VM36A_BOTIN
ID VM36A_BOTIN Reviewed; 610 AA.
AC Q8QG88;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Zinc metalloproteinase-disintegrin-like BITM06A;
DE EC=3.4.24.-;
DE AltName: Full=Snake venom metalloproteinase;
DE Short=SVMP;
DE Flags: Precursor;
OS Bothrops insularis (Golden lancehead) (Lachesis insularis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
OX NCBI_TaxID=8723;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RX PubMed=12459276; DOI=10.1016/s0378-1119(02)01080-6;
RA Junqueira-de-Azevedo I.L.M., Ho P.L.;
RT "A survey of gene expression and diversity in the venom glands of the
RT pitviper snake Bothrops insularis through the generation of expressed
RT sequence tags (ESTs).";
RL Gene 299:279-291(2002).
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 -!- 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; AF490534; AAM09693.1; -; mRNA.
DR AlphaFoldDB; Q8QG88; -.
DR SMR; Q8QG88; -.
DR MEROPS; M12.140; -.
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 2: Evidence at transcript level;
KW Calcium; Disulfide bond; Glycoprotein; Hemostasis impairing toxin;
KW Hydrolase; Metal-binding; Metalloprotease; Protease; Secreted; Signal;
KW Toxin; Zinc.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..189
FT /evidence="ECO:0000250"
FT /id="PRO_0000330005"
FT CHAIN 190..610
FT /note="Zinc metalloproteinase-disintegrin-like BITM06A"
FT /id="PRO_0000330006"
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 ECO:0000255|PROSITE-ProRule:PRU10095"
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:0000250"
FT BINDING 338
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 344
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
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 409
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 BINDING 468
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 469
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 471
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 483
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 484
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT CARBOHYD 372
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; 68284 MW; 8B322E1EACE4C106 CRC64;
MIQVLLVTIC LAAFPYQGSS IILESGNVND YEVVYPRKVT ALPKGAVQPK YEDAMQYEFK
VNGEPVVLHL EKNKGLFSKD YSETHYSPDG REITTYPAVE DHCYYHGRIE NDADSTASIS
ACNGLKGHFK LQRETYFIEP LKLSNSEAHA VFKYENVEKE DEAPKMCGVT QNWKSYEPIK
KASQLVVTAE QQKYNPFRYV ELFIVVDQEM VTKNNGDLDK IKARMYELAN IVNEILRYLY
MHAALVGLEI WSNGDKITVK PDVDYTLNSF AEWRKTDLLT RKKHDNAQLL TAIDFNGPTI
GYAYIGSMCH PKRSVAIVED YSPINLVVAV IMAHEMGHNL GIHHDTDFCS CGDYPCIMGP
TISNEPSKFF SNCSYIQCWD FIMKENPQCI LNEPLGTDIV SPPVCGNELL EVGEECDCGT
PENCQNECCD AATCKLKSGS QCGHGDCCEQ CKFSKSGTEC RASMSECDPA EHCTGQSSEC
PADVFHKNGQ PCLDNYGYCY NGNCPIMYHQ CYALFGADVY EAEDSCFKDN QKGNYYGYCR
KENGKKIPCA PEDVKCGRLY CKDNSPGQNN PCKMFYSNDD EHKGMVLPGT KCADGKVCSN
GHCVDVATAY
