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Protein

Zinc metalloproteinase-disintegrin-like VAP2B

Gene
N/A
Organism
Crotalus atrox (Western diamondback rattlesnake)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Zinc metalloproteinase-disintegrin-like VAP2B: zinc metalloprotease that abolishes platelet aggregation induced by collagen, but has no effect on platelet aggregation induced by ADP or thromboxane analog. This inhibition may be due to its ability to bind collagen and block the binding site on collagen for platelets and/or to its ability to bind to the platelet alpha-2/beta-1 collagen receptor (ITGA2/ITGB1) to block its interaction with collagen and hence prevent platelet stimulation.
Disintegrin catrocollastatin-C: abolishes platelet aggregation induced by collagen (IC50=66 nM) but not ADP-stimulated platelet aggregation. This inhibition may be due to its ability to bind collagen and block the binding site on collagen for platelets and/or to its ability to bind to the platelet alpha-2/beta-1 collagen receptor (ITGA2/ITGB1) to block its interaction with collagen and hence prevent platelet stimulation.

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi201 – 2011Calcium 1
Metal bindingi285 – 2851Calcium 1
Metal bindingi333 – 3331Zinc; catalytic
Active sitei334 – 3341PROSITE-ProRule annotation
Metal bindingi337 – 3371Zinc; catalytic
Metal bindingi343 – 3431Zinc; catalytic
Metal bindingi388 – 3881Calcium 1; via carbonyl oxygen
Metal bindingi391 – 3911Calcium 1
Metal bindingi403 – 4031Calcium 2; via carbonyl oxygen
Metal bindingi406 – 4061Calcium 2
Metal bindingi408 – 4081Calcium 2; via carbonyl oxygen
Metal bindingi410 – 4101Calcium 2
Metal bindingi413 – 4131Calcium 2
Metal bindingi416 – 4161Calcium 2
Metal bindingi467 – 4671Calcium 3
Metal bindingi468 – 4681Calcium 3; via carbonyl oxygen
Metal bindingi470 – 4701Calcium 3
Metal bindingi482 – 4821Calcium 3
Metal bindingi483 – 4831Calcium 3; via carbonyl oxygen

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Cell adhesion impairing toxin, Hemostasis impairing toxin, Hydrolase, Metalloprotease, Platelet aggregation inhibiting toxin, Protease, Toxin

Keywords - Ligandi

Calcium, Metal-binding, Zinc

Protein family/group databases

MEROPSiM12.332.

Names & Taxonomyi

Protein namesi
Recommended name:
Zinc metalloproteinase-disintegrin-like VAP2B (EC:3.4.24.-)
Alternative name(s):
Catrocollastatin
Snake venom metalloproteinase
Short name:
SVMP
Vascular apoptosis-inducing protein 2B
Short name:
VAP2B
Cleaved into the following chain:
OrganismiCrotalus atrox (Western diamondback rattlesnake)
Taxonomic identifieri8730 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaViperidaeCrotalinaeCrotalus

Subcellular locationi

  • Secreted 1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Sequence analysisAdd
BLAST
Propeptidei21 – 189169By similarityPRO_0000406909Add
BLAST
Chaini190 – 609420Zinc metalloproteinase-disintegrin-like VAP2BPRO_5000144525Add
BLAST
Chaini394 – 609216Disintegrin-like catrocollastatin-CPRO_0000406910Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei190 – 1901Pyrrolidone carboxylic acid (Glu)By similarity
Disulfide bondi308 ↔ 388In zinc metalloproteinase-disintegrin-like VAP2B
Disulfide bondi348 ↔ 372In zinc metalloproteinase-disintegrin-like VAP2B
Disulfide bondi350 ↔ 355In zinc metalloproteinase-disintegrin-like VAP2B
Glycosylationi371 – 3711N-linked (GlcNAc...)1 Publication
Disulfide bondi404 ↔ 433In zinc metalloproteinase-disintegrin-like VAP2B; alternate
Disulfide bondi404 ↔ 423In disintegrin-like catrocollastatin-C; alternate
Disulfide bondi415 ↔ 433In disintegrin-like catrocollastatin-C; alternate
Disulfide bondi415 ↔ 428In zinc metalloproteinase-disintegrin-like VAP2B; alternate
Disulfide bondi417 ↔ 423In zinc metalloproteinase-disintegrin-like VAP2B; alternate
Disulfide bondi427 ↔ 450In zinc metalloproteinase-disintegrin-like VAP2B
Disulfide bondi441 ↔ 447In zinc metalloproteinase-disintegrin-like VAP2B
Disulfide bondi446 ↔ 472In zinc metalloproteinase-disintegrin-like VAP2B
Disulfide bondi459 ↔ 479In both disintegrin-like catrocollastatin-C and zinc metalloproteinase-disintegrin-like VAP2B
Disulfide bondi466 ↔ 498In zinc metalloproteinase-disintegrin-like VAP2B; alternate
Disulfide bondi466 ↔ 491In disintegrin-like catrocollastatin-C; alternate
Disulfide bondi491 ↔ 503In zinc metalloproteinase-disintegrin-like VAP2B; alternate
Disulfide bondi498 ↔ 503In disintegrin-like catrocollastatin-C
Disulfide bondi510 ↔ 560In zinc metalloproteinase-disintegrin-like VAP2B; alternate
Disulfide bondi510 ↔ 525In disintegrin-like catrocollastatin-C; alternate
Disulfide bondi525 ↔ 571In zinc metalloproteinase-disintegrin-like VAP2B; alternate
Disulfide bondi538 ↔ 548In zinc metalloproteinase-disintegrin-like VAP2B; alternate
Disulfide bondi548 ↔ 555In disintegrin-like catrocollastatin-C; alternate
Disulfide bondi555 ↔ 597In zinc metalloproteinase-disintegrin-like VAP2B; alternate
Disulfide bondi560 ↔ 571In disintegrin-like catrocollastatin-C
Disulfide bondi591 ↔ 602In zinc metalloproteinase-disintegrin-like VAP2B; alternate
Disulfide bondi597 ↔ 602In disintegrin-like catrocollastatin-C

Post-translational modificationi

The N-terminus is blocked.

Keywords - PTMi

Disulfide bond, Glycoprotein, Pyrrolidone carboxylic acid, Zymogen

Expressioni

Tissue specificityi

Expressed by the venom gland.1 Publication

Interactioni

Subunit structurei

Monomer (PubMed:17485084) or heterodimer; non-covalently linked (PubMed:17497365). Interacts with fibrillar collagen.4 Publications

Structurei

Secondary structure

1
609
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi198 – 2069Combined sources
Helixi208 – 2136Combined sources
Turni214 – 2163Combined sources
Helixi218 – 23720Combined sources
Turni238 – 2403Combined sources
Beta strandi241 – 25010Combined sources
Helixi263 – 27614Combined sources
Helixi278 – 2814Combined sources
Beta strandi285 – 2939Combined sources
Beta strandi299 – 3024Combined sources
Turni310 – 3123Combined sources
Beta strandi313 – 3186Combined sources
Helixi324 – 33815Combined sources
Beta strandi351 – 3533Combined sources
Beta strandi358 – 3603Combined sources
Beta strandi363 – 3653Combined sources
Helixi371 – 38414Combined sources
Helixi387 – 3893Combined sources
Helixi395 – 3973Combined sources
Beta strandi406 – 4083Combined sources
Turni420 – 4223Combined sources
Turni430 – 4323Combined sources
Beta strandi442 – 4443Combined sources
Beta strandi447 – 4526Combined sources
Beta strandi458 – 4603Combined sources
Turni492 – 4954Combined sources
Helixi506 – 5149Combined sources
Beta strandi518 – 5203Combined sources
Helixi523 – 5264Combined sources
Helixi527 – 5304Combined sources
Beta strandi533 – 5353Combined sources
Beta strandi538 – 5414Combined sources
Beta strandi544 – 5463Combined sources
Helixi550 – 5556Combined sources
Beta strandi560 – 5623Combined sources
Beta strandi569 – 5724Combined sources
Turni580 – 5834Combined sources
Beta strandi590 – 5923Combined sources
Beta strandi595 – 5984Combined sources
Beta strandi601 – 6044Combined sources
Helixi605 – 6073Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DW0X-ray2.15A/B191-609[»]
2DW1X-ray2.50A/B191-609[»]
2DW2X-ray2.70A/B191-609[»]
ProteinModelPortaliQ90282.
SMRiQ90282. Positions 195-609.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ90282.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini198 – 393196Peptidase M12BPROSITE-ProRule annotationAdd
BLAST
Domaini401 – 48787DisintegrinPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni459 – 47214Inhibits platelet aggregationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi465 – 4673D/ECD-tripeptide

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi488 – 609122Cys-richAdd
BLAST

Sequence similaritiesi

Contains 1 disintegrin domain.PROSITE-ProRule annotation
Contains 1 peptidase M12B domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

HOVERGENiHBG006978.

