P20165 (VMHR2_PROFL) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Zinc metalloproteinase trimerelysin-2 EC=3.4.24.53 Alternative name(s): H2 metalloproteinase Short name=H2-proteinase Trimerelysin II
Organism	Protobothrops flavoviridis (Habu) (Trimeresurus flavoviridis)
Taxonomic identifier	88087 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Viperidae › Crotalinae › Trimeresurus

Protein attributes

Sequence length	201 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Major venom non-hemorrhagic metalloproteinase.
Catalytic activity	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.
Cofactor	Binds 1 calcium ion per subunit. Binds 1 zinc ion per subunit.
Subcellular location	Secreted.
Tissue specificity	Expressed by the venom gland.
Sequence similarities	Belongs to the venom metalloproteinase family. P-I subfamily. Contains 1 peptidase M12B domain.

Ontologies

Keywords
Cellular component	Secreted
Ligand	Calcium Metal-binding Zinc
Molecular function	Hydrolase Metalloprotease Protease
PTM	Disulfide bond Glycoprotein Pyrrolidone carboxylic acid
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW metalloendopeptidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 201

201

Zinc metalloproteinase trimerelysin-2

PRO_0000078195

Regions

Domain

6 – 201

196

Peptidase M12B

Sites

Active site

143

1

Metal binding

9

1

Calcium By similarity

Metal binding

93

1

Calcium By similarity

Metal binding

142

1

Zinc; catalytic

Metal binding

146

1

Zinc; catalytic

Metal binding

152

1

Zinc; catalytic

Metal binding

196

1

Calcium; via carbonyl oxygen By similarity

Metal binding

199

1

Calcium By similarity

Amino acid modifications

Modified residue

1

1

Pyrrolidone carboxylic acid Ref.1

Glycosylation

72

1

N-linked (GlcNAc...) Potential

Disulfide bond

117 ↔ 196

Ref.1

Disulfide bond

158 ↔ 180

Ref.1

Disulfide bond

160 ↔ 163

Ref.1

Secondary structure

1

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201

Helix Strand Turn

Details...

Beta strand

6 – 14

9

Helix

16 – 21

6

Turn

22 – 24

3

Helix

26 – 44

19

Helix

45 – 47

3

Beta strand

49 – 58

10

Helix

71 – 84

14

Helix

86 – 89

4

Beta strand

93 – 99

7

Helix

104 – 106

3

Beta strand

109 – 111

3

Turn

119 – 121

3

Beta strand

122 – 127

6

Helix

133 – 147

15

Helix

155 – 158

4

Beta strand

161 – 163

3

Helix

179 – 192

14

Helix

195 – 197

3

Sequences

	Sequence		Length	Mass (Da)
	P20165 [UniParc]. Last modified February 1, 1994. Version 3. Checksum: 31DFA648717ADC10	FASTA	201	23,014
	10 20 30 40 50 60 QRFPQRYIEL AIVVDHGMYK KYNQNSDKIK VRVHQMVNHI NEMYRPLNIA ISLNRLQIWS 70 80 90 100 110 120 KKDLITVKSA SNVTLESFGN WRETVLLKQQ NNDCAHLLTA TNLNDNTIGL AYKKGMCNPK 130 140 150 160 170 180 LSVGLVQDYS PNVFMVAVTM THELGHNLGM EHDDKDKCKC EACIMSDVIS DKPSKLFSDC 190 200 SKNDYQTFLT KYNPQCILNA P

References

[1]	"Primary structure of H2-proteinase, a non-hemorrhagic metalloproteinase, isolated from the venom of the habu snake, Trimeresurus flavoviridis." Takeya H., Arakawa M., Miyata T., Iwanaga S., Omori-Satoh T. J. Biochem. 106:151-157(1989) [PubMed: 2777746] [Abstract] Cited for: PROTEIN SEQUENCE, DISULFIDE BONDS. Tissue: Venom.
[2]	"Crystal structure of H2-proteinase from the venom of Trimeresurus flavoviridis." Kumasaka T., Yamamoto M., Moriyama H., Tanaka N., Sato M., Katsube Y., Yamakawa Y., Omori-Satoh T., Iwanaga S., Ueki T. J. Biochem. 119:49-57(1996) [PubMed: 8907175] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH ZINC IONS, METAL-BINDING SITES, DISULFIDES BONDS.
+	Additional computationally mapped references.

Cross-references

Sequence databases

PIR

HYTV2. JU0037.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1WNI	X-ray	2.20	A	1-201	[»]

ProteinModelPortal

P20165.

SMR

P20165. Positions 3-200.

ModBase

Search...

Protein family/group databases

MEROPS

M12.155.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Phylogenomic databases

HOVERGEN

HBG006978.

Family and domain databases

InterPro

IPR024079. MetalloPept_cat_dom.
IPR001590. Peptidase_M12B.
[Graphical view]

Gene3D

G3DSA:3.40.390.10. G3DSA:3.40.390.10. 1 hit.

Pfam

PF01421. Reprolysin. 1 hit.
[Graphical view]

PROSITE

PS50215. ADAM_MEPRO. 1 hit.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

VMHR2_PROFL

Accession

Primary (citable) accession number: P20165

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	February 1, 1994
Last modified:	November 16, 2011
This is version 80 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program