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CBR1_BOVIN
ID   CBR1_BOVIN              Reviewed;         277 AA.
AC   Q3SZD7;
DT   17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Carbonyl reductase [NADPH] 1;
DE            EC=1.1.1.184 {ECO:0000250|UniProtKB:P16152};
DE   AltName: Full=15-hydroxyprostaglandin dehydrogenase [NADP(+)];
DE            EC=1.1.1.196 {ECO:0000250|UniProtKB:Q28960};
DE            EC=1.1.1.197 {ECO:0000250|UniProtKB:P16152};
DE   AltName: Full=20-beta-hydroxysteroid dehydrogenase {ECO:0000250|UniProtKB:Q28960};
DE   AltName: Full=Alcohol dehydrogenase [NAD(P)+] CBR1;
DE            EC=1.1.1.71 {ECO:0000250|UniProtKB:P16152};
DE   AltName: Full=NADPH-dependent carbonyl reductase 1;
DE   AltName: Full=Prostaglandin 9-ketoreductase {ECO:0000250|UniProtKB:Q28960};
DE            Short=PG-9-KR {ECO:0000250|UniProtKB:Q28960};
DE   AltName: Full=Prostaglandin-E(2) 9-reductase {ECO:0000250|UniProtKB:Q28960};
DE            EC=1.1.1.189 {ECO:0000250|UniProtKB:Q28960};
GN   Name=CBR1 {ECO:0000250|UniProtKB:P16152};
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=Crossbred X Angus; TISSUE=Ileum;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: NADPH-dependent reductase with broad substrate specificity.
CC       Catalyzes the reduction of a wide variety of carbonyl compounds
CC       including quinones, prostaglandins, menadione, plus various
CC       xenobiotics. Catalyzes the reduction of the antitumor anthracyclines
CC       doxorubicin and daunorubicin to the cardiotoxic compounds doxorubicinol
CC       and daunorubicinol (By similarity). Can convert prostaglandin E to
CC       prostaglandin F2-alpha (By similarity). Can bind glutathione, which
CC       explains its higher affinity for glutathione-conjugated substrates.
CC       Catalyzes the reduction of S-nitrosoglutathione. In addition,
CC       participates in the glucocorticoid metabolism by catalyzing the NADPH-
CC       dependent cortisol/corticosterone into 20beta-dihydrocortisol (20b-DHF)
CC       or 20beta-corticosterone (20b-DHB), which are weak agonists of NR3C1
CC       and NR3C2 in adipose tissue (By similarity).
CC       {ECO:0000250|UniProtKB:P16152, ECO:0000250|UniProtKB:Q28960}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a secondary alcohol + NADP(+) = a ketone + H(+) + NADPH;
CC         Xref=Rhea:RHEA:19257, ChEBI:CHEBI:15378, ChEBI:CHEBI:17087,
CC         ChEBI:CHEBI:35681, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC         EC=1.1.1.184; Evidence={ECO:0000250|UniProtKB:P16152};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NADP(+) + prostaglandin F2alpha = H(+) + NADPH + prostaglandin
CC         E2; Xref=Rhea:RHEA:24508, ChEBI:CHEBI:15378, ChEBI:CHEBI:57404,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:606564;
CC         EC=1.1.1.189; Evidence={ECO:0000250|UniProtKB:Q28960};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:24510;
CC         Evidence={ECO:0000250|UniProtKB:Q28960};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NADP(+) + prostaglandin E1 = 15-oxoprostaglandin E1 + H(+) +
CC         NADPH; Xref=Rhea:RHEA:11636, ChEBI:CHEBI:15378, ChEBI:CHEBI:57397,
CC         ChEBI:CHEBI:57401, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC         EC=1.1.1.197; Evidence={ECO:0000250|UniProtKB:P16152};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11637;
CC         Evidence={ECO:0000250|UniProtKB:P16152};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + menadione + NADPH = menadiol + NADP(+);
CC         Xref=Rhea:RHEA:63492, ChEBI:CHEBI:6746, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:28869, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC         Evidence={ECO:0000250|UniProtKB:P16152};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NADP(+) + prostaglandin D2 = 15-oxoprostaglandin D2 + H(+) +
CC         NADPH; Xref=Rhea:RHEA:20744, ChEBI:CHEBI:15378, ChEBI:CHEBI:57406,
CC         ChEBI:CHEBI:57408, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC         EC=1.1.1.196; Evidence={ECO:0000250|UniProtKB:Q28960};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20745;
CC         Evidence={ECO:0000250|UniProtKB:Q28960};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NADP(+) + prostaglandin E2 = 15-oxoprostaglandin E2 + H(+) +
CC         NADPH; Xref=Rhea:RHEA:63476, ChEBI:CHEBI:15378, ChEBI:CHEBI:57400,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:606564;
CC         Evidence={ECO:0000250|UniProtKB:Q28960};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63477;
CC         Evidence={ECO:0000250|UniProtKB:Q28960};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NADP(+) + prostaglandin F2alpha = 15-oxoprostaglandin F2alpha
CC         + H(+) + NADPH; Xref=Rhea:RHEA:63480, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57404, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:133409; Evidence={ECO:0000250|UniProtKB:Q28960};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63481;
CC         Evidence={ECO:0000250|UniProtKB:Q28960};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=daunorubicin + H(+) + NADPH = 13-dihydrodaunorubicin +
CC         NADP(+); Xref=Rhea:RHEA:63504, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349, ChEBI:CHEBI:64677, ChEBI:CHEBI:75296;
CC         Evidence={ECO:0000250|UniProtKB:P16152};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63505;
CC         Evidence={ECO:0000250|UniProtKB:P16152};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + NADPH + S-nitrosoglutathione = NADP(+) + sulfinamide
CC         glutathione; Xref=Rhea:RHEA:63500, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:145544,
CC         ChEBI:CHEBI:145547; Evidence={ECO:0000250|UniProtKB:Q28960};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a primary alcohol + NADP(+) = an aldehyde + H(+) + NADPH;
CC         Xref=Rhea:RHEA:15937, ChEBI:CHEBI:15378, ChEBI:CHEBI:15734,
CC         ChEBI:CHEBI:17478, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.71;
CC         Evidence={ECO:0000250|UniProtKB:P16152};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=cortisol + H(+) + NADPH = 20beta-dihydrocortisol + NADP(+);
CC         Xref=Rhea:RHEA:70215, ChEBI:CHEBI:15378, ChEBI:CHEBI:17650,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:139311;
CC         Evidence={ECO:0000250|UniProtKB:P16152};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70216;
CC         Evidence={ECO:0000250|UniProtKB:P16152};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=corticosterone + H(+) + NADPH = 20beta-dihydrocorticosterone +
CC         NADP(+); Xref=Rhea:RHEA:70219, ChEBI:CHEBI:15378, ChEBI:CHEBI:16827,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:189050;
CC         Evidence={ECO:0000250|UniProtKB:P48758};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70220;
CC         Evidence={ECO:0000250|UniProtKB:P48758};
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q28960}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q28960}.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
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DR   EMBL; BC102943; AAI02944.1; -; mRNA.
