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O42138 (VM3AD_AGKCL) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Zinc metalloproteinase-disintegrin-like ACLD

EC=3.4.24.-
Alternative name(s):
Snake venom metalloproteinase
Short name=SVMP
VMP-III
Short name=AclVMP-III
OrganismAgkistrodon contortrix laticinctus (Broad-banded copperhead) (Agkistrodon mokasen laticinctus)
Taxonomic identifier37195 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaViperidaeCrotalinaeAgkistrodon

Protein attributes

Sequence length620 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Is a potent activator of prothrombin (F2). Does not elicit any hemorrhagic response. Barely inhibits collagen-induced platelet aggregation. Binds neither collagen, nor the jararhagin-monoclonal antibody MAJar3. Hydrolyzes the Aalpha-chain of fibrin and fibrinogen, without affecting the Bbeta- and gamma-chains. Is capable of triggering endothelial proinflammatory and procoagulant cell responses, but fails to trigger apoptosis. Induces von Willebrand factor release, and the expression of both ICAM1 and E-selectin (SELE) (without increase in VCAM1) in endothelial cells (HUVEC). Is also able to up-regulate the synthesis of the coagulation factor TF (F3). Enhances nitric oxide (NO) generation, prostacyclin production and interleukin-8 release By similarity.

Cofactor

Binds 1 zinc ion per subunit By similarity.

Enzyme regulation

Inhibited by EDTA and O-phenanthroline. Not inhibited by PMSF, benzamidine, irreversible serine-proteinase inhibitors and cysteine proteinase inhibitor E-64 By similarity.

Subunit structure

Monomer By similarity.

Subcellular location

Secreted By similarity.

Tissue specificity

Expressed by the venom gland.

Sequence similarities

Belongs to the venom metalloproteinase (M12B) family. P-III subfamily. P-IIIa sub-subfamily.

Contains 1 disintegrin domain.

Contains 1 peptidase M12B domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Propeptide21 – 189169 By similarity
PRO_0000326416
Chain190 – 620431Zinc metalloproteinase-disintegrin-like ACLD
PRO_0000326417

Regions

Domain199 – 395197Peptidase M12B
Domain403 – 48987Disintegrin
Motif467 – 4693D/ECD-tripeptide
Compositional bias490 – 620131Cys-rich

Sites

Active site3361 By similarity
Metal binding2021Calcium 1 By similarity
Metal binding2861Calcium 1 By similarity
Metal binding3351Zinc; catalytic By similarity
Metal binding3391Zinc; catalytic By similarity
Metal binding3451Zinc; catalytic By similarity
Metal binding3901Calcium 1; via carbonyl oxygen By similarity
Metal binding3931Calcium 1 By similarity
Metal binding4051Calcium 2; via carbonyl oxygen By similarity
Metal binding4081Calcium 2 By similarity
Metal binding4101Calcium 2; via carbonyl oxygen By similarity
Metal binding4121Calcium 2 By similarity
Metal binding4151Calcium 2 By similarity
Metal binding4181Calcium 2 By similarity

Amino acid modifications

Glycosylation2591N-linked (GlcNAc...) Potential
Glycosylation2651N-linked (GlcNAc...) Potential
Glycosylation3731N-linked (GlcNAc...) Potential
Glycosylation3961N-linked (GlcNAc...) Potential
Glycosylation5021N-linked (GlcNAc...) Potential
Glycosylation5361N-linked (GlcNAc...) Potential
Disulfide bond310 ↔ 390 By similarity
Disulfide bond350 ↔ 374 By similarity
Disulfide bond352 ↔ 357 By similarity
Disulfide bond406 ↔ 435 By similarity
Disulfide bond417 ↔ 430 By similarity
Disulfide bond419 ↔ 425 By similarity
Disulfide bond429 ↔ 452 By similarity
Disulfide bond443 ↔ 449 By similarity
Disulfide bond448 ↔ 474 By similarity
Disulfide bond461 ↔ 481 By similarity
Disulfide bond468 ↔ 500 By similarity
Disulfide bond493 ↔ 505 By similarity
Disulfide bond512 ↔ 562 By similarity
Disulfide bond527 ↔ 573 By similarity
Disulfide bond540 ↔ 550 By similarity
Disulfide bond557 ↔ 599 By similarity
Disulfide bond593 ↔ 604 By similarity

Experimental info

Sequence conflict961Y → H in ACV83929. Ref.2
Sequence conflict1391D → E in ACV83929. Ref.2
Sequence conflict2681S → L in ACV83929. Ref.2
Sequence conflict3061M → K in ACV83929. Ref.2
Sequence conflict4631Q → A in ACV83929. Ref.2

Sequences

Sequence LengthMass (Da)Tools
O42138 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 9016AFEB5AE0BB87

FASTA62069,512
        10         20         30         40         50         60 
MIQVLLVTLC LAVFPYQGSS IILESGNVND YEVVYPRKVT VLPKGAVQPK YEDAMQYEFK 

        70         80         90        100        110        120 
VNGEPVVLHL EKNKQLFSKD YSETHYSPDG REITTYPLVE DHCYYHGRIE NDADSTASIS 

       130        140        150        160        170        180 
ACNGLKGHFK LQGEMYLIDP LKLPDSEAHA VFKYENVEKE DEAPKMCGVT QNWESYEPIK 

       190        200        210        220        230        240 
KASQLNLTPE QQAYLDAKKY VEFVVVLDHG MYTKYKDNLD KIKTRIFEIV NTMNEMFIPL 

       250        260        270        280        290        300 
NIRVALICLE IWSDKDKFNM TSAANVTSIS FRNWRATDLL KRKSHDNAQL LTVIDFDGPT 

       310        320        330        340        350        360 
IGKAYMASMC DPKRSVGIIQ DHSTINLMMA VTMAHEMGHN LGMDHDEKYC TCGAKSCVMA 

       370        380        390        400        410        420 
KALSRQPSKL FSNCSQEDYR KYLIKRRPKC ILNEPNGTDI VSPPVCGNEL LEVGEECDCG 

       430        440        450        460        470        480 
SPTNCQNPCC DAATCKLTPG SQCADGVCCD QCRFTRAGTE CRQAKDDCDM ADLCTGQSAE 

       490        500        510        520        530        540 
CPTDRFQRNG HPCLNDNGYC YNRTCPTLKN QCIYFFGPNA AVAKDSCFKG NQKSNNHTYC 

       550        560        570        580        590        600 
RKENGKKIPC APQDIKCGRL YCFRNLPGKK NICSVIYTPT DEDIGMVLPG TKCEDGKVCS 

       610        620 
NGHCVDVNIA YKSTTGFSQI 

« Hide

References

[1]"Analysis of a cDNA sequence encoding a novel member of the snake venom metalloproteinase, disintegrin-like, cysteine-rich (MDC) protein family from Agkistrodon contortrix laticinctus."
Selistre de Araujo H.S., de Souza D.H.F., Ownby C.L.
Biochim. Biophys. Acta 1342:109-115(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: 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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U86634 mRNA. Translation: AAC18911.1.
GQ451435 mRNA. Translation: ACV83929.1.

3D structure databases

ProteinModelPortalO42138.
SMRO42138. Positions 186-611.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG006978.

Family and domain databases

Gene3D3.40.390.10. 1 hit.
4.10.70.10. 1 hit.
InterProIPR006586. ADAM_Cys-rich.
IPR001762. Blood-coag_inhib_Disintegrin.
IPR018358. Disintegrin_CS.
IPR024079. MetalloPept_cat_dom.
IPR001590. Peptidase_M12B.
IPR002870. Peptidase_M12B_N.
[Graphical view]
PfamPF08516. ADAM_CR. 1 hit.
PF00200. Disintegrin. 1 hit.
PF01562. Pep_M12B_propep. 1 hit.
PF01421. Reprolysin. 1 hit.
[Graphical view]
PRINTSPR00289. DISINTEGRIN.
SMARTSM00608. ACR. 1 hit.
SM00050. DISIN. 1 hit.
[Graphical view]
SUPFAMSSF57552. SSF57552. 1 hit.
PROSITEPS50215. ADAM_MEPRO. 1 hit.
PS00427. DISINTEGRIN_1. 1 hit.
PS50214. DISINTEGRIN_2. 1 hit.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameVM3AD_AGKCL
AccessionPrimary (citable) accession number: O42138
Secondary accession number(s): C9E1R4
Entry history
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: January 1, 1998
Last modified: May 14, 2014
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programAnimal Toxin Annotation Program
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries