp
1sfp
protein domain
Cricetidae sp.
enteropeptidase

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