DR   RefSeq; NP_001029685.1; NM_001034513.1.
DR   AlphaFoldDB; Q3SZD7; -.
DR   SMR; Q3SZD7; -.
DR   STRING; 9913.ENSBTAP00000031784; -.
DR   PaxDb; Q3SZD7; -.
DR   PeptideAtlas; Q3SZD7; -.
DR   PRIDE; Q3SZD7; -.
DR   Ensembl; ENSBTAT00000031838; ENSBTAP00000031784; ENSBTAG00000023384.
DR   GeneID; 515946; -.
DR   KEGG; bta:515946; -.
DR   CTD; 873; -.
DR   VEuPathDB; HostDB:ENSBTAG00000023384; -.
DR   eggNOG; KOG1208; Eukaryota.
DR   GeneTree; ENSGT00510000046499; -.
DR   InParanoid; Q3SZD7; -.
DR   OMA; LALQYPK; -.
DR   OrthoDB; 1259665at2759; -.
DR   Proteomes; UP000009136; Chromosome 1.
DR   Bgee; ENSBTAG00000023384; Expressed in cortex of kidney and 103 other tissues.
DR   ExpressionAtlas; Q3SZD7; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0047021; F:15-hydroxyprostaglandin dehydrogenase (NADP+) activity; ISS:UniProtKB.
DR   GO; GO:0047020; F:15-hydroxyprostaglandin-D dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0008106; F:alcohol dehydrogenase (NADP+) activity; IEA:RHEA.
DR   GO; GO:0004090; F:carbonyl reductase (NADPH) activity; ISS:UniProtKB.
DR   GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR   GO; GO:0050221; F:prostaglandin-E2 9-reductase activity; ISS:UniProtKB.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0042373; P:vitamin K metabolic process; ISS:UniProtKB.
DR   GO; GO:0006805; P:xenobiotic metabolic process; ISS:UniProtKB.
DR   CDD; cd05324; carb_red_PTCR-like_SDR_c; 1.
DR   InterPro; IPR045313; CBR1-like.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR   InterPro; IPR002347; SDR_fam.
DR   Pfam; PF00106; adh_short; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   PRINTS; PR00080; SDRFAMILY.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS00061; ADH_SHORT; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Cytoplasm; Lipid metabolism; NADP; Oxidoreductase;
KW   Phosphoprotein; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P16152"
FT   CHAIN           2..277
FT                   /note="Carbonyl reductase [NADPH] 1"
FT                   /id="PRO_0000284143"
FT   ACT_SITE        194
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT   BINDING         10..34
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P16152"
FT   BINDING         63..64
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P16152"
FT   BINDING         90
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P16152"
FT   BINDING         95..97
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P16152"
FT   BINDING         106
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P16152"
FT   BINDING         140
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P16152"
FT   BINDING         193..194
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P16152"
FT   BINDING         194..198
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P16152"
FT   BINDING         231..233
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P16152"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250|UniProtKB:P16152"
FT   MOD_RES         2
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P47727"
FT   MOD_RES         30
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P48758"
FT   MOD_RES         239
FT                   /note="N6-1-carboxyethyl lysine"
FT                   /evidence="ECO:0000250|UniProtKB:P16152"
SQ   SEQUENCE   277 AA;  30533 MW;  04B641F931BCD6DF CRC64;
     MSSSNCVALV TGANKGIGFV IVRDLCRRFS GDVVLTARDE ARGRAAVQQL QAEGLSPLFH
     QLDIDDRQSI RALRDFLRKE YGGLDVLVNN AGIAFKTADT TPFHIQAEVT MKTNFFGTRD
     VCTELLPLIK PQGRVVNVSS FVSVNSLKKC SRELQQKFRS ETITEEELVG LMNKFVEDTK
     NGVHRKEGWP DTAYGVTKIG VTVLSRIHAR KLSEQRGGDK ILLNACCPGW VRTDMGGPKA
     SKSPEEGAET PVYLALLPSD AEGPHGEFIS EKRVVQW
 
 
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