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O42138

- VM3AD_AGKCL

UniProt

O42138 - VM3AD_AGKCL

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Protein

Zinc metalloproteinase-disintegrin-like ACLD

Gene
N/A
Organism
Agkistrodon contortrix laticinctus (Broad-banded copperhead) (Agkistrodon mokasen laticinctus)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli

Functioni

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).By similarity

Cofactori

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

Enzyme regulationi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi202 – 2021Calcium 1By similarity
Metal bindingi286 – 2861Calcium 1By similarity
Metal bindingi335 – 3351Zinc; catalyticBy similarity
Active sitei336 – 3361PROSITE-ProRule annotation
Metal bindingi339 – 3391Zinc; catalyticBy similarity
Metal bindingi345 – 3451Zinc; catalyticBy similarity
Metal bindingi390 – 3901Calcium 1; via carbonyl oxygenBy similarity
Metal bindingi393 – 3931Calcium 1By similarity
Metal bindingi405 – 4051Calcium 2; via carbonyl oxygenBy similarity
Metal bindingi408 – 4081Calcium 2By similarity
Metal bindingi410 – 4101Calcium 2; via carbonyl oxygenBy similarity
Metal bindingi412 – 4121Calcium 2By similarity
Metal bindingi415 – 4151Calcium 2By similarity
Metal bindingi418 – 4181Calcium 2By similarity

GO - Molecular functioni

  1. metalloendopeptidase activity Source: InterPro
  2. peptidase activator activity Source: UniProtKB-KW
  3. zinc ion binding Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Blood coagulation cascade activating toxin, Cell adhesion impairing toxin, Hemostasis impairing toxin, Hydrolase, Metalloprotease, Platelet aggregation inhibiting toxin, Protease, Prothrombin activator, Toxin

Keywords - Ligandi

Calcium, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended 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
OrganismiAgkistrodon contortrix laticinctus (Broad-banded copperhead) (Agkistrodon mokasen laticinctus)
Taxonomic identifieri37195 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaViperidaeCrotalinaeAgkistrodon

Subcellular locationi

Secreted By similarity

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-KW
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_0000326416Add
BLAST
Chaini190 – 620431Zinc metalloproteinase-disintegrin-like ACLDPRO_0000326417Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi259 – 2591N-linked (GlcNAc...)Sequence Analysis
Glycosylationi265 – 2651N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi310 ↔ 390By similarity
Disulfide bondi350 ↔ 374By similarity
Disulfide bondi352 ↔ 357By similarity
Glycosylationi373 – 3731N-linked (GlcNAc...)Sequence Analysis
Glycosylationi396 – 3961N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi406 ↔ 435By similarity
Disulfide bondi417 ↔ 430By similarity
Disulfide bondi419 ↔ 425By similarity
Disulfide bondi429 ↔ 452By similarity
Disulfide bondi443 ↔ 449By similarity
Disulfide bondi448 ↔ 474By similarity
Disulfide bondi461 ↔ 481By similarity
Disulfide bondi468 ↔ 500By similarity
Disulfide bondi493 ↔ 505By similarity
Glycosylationi502 – 5021N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi512 ↔ 562By similarity
Disulfide bondi527 ↔ 573By similarity
Glycosylationi536 – 5361N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi540 ↔ 550By similarity
Disulfide bondi557 ↔ 599By similarity
Disulfide bondi593 ↔ 604By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Expressioni

Tissue specificityi

Expressed by the venom gland.

Interactioni

Subunit structurei

Monomer.By similarity

Structurei

3D structure databases

ProteinModelPortaliO42138.
SMRiO42138. Positions 186-611.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini199 – 395197Peptidase M12BPROSITE-ProRule annotationAdd
BLAST
Domaini403 – 48987DisintegrinPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi467 – 4693D/ECD-tripeptide

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi490 – 620131Cys-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.
IPR001762. Blood-coag_inhib_Disintegrin.
IPR018358. Disintegrin_CS.
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.

