VM2J_PROJR
ID VM2J_PROJR Reviewed; 481 AA.
AC Q7ZZS9;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Zinc metalloproteinase/disintegrin;
DE Contains:
DE RecName: Full=Snake venom metalloproteinase TJM-1;
DE Short=SVMP;
DE EC=3.4.24.-;
DE Contains:
DE RecName: Full=Disintegrin jerdonin;
DE Flags: Precursor;
OS Protobothrops jerdonii (Jerdon's pitviper) (Trimeresurus jerdonii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Protobothrops.
OX NCBI_TaxID=242841;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 411-435, FUNCTION, AND MASS
RP SPECTROMETRY.
RC TISSUE=Venom {ECO:0000269|PubMed:15037031}, and Venom gland;
RX PubMed=15037031; DOI=10.1016/j.toxicon.2003.10.023;
RA Zhou X.-D., Jin Y., Chen R.-Q., Lu Q.-M., Wu J.-B., Wang W.-Y.,
RA Xiong Y.-L.;
RT "Purification, cloning and biological characterization of a novel
RT disintegrin from Trimeresurus jerdonii venom.";
RL Toxicon 43:69-75(2004).
CC -!- FUNCTION: [Snake venom metalloproteinase TJM-1]: Impairs hemostasis in
CC the envenomed animal. {ECO:0000250}.
CC -!- FUNCTION: [Disintegrin jerdonin]: Inhibits platelet aggregation induced
CC by ADP and collagen. Acts by inhibiting fibrinogen interaction with
CC platelet receptors GPIIb/GPIIIa (ITGA2B/ITGB3). Has antitumor-growth
CC activity. {ECO:0000269|PubMed:15037031}.
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 -!- MASS SPECTROMETRY: [Disintegrin jerdonin]: Mass=7483; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:15037031};
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}.
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DR EMBL; AY267902; AAP23053.1; -; mRNA.
DR AlphaFoldDB; Q7ZZS9; -.
DR SMR; Q7ZZS9; -.
DR MEROPS; M12.156; -.
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 1: Evidence at protein level;
KW Calcium; Cell adhesion impairing toxin; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Hemostasis impairing toxin; Hydrolase;
KW Metal-binding; Metalloprotease; Platelet aggregation inhibiting toxin;
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_0000028973"
FT CHAIN 191..392
FT /note="Snake venom metalloproteinase TJM-1"
FT /id="PRO_0000028974"
FT PROPEP 393..410
FT /evidence="ECO:0000269|PubMed:15037031"
FT /id="PRO_0000028975"
FT CHAIN 411..481
FT /note="Disintegrin jerdonin"
FT /id="PRO_0000028976"
FT DOMAIN 197..392
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 400..481
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT MOTIF 459..461
FT /note="Cell attachment site"
FT ACT_SITE 334
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 200
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 284
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
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 BINDING 387
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 390
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT CARBOHYD 293
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT DISULFID 308..387
FT /evidence="ECO:0000250"
FT DISULFID 349..371
FT /evidence="ECO:0000250"
FT DISULFID 351..354
FT /evidence="ECO:0000250"
FT DISULFID 414..429
FT /evidence="ECO:0000250|UniProtKB:P18619"
FT DISULFID 416..424
FT /evidence="ECO:0000250|UniProtKB:P18619"
FT DISULFID 423..446
FT /evidence="ECO:0000250|UniProtKB:P18619"
FT DISULFID 437..443
FT /evidence="ECO:0000250|UniProtKB:P18619"
FT DISULFID 442..467
FT /evidence="ECO:0000250|UniProtKB:P18619"
FT DISULFID 455..474
FT /evidence="ECO:0000250|UniProtKB:P18619"
SQ SEQUENCE 481 AA; 53707 MW; 2BB12B491CDF82A9 CRC64;
MIQVLLVTIC LAVFPYQGSS IILESGNVDD YEVVYPQKVT ALPKGAVQPK YEDAMQYEFK
VNGEPVVLHL EKNKGLFSED YSETHYSPDG REITTYPSVE DHCYHHGRVH NDADSTASIS
ACDGLKGHFK LQGEMYLIEP LELSDSEAHA VFKYENVEKE DEAPKMCGVT QNWESDESIK
KASQLYLTPE QQRFPQRHIE LAIVVDHGMY TKYSSNFKKI RKRVHQMVSN INEMCRPLNI
AITLSLLDVW SEKDLITVQA DAPTTAGLFG DWRERVLLKK KNHDHAQLLT DINFTGDTIG
WAYVGGMCNA KYSVGTVKDH SSNVFVVAVT MTHEIGHNLG MEHDDKDKCK CEACIMAPVI
SDKQSKLFSD CSKDYYQTFL TNKKPQCILN APLRTDTVST PISGNEFLEA GEECDCGSPS
NPCCDVGTCK LSPGAQCADG LCCDQCRFKK KGKICRRARG DNPDDRCTGQ SADCPRNGLY
G
