ID VM39_DRYCN Reviewed; 611 AA.
AC F8RKV9;
DT 19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 1.
DT 22-FEB-2023, entry version 42.
DE RecName: Full=Zinc metalloproteinase-disintegrin-like MTP9;
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; HM627202; AEH95529.1; -; mRNA.
DR AlphaFoldDB; F8RKV9; -.
DR SMR; F8RKV9; -.
DR MEROPS; M12.159; -.
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; Collagenase (Catalytic Domain); 1.
DR Gene3D; 4.10.70.10; Disintegrin domain; 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 PANTHER; PTHR11905; ADAM A DISINTEGRIN AND METALLOPROTEASE DOMAIN; 1.
DR PANTHER; PTHR11905:SF32; DISINTEGRIN AND METALLOPROTEINASE DOMAIN-CONTAINING PROTEIN 28; 1.
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; Blood coagulation inhibitor (disintegrin); 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 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_0000425502"
FT CHAIN 192..611
FT /note="Zinc metalloproteinase-disintegrin-like MTP9"
FT /id="PRO_0000425503"
FT DOMAIN 205..401
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 409..493
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT MOTIF 471..473
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 473
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 474
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 488
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 548
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 570
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..456
FT /evidence="ECO:0000250"
FT DISULFID 447..453
FT /evidence="ECO:0000250"
FT DISULFID 452..478
FT /evidence="ECO:0000250"
FT DISULFID 465..485
FT /evidence="ECO:0000250"
FT DISULFID 472..504
FT /evidence="ECO:0000250"
FT DISULFID 497..509
FT /evidence="ECO:0000250"
FT DISULFID 516..566
FT /evidence="ECO:0000250"
FT DISULFID 531..573
FT /evidence="ECO:0000250"
FT DISULFID 541..575
FT /evidence="ECO:0000250"
FT DISULFID 544..554
FT /evidence="ECO:0000250"
FT DISULFID 561..599
FT /evidence="ECO:0000250"
FT DISULFID 593..604
FT /evidence="ECO:0000250"
SQ SEQUENCE 611 AA; 68086 MW; A955D25AFBA7CD97 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 YVGTLCRPTQ SVAVIQDHSK RTSMVASTMA HELGHNLGIN HDSASCNCNA
GPCIMSATIS NQPLSEFSSC SVQEHQRYLL RVRPQCILNK PLSTDIVTPP VCGNYFVERG
EECDCGSPQD CQDACCNAAT CKLQHDCDSG ECCEQCKFKK AGAECRAAKD DCDLPESCTG
QSAECPTDSF QRNGHPCQNN QGYCYNGKCP IMTNQCIALK GPGVNVSPDE CFTLKQNDPE
CGFCRIENGT KIPCAEKDKM CGKLLCQEGN ATCICFPTTD DPDYGMVEPG TKCGDGKVCI
NRQCVDVQTA Y
//
