VM2JN_PROJR
ID VM2JN_PROJR Reviewed; 483 AA.
AC P0C6E4;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 60.
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 jerdonatin;
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]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 412-436, FUNCTION, AND MASS
RP SPECTROMETRY.
RC TISSUE=Venom, and Venom gland;
RX PubMed=15364294; DOI=10.1016/j.cbpc.2004.06.012;
RA Zhou X.-D., Ding C.-H., Tai H., Jin Y., Chen R.-Q., Lu Q.-M., Wang W.-Y.,
RA Xiong Y.-L.;
RT "A novel disintegrin, jerdonatin, inhibits platelet aggregation and sperm-
RT egg binding.";
RL Comp. Biochem. Physiol. 139B:117-122(2004).
CC -!- FUNCTION: [Snake venom metalloproteinase]: Impairs hemostasis in the
CC envenomed animal. {ECO:0000250}.
CC -!- FUNCTION: [Disintegrin jerdonatin]: Inhibits ADP- and collagen-induced
CC human platelet aggregation with IC(50) of 123 and 135 nM, respectively.
CC Inhibits sperm-egg binding in a concentration-dependent manner, but has
CC no effect on the fusion of sperm-egg. {ECO:0000269|PubMed:15364294}.
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 jerdonatin]: Mass=8011; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:15364294};
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; P0C6E4; -.
DR SMR; P0C6E4; -.
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 Cell adhesion impairing toxin; Direct protein sequencing; Disulfide bond;
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_0000321890"
FT CHAIN 191..395
FT /note="Snake venom metalloproteinase"
FT /id="PRO_0000321891"
FT PROPEP 396..411
FT /evidence="ECO:0000269|PubMed:15364294"
FT /id="PRO_0000321892"
FT CHAIN 412..483
FT /note="Disintegrin jerdonatin"
FT /id="PRO_0000321893"
FT DOMAIN 197..395
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 403..483
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT MOTIF 462..464
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 DISULFID 308..390
FT /evidence="ECO:0000250"
FT DISULFID 352..374
FT /evidence="ECO:0000250"
FT DISULFID 354..357
FT /evidence="ECO:0000250"
FT DISULFID 417..432
FT /evidence="ECO:0000250"
FT DISULFID 419..427
FT /evidence="ECO:0000250"
FT DISULFID 426..449
FT /evidence="ECO:0000250"
FT DISULFID 440..446
FT /evidence="ECO:0000250"
FT DISULFID 445..470
FT /evidence="ECO:0000250"
FT DISULFID 458..477
FT /evidence="ECO:0000250"
SQ SEQUENCE 483 AA; 54880 MW; 5C69DE3571CB6E78 CRC64;
MIQVLLVTVC LAVFPYQGSS IILESGNVND YEVVYPRKVT ALPKRAVQQK YEDAMQYEFK
VNGEPVVLHL EKNKGLFSED YSETHYSPDG REITTYPSVE DHCYYHGRIH NDADSTASIS
ACDGLKGYFK LQGETYLIEP LKLPDSEAHA VYKYENIEKE DEAPKMCGVT QNWESDESIK
KASQLYLTPE QQRFPQRYVK LAIVVDYGMY TKYNRDSDKI TVRVHEMVNH ITEMYRPLNI
DITLSLLDVW SEKDLITVQS DSDVTLEVFG DWRESVLLKR RSHDCAHLLT DTKLNDNTIG
VAYKKGMCDP KLSVGLVQDY SKNVFMVAVT MTHEIGHNLG MEHDEDKNGK KCKCDTCIMS
PVISDKQSKL FSDCSKNDYQ TFLTNYKPQC ILNAPLRTDT VSTPVSGNEL LEEGEDCYCH
IPPNPCCDPA TCKLTPGSQC AEGLCCDQCR FKKKGTICRF ARGDYPDDRC TGLSDDCPRW
NDL
