VM34_DRYCN
ID VM34_DRYCN Reviewed; 613 AA.
AC F8RKW1;
DT 19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 1.
DT 03-AUG-2022, entry version 39.
DE RecName: Full=Zinc metalloproteinase-disintegrin-like MTP4;
DE EC=3.4.24.-;
DE AltName: Full=Snake venom metalloproteinase;
DE Short=SVMP;
DE Flags: Precursor;
OS Drysdalia coronoides (White-lipped snake) (Hoplocephalus coronoides).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Notechinae; Drysdalia.
OX NCBI_TaxID=66186;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Venom, and Venom gland;
RX PubMed=21133350; DOI=10.1021/pr1008916;
RA Chatrath S.T., Chapeaurouge A., Lin Q., Lim T.K., Dunstan N., Mirtschin P.,
RA Kumar P.P., Kini R.M.;
RT "Identification of novel proteins from the venom of a cryptic snake
RT Drysdalia coronoides by a combined transcriptomics and proteomics
RT approach.";
RL J. Proteome Res. 10:739-750(2011).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Venom;
RX PubMed=24297900; DOI=10.1073/pnas.1314702110;
RA Vonk F.J., Casewell N.R., Henkel C.V., Heimberg A.M., Jansen H.J.,
RA McCleary R.J., Kerkkamp H.M., Vos R.A., Guerreiro I., Calvete J.J.,
RA Wuster W., Woods A.E., Logan J.M., Harrison R.A., Castoe T.A.,
RA de Koning A.P., Pollock D.D., Yandell M., Calderon D., Renjifo C.,
RA Currier R.B., Salgado D., Pla D., Sanz L., Hyder A.S., Ribeiro J.M.,
RA Arntzen J.W., van den Thillart G.E., Boetzer M., Pirovano W., Dirks R.P.,
RA Spaink H.P., Duboule D., McGlinn E., Kini R.M., Richardson M.K.;
RT "The king cobra genome reveals dynamic gene evolution and adaptation in the
RT snake venom system.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:20651-20656(2013).
CC -!- FUNCTION: Snake venom zinc metalloproteinase that may impair hemostasis
CC in the prey.
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. {ECO:0000305}.
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DR EMBL; HM627204; AEH95531.1; -; mRNA.
DR AlphaFoldDB; F8RKW1; -.
DR SMR; F8RKW1; -.
DR MEROPS; M12.159; -.
DR PRIDE; F8RKW1; -.
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.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW Calcium; Disulfide bond; Glycoprotein; Hemostasis impairing toxin;
KW Hydrolase; Metal-binding; Metalloprotease; Protease; Secreted; Signal;
KW Toxin; Zinc; Zymogen.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..191
FT /evidence="ECO:0000255"
FT /id="PRO_0000425506"
FT CHAIN 192..613
FT /note="Zinc metalloproteinase-disintegrin-like MTP4"
FT /id="PRO_0000425507"
FT DOMAIN 205..401
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 409..495
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT REGION 561..574
FT /note="Hypervariable region that may play important roles
FT toward cell migration"
FT /evidence="ECO:0000250"
FT MOTIF 473..475
FT /note="D/ECD-tripeptide"
FT BINDING 208
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 292
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 341
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 345
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 351
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 396
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 399
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
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 416
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 418
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 421
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 424
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 475
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 476
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 478
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 490
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT CARBOHYD 282
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 437
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 572
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 316..396
FT /evidence="ECO:0000250"
FT DISULFID 356..380
FT /evidence="ECO:0000250"
FT DISULFID 358..363
FT /evidence="ECO:0000250"
FT DISULFID 412..441
FT /evidence="ECO:0000250"
FT DISULFID 423..436
FT /evidence="ECO:0000250"
FT DISULFID 425..431
FT /evidence="ECO:0000250"
FT DISULFID 435..458
FT /evidence="ECO:0000250"
FT DISULFID 449..455
FT /evidence="ECO:0000250"
FT DISULFID 454..480
FT /evidence="ECO:0000250"
FT DISULFID 467..487
FT /evidence="ECO:0000250"
FT DISULFID 474..506
FT /evidence="ECO:0000250"
FT DISULFID 499..511
FT /evidence="ECO:0000250"
FT DISULFID 518..568
FT /evidence="ECO:0000250"
FT DISULFID 533..575
FT /evidence="ECO:0000250"
FT DISULFID 543..577
FT /evidence="ECO:0000250"
FT DISULFID 546..556
FT /evidence="ECO:0000250"
FT DISULFID 563..601
FT /evidence="ECO:0000250"
FT DISULFID 595..606
FT /evidence="ECO:0000250"
SQ SEQUENCE 613 AA; 68240 MW; CBE2ECC3F9C0C340 CRC64;
MIEVLLVTIC FTVFPYQGSS IILESGNVND YEVVYPQKVP ALPKGGVQNP QPETKYEDTM
QYEFHVNGEP VVLHLERNKG LFSEDYTETH YAPDGREITT SPPVQDHCYY HGYIQNEADS
SAAISACDGL KGHFKHRGET YFIEPLKLSN SESHAIYKDE HVEKEDEIPK ICGVTQTTSE
SDEPIEKISQ LTNTPEQDRY LQVKKYIELY VVVDNRMYRN YNSNRDAINE RVYEMVNTLN
VMYRPLNFFI ALIGLEIWSN QDEINIEPEV AVTLRSFGEW RNTTLLPRKR NDNAQLLTGI
DFNGATVGLA YVGTLCSPTQ SVAVIQDHSK RTSMVASTMA HELGHNLGIN HDSASCNCNA
GPCIMSATIS NQPFSKFSSC SVQEHQRYLL RVRPQCILNK PLSTDIVTPP VCGNYFVERG
EECDCGSPQD CQSACCNATT CKPQHEAQCD SGECCEKCKF KKAGAECRAA KDDCDLPESC
TGQSAKCPTD SFQRNGHPCQ NNEGYCYNGK CPIMTNQCIA LGGPGVNVSP DECFTLKQNV
PECGFCRIEN GRKIPCAEKD KMCGKLLCEK GNATCICFPT THDPDYGMVE PGTKCGDGKV
CINRQCVDVQ TAY
