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PA2B1_BUNFL
ID   PA2B1_BUNFL             Reviewed;         146 AA.
AC   Q7T1R0;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Basic phospholipase A2 beta-bungarotoxin A1 chain;
DE            Short=Beta-BuTX A1 chain;
DE            Short=svPLA2;
DE            EC=3.1.1.4;
DE   AltName: Full=Phosphatidylcholine 2-acylhydrolase;
DE   Flags: Precursor;
OS   Bungarus flaviceps flaviceps (Red-headed krait).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Bungarinae; Bungarus.
OX   NCBI_TaxID=8615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 28-50; 59-70; 93-97 AND
RP   101-143, IDENTIFICATION BY MASS SPECTROMETRY, AND SUBUNIT.
RC   TISSUE=Venom gland;
RX   PubMed=16458338; DOI=10.1016/j.toxicon.2005.12.004;
RA   Yanoshita R., Ogawa Y., Murayama N., Omori-Satoh T., Saguchi K.,
RA   Higuchi S., Khow O., Chanhome L., Samejima Y., Sitprija V.;
RT   "Molecular cloning of the major lethal toxins from two kraits (Bungarus
RT   flaviceps and Bungarus candidus).";
RL   Toxicon 47:416-424(2006).
RN   [2]
RP   FUNCTION, AND SUBUNIT.
RC   TISSUE=Venom;
RX   PubMed=11738240; DOI=10.1016/s0041-0101(01)00235-5;
RA   Khow O., Chanhome L., Omori-Satoh T., Sitprija V.;
RT   "Isolation of the major lethal toxin in the venom of Bungarus flaviceps.";
RL   Toxicon 40:463-469(2002).
CC   -!- FUNCTION: Snake venom phospholipase A2 (PLA2) that inhibits
CC       neuromuscular transmission by blocking acetylcholine release from the
CC       nerve termini. PLA2 catalyzes the calcium-dependent hydrolysis of the
CC       2-acyl groups in 3-sn-phosphoglycerides. {ECO:0000269|PubMed:11738240}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-
CC         glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868,
CC         ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU10035, ECO:0000255|PROSITE-
CC         ProRule:PRU10036};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC       Note=Binds 1 Ca(2+) ion. {ECO:0000250};
CC   -!- SUBUNIT: Heterodimer with beta-bungarotoxin B chain; disulfide-linked.
CC       The A chain has phospholipase A2 activity and the B chain shows
CC       homology with the basic protease inhibitors.
CC       {ECO:0000269|PubMed:11738240, ECO:0000269|PubMed:16458338}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- SIMILARITY: Belongs to the phospholipase A2 family. Group I subfamily.
CC       D49 sub-subfamily. {ECO:0000305}.
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DR   EMBL; AB112357; BAC77653.1; -; mRNA.
DR   AlphaFoldDB; Q7T1R0; -.
DR   SMR; Q7T1R0; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0004623; F:phospholipase A2 activity; IEA:UniProtKB-EC.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0050482; P:arachidonic acid secretion; IEA:InterPro.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006644; P:phospholipid metabolic process; IEA:InterPro.
DR   CDD; cd00125; PLA2c; 1.
DR   Gene3D; 1.20.90.10; -; 1.
DR   InterPro; IPR001211; PLipase_A2.
DR   InterPro; IPR033112; PLipase_A2_Asp_AS.
DR   InterPro; IPR016090; PLipase_A2_dom.
DR   InterPro; IPR036444; PLipase_A2_dom_sf.
DR   InterPro; IPR033113; PLipase_A2_His_AS.
DR   PANTHER; PTHR11716; PTHR11716; 1.
DR   Pfam; PF00068; Phospholip_A2_1; 1.
DR   PRINTS; PR00389; PHPHLIPASEA2.
DR   SMART; SM00085; PA2c; 1.
DR   SUPFAM; SSF48619; SSF48619; 1.
DR   PROSITE; PS00119; PA2_ASP; 1.
DR   PROSITE; PS00118; PA2_HIS; 1.
PE   1: Evidence at protein level;
KW   Calcium; Direct protein sequencing; Disulfide bond; Hydrolase;
KW   Lipid degradation; Lipid metabolism; Metal-binding; Neurotoxin;
KW   Presynaptic neurotoxin; Secreted; Signal; Toxin.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..27
FT                   /evidence="ECO:0000269|PubMed:16458338"
FT                   /id="PRO_0000271455"
FT   CHAIN           28..146
FT                   /note="Basic phospholipase A2 beta-bungarotoxin A1 chain"
FT                   /id="PRO_5000050833"
FT   ACT_SITE        75
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        120
FT                   /evidence="ECO:0000250"
FT   BINDING         55
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         57
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         59
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         76
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   DISULFID        42
FT                   /note="Interchain (with a B chain)"
FT                   /evidence="ECO:0000250"
FT   DISULFID        54..145
FT                   /evidence="ECO:0000250"
FT   DISULFID        56..72
FT                   /evidence="ECO:0000250"
FT   DISULFID        71..126
FT                   /evidence="ECO:0000250"
FT   DISULFID        78..119
FT                   /evidence="ECO:0000250"
FT   DISULFID        87..112
FT                   /evidence="ECO:0000250"
FT   DISULFID        105..117
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   146 AA;  16394 MW;  64C0C4D991908662 CRC64;
     MNPAHLLVLP AVCVSFLGAS IIPPQSLNLI QFKDMIRCTI PCERTWGEYA DYGCYCGKGG
     SGRPVDALDR CCYVHDNCYG EAQKRNCNPY MKSYSFKCAK RTLFCYDAPG SCARFVCDCD
     RTAALCFGDS EYIGRHKNID TKRHCQ
 
 
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