VM2H1_GLOHA
ID VM2H1_GLOHA Reviewed; 480 AA.
AC Q90220;
DT 13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Zinc metalloproteinase/disintegrin;
DE Contains:
DE RecName: Full=Snake venom metalloproteinase;
DE Short=SVMP;
DE EC=3.4.24.-;
DE Contains:
DE RecName: Full=Disintegrin halystatin;
DE AltName: Full=Disintegrin adinbitor;
DE AltName: Full=Disintegrin brevicaudin-1b;
DE Flags: Precursor;
OS Gloydius halys (Chinese water mocassin) (Agkistrodon halys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Gloydius.
OX NCBI_TaxID=8714;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC TISSUE=Venom gland;
RA Fujisawa Y., Kuroda S., Notoya K., Konishi H., Terashita Z.;
RT "Halystatin, a novel disintegrin from agkistrodon halys, is a potent
RT inhibitor of bone resorption and platelet aggregation.";
RL Takeda Kenkyusho Ho 53:39-56(1994).
CC -!- FUNCTION: [Snake venom metalloproteinase]: Impairs hemostasis in the
CC envenomed animal. {ECO:0000250}.
CC -!- FUNCTION: [Disintegrin halystatin]: Inhibits platelet aggregation and
CC bone resorption. {ECO:0000269|Ref.1}.
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 -!- MISCELLANEOUS: The disintegrin belongs to the medium disintegrin
CC subfamily.
CC -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-II
CC subfamily. P-IIa sub-subfamily. {ECO:0000305}.
CC -!- CAUTION: The disintegrin is also encoded by another precursor (AC
CC Q1PBD1). {ECO:0000305}.
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DR EMBL; D28870; BAA06025.1; -; mRNA.
DR AlphaFoldDB; Q90220; -.
DR SMR; Q90220; -.
DR MEROPS; M12.134; -.
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:0090729; F:toxin activity; IEA:UniProtKB-KW.
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 Gene3D; 4.10.70.10; -; 1.
DR InterPro; IPR018358; Disintegrin_CS.
DR InterPro; IPR001762; Disintegrin_dom.
DR InterPro; IPR036436; Disintegrin_dom_sf.
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; PF00200; Disintegrin; 1.
DR Pfam; PF01562; Pep_M12B_propep; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR PRINTS; PR00289; DISINTEGRIN.
DR SMART; SM00050; DISIN; 1.
DR SUPFAM; SSF57552; SSF57552; 1.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS00427; DISINTEGRIN_1; 1.
DR PROSITE; PS50214; DISINTEGRIN_2; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 2: Evidence at transcript level;
KW Cell adhesion impairing toxin; Disulfide bond; Glycoprotein;
KW Hemostasis impairing toxin; Hydrolase; Metal-binding; Metalloprotease;
KW Platelet aggregation inhibiting toxin; Protease; Secreted; Signal; Toxin;
KW Zinc; Zymogen.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..190
FT /evidence="ECO:0000250"
FT /id="PRO_0000424450"
FT CHAIN 191..407
FT /note="Snake venom metalloproteinase"
FT /id="PRO_5000139751"
FT CHAIN 408..480
FT /note="Disintegrin halystatin"
FT /id="PRO_5000139752"
FT DOMAIN 197..391
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 399..480
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT MOTIF 458..460
FT /note="Cell attachment site"
FT ACT_SITE 334
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 333
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 337
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 343
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT CARBOHYD 259
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 279
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 308..386
FT /evidence="ECO:0000250"
FT DISULFID 348..370
FT /evidence="ECO:0000250"
FT DISULFID 350..353
FT /evidence="ECO:0000250"
FT DISULFID 413..428
FT /evidence="ECO:0000250"
FT DISULFID 415..423
FT /evidence="ECO:0000250"
FT DISULFID 422..445
FT /evidence="ECO:0000250"
FT DISULFID 436..442
FT /evidence="ECO:0000250"
FT DISULFID 441..466
FT /evidence="ECO:0000250"
FT DISULFID 454..473
FT /evidence="ECO:0000250"
SQ SEQUENCE 480 AA; 53620 MW; 5CF5E6476511B3D7 CRC64;
MIQVLLITIC LAVFPFQGSS IVLDSGNLNE FEVVYPEKVT ALPRAAVKNK YEDAMQYEFK
VNGEPLLLHL ERNKGLFSDD YSEIHYSPDA REISAYPSVE DHCFYHGRVE NDADSTASLS
ACDGLKAHFK IQGEMYLIEP LEVSDTDAHA VFKYENVEKE DEPPKMCGVT QNWESYESTK
KASQLNVSPD QQRFPQRFIK LAIYVDHGMY TKYAGNSERI TKRVHQMINN INMMCRALNI
VTSLSVLRIW SEKDLITVNA SAPSSLTLFG AWRETVLLNR TSHDHAQLMT ATIFNGNVIG
RAPVGGMCDP KRSVAIVRDH NAILFIVAVT MTHEMGHNLG MHHDEDKCNC NTCIMSKVLS
RQPSYEFSDC NENEYQTYVT DHSPQCILND PLRPDTVSTP VSGNELLEAG EECDCGSPGN
PCCDAATCKL RQGAQCAEGL CCDQCRFMKK GTVCRIARGD DMDDYCNGIS AGCPRNPFHA
