VM2SA_GLOSA
ID VM2SA_GLOSA Reviewed; 483 AA.
AC Q7SZE0; Q7SZD6; Q7SZD7;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Zinc metalloproteinase/disintegrin;
DE Contains:
DE RecName: Full=Snake venom metalloproteinase saxin;
DE Short=SVMP;
DE EC=3.4.24.-;
DE Contains:
DE RecName: Full=Disintegrin;
DE Flags: Precursor;
OS Gloydius saxatilis (Rock mamushi) (Gloydius intermedius saxatilis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Gloydius.
OX NCBI_TaxID=92067;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RA Sun D.-J., Yang T.-S.;
RL Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: [Snake venom metalloproteinase saxin]: Impairs hemostasis in
CC the envenomed animal. {ECO:0000250}.
CC -!- FUNCTION: [Disintegrin]: Binds and inhibits integrins. {ECO:0000250}.
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: Homodimer; disulfide-linked (disintegrin). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- MISCELLANEOUS: The disintegrin belongs to the dimeric disintegrin
CC subfamily.
CC -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-II
CC subfamily. P-IId sub-subfamily. {ECO:0000305}.
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DR EMBL; AY204244; AAP20639.1; -; mRNA.
DR EMBL; AY204247; AAP20642.1; -; mRNA.
DR EMBL; AY204248; AAP20643.1; -; mRNA.
DR AlphaFoldDB; Q7SZE0; -.
DR SMR; Q7SZE0; -.
DR MEROPS; M12.178; -.
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 Calcium; Cell adhesion impairing toxin; Disulfide bond;
KW Hemostasis impairing toxin; Hydrolase; Metal-binding; Metalloprotease;
KW Protease; Secreted; Signal; Toxin; Zinc; Zymogen.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..190
FT /evidence="ECO:0000250"
FT /id="PRO_0000322632"
FT CHAIN 191..394
FT /note="Snake venom metalloproteinase saxin"
FT /id="PRO_0000322633"
FT PROPEP 395..418
FT /evidence="ECO:0000250"
FT /id="PRO_0000322634"
FT CHAIN 419..483
FT /note="Disintegrin"
FT /id="PRO_0000322635"
FT DOMAIN 198..394
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 402..483
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT REGION 461..483
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 461..463
FT /note="Cell attachment site"
FT ACT_SITE 335
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 201
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 285
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 334
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 338
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 344
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 389
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 392
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT DISULFID 309..389
FT /evidence="ECO:0000250"
FT DISULFID 349..373
FT /evidence="ECO:0000250"
FT DISULFID 351..356
FT /evidence="ECO:0000250"
FT DISULFID 425..448
FT /evidence="ECO:0000250"
FT DISULFID 439..445
FT /evidence="ECO:0000250"
FT DISULFID 444..469
FT /evidence="ECO:0000250"
FT DISULFID 457..476
FT /evidence="ECO:0000250"
SQ SEQUENCE 483 AA; 54011 MW; 9F144352C32F5567 CRC64;
MIQVLLVTIC LVIFPYQGSS IILESGNVND YEVVYPQKVT ALPKGAVQPK YEDAMQYEFK
VNGEPVVLHL EKNKGLFSED YSETHYSPDG RKITTNPPVE DHCYYHGRIQ NDADSTASIS
ACNGLKGHFK HQGEMYLIEP LKLSDSEAHA VYKYENVEKE DEAPKMCGVT QTNWKSDEPI
KKASQLVVTP EQQRFPQRYI ELVVVADQGM FTKYNSNLDT IRTWVHELVD TINEFYRSLN
VRVSLTELEI WSNEDLINVQ PAAPHTLDSF GEWRQRDLLH RISHDNAMLL TSTDFDGDTI
GFAHVGTMCD PKRSVGIVQD HSAINLLVAV TMAHELGHNL GTDHDGNQCH CSANSCIMGD
VLREGLSYEF SDCSQNQYQT YLTDHNPQCI LNEPLRTDTV STPVSGNELL ETGEECDCGT
PANPCCDAAT CKLRPGAQCA EGLCCDQCKF TRAGKICRRA RGDNPDDRCT GQSSDCPRNP
FHA
