VM1H5_DEIAC
ID VM1H5_DEIAC Reviewed; 404 AA.
AC Q9IAY2;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Snake venom metalloproteinase H5;
DE Short=SVMP;
DE EC=3.4.24.-;
DE Flags: Precursor; Fragment;
OS Deinagkistrodon acutus (Hundred-pace snake) (Agkistrodon acutus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Deinagkistrodon.
OX NCBI_TaxID=36307;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 180-186, FUNCTION, AND MASS
RP SPECTROMETRY.
RC TISSUE=Venom gland;
RX PubMed=10691973; DOI=10.1046/j.1432-1327.2000.01129.x;
RA Tsai I.-H., Wang Y.-M., Chiang T.-Y., Chen Y.-L., Huang R.-J.;
RT "Purification, cloning and sequence analyses for pro-metalloprotease-
RT disintegrin variants from Deinagkistrodon acutus venom and
RT subclassification of the small venom metalloproteases.";
RL Eur. J. Biochem. 267:1359-1367(2000).
CC -!- FUNCTION: This probable venom zinc protease is not hemorrhagic when 3
CC ug are injected onto the back skin of guinea pig.
CC {ECO:0000269|PubMed:10691973}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- MASS SPECTROMETRY: Mass=23922; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:10691973};
CC -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-I
CC subfamily. {ECO:0000305}.
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DR EMBL; AF098310; AAF61185.1; -; mRNA.
DR AlphaFoldDB; Q9IAY2; -.
DR SMR; Q9IAY2; -.
DR MEROPS; M12.337; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04269; ZnMc_adamalysin_II_like; 1.
DR Gene3D; 3.40.390.10; -; 1.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001590; Peptidase_M12B.
DR InterPro; IPR002870; Peptidase_M12B_N.
DR InterPro; IPR034027; Reprolysin_adamalysin.
DR Pfam; PF01562; Pep_M12B_propep; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Hydrolase; Metal-binding;
KW Metalloprotease; Protease; Secreted; Signal; Zinc; Zymogen.
FT SIGNAL <1..6
FT /evidence="ECO:0000255"
FT PROPEP 7..177
FT /evidence="ECO:0000250"
FT /id="PRO_0000322623"
FT CHAIN 178..378
FT /note="Snake venom metalloproteinase H5"
FT /id="PRO_5000055236"
FT PROPEP 379..404
FT /evidence="ECO:0000250"
FT /id="PRO_0000322624"
FT DOMAIN 184..379
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT REGION 385..404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 321
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 320
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 324
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 330
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT DISULFID 295..374
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DISULFID 336..358
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DISULFID 338..341
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT NON_TER 1
SQ SEQUENCE 404 AA; 46034 MW; 06EFFC4D727F416F CRC64;
FPYQGSSIML ESGKVNDYEV VYPQRLAPLP EGAVQQKYED TMQYEFKVNG ETIGLHMEKS
KGLFSKDYSE THYSPDGRKI TTYPSVEDHC YYHGRIENYE DSTASISACN GLKGHFKIQG
ETYFIESLKL SDSEAHAVFK YENVEKEDET HKMCGVTQNW KSYDPIKKPS WVNLTPKQQT
WPQTSVNLQL VVDRSMYAKY NSDSEKITQT LQERVNIMKE IFKPLNLDIT LSVIEMWDKK
DLITVKTAAT DTLKLFPKWR QTDLLKRIDN DNAQLQTAVD FDGETVGLAF KGTMCDKRYS
AGIIQDHSAI PLLMAVTMAH ELGHNLGMDH DDTYKCNCNV CIMPPRLNTN PSKTFSDCSN
NDYQKFLTDK KPKCIHKKSL KTDTVSTSVS GNEPLDDNVD GFHA