O42138-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MIQVLLVTLC LAVFPYQGSS IILESGNVND YEVVYPRKVT VLPKGAVQPK
60 70 80 90 100
YEDAMQYEFK VNGEPVVLHL EKNKQLFSKD YSETHYSPDG REITTYPLVE
110 120 130 140 150
DHCYYHGRIE NDADSTASIS ACNGLKGHFK LQGEMYLIDP LKLPDSEAHA
160 170 180 190 200
VFKYENVEKE DEAPKMCGVT QNWESYEPIK KASQLNLTPE QQAYLDAKKY
210 220 230 240 250
VEFVVVLDHG MYTKYKDNLD KIKTRIFEIV NTMNEMFIPL NIRVALICLE
260 270 280 290 300
IWSDKDKFNM TSAANVTSIS FRNWRATDLL KRKSHDNAQL LTVIDFDGPT
310 320 330 340 350
IGKAYMASMC DPKRSVGIIQ DHSTINLMMA VTMAHEMGHN LGMDHDEKYC
360 370 380 390 400
TCGAKSCVMA KALSRQPSKL FSNCSQEDYR KYLIKRRPKC ILNEPNGTDI
410 420 430 440 450
VSPPVCGNEL LEVGEECDCG SPTNCQNPCC DAATCKLTPG SQCADGVCCD
460 470 480 490 500
QCRFTRAGTE CRQAKDDCDM ADLCTGQSAE CPTDRFQRNG HPCLNDNGYC
510 520 530 540 550
YNRTCPTLKN QCIYFFGPNA AVAKDSCFKG NQKSNNHTYC RKENGKKIPC
560 570 580 590 600
APQDIKCGRL YCFRNLPGKK NICSVIYTPT DEDIGMVLPG TKCEDGKVCS
610 620
NGHCVDVNIA YKSTTGFSQI
Length:620
Mass (Da):69,512
Last modified:January 1, 1998 - v1
Checksum:i9016AFEB5AE0BB87
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti96 – 961Y → H in ACV83929. (PubMed:19799929)Curated
Sequence conflicti139 – 1391D → E in ACV83929. (PubMed:19799929)Curated
Sequence conflicti268 – 2681S → L in ACV83929. (PubMed:19799929)Curated
Sequence conflicti306 – 3061M → K in ACV83929. (PubMed:19799929)Curated
Sequence conflicti463 – 4631Q → A in ACV83929. (PubMed:19799929)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U86634 mRNA. Translation: AAC18911.1.
GQ451435 mRNA. Translation: ACV83929.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U86634 mRNA. Translation: AAC18911.1 .
GQ451435 mRNA. Translation: ACV83929.1 .

3D structure databases

ProteinModelPortali O42138.
SMRi O42138. Positions 186-611.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

HOVERGENi HBG006978.

Family and domain databases

Gene3Di 3.40.390.10. 1 hit.
4.10.70.10. 1 hit.
InterProi IPR006586. ADAM_Cys-rich.
IPR001762. Blood-coag_inhib_Disintegrin.
IPR018358. Disintegrin_CS.
IPR024079. MetalloPept_cat_dom.
IPR001590. Peptidase_M12B.
IPR002870. Peptidase_M12B_N.
[Graphical view ]
Pfami PF08516. ADAM_CR. 1 hit.
PF00200. Disintegrin. 1 hit.
PF01562. Pep_M12B_propep. 1 hit.
PF01421. Reprolysin. 1 hit.
[Graphical view ]
PRINTSi PR00289. DISINTEGRIN.
SMARTi SM00608. ACR. 1 hit.
SM00050. DISIN. 1 hit.
[Graphical view ]
SUPFAMi SSF57552. SSF57552. 1 hit.
PROSITEi PS50215. ADAM_MEPRO. 1 hit.
PS00427. DISINTEGRIN_1. 1 hit.
PS50214. DISINTEGRIN_2. 1 hit.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiVM3AD_AGKCL
AccessioniPrimary (citable) accession number: O42138
Secondary accession number(s): C9E1R4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: January 1, 1998
Last modified: November 26, 2014
This is version 89 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

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3