Family and domain databases

Gene3Di3.40.390.10. 1 hit.
4.10.70.10. 1 hit.
InterProiIPR006586. ADAM_Cys-rich.
IPR018358. Disintegrin_CS.
IPR001762. Disintegrin_dom.
IPR024079. MetalloPept_cat_dom.
IPR001590. Peptidase_M12B.
IPR002870. Peptidase_M12B_N.
[Graphical view]
PfamiPF08516. ADAM_CR. 1 hit.
PF00200. Disintegrin. 1 hit.
PF01562. Pep_M12B_propep. 1 hit.
PF01421. Reprolysin. 1 hit.
[Graphical view]
PRINTSiPR00289. DISINTEGRIN.
SMARTiSM00608. ACR. 1 hit.
SM00050. DISIN. 1 hit.
[Graphical view]
SUPFAMiSSF57552. SSF57552. 1 hit.
PROSITEiPS50215. ADAM_MEPRO. 1 hit.
PS00427. DISINTEGRIN_1. 1 hit.
PS50214. DISINTEGRIN_2. 1 hit.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q90282-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIQVLLVTIC LAAFPYQGSS IILESGNVND YEVIYPRKVT ALPKGAVQPK
60 70 80 90 100
YEDAMQYELK VNGEPVVLHL GKNKGLFSKD YSETHYSPDG REITTYPLVE
110 120 130 140 150
DHCYYHGRIE NDADSTASIS ACNGLKGHFK LQGEMYLIEP LKLPDSEAHA
160 170 180 190 200
VYKYENVEKE DEALKMCGVT QNWESYEPIK KASQLVVTAE HQKYNPFRFV
210 220 230 240 250
ELFLVVDKAM VTKNNGDLDK IKTRMYEIVN TVNEIYRYMY IHVALVGLEI
260 270 280 290 300
WSNEDKITVK PEAGYTLNAF GEWRKTDLLT RKKHDNAQLL TAIDLDRVIG
310 320 330 340 350
LAYVGSMCHP KRSTGIIQDY SEINLVVAVI MAHEMGHNLG INHDSGYCSC
360 370 380 390 400
GDYACIMRPE ISPEPSTFFS NCSYFECWDF IMNHNPECIL NEPLGTDIIS
410 420 430 440 450
PPVCGNELLE VGEECDCGTP ENCQNECCDA ATCKLKSGSQ CGHGDCCEQC
460 470 480 490 500
KFSKSGTECR ASMSECDPAE HCTGQSSECP ADVFHKNGQP CLDNYGYCYN
510 520 530 540 550
GNCPIMYHQC YDLFGADVYE AEDSCFERNQ KGNYYGYCRK ENGNKIPCAP
560 570 580 590 600
EDVKCGRLYC KDNSPGQNNP CKMFYSNEDE HKGMVLPGTK CADGKVCSNG

HCVDVATAY
Length:609
Mass (Da):68,248
Last modified:November 1, 1996 - v1
Checksum:iD58876161F64FAA5
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti33 – 342VI → IV in ACV83931 (PubMed:19799929).Curated
Sequence conflicti71 – 711G → E in ACV83931 (PubMed:19799929).Curated
Sequence conflicti75 – 751G → Q in ACV83931 (PubMed:19799929).Curated
Sequence conflicti144 – 1441P → S in ACV83931 (PubMed:19799929).Curated
Sequence conflicti203 – 2031F → V in ACV83931 (PubMed:19799929).Curated
Sequence conflicti217 – 2171D → N in ACV83931 (PubMed:19799929).Curated
Sequence conflicti307 – 3071M → V in ACV83931 (PubMed:19799929).Curated
Sequence conflicti507 – 5082YH → VL AA sequence (PubMed:7733877).Curated
Sequence conflicti516 – 5161A → G AA sequence (PubMed:7733877).Curated
Sequence conflicti519 – 5191Y → V AA sequence (PubMed:7733877).Curated
Sequence conflicti524 – 5241S → D AA sequence (PubMed:7733877).Curated
Sequence conflicti597 – 5971C → G in ACV83931 (PubMed:19799929).Curated

Mass spectrometryi

Molecular mass is 23532±2 Da from positions 394 - 609. Determined by ESI. Average mass.1 Publication
Molecular mass is 23572 Da from positions 394 - 609. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U21003 mRNA. Translation: AAC59672.1.
GQ451437 mRNA. Translation: ACV83931.1.
PIRiS55264.
S55270.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U21003 mRNA. Translation: AAC59672.1.
GQ451437 mRNA. Translation: ACV83931.1.
PIRiS55264.
S55270.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DW0X-ray2.15A/B191-609[»]
2DW1X-ray2.50A/B191-609[»]
2DW2X-ray2.70A/B191-609[»]
ProteinModelPortaliQ90282.
SMRiQ90282. Positions 195-609.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiM12.332.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG006978.

Miscellaneous databases

EvolutionaryTraceiQ90282.

