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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)DescriptionActionsGraphical viewLength
Metal bindingi201Calcium 11
Metal bindingi285Calcium 11
Metal bindingi333Zinc; catalytic1
Active sitei334PROSITE-ProRule annotation1
Metal bindingi337Zinc; catalytic1
Metal bindingi343Zinc; catalytic1
Metal bindingi388Calcium 1; via carbonyl oxygen1
Metal bindingi391Calcium 11
Metal bindingi403Calcium 2; via carbonyl oxygen1
Metal bindingi406Calcium 21
Metal bindingi408Calcium 2; via carbonyl oxygen1
Metal bindingi410Calcium 21
Metal bindingi413Calcium 21
Metal bindingi416Calcium 21
Metal bindingi467Calcium 31
Metal bindingi468Calcium 3; via carbonyl oxygen1
Metal bindingi470Calcium 31
Metal bindingi482Calcium 31
Metal bindingi483Calcium 3; via carbonyl oxygen1

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)DescriptionActionsGraphical viewLength
Signal peptidei1 – 20Sequence analysisAdd BLAST20
PropeptideiPRO_000040690921 – 189By similarityAdd BLAST169
ChainiPRO_5000144525190 – 609Zinc metalloproteinase-disintegrin-like VAP2BAdd BLAST420
ChainiPRO_0000406910394 – 609Disintegrin-like catrocollastatin-CAdd BLAST216

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei190Pyrrolidone carboxylic acid (Glu)By similarity1
Disulfide bondi308 ↔ 388In zinc metalloproteinase-disintegrin-like VAP2B
Disulfide bondi348 ↔ 372In zinc metalloproteinase-disintegrin-like VAP2B
Disulfide bondi350 ↔ 355In zinc metalloproteinase-disintegrin-like VAP2B
Glycosylationi371N-linked (GlcNAc...)1 Publication1
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

1609
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi198 – 206Combined sources9
Helixi208 – 213Combined sources6
Turni214 – 216Combined sources3
Helixi218 – 237Combined sources20
Turni238 – 240Combined sources3
Beta strandi241 – 250Combined sources10
Helixi263 – 276Combined sources14
Helixi278 – 281Combined sources4
Beta strandi285 – 293Combined sources9
Beta strandi299 – 302Combined sources4
Turni310 – 312Combined sources3
Beta strandi313 – 318Combined sources6
Helixi324 – 338Combined sources15
Beta strandi351 – 353Combined sources3
Beta strandi358 – 360Combined sources3
Beta strandi363 – 365Combined sources3
Helixi371 – 384Combined sources14
Helixi387 – 389Combined sources3
Helixi395 – 397Combined sources3
Beta strandi406 – 408Combined sources3
Turni420 – 422Combined sources3
Turni430 – 432Combined sources3
Beta strandi442 – 444Combined sources3
Beta strandi447 – 452Combined sources6
Beta strandi458 – 460Combined sources3
Turni492 – 495Combined sources4
Helixi506 – 514Combined sources9
Beta strandi518 – 520Combined sources3
Helixi523 – 526Combined sources4
Helixi527 – 530Combined sources4
Beta strandi533 – 535Combined sources3
Beta strandi538 – 541Combined sources4
Beta strandi544 – 546Combined sources3
Helixi550 – 555Combined sources6
Beta strandi560 – 562Combined sources3
Beta strandi569 – 572Combined sources4
Turni580 – 583Combined sources4
Beta strandi590 – 592Combined sources3
Beta strandi595 – 598Combined sources4
Beta strandi601 – 604Combined sources4
Helixi605 – 607Combined sources3

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ90282.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini198 – 393Peptidase M12BPROSITE-ProRule annotationAdd BLAST196
Domaini401 – 487DisintegrinPROSITE-ProRule annotationAdd BLAST87

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni459 – 472Inhibits platelet aggregationAdd BLAST14

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi465 – 467D/ECD-tripeptide3

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi488 – 609Cys-richAdd BLAST122

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)DescriptionActionsGraphical viewLength
Sequence conflicti33 – 34VI → IV in ACV83931 (PubMed:19799929).Curated2
Sequence conflicti71G → E in ACV83931 (PubMed:19799929).Curated1
Sequence conflicti75G → Q in ACV83931 (PubMed:19799929).Curated1
Sequence conflicti144P → S in ACV83931 (PubMed:19799929).Curated1
Sequence conflicti203F → V in ACV83931 (PubMed:19799929).Curated1
Sequence conflicti217D → N in ACV83931 (PubMed:19799929).Curated1
Sequence conflicti307M → V in ACV83931 (PubMed:19799929).Curated1
Sequence conflicti507 – 508YH → VL AA sequence (PubMed:7733877).Curated2
Sequence conflicti516A → G AA sequence (PubMed:7733877).Curated1
Sequence conflicti519Y → V AA sequence (PubMed:7733877).Curated1
Sequence conflicti524S → D AA sequence (PubMed:7733877).Curated1
Sequence conflicti597C → G in ACV83931 (PubMed:19799929).Curated1

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2DW0X-ray2.15A/B191-609[»]
2DW1X-ray2.50A/B191-609[»]
2DW2X-ray2.70A/B191-609[»]
ProteinModelPortaliQ90282.
SMRiQ90282.
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...

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: November 2, 2016
This is version 108 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.