P34179 (VM1A2_CROAD) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Snake venom metalloproteinase adamalysin-2 Short name=SVMP EC=3.4.24.46 Alternative name(s): Adamalysin II Proteinase II
Organism	Crotalus adamanteus (Eastern diamondback rattlesnake)
Taxonomic identifier	8729 [NCBI]
Taxonomic lineage	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Sauropsida › Sauria › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Viperidae › Crotalinae › Crotalus

Protein attributes

Sequence length	203 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Has no significant hemorrhagic activity, but inactivates serpins by limited proteolysis of their reactive-site loops.
Catalytic activity	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.
Cofactor	Binds 1 calcium ion per subunit. Binds 1 zinc ion per subunit.
Subunit structure	Monomer.
Subcellular location	Secreted.
Tissue specificity	Expressed by the venom gland.
Sequence similarities	Belongs to the venom metalloproteinase (M12B) 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
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 – 203

203

Snake venom metalloproteinase adamalysin-2

PRO_0000078196

Regions

Domain

7 – 203

197

Peptidase M12B

Sites

Active site

144

1

By similarity

Metal binding

10

1

Calcium

Metal binding

94

1

Calcium

Metal binding

143

1

Zinc; catalytic

Metal binding

147

1

Zinc; catalytic

Metal binding

153

1

Zinc; catalytic

Metal binding

198

1

Calcium; via carbonyl oxygen

Metal binding

201

1

Calcium

Amino acid modifications

Disulfide bond

118 ↔ 198

Disulfide bond

158 ↔ 165

Secondary structure

1

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203

Helix Strand Turn

Details...

Beta strand

7 – 15

9

Helix

17 – 22

6

Turn

23 – 25

3

Helix

27 – 45

19

Helix

46 – 48

3

Beta strand

50 – 59

10

Helix

72 – 85

14

Turn

86 – 89

4

Beta strand

94 – 100

7

Helix

105 – 107

3

Beta strand

110 – 112

3

Turn

120 – 122

3

Beta strand

123 – 128

6

Helix

134 – 148

15

Beta strand

163 – 165

3

Beta strand

168 – 170

3

Helix

181 – 194

14

Helix

197 – 199

3

Sequences

	Sequence		Length	Mass (Da)
	P34179 [UniParc]. Last modified October 1, 1994. Version 2. Checksum: DAC61380F3C93E48	FASTA	203	23,076
	10 20 30 40 50 60 QQNLPQRYIE LVVVADRRVF MKYNSDLNII RTRVHEIVNI INGFYRSLNI DVSLVNLEIW 70 80 90 100 110 120 SGQDPLTIQS SSSNTLNSEG LWREKVLLNK KKKDNAQLLT AIEFKCETLG KAYLNSMCNP 130 140 150 160 170 180 RSSVGIVKDH SPINLLVAVT MAHELGHNLG MEHDGKDCLR GASLCIMRPG LTPGRSYEFS 190 200 DDSMGYYQKF LNQYKPQCIL NKP

References

[1]	"First structure of a snake venom metalloproteinase: a prototype for matrix metalloproteinases/collagenases." Gomis-Rueth F.-X., Kress L.F., Bode W. EMBO J. 12:4151-4157(1993) [PubMed] [Europe PMC] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE, X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS). Tissue: Venom.
[2]	"Refined 2.0 A X-ray crystal structure of the snake venom zinc-endopeptidase adamalysin II. Primary and tertiary structure determination, refinement, molecular structure and comparison with astacin, collagenase and thermolysin." Gomis-Rueth F.-X., Kress L.F., Kellerman J., Mayr I., Lee X., Huber R., Bode W. J. Mol. Biol. 239:513-544(1994) [PubMed] [Europe PMC] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE, X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS). Tissue: Venom.
[3]	"2-A X-ray structure of adamalysin II complexed with a peptide phosphonate inhibitor adopting a retro-binding mode." Cirilli M., Gallina C., Gavuzzo E., Giordano C., Gomis-Rueth F.-X., Gorini B., Kress L.F., Mazza F., Paradisi M.P., Pochetti G., Politi V. FEBS Lett. 418:319-322(1997) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF COMPLEX WITH AN INHIBITOR.
[4]	"Structures of adamalysin II with peptidic inhibitors. Implications for the design of tumor necrosis factor alpha convertase inhibitors." Gomis-Rueth F.-X., Meyer E.F., Kress L.F., Politi V. Protein Sci. 7:283-292(1998) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH CALCIUM AND ZINC IONS, METAL-BINDING SITES.

Cross-references

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1IAG	X-ray	2.00	A	3-203	[»]
2AIG	X-ray	2.60	P	3-203	[»]
3AIG	X-ray	2.80	A	3-203	[»]
4AIG	X-ray	2.00	A	3-203	[»]

ProteinModelPortal

P34179.

SMR

P34179. Positions 3-203.

ModBase

Search...

Protein family/group databases

MEROPS

M12.141.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Phylogenomic databases

HOVERGEN

HBG006978.

Family and domain databases

Gene3D

3.40.390.10. 1 hit.

InterPro

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

Pfam

PF01421. Reprolysin. 1 hit.
[Graphical view]

PROSITE

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

ProtoNet

Search...

Other

EvolutionaryTrace

P34179.

Entry information

Entry name

VM1A2_CROAD

Accession

Primary (citable) accession number: P34179

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	October 1, 1994
Last modified:	April 3, 2013
This is version 86 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program