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O42138

- VM3AD_AGKCL

UniProt

O42138 - VM3AD_AGKCL

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
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    • History
      Entry version 87 (01 Oct 2014)
      Sequence version 1 (01 Jan 1998)
      Previous versions | rss
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    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

    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

    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-SubCell

    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

    MIQVLLVTLC LAVFPYQGSS IILESGNVND YEVVYPRKVT VLPKGAVQPK    50
    YEDAMQYEFK VNGEPVVLHL EKNKQLFSKD YSETHYSPDG REITTYPLVE 100
    DHCYYHGRIE NDADSTASIS ACNGLKGHFK LQGEMYLIDP LKLPDSEAHA 150
    VFKYENVEKE DEAPKMCGVT QNWESYEPIK KASQLNLTPE QQAYLDAKKY 200
    VEFVVVLDHG MYTKYKDNLD KIKTRIFEIV NTMNEMFIPL NIRVALICLE 250
    IWSDKDKFNM TSAANVTSIS FRNWRATDLL KRKSHDNAQL LTVIDFDGPT 300
    IGKAYMASMC DPKRSVGIIQ DHSTINLMMA VTMAHEMGHN LGMDHDEKYC 350
    TCGAKSCVMA KALSRQPSKL FSNCSQEDYR KYLIKRRPKC ILNEPNGTDI 400
    VSPPVCGNEL LEVGEECDCG SPTNCQNPCC DAATCKLTPG SQCADGVCCD 450
    QCRFTRAGTE CRQAKDDCDM ADLCTGQSAE CPTDRFQRNG HPCLNDNGYC 500
    YNRTCPTLKN QCIYFFGPNA AVAKDSCFKG NQKSNNHTYC RKENGKKIPC 550
    APQDIKCGRL YCFRNLPGKK NICSVIYTPT DEDIGMVLPG TKCEDGKVCS 600
    NGHCVDVNIA YKSTTGFSQI 620
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U86634 mRNA. Translation: AAC18911.1.
    GQ451435 mRNA. Translation: ACV83929.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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: October 1, 2014
    This is version 87 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programAnimal Toxin Annotation Program
    Annotation programChordata Protein 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