VM38_DRYCN
ID VM38_DRYCN Reviewed; 613 AA.
AC F8RKW0;
DT 19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 1.
DT 03-AUG-2022, entry version 41.
DE RecName: Full=Zinc metalloproteinase-disintegrin-like MTP8;
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).
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; HM627203; AEH95530.1; -; mRNA.
DR AlphaFoldDB; F8RKW0; -.
DR SMR; F8RKW0; -.
DR MEROPS; M12.159; -.
DR PRIDE; F8RKW0; -.
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_0000425504"
FT CHAIN 192..613
FT /note="Zinc metalloproteinase-disintegrin-like MTP8"
FT /id="PRO_0000425505"
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 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 550
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; 68427 MW; 77FAF32F56BC15C2 CRC64;
MIEVLLVTIC FTVFPYQGSP IILESGNVND YEVVYPQKVP ALPKGGVQNP QPETKYEDTM
QYEFHVNGEP VVLHLERNKG LFSEDYTETH YAPDGREITT SPPVQDHCYY HGYIQNEADS
SAAISACDGL KGHFKHRGET YFIEPLKLSN SESHAIYKDE HVEKEDEIPK ICGVTQTTSE
SDETIEKISQ LTNTPEQDRY LQVKKYIELY VVVDNRMYRN YNSNRDAINE RVYEMVNTLN
VMYRPLNFFI ALIGLEIWSN QDEINIEPEV AVTLRSFGEW RNTTLLPRKR NDNAQLLTGI
DFNGATVGLA YVGTLCRPTQ SVAVIQDHSK RTSMVASTMA HELGHNLGIN HDSASCNCNA
GPCIMSATIS NQPLSEFSSC SVQEHQRYLL RVRPQCILNK PLRKDIVTPP VCGNYFVERG
EECDCGSPQD CQSACCNATT CKLQHEAQCD SGECCEQCKF KKAGAECRAA KDDCDLPESC
TGQSAKCPTD SFQRNGHPCQ NNQGYCYNGK CLIMTNQCIA LKGPGVNVSP DECFTLKQND
PECGFCRIEN GTKIPCAEKD KMCGKLLCQE GNATCICFPT TDDPDYGMVE PGTKCGDGKV
CINRQCVDVQ TAY
