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Protein

Snake venom metalloproteinase trimerelysin-2

Gene
N/A
Organism
Protobothrops flavoviridis (Habu) (Trimeresurus flavoviridis)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Major venom non-hemorrhagic metalloproteinase.

Catalytic activityi

Cleavage of 3-Asn-|-Gln-4, 10-His-|-Leu-11 and 14-Ala-|-Leu-15 in the insulin B chain, and the bond Z-Gly-Pro-|-Leu-Gly-Pro in a small molecule substrate of microbial collagenase.

Cofactori

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi142 – 1421Zinc; catalytic
Active sitei143 – 1431
Metal bindingi146 – 1461Zinc; catalytic
Metal bindingi152 – 1521Zinc; catalytic

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Protein family/group databases

MEROPSiM12.155.

Names & Taxonomyi

Protein namesi
Recommended name:
Snake venom metalloproteinase trimerelysin-2 (EC:3.4.24.53)
Short name:
SVMP
Alternative name(s):
H2 metalloproteinase
Short name:
H2-proteinase
Trimerelysin II
OrganismiProtobothrops flavoviridis (Habu) (Trimeresurus flavoviridis)
Taxonomic identifieri88087 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaViperidaeCrotalinaeProtobothrops

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 201201Snake venom metalloproteinase trimerelysin-2PRO_0000078195Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11Pyrrolidone carboxylic acid1 Publication
Glycosylationi72 – 721N-linked (GlcNAc...)Sequence analysis
Disulfide bondi117 ↔ 196PROSITE-ProRule annotation1 Publication
Disulfide bondi158 ↔ 180PROSITE-ProRule annotation1 Publication
Disulfide bondi160 ↔ 163PROSITE-ProRule annotation1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Pyrrolidone carboxylic acid

Expressioni

Tissue specificityi

Expressed by the venom gland.

Interactioni

Subunit structurei

Monomer.By similarity

Structurei

Secondary structure

1
201
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 149Combined sources
Helixi16 – 216Combined sources
Turni22 – 243Combined sources
Helixi26 – 4419Combined sources
Helixi45 – 473Combined sources
Beta strandi49 – 5810Combined sources
Helixi71 – 8414Combined sources
Helixi86 – 894Combined sources
Beta strandi93 – 997Combined sources
Helixi104 – 1063Combined sources
Beta strandi109 – 1113Combined sources
Turni119 – 1213Combined sources
Beta strandi122 – 1276Combined sources
Helixi133 – 14715Combined sources
Helixi155 – 1584Combined sources
Beta strandi161 – 1633Combined sources
Helixi179 – 19214Combined sources
Helixi195 – 1973Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WNIX-ray2.20A1-201[»]
ProteinModelPortaliP20165.
SMRiP20165. Positions 3-200.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP20165.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini6 – 201196Peptidase M12BPROSITE-ProRule annotationAdd
BLAST

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.

P20165-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
QRFPQRYIEL AIVVDHGMYK KYNQNSDKIK VRVHQMVNHI NEMYRPLNIA
60 70 80 90 100
ISLNRLQIWS KKDLITVKSA SNVTLESFGN WRETVLLKQQ NNDCAHLLTA
110 120 130 140 150
TNLNDNTIGL AYKKGMCNPK LSVGLVQDYS PNVFMVAVTM THELGHNLGM
160 170 180 190 200
EHDDKDKCKC EACIMSDVIS DKPSKLFSDC SKNDYQTFLT KYNPQCILNA

P
Length:201
Mass (Da):23,014
Last modified:February 1, 1994 - v3
Checksum:i31DFA648717ADC10
GO

Sequence databases

PIRiJU0037. HYTV2.

Cross-referencesi

Sequence databases

PIRiJU0037. HYTV2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WNIX-ray2.20A1-201[»]
ProteinModelPortaliP20165.
SMRiP20165. Positions 3-200.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiM12.155.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG006978.

Miscellaneous databases

EvolutionaryTraceiP20165.

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 nameiVM1T2_PROFL
AccessioniPrimary (citable) accession number: P20165
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1994
Last modified: October 14, 2015
This is version 100 of the entry and version 3 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.