VM33_CROAD
ID VM33_CROAD Reviewed; 610 AA.
AC J3S830;
DT 19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2012, sequence version 1.
DT 03-AUG-2022, entry version 32.
DE RecName: Full=Zinc metalloproteinase-disintegrin-like 3a;
DE EC=3.4.24.-;
DE AltName: Full=Snake venom metalloproteinase;
DE Short=SVMP;
DE Flags: Precursor;
OS Crotalus adamanteus (Eastern diamondback rattlesnake).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Crotalus.
OX NCBI_TaxID=8729;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RA Rokyta D.R., Lemmon A.R., Margres M.J., Aronow K.;
RT "The venom-gland transcriptome of the eastern diamondback rattlesnake
RT (Crotalus adamanteus).";
RL BMC Genomics 13:312-312(2012).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Venom;
RX PubMed=24231107; DOI=10.1016/j.jprot.2013.11.001;
RA Margres M.J., McGivern J.J., Wray K.P., Seavy M., Calvin K., Rokyta D.R.;
RT "Linking the transcriptome and proteome to characterize the venom of the
RT eastern diamondback rattlesnake (Crotalus adamanteus).";
RL J. Proteomics 96:145-158(2014).
CC -!- FUNCTION: Snake venom metalloproteinase that impairs hemostasis in the
CC envenomed animal. {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 -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- MISCELLANEOUS: The disintegrin domain belongs to the long disintegrin
CC subfamily.
CC -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-III
CC subfamily. {ECO:0000305}.
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DR EMBL; JU173712; AFJ49238.1; -; mRNA.
DR AlphaFoldDB; J3S830; -.
DR SMR; J3S830; -.
DR MEROPS; M12.022; -.
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; 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; 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; PS00427; DISINTEGRIN_1; 1.
DR PROSITE; PS50214; DISINTEGRIN_2; 1.
PE 1: Evidence at protein level;
KW Calcium; Cell adhesion impairing toxin; Disulfide bond; Glycoprotein;
KW Hemostasis impairing toxin; Hydrolase; Metal-binding; Metalloprotease;
KW Protease; Secreted; Signal; Toxin; Zinc; Zymogen.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT PROPEP 20..188
FT /evidence="ECO:0000250"
FT /id="PRO_0000425627"
FT CHAIN 189..610
FT /note="Zinc metalloproteinase-disintegrin-like 3a"
FT /id="PRO_0000425628"
FT DOMAIN 198..394
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 402..488
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT MOTIF 466..468
FT /note="D/ECD-tripeptide"
FT ACT_SITE 335
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT BINDING 201
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 285
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 334
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT BINDING 338
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT BINDING 344
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT BINDING 389
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 392
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 404
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 407
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 411
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 414
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 417
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT CARBOHYD 217
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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 405..434
FT /evidence="ECO:0000250"
FT DISULFID 416..429
FT /evidence="ECO:0000250"
FT DISULFID 418..424
FT /evidence="ECO:0000250"
FT DISULFID 428..451
FT /evidence="ECO:0000250"
FT DISULFID 442..448
FT /evidence="ECO:0000250"
FT DISULFID 447..473
FT /evidence="ECO:0000250"
FT DISULFID 460..480
FT /evidence="ECO:0000250"
FT DISULFID 467..499
FT /evidence="ECO:0000250"
FT DISULFID 492..504
FT /evidence="ECO:0000250"
FT DISULFID 511..561
FT /evidence="ECO:0000250"
FT DISULFID 526..572
FT /evidence="ECO:0000250"
FT DISULFID 539..549
FT /evidence="ECO:0000250"
FT DISULFID 556..598
FT /evidence="ECO:0000250"
FT DISULFID 592..603
FT /evidence="ECO:0000250"
SQ SEQUENCE 610 AA; 68840 MW; 989717660103E466 CRC64;
MIQVLLVTIL AVFPYQGSSI ILGSGNVNDY EVVYPRKVTA LPKGAVQPKY EDAMQYELKV
NGEPMVLHLE KNKQLFSKDY SETHYSPDGR EITTYPLVED HCYYHGRIEN DADSTASISA
CNGLKGHFKL QGEIYLIEPL KLRDSEAHAV FKYENVEKED EAPKMCGVTQ NWESYEPIKK
ASQLVVTAEQ QRYLNPYRYV ELVIVADHGM FTKYNRNLTE VKTWVYEIVN TLNEIYRYLY
IRVALVGLEI WSDGDLSNVT LSSGNTLDSF GEWRKRDLLR RKRHDNAQLL TAIDFSGNTI
GRASIANMCD PKYSTGIVQD HSPINLLVAV TMAHEMGHNL GLHHDGKSCT CGDYICIMNA
TLSHQHSKYF SNCSYNQYWD YINTYTPKCI LNEPLRTDII SPPVCGNELL EAGEECDCGS
PRNCQYQCCD AATCKLHSWV ECESGVCCEQ CKFRTAGTEC RARRSECDIA ESCTGQSADC
PTDDFHKNGQ PCLNNFGYCY NGNCPIMYHQ CYALFGSNVY EAEDSCFESN QKGDDYGYCR
KENGEKIPCA PEDVKCGRLY CNDNSPGQND PCKIFPSNED EHKEMVLPGT KCADGKFCTN
GHCVDVATAY