Family and domain databases

Gene3Di3.40.390.10. 1 hit.
4.10.70.10. 1 hit.
InterProiIPR006586. ADAM_Cys-rich.
IPR018358. Disintegrin_CS.
IPR001762. Disintegrin_dom.
IPR024079. MetalloPept_cat_dom.
IPR001590. Peptidase_M12B.
IPR002870. Peptidase_M12B_N.
[Graphical view]
PfamiPF08516. ADAM_CR. 1 hit.
PF00200. Disintegrin. 1 hit.
PF01562. Pep_M12B_propep. 1 hit.
PF01421. Reprolysin. 1 hit.
[Graphical view]
PRINTSiPR00289. DISINTEGRIN.
SMARTiSM00608. ACR. 1 hit.
SM00050. DISIN. 1 hit.
[Graphical view]
SUPFAMiSSF57552. SSF57552. 1 hit.
PROSITEiPS50215. ADAM_MEPRO. 1 hit.
PS00427. DISINTEGRIN_1. 1 hit.
PS50214. DISINTEGRIN_2. 1 hit.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Molecular cloning and expression of catrocollastatin, a snake-venom protein from Crotalus atrox (western diamondback rattlesnake) which inhibits platelet adhesion to collagen."
    Zhou Q., Smith J.B., Grossman M.H.
    Biochem. J. 307:411-417(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 240-279 AND 507-537, FUNCTION, SUBUNIT.
    Tissue: Venom and Venom gland.
  2. "Molecular cloning and characterization of cDNAs encoding metalloproteinases from snake venom glands."
    Jia Y., Perez J.C.
    Toxicon 55:462-469(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Venom gland.
  3. "Exploring the venom proteome of the western diamondback rattlesnake, Crotalus atrox, via snake venomics and combinatorial peptide ligand library approaches."
    Calvete J.J., Fasoli E., Sanz L., Boschetti E., Righetti P.G.
    J. Proteome Res. 8:3055-3067(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 199-208; 225-237; 257-274; 284-297; 298-312; 437-451; 532-539 AND 596-609, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Venom.
  4. "cDNA cloning and some additional peptide characterization of a single-chain vascular apoptosis-inducing protein, VAP2."
    Masuda S., Maeda H., Miao J.Y., Hayashi H., Araki S.
    Endothelium 14:89-96(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 226-236 AND 240-250, SUBUNIT.
    Tissue: Venom and Venom gland.
  5. "Sequence and biological activity of catrocollastatin-C: a disintegrin-like/cysteine-rich two-domain protein from Crotalus atrox venom."
    Shimokawa K., Shannon J.D., Jia L.-G., Fox J.W.
    Arch. Biochem. Biophys. 343:35-43(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 394-609, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MASS SPECTROMETRY (CATROCOLLASTATIN-C), SYNTHESIS OF CYCLIC PEPTIDE OF 459-472.
    Tissue: Venom.
  6. "The disulfide bond pattern of catrocollastatin C, a disintegrin-like/cysteine-rich protein isolated from Crotalus atrox venom."
    Calvete J.J., Moreno-Murciano M.P., Sanz L., Jurgens M., Schrader M., Raida M., Benjamin D.C., Fox J.W.
    Protein Sci. 9:1365-1373(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 394-609, MASS SPECTROMETRY, DISULFIDE BONDS (CATROCOLLASTATIN-C).
  7. "The hemorrhagin catrocollastatin inhibits collagen-induced platelet aggregation by binding to collagen via its disintegrin-like domain."
    Zhou Q., Dangelmaier C., Smith J.B.
    Biochem. Biophys. Res. Commun. 219:720-726(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, INTERACTION WITH COLLAGEN, SYNTHESIS OF CYCLIC PEPTIDE OF 459-472 (CATROCOLLASTATIN).
  8. "Crystallization and preliminary X-ray crystallographic analysis of two vascular apoptosis-inducing proteins (VAPs) from Crotalus atrox venom."
    Igarashi T., Oishi Y., Araki S., Mori H., Takeda S.
    Acta Crystallogr. F 62:688-691(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: CRYSTALLIZATION.
    Tissue: Venom.
  9. "Crystal structures of catrocollastatin/VAP2B reveal a dynamic, modular architecture of ADAM/adamalysin/reprolysin family proteins."
    Igarashi T., Araki S., Mori H., Takeda S.
    FEBS Lett. 581:2416-2422(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 191-609, METAL-BINDING SITES, DISULFIDE BONDS, GLYCOSYLATION AT ASN-371.
    Tissue: Venom.

Entry informationi

Entry nameiVM3VB_CROAT
AccessioniPrimary (citable) accession number: Q90282
Secondary accession number(s): C9E1R6, Q7LZK3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 5, 2011
Last sequence update: November 1, 1996
Last modified: October 14, 2015
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
Annotation programAnimal Toxin Annotation Program

Miscellaneousi

Miscellaneous

Catrocollastatin-C represents at least 0.5% of the total protein in the venom.

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.