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THAS_BOVIN
ID   THAS_BOVIN              Reviewed;         533 AA.
AC   Q2KIG5;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Thromboxane-A synthase;
DE            Short=TXA synthase;
DE            Short=TXS;
DE            EC=5.3.99.5 {ECO:0000250|UniProtKB:P24557};
DE   AltName: Full=Cytochrome P450 5A1;
DE   AltName: Full=Hydroperoxy icosatetraenoate dehydratase;
DE            EC=4.2.1.152 {ECO:0000250|UniProtKB:P24557};
GN   Name=TBXAS1; Synonyms=CYP5A1;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Testis;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the conversion of prostaglandin H2 (PGH2) to
CC       thromboxane A2 (TXA2), a potent inducer of blood vessel constriction
CC       and platelet aggregation. Cleaves also PGH2 to 12-hydroxy-
CC       heptadecatrienoicacid (12-HHT) and malondialdehyde, which is known to
CC       act as a mediator of DNA damage. 12-HHT and malondialdehyde are formed
CC       stoichiometrically in the same amounts as TXA2. Additionally, displays
CC       dehydratase activity, toward (15S)-hydroperoxy-(5Z,8Z,11Z,13E)-
CC       eicosatetraenoate (15(S)-HPETE) producing 15-KETE and 15-HETE.
CC       {ECO:0000250|UniProtKB:P24557}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=prostaglandin H2 = thromboxane A2; Xref=Rhea:RHEA:17137,
CC         ChEBI:CHEBI:57405, ChEBI:CHEBI:57445; EC=5.3.99.5;
CC         Evidence={ECO:0000250|UniProtKB:P24557};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17138;
CC         Evidence={ECO:0000250|UniProtKB:P24557};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=prostaglandin H2 = (12S)-hydroxy-(5Z,8E,10E)-
CC         heptadecatrienoate + malonaldehyde; Xref=Rhea:RHEA:48644,
CC         ChEBI:CHEBI:57405, ChEBI:CHEBI:90694, ChEBI:CHEBI:566274;
CC         Evidence={ECO:0000250|UniProtKB:P24557};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a hydroperoxyeicosatetraenoate = an oxoeicosatetraenoate +
CC         H2O; Xref=Rhea:RHEA:55556, ChEBI:CHEBI:15377, ChEBI:CHEBI:59720,
CC         ChEBI:CHEBI:131859; EC=4.2.1.152;
CC         Evidence={ECO:0000250|UniProtKB:P24557};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55557;
CC         Evidence={ECO:0000250|UniProtKB:P24557};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(15S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoate = 15-oxo-
CC         (5Z,8Z,11Z,13E)-eicosatetraenoate + H2O; Xref=Rhea:RHEA:48636,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:57410, ChEBI:CHEBI:57446;
CC         Evidence={ECO:0000250|UniProtKB:P24557};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48637;
CC         Evidence={ECO:0000250|UniProtKB:P24557};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(15S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoate + AH2 =
CC         (5Z,8Z,11Z,13E,15S)-hydroxyeicosatetraenoate + A + H2O;
CC         Xref=Rhea:RHEA:48856, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:17499, ChEBI:CHEBI:57409, ChEBI:CHEBI:57446;
CC         Evidence={ECO:0000250|UniProtKB:P24557};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48857;
CC         Evidence={ECO:0000250|UniProtKB:P24557};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000250|UniProtKB:P24557};
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P24557}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:P24557}; Multi-pass membrane protein
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; BC112647; AAI12648.1; -; mRNA.
DR   RefSeq; NP_001039492.1; NM_001046027.2.
DR   AlphaFoldDB; Q2KIG5; -.
DR   SMR; Q2KIG5; -.
DR   STRING; 9913.ENSBTAP00000026934; -.
DR   BindingDB; Q2KIG5; -.
DR   PaxDb; Q2KIG5; -.
DR   GeneID; 509326; -.
DR   KEGG; bta:509326; -.
DR   CTD; 6916; -.
DR   eggNOG; KOG0158; Eukaryota.
DR   InParanoid; Q2KIG5; -.
DR   OrthoDB; 786853at2759; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0036134; F:12-hydroxyheptadecatrienoic acid synthase activity; IEA:RHEA.
DR   GO; GO:0020037; F:heme binding; ISS:UniProtKB.
DR   GO; GO:0106256; F:hydroperoxy icosatetraenoate dehydratase activity; ISS:UniProtKB.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR   GO; GO:0004796; F:thromboxane-A synthase activity; IBA:GO_Central.
DR   GO; GO:0006690; P:icosanoid metabolic process; ISS:UniProtKB.
DR   GO; GO:0001516; P:prostaglandin biosynthetic process; ISS:UniProtKB.
DR   Gene3D; 1.10.630.10; -; 1.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR002401; Cyt_P450_E_grp-I.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   Pfam; PF00067; p450; 2.
DR   PRINTS; PR00463; EP450I.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; SSF48264; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Fatty acid biosynthesis; Fatty acid metabolism;
KW   Heme; Iron; Isomerase; Lipid biosynthesis; Lipid metabolism; Lyase;
KW   Membrane; Metal-binding; Monooxygenase; Oxidoreductase;
KW   Prostaglandin biosynthesis; Prostaglandin metabolism; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..533
FT                   /note="Thromboxane-A synthase"
FT                   /id="PRO_0000240341"
FT   TOPO_DOM        1..10
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P24557"
FT   TRANSMEM        11..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        32..75
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250|UniProtKB:P24557"
FT   TRANSMEM        76..96
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        97..223
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P24557"
FT   TRANSMEM        224..244
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        245..335
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250|UniProtKB:P24557"
FT   TRANSMEM        336..356
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        357..533
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P24557"
FT   BINDING         479
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250|UniProtKB:P14779"
SQ   SEQUENCE   533 AA;  60539 MW;  D3D93FA7B8153220 CRC64;
     MEVLGLFRLE VSGPMVTVAL SVVFLALLKW YSTSAFSRLE KLGIRHPKPS PFIGNLAFFR
     QGFWESHMEL RKQYGPLSGY YLGRLMFIVI SEPDMIEQVL VEKFSNFTNR MATGLEPKPV
     ADSVLFLRDK RWEEVRSVLT VAFSPEKLSE MTPLISRACD VLLAHLERHA QSGEAFDIQR
     TYCCYTTDVV ASVAFGTEVN SQEAPEHPFV EHCRRFFASS IPKPLLVLLL SFPSIMVPLA
     RILPNKNRDE LNGFFNKLIR NVIALRDQQA AEERRRDFLQ MVQDVRHSAA TVGVEKFDIV
     RQVFSATKCP ANPPRRHSPR PLSKPLSVDE VVGQAFIFLI AGYEIVTNTL SFATYLLATN
     PECQEKLLEE VDCFSKEHLA PEYCSLQEGL PYLDMVIKET LRMYPPAFRF TRVAAQDCEV
     LGQRIPAGAV LETAVGALHY DPEHWPNPEN FNPERFTAEA QQRRRPYTYL PFGAGPRSCL
     GVRLGLLELK LTLLHILRKF RFEACPETQV PLQLESKSAL GPKNGVYIRI VSR
 
 
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