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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: 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)DescriptionActionsGraphical viewLength
Metal bindingi202Calcium 1By similarity1
Metal bindingi286Calcium 1By similarity1
Metal bindingi335Zinc; catalyticBy similarity1
Active sitei336PROSITE-ProRule annotation1
Metal bindingi339Zinc; catalyticBy similarity1
Metal bindingi345Zinc; catalyticBy similarity1
Metal bindingi390Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi393Calcium 1By similarity1
Metal bindingi405Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi408Calcium 2By similarity1
Metal bindingi410Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi412Calcium 2By similarity1
Metal bindingi415Calcium 2By similarity1
Metal bindingi418Calcium 2By similarity1

GO - Molecular functioni

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

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_000032641621 – 189By similarityAdd BLAST169
ChainiPRO_0000326417190 – 620Zinc metalloproteinase-disintegrin-like ACLDAdd BLAST431

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi259N-linked (GlcNAc...)Sequence analysis1
Glycosylationi265N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi310 ↔ 390By similarity
Disulfide bondi350 ↔ 374By similarity
Disulfide bondi352 ↔ 357By similarity
Glycosylationi373N-linked (GlcNAc...)Sequence analysis1
Glycosylationi396N-linked (GlcNAc...)Sequence analysis1
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
Glycosylationi502N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi512 ↔ 562By similarity
Disulfide bondi527 ↔ 573By similarity
Glycosylationi536N-linked (GlcNAc...)Sequence analysis1
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.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini199 – 395Peptidase M12BPROSITE-ProRule annotationAdd BLAST197
Domaini403 – 489DisintegrinPROSITE-ProRule annotationAdd BLAST87

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi467 – 469D/ECD-tripeptide3

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi490 – 620Cys-richAdd BLAST131

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.

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)DescriptionActionsGraphical viewLength
Sequence conflicti96Y → H in ACV83929 (PubMed:19799929).Curated1
Sequence conflicti139D → E in ACV83929 (PubMed:19799929).Curated1
Sequence conflicti268S → L in ACV83929 (PubMed:19799929).Curated1
Sequence conflicti306M → K in ACV83929 (PubMed:19799929).Curated1
Sequence conflicti463Q → A in ACV83929 (PubMed:19799929).Curated1

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

ProteinModelPortaliO42138.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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]
ProtoNetiSearch...

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 2, 2016
This is version 94 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

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.