Reviewed, UniProtKB/Swiss-Prot Q90391 (VMATB_CROAT)

Names and origin

Protein names	Recommended name:     Zinc metalloproteinase atrolysin-B     EC=3.4.24.41 Alternative name(s):     Metalloendopeptidase B     Hemorrhagic toxin B       Short name=HT-B
Organism	Crotalus atrox (Western diamondback rattlesnake)
Taxonomic identifier	8730 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Viperidae › Crotalinae › Crotalus

Protein attributes

Sequence length	414 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

General annotation (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 structure	Monomer By similarity.
Subcellular location	Secreted By similarity.
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
Domain	Signal
Ligand	Calcium Metal-binding Zinc
Molecular function	Hydrolase Metalloprotease Protease Toxin
PTM	Disulfide bond Pyrrolidone carboxylic acid Zymogen
Gene Ontology (GO)
Biological process	pathogenesis Inferred from electronic annotation. Source: UniProtKB-KW proteolysis Inferred from electronic annotation. Source: InterPro
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW metalloendopeptidase activity Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 20	20	Potential
	Propeptide	21 – 190	170	By similarity		PRO_0000329995
	Chain	191 – 393	203	Zinc metalloproteinase atrolysin-B		PRO_0000329996
	Propeptide	394 – 414	21	By similarity		PRO_0000329997
Regions
	Domain	197 – 393	197	Peptidase M12B
Sites
	Active site	334	1	By similarity
	Metal binding	200	1	Calcium By similarity
	Metal binding	284	1	Calcium By similarity
	Metal binding	333	1	Zinc; catalytic By similarity
	Metal binding	337	1	Zinc; catalytic By similarity
	Metal binding	343	1	Zinc; catalytic By similarity
	Metal binding	388	1	Calcium; via carbonyl oxygen By similarity
	Metal binding	391	1	Calcium By similarity
Amino acid modifications
	Modified residue	191	1	Pyrrolidone carboxylic acid By similarity
	Disulfide bond	308 ↔ 388		By similarity
	Disulfide bond	348 ↔ 355		By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q90391-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: EBF3D87597355368	FASTA	414	46,806
	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

References

[1]

"cDNA sequences for four snake venom metalloproteinases: structure, classification, and their relationship to mammalian reproductive proteins." Hite L.A., Jia L.-G., Bjarnason J.B., Fox J.W. Arch. Biochem. Biophys. 308:182-191(1994) [PubMed: 8311451] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Venom gland.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U01235 mRNA. Translation: AAA03327.1.
PIR	S41608.
3D structure databases
HSSP	HSSP built from PDB template 4AIG based on UniProtKB P34179.
SMR	Q90391. Positions 193-393.
ModBase	Search...
Protein family/group databases
MEROPS	M12.143.
Phylogenomic databases
HOVERGEN	Q90391.
Family and domain databases
InterPro	IPR006025. Pept_M_Zn_BS. IPR001590. Peptidase_M12B. IPR002870. Peptidase_M12B_N. [Graphical view]
Pfam	PF01562. Pep_M12B_propep. 1 hit. 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

VMATB_CROAT

Accession

Primary (citable) accession number: Q90391

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 29, 2008
Last sequence update:	November 1, 1996
Last modified:	June 16, 2009
This is version 51 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Tox-Prot (Toxin Annotation Project)