VM2C1_CRODO
ID VM2C1_CRODO Reviewed; 478 AA.
AC C0L2T8;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Zinc metalloproteinase/disintegrin {ECO:0000305};
DE AltName: Full=Metalloproteinase PII {ECO:0000303|PubMed:19230843};
DE Short=MPII {ECO:0000303|PubMed:19230843};
DE Contains:
DE RecName: Full=Snake venom metalloproteinase {ECO:0000305};
DE Short=SVMP {ECO:0000305};
DE EC=3.4.24.- {ECO:0000250|UniProtKB:Q98SP2};
DE Contains:
DE RecName: Full=Disintegrin Cdc {ECO:0000303|PubMed:30377432};
DE Flags: Precursor;
GN Name=MPII {ECO:0000312|EMBL:ACN38267.1};
OS Crotalus durissus collilineatus (Brazilian rattlesnake).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Crotalus.
OX NCBI_TaxID=221569 {ECO:0000303|PubMed:19230843};
RN [1] {ECO:0000312|EMBL:ACN38267.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Venom gland {ECO:0000303|PubMed:19230843};
RX PubMed=19230843; DOI=10.1016/j.biochi.2009.02.001;
RA Boldrini-Franca J., Rodrigues R.S., Fonseca F.P., Menaldo D.L.,
RA Ferreira F.B., Henrique-Silva F., Soares A.M., Hamaguchi A.,
RA Rodrigues V.M., Otaviano A.R., Homsi-Brandeburgo M.I.;
RT "Crotalus durissus collilineatus venom gland transcriptome: analysis of
RT gene expression profile.";
RL Biochimie 91:586-595(2009).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 409-451, IDENTIFICATION BY MASS SPECTROMETRY
RP (DISINTEGRIN CDC), FUNCTION (DISINTEGRIN CDC), SUBCELLULAR LOCATION
RP (DISINTEGRIN CDC), TISSUE SPECIFICITY (DISINTEGRIN CDC), AND MASS
RP SPECTROMETRY.
RC TISSUE=Venom {ECO:0000303|PubMed:30377432};
RX PubMed=30377432; DOI=10.1186/s40409-018-0167-6;
RA Oliveira I.S., Manzini R.V., Ferreira I.G., Cardoso I.A., Bordon K.C.F.,
RA Machado A.R.T., Antunes L.M.G., Rosa J.C., Arantes E.C.;
RT "Cell migration inhibition activity of a non-RGD disintegrin from Crotalus
RT durissus collilineatus venom.";
RL J. Venom. Anim. Toxins Incl. Trop. Dis. 24:28-28(2018).
CC -!- FUNCTION: [Snake venom metalloproteinase]: Snake venom zinc
CC metalloproteinase that causes hemorrhage by provoking the degradation
CC of the sub-endothelial matrix proteins (fibronectin, laminin, type IV
CC collagen, nidogen, and gelatins). {ECO:0000250|UniProtKB:P34182}.
CC -!- FUNCTION: [Disintegrin Cdc]: Displays low cytotoxicity and inhibits
CC cell migration. {ECO:0000269|PubMed:30377432}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:O93523};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:O93523};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19230843}.
CC -!- SUBCELLULAR LOCATION: [Disintegrin Cdc]: Secreted
CC {ECO:0000269|PubMed:30377432}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000269|PubMed:19230843}.
CC -!- TISSUE SPECIFICITY: [Disintegrin Cdc]: Expressed by the venom gland.
CC {ECO:0000269|PubMed:30377432}.
CC -!- MASS SPECTROMETRY: [Disintegrin Cdc]: Mass=7287.4; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:30377432};
CC -!- MISCELLANEOUS: The disintegrin belongs to the medium disintegrin
CC subfamily. {ECO:0000305}.
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; FJ654661; ACN38267.1; -; mRNA.
DR SMR; C0L2T8; -.
DR MEROPS; M12.145; -.
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:0030574; P:collagen catabolic process; 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; Collagen degradation;
KW Direct protein sequencing; Disulfide bond; Hemorrhagic toxin;
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..187
FT /evidence="ECO:0000250|UniProtKB:Q98SP2"
FT /id="PRO_0000453668"
FT CHAIN 188..389
FT /note="Snake venom metalloproteinase"
FT /id="PRO_0000453669"
FT PROPEP 390..408
FT /evidence="ECO:0000269|PubMed:30377432"
FT /id="PRO_0000453670"
FT CHAIN 409..473
FT /note="Disintegrin Cdc"
FT /evidence="ECO:0000269|PubMed:30377432"
FT /id="PRO_0000453671"
FT PROPEP 474..478
FT /evidence="ECO:0000269|PubMed:30377432"
FT /id="PRO_0000453672"
FT DOMAIN 193..389
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 397..478
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT ACT_SITE 330
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT BINDING 329
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT BINDING 333
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT BINDING 339
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DISULFID 304..384
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DISULFID 344..368
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DISULFID 346..351
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DISULFID 411..420
FT /evidence="ECO:0000250|UniProtKB:Q90WC0"
FT DISULFID 413..421
FT /evidence="ECO:0000250|UniProtKB:Q90WC0"
FT DISULFID 426..440
FT /evidence="ECO:0000250|UniProtKB:Q90WC0"
FT DISULFID 434..464
FT /evidence="ECO:0000250|UniProtKB:Q90WC0"
FT DISULFID 439..443
FT /evidence="ECO:0000250|UniProtKB:Q90WC0"
FT DISULFID 452..471
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
SQ SEQUENCE 478 AA; 53639 MW; F47DCE7A53AB2114 CRC64;
MIQVLLVTIC LAAFPYQGSS IILESGNVND YEVIYPRKVT ALPKGAVQPK YEDTMQYELK
VNGQPVVLHL EKNKGLFSKD YSETHYSPDG RKITTNPSVE DHCYYHGRIE NDADSTASIS
ACNGLKGHFK LQGEMYIIEP LELSDSEDHA VFKLENVEKE DEAPKMCGVT QNWESNEPIK
KASHLNLNPE HQRYVEIVIV VDHGMFTKYN GDSDKIRQRV HQMVNIMKES YRYMYIDISL
AGIEIWSNKD LINVQPAAPN TLKSFGEWRE TDLPKRKSHD NAQLLTSIDF NGQTIGIANI
GAICDPKPST RVVQDHSKIN LRVALTMTHE LSHNLGIHHD TGSCSCSGYS CIMSPVISDE
PSKYFSDCSY IQCWNFIMNQ KPQCILKKPL RTDTVSTPVS GNELLEARIE CDCGSIENPC
CYATTCKLRP GSQCAEGMCC DQCRFMKKGT VCRVSLVNKN DDTCTGQSAD CPRNVLYG
