VM3_CERRY
ID VM3_CERRY Reviewed; 615 AA.
AC D8VNS0;
DT 25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 1.
DT 03-AUG-2022, entry version 42.
DE RecName: Full=Zinc metalloproteinase-disintegrin-like;
DE EC=3.4.24.-;
DE AltName: Full=Snake venom metalloproteinase;
DE Short=SVMP;
DE Flags: Precursor;
OS Cerberus rynchops (Dog-faced water snake).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Homalopsidae; Cerberus.
OX NCBI_TaxID=46267;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION BY MASS SPECTROMETRY, AND
RP FUNCTION.
RC TISSUE=Venom, and Venom gland;
RX PubMed=20158271; DOI=10.1021/pr901044x;
RA Ompraba G., Chapeaurouge A., Doley R., Devi K.R., Padmanaban P.,
RA Venkatraman C., Velmurugan D., Lin Q., Kini R.M.;
RT "Identification of a novel family of snake venom proteins Veficolins from
RT Cerberus rynchops using a venom gland transcriptomics and proteomics
RT approach.";
RL J. Proteome Res. 9:1882-1893(2010).
CC -!- FUNCTION: Snake venom zinc metalloprotease that may induce platelet
CC aggregation. {ECO:0000269|PubMed:20158271}.
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.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-III
CC subfamily. P-IIIa sub-subfamily. {ECO:0000305}.
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DR EMBL; GU065316; ADJ51055.1; -; mRNA.
DR AlphaFoldDB; D8VNS0; -.
DR SMR; D8VNS0; -.
DR MEROPS; M12.315; -.
DR PRIDE; D8VNS0; -.
DR TopDownProteomics; D8VNS0; -.
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; IPR006586; ADAM_Cys-rich.
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; PF08516; ADAM_CR; 1.
DR Pfam; PF00200; Disintegrin; 1.
DR Pfam; PF01562; Pep_M12B_propep; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR PRINTS; PR00289; DISINTEGRIN.
DR SMART; SM00608; ACR; 1.
DR SMART; SM00050; DISIN; 1.
DR SUPFAM; SSF57552; SSF57552; 1.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS50214; DISINTEGRIN_2; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW Calcium; Disulfide bond; Hemostasis impairing toxin; Hydrolase;
KW Metal-binding; Metalloprotease; Platelet aggregation activating toxin;
KW Protease; Secreted; Signal; Toxin; Zinc; Zymogen.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..195
FT /evidence="ECO:0000250"
FT /id="PRO_0000414916"
FT CHAIN 196..615
FT /note="Zinc metalloproteinase-disintegrin-like"
FT /id="PRO_0000414917"
FT DOMAIN 204..400
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 408..494
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT MOTIF 472..474
FT /note="D/ECD-tripeptide"
FT ACT_SITE 341
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 340
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 350
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 410
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 413
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 415
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 417
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 423
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT DISULFID 315..395
FT /evidence="ECO:0000250"
FT DISULFID 355..379
FT /evidence="ECO:0000250"
FT DISULFID 357..362
FT /evidence="ECO:0000250"
FT DISULFID 411..440
FT /evidence="ECO:0000250"
FT DISULFID 422..435
FT /evidence="ECO:0000250"
FT DISULFID 424..430
FT /evidence="ECO:0000250"
FT DISULFID 434..457
FT /evidence="ECO:0000250"
FT DISULFID 448..454
FT /evidence="ECO:0000250"
FT DISULFID 453..479
FT /evidence="ECO:0000250"
FT DISULFID 466..486
FT /evidence="ECO:0000250"
FT DISULFID 473..505
FT /evidence="ECO:0000250"
FT DISULFID 498..510
FT /evidence="ECO:0000250"
FT DISULFID 517..567
FT /evidence="ECO:0000250"
FT DISULFID 532..576
FT /evidence="ECO:0000250"
FT DISULFID 545..555
FT /evidence="ECO:0000250"
FT DISULFID 562..602
FT /evidence="ECO:0000250"
FT DISULFID 596..608
FT /evidence="ECO:0000250"
SQ SEQUENCE 615 AA; 68956 MW; D59C2FEAAE5F6C36 CRC64;
MIQALLVTIC LVGFPHQGSS IILESGNVKD YEVVYPQKIP ALPKGGIQRA EPETKYEDTM
QYQFKVNGEP VVLHLERNKG LFSEDYSETH YSPDGREITT SPPVQDHCYY HGRIQNDADS
TASISACNGL KGRFKHQGET YLIEPLKISD SEAHKIYKSE NLEKEDEAPK TCGVTQTSLE
TDETIKMNFQ SANNPEEDYV RKRKYIKLAV VVDNSMYIKY DRNLNDIRSR IYEIVNDVNV
FYRLLNIHIA LIFIEIWSHQ DKINVQPMVR VTLDSFGTWR ETDLLPRRSH DNAQLYTNVD
FDGPTVGYAY VGSLCKPKHS VAIIQDHTET ANMMASTVAH ELGHNLGMNH DSGNCICQPT
LCVMSETLSS VPFNDFSACS RVDHRNYLIR DLPQCILNKP LRTDIVAPAV CGNNFVEVGG
ECDCGSPQDC QSTCCDAATC RLRDGAQCDT EECCEQCRFR RAGTVCRAAK DDCDVAEFCT
GRTADCPMDG LQRNGEPCQH NQGYCYNGKC PIMTNQCIAL WGPDATVSQD GCFHFNENGQ
GDLYCRRENG VNIQCEPQDN KCGRLFCVQS TSTVQCNYRS SATDPDYGMV AIGTKCGDGR
VCNNNRFCVD IRIAY
