VM3A_NAJAT
ID VM3A_NAJAT Reviewed; 607 AA.
AC D5LMJ3;
DT 13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 1.
DT 03-AUG-2022, entry version 45.
DE RecName: Full=Zinc metalloproteinase-disintegrin-like atrase-A;
DE EC=3.4.24.-;
DE AltName: Full=Snake venom metalloproteinase;
DE Short=SVMP;
DE Flags: Precursor;
OS Naja atra (Chinese cobra).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Elapinae; Naja.
OX NCBI_TaxID=8656;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RA Sun Q.Y., Bao J.;
RT "Purification, characterization, and cloning of metalloproteinase from Naja
RT atra venom.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Snake venom zinc metalloproteinase that inhibits platelet
CC aggregation by cleaving platelet glycoprotein Ib alpha (GP1BA) at Glu-
CC 298/Asp-299, and abolishes binding of von Willebrand factor (VWF) to
CC GPIBA. {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 -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-III
CC subfamily. P-IIIa sub-subfamily. {ECO:0000305}.
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DR EMBL; GU944972; ADF43026.1; -; mRNA.
DR AlphaFoldDB; D5LMJ3; -.
DR SMR; D5LMJ3; -.
DR MEROPS; M12.236; -.
DR PRIDE; D5LMJ3; -.
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; 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; PS50214; DISINTEGRIN_2; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 2: Evidence at transcript level;
KW Calcium; Cell adhesion impairing toxin; Disulfide bond; Glycoprotein;
KW Hemostasis impairing toxin; Hydrolase; Metal-binding; Metalloprotease;
KW Platelet aggregation inhibiting toxin; Protease; Secreted; Signal; Toxin;
KW Zinc; Zymogen.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..196
FT /evidence="ECO:0000250"
FT /id="PRO_0000418029"
FT CHAIN 197..607
FT /note="Zinc metalloproteinase-disintegrin-like atrase-A"
FT /id="PRO_0000418030"
FT DOMAIN 205..398
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 406..492
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT MOTIF 470..472
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 290
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 338
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 342
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 348
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 393
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
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 411
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 413
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 415
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 472
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
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 475
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 487
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 220
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 270
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 301
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 434
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 522
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 314..393
FT /evidence="ECO:0000250"
FT DISULFID 353..377
FT /evidence="ECO:0000250"
FT DISULFID 355..360
FT /evidence="ECO:0000250"
FT DISULFID 409..438
FT /evidence="ECO:0000250"
FT DISULFID 420..433
FT /evidence="ECO:0000250"
FT DISULFID 422..428
FT /evidence="ECO:0000250"
FT DISULFID 432..455
FT /evidence="ECO:0000250"
FT DISULFID 446..452
FT /evidence="ECO:0000250"
FT DISULFID 451..477
FT /evidence="ECO:0000250"
FT DISULFID 464..484
FT /evidence="ECO:0000250"
FT DISULFID 471..503
FT /evidence="ECO:0000250"
FT DISULFID 496..508
FT /evidence="ECO:0000250"
FT DISULFID 515..565
FT /evidence="ECO:0000250"
FT DISULFID 530..573
FT /evidence="ECO:0000250"
FT DISULFID 543..553
FT /evidence="ECO:0000250"
FT DISULFID 560..599
FT /evidence="ECO:0000250"
FT DISULFID 593..604
FT /evidence="ECO:0000250"
SQ SEQUENCE 607 AA; 68254 MW; 38E9A800C2FD7D65 CRC64;
MIQALLVIIC LAVFPHQGSS IILESGNVND YEVVYPQKVP ALLKGGVQNP QPETKYEDTM
RYEFQVNGEP VVLHLERNKG LFSEDYTETH YAPDGREITT SPPVQDHCYY HGYIQNEADS
SAVISACNGL KGHFKHQGET YFIEPLELSE SEAHAIYKDE NVEKEDETPK ICAVTQTTWE
SDESIEKTSQ LTNTPEQDRY LQVKKYIEFY LVVDNKMYKN HTSNQELRTR VYEMVNYLNT
KYRRLNFHIA LIGLEIWSNQ DKVDMDPGAN VTLKSFAEWR AKLPPHKRND NAQLLTGIDF
NGTTVGLAYT GTLCTWGSVA VVQDYSRRTI LMASTMAHEL GHNMGIHHDK ANCRCSHSPC
IMSDTISDEP FYEFSSCSVR EHQEYLLRER PQCILNKPSR KAIVSRPVCG NNFVEVGEQC
DCGSLQDCQS TCCNATTCKL QPHAQCDSEE CCEKCKFKGA ETECRAAKDD CDLPEFCTGQ
SAECPTDSLQ RNGHPCQNNQ GYCYNGKCPT MENQCITLLG PNYTVGPAGC FKNNRKGDDV
SHCRKENGAK IPCAAKDEKC GTLYCTEIKK TGCIVPVSPR DPDSRMVEPG TKCEDKKVCS
KSQCVKV
