NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Venom gland;
DOI=10.1006/abbi.1994.1026; PubMed=8311451 [NCBI, ExPASy, EBI, Israel, Japan]
Hite L.A., Jia L.-G., Bjarnason J.B., Fox J.W.;
"cDNA sequences for four snake venom metalloproteinases: structure, classification, and their relationship to mammalian reproductive proteins.";
Arch. Biochem. Biophys. 308:182-191(1994).

Comments

FUNCTION: This protein is a zinc metalloprotease from snake venom that possesses hemorrhagic activity (By similarity).
CATALYTIC ACTIVITY: Cleavage of 5-His-|-Leu-6, 10-His-|-Leu-11, 14-Ala-|-Leu-15, 16-Tyr-|-Leu-17 and 23-Gly-|-Phe-24 of insulin B chain; identical to the cleavage of insulin B chain by atrolysin C. Also cleaves Xaa-|-Ser bonds in glucagon.
COFACTOR: Binds 1 zinc ion per subunit (By similarity).
SUBUNIT: Monomer (By similarity).
SUBCELLULAR LOCATION: Secreted (By similarity).
TISSUE SPECIFICITY: Expressed by the venom gland.
SIMILARITY: Belongs to the snake venom metalloproteinase family. P-I subfamily.
SIMILARITY: Contains 1 peptidase M12B domain [view classification].

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

U01235; AAA03327.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S41608; S41608.

3D structure databases

HSSP

P34179; 4AIG. [HSSP ENTRY / PDB]

SMR

Q90391; 193-393.

ModBase

Q90391.

Protein family/group databases

MEROPS

M12.143; -.

Ontologies

GO:0005576;	Cellular component: extracellular region (inferred from electronic annotation from UniProtKB-KW).
GO:0005509;	Molecular function: calcium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0004222;	Molecular function: metalloendopeptidase activity (inferred from electronic annotation from InterPro).
GO:0008270;	Molecular function: zinc ion binding (inferred from electronic annotation from InterPro).
GO:0009405;	Biological process: pathogenesis (inferred from electronic annotation from UniProtKB-KW).
GO:0006508;	Biological process: proteolysis (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR006025; Pept_M_Zn_BS.
IPR001590; Peptidase_M12B.
IPR002870; Peptidase_M12B_N.
Graphical view of domain structure.

Pfam

PF01562; Pep_M12B_propep; 1.
PF01421; Reprolysin; 1.
Pfam graphical view of domain structure.

PROSITE

PS50215; ADAM_MEPRO; 1.
PS00142; ZINC_PROTEASE; 1.
PROSITE graphical view of domain structure (profiles).

ProtoNet

Q90391.

Phylogenomic databases

HOVERGEN

Q90391; -.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Calcium; Hydrolase; Metal-binding; Metalloprotease; Protease; Pyrrolidone carboxylic acid; Secreted; Signal; Toxin; Zinc; Zymogen.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 20`	`20`	`Potential.`
`PROPEP`	`21 190`	`170`	`By similarity.`	`PRO_0000329995`
`CHAIN`	`191 393`	`203`	`Zinc metalloproteinase atrolysin-B.`	`PRO_0000329996`
`PROPEP`	`394 414`	`21`	`By similarity.`	`PRO_0000329997`
`DOMAIN`	`197 393`	`197`	`Peptidase M12B.`
`ACT_SITE`	`334 334`		`By similarity.`
`METAL`	`200 200`		`Calcium (By similarity).`
`METAL`	`284 284`		`Calcium (By similarity).`
`METAL`	`333 333`		`Zinc; catalytic (By similarity).`
`METAL`	`337 337`		`Zinc; catalytic (By similarity).`
`METAL`	`343 343`		`Zinc; catalytic (By similarity).`
`METAL`	`388 388`		`Calcium; via carbonyl oxygen (By similarity).`
`METAL`	`391 391`		`Calcium (By similarity).`
`MOD_RES`	`191 191`		`Pyrrolidone carboxylic acid (By similarity).`
`DISULFID`	`308 388`		`By similarity.`
`DISULFID`	`348 355`		`By similarity.`

Sequence information

Length: 414 AA [This is the length of the unprocessed precursor]

Molecular weight: 46806 Da [This is the MW of the unprocessed precursor]

CRC64: EBF3D87597355368 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MIEVLLVTIC LAVFPYQGSS IILESGNVND YEVVYPRKVT ALPKGAVQPK YEDAMQYELK 

        70         80         90        100        110        120 
VNGEPVVLHL EKNKELFSKD YSETHYSPDG RKITTNPSVE DHCYYRGRIE NDADSTASIS 

       130        140        150        160        170        180 
ACNGLKGHFK LQGEMYLIEP LELSDSEAHA VFKYENVEKE DEAPKMCGVT QNWESYEPIK 

       190        200        210        220        230        240 
KASDLNLNPD QQNLPQRYIE LVVVADHRVF MKYNSDLNII RKRVHELVNT INGFYRSLNI 

       250        260        270        280        290        300 
DVSLTDLEIW SDQDFITVQS SAKNTLNSFG EWREADLLRR KSHDHAQLLT AINFEGKIIG 

       310        320        330        340        350        360 
RAYTSSMCNP RKSVGIVKDH SPINLLVGVT MAHELGHNLG MNHDGDKCLR GASLCIMRPG 

       370        380        390        400        410 
LTPGRSYEFS DDSMGYYQSF LNQYKPQCIL NKPLRIDPVS TPVSGNELLE AGEE

Q90391 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools