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Protein

Snake venom metalloproteinase adamalysin-2

Gene
N/A
Organism
Crotalus adamanteus (Eastern diamondback rattlesnake)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Has no significant hemorrhagic activity, but inactivates serpins by limited proteolysis of their reactive-site loops.

Catalytic activityi

Cleavage of 1-Phe-|-Val-2, 5-His-|-Leu-6, 14-Ala-|-Leu-15, 15-Leu-|-Tyr-16, and 16-Tyr-|-Leu-17 of insulin B chain.

Cofactori

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi10Calcium1 Publication1
Metal bindingi94Calcium1 Publication1
Metal bindingi143Zinc; catalytic1
Active sitei144PROSITE-ProRule annotation1
Metal bindingi147Zinc; catalytic1
Metal bindingi153Zinc; catalytic1
Metal bindingi198Calcium; via carbonyl oxygen1 Publication1
Metal bindingi201Calcium1 Publication1

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Calcium, Metal-binding, Zinc

Protein family/group databases

MEROPSiM12.141.

Names & Taxonomyi

Protein namesi
Recommended name:
Snake venom metalloproteinase adamalysin-2 (EC:3.4.24.46)
Short name:
SVMP
Alternative name(s):
Adamalysin II
Proteinase II
OrganismiCrotalus adamanteus (Eastern diamondback rattlesnake)
Taxonomic identifieri8729 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaViperidaeCrotalinaeCrotalus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000781961 – 203Snake venom metalloproteinase adamalysin-2Add BLAST203

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi118 ↔ 198
Disulfide bondi158 ↔ 165

Keywords - PTMi

Disulfide bond

Expressioni

Tissue specificityi

Expressed by the venom gland.

Interactioni

Subunit structurei

Monomer.1 Publication

Structurei

Secondary structure

1203
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi7 – 15Combined sources9
Helixi17 – 22Combined sources6
Turni23 – 25Combined sources3
Helixi27 – 45Combined sources19
Helixi46 – 48Combined sources3
Beta strandi50 – 59Combined sources10
Helixi72 – 85Combined sources14
Turni86 – 89Combined sources4
Beta strandi94 – 100Combined sources7
Helixi105 – 107Combined sources3
Beta strandi110 – 112Combined sources3
Turni120 – 122Combined sources3
Beta strandi123 – 128Combined sources6
Helixi134 – 148Combined sources15
Beta strandi163 – 165Combined sources3
Beta strandi168 – 170Combined sources3
Helixi181 – 194Combined sources14
Helixi197 – 199Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1IAGX-ray2.00A3-203[»]
2AIGX-ray2.60P3-203[»]
3AIGX-ray2.80A3-203[»]
4AIGX-ray2.00A3-203[»]
ProteinModelPortaliP34179.
SMRiP34179.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP34179.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini7 – 203Peptidase M12BPROSITE-ProRule annotationAdd BLAST197

Sequence similaritiesi

Contains 1 peptidase M12B domain.PROSITE-ProRule annotation

Phylogenomic databases

HOVERGENiHBG006978.

Family and domain databases

Gene3Di3.40.390.10. 1 hit.
InterProiIPR024079. MetalloPept_cat_dom.
IPR001590. Peptidase_M12B.
[Graphical view]
PfamiPF01421. Reprolysin. 1 hit.
[Graphical view]
PROSITEiPS50215. ADAM_MEPRO. 1 hit.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P34179-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
QQNLPQRYIE LVVVADRRVF MKYNSDLNII RTRVHEIVNI INGFYRSLNI
60 70 80 90 100
DVSLVNLEIW SGQDPLTIQS SSSNTLNSEG LWREKVLLNK KKKDNAQLLT
110 120 130 140 150
AIEFKCETLG KAYLNSMCNP RSSVGIVKDH SPINLLVAVT MAHELGHNLG
160 170 180 190 200
MEHDGKDCLR GASLCIMRPG LTPGRSYEFS DDSMGYYQKF LNQYKPQCIL

NKP
Length:203
Mass (Da):23,076
Last modified:October 1, 1994 - v2
Checksum:iDAC61380F3C93E48
GO

Cross-referencesi

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1IAGX-ray2.00A3-203[»]
2AIGX-ray2.60P3-203[»]
3AIGX-ray2.80A3-203[»]
4AIGX-ray2.00A3-203[»]
ProteinModelPortaliP34179.
SMRiP34179.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiM12.141.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG006978.

Miscellaneous databases

EvolutionaryTraceiP34179.

Family and domain databases

Gene3Di3.40.390.10. 1 hit.
InterProiIPR024079. MetalloPept_cat_dom.
IPR001590. Peptidase_M12B.
[Graphical view]
PfamiPF01421. Reprolysin. 1 hit.
[Graphical view]
PROSITEiPS50215. ADAM_MEPRO. 1 hit.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiVM12_CROAD
AccessioniPrimary (citable) accession number: P34179
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: October 1, 1994
Last modified: November 2, 2016
This is version 101 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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.