AK1CN_HORSE
ID AK1CN_HORSE Reviewed; 322 AA.
AC Q1XAA8;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Aldo-keto reductase family 1 member C23;
DE EC=1.1.1.-;
GN Name=AKR1C23;
OS Equus caballus (Horse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9796;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INDUCTION, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND TISSUE SPECIFICITY.
RC TISSUE=Ovary;
RX PubMed=16720716; DOI=10.1677/jme.1.01987;
RA Brown K.A., Boerboom D., Bouchard N., Dore M., Lussier J.G., Sirois J.;
RT "Human chorionic gonadotropin-dependent induction of an equine aldo-keto
RT reductase (AKR1C23) with 20alpha-hydroxysteroid dehydrogenase activity
RT during follicular luteinization in vivo.";
RL J. Mol. Endocrinol. 36:449-461(2006).
CC -!- FUNCTION: NADP-dependent oxidoreductase that has 20-alpha-
CC hydroxysteroid dehydrogenase activity. {ECO:0000269|PubMed:16720716}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.12 uM for progesterone {ECO:0000269|PubMed:16720716};
CC Vmax=0.086 pmol/min/ug enzyme {ECO:0000269|PubMed:16720716};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Detected in follicle granulosa cells (at protein
CC level). Detected in heart, lung, liver, kidney, stomach, uterus,
CC testis, skeletal muscle and granulosa cells of the follicle wall.
CC {ECO:0000269|PubMed:16720716}.
CC -!- INDUCTION: Detected at low levels in preovulatory follicles. Up-
CC regulated in preovulatory follicles during luteinization 12 to 36 hours
CC after stimulation with human chorionic gonadotropin. Up-regulated in
CC granulosa cells 12 to 39 hours after stimulation with human chorionic
CC gonadotropin. Detected at low levels in corpora lutea. Detected at
CC constant low levels in theca interna. {ECO:0000269|PubMed:16720716}.
CC -!- SIMILARITY: Belongs to the aldo/keto reductase family. {ECO:0000305}.
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DR EMBL; AY955082; AAY16444.1; -; mRNA.
DR RefSeq; NP_001075377.1; NM_001081908.1.
DR AlphaFoldDB; Q1XAA8; -.
DR SMR; Q1XAA8; -.
DR PaxDb; Q1XAA8; -.
DR PeptideAtlas; Q1XAA8; -.
DR PRIDE; Q1XAA8; -.
DR GeneID; 100034073; -.
DR KEGG; ecb:100034073; -.
DR CTD; 1645; -.
DR HOGENOM; CLU_023205_0_0_1; -.
DR InParanoid; Q1XAA8; -.
DR OMA; DMMINPQ; -.
DR OrthoDB; 1016440at2759; -.
DR TreeFam; TF106492; -.
DR BRENDA; 1.1.1.149; 2120.
DR SABIO-RK; Q1XAA8; -.
DR Proteomes; UP000002281; Unplaced.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004032; F:alditol:NADP+ 1-oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0047023; F:androsterone dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0032052; F:bile acid binding; IBA:GO_Central.
DR GO; GO:0047086; F:ketosteroid monooxygenase activity; IBA:GO_Central.
DR GO; GO:0016229; F:steroid dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0044597; P:daunorubicin metabolic process; IBA:GO_Central.
DR GO; GO:0044598; P:doxorubicin metabolic process; IBA:GO_Central.
DR GO; GO:0042448; P:progesterone metabolic process; IBA:GO_Central.
DR GO; GO:0006693; P:prostaglandin metabolic process; IBA:GO_Central.
DR GO; GO:0008202; P:steroid metabolic process; IBA:GO_Central.
DR CDD; cd19108; AKR_AKR1C1-35; 1.
DR Gene3D; 3.20.20.100; -; 1.
DR InterPro; IPR020471; AKR.
DR InterPro; IPR044482; AKR1C.
DR InterPro; IPR018170; Aldo/ket_reductase_CS.
DR InterPro; IPR023210; NADP_OxRdtase_dom.
DR InterPro; IPR036812; NADP_OxRdtase_dom_sf.
DR Pfam; PF00248; Aldo_ket_red; 1.
DR PIRSF; PIRSF000097; AKR; 1.
DR PRINTS; PR00069; ALDKETRDTASE.
DR SUPFAM; SSF51430; SSF51430; 1.
DR PROSITE; PS00798; ALDOKETO_REDUCTASE_1; 1.
DR PROSITE; PS00062; ALDOKETO_REDUCTASE_2; 1.
DR PROSITE; PS00063; ALDOKETO_REDUCTASE_3; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Lipid metabolism; NADP; Oxidoreductase; Reference proteome;
KW Steroid metabolism.
FT CHAIN 1..322
FT /note="Aldo-keto reductase family 1 member C23"
FT /id="PRO_0000326224"
FT ACT_SITE 55
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 20..24
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 31
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 50
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 117
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 166..167
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 190
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 216..221
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 269..279
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT SITE 84
FT /note="Lowers pKa of active site Tyr"
FT /evidence="ECO:0000250"
SQ SEQUENCE 322 AA; 36672 MW; CF10B897919A662B CRC64;
MDPKGWRVEL NDGHFIHALG FGTYAPNEVP KSKAVEATKS AIDAGFRHID CAHLYDNEKE
VGLAIRSKIQ DGTVKREDIF CTSKLWATSL RLQLVRPALE KSLKNLQLDY VDLYIIHFPV
AVKPGEEHLP QDEQGRMIFD TVDLCATWEA MEKCKDAGLT KSIGVSNFNR RQLEMILNKP
GLKHKPVCNQ VECHPYLNQS KLLDFCKSKD IVLVAYSALG SQREHWIDQS SPVLLEDPVL
CAMAKKYKRT PALIALRYQL QRGVVVLAKS YNEKRIKENV QAFGFQLTSE DMKVLDGLNR
NLRYVTLEMF AGHPEYPFSD DY
