DHR13_BOVIN
ID DHR13_BOVIN Reviewed; 377 AA.
AC Q17QU7;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Dehydrogenase/reductase SDR family member 13;
DE EC=1.1.-.- {ECO:0000305};
DE AltName: Full=Short chain dehydrogenase/reductase family 7C member 5 {ECO:0000250|UniProtKB:Q6UX07};
DE Short=Protein SDR7C5 {ECO:0000250|UniProtKB:Q6UX07};
DE Flags: Precursor;
GN Name=DHRS13; Synonyms=SDR7C5 {ECO:0000250|UniProtKB:Q6UX07};
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=Thalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Putative oxidoreductase. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; BC118170; AAI18171.1; -; mRNA.
DR RefSeq; NP_001069155.1; NM_001075687.1.
DR AlphaFoldDB; Q17QU7; -.
DR SMR; Q17QU7; -.
DR STRING; 9913.ENSBTAP00000017950; -.
DR PaxDb; Q17QU7; -.
DR PRIDE; Q17QU7; -.
DR Ensembl; ENSBTAT00000017950; ENSBTAP00000017950; ENSBTAG00000013501.
DR GeneID; 514903; -.
DR KEGG; bta:514903; -.
DR CTD; 147015; -.
DR VEuPathDB; HostDB:ENSBTAG00000013501; -.
DR VGNC; VGNC:28042; DHRS13.
DR eggNOG; KOG1208; Eukaryota.
DR GeneTree; ENSGT00940000155599; -.
DR HOGENOM; CLU_010194_44_5_1; -.
DR InParanoid; Q17QU7; -.
DR OMA; NRPVVGW; -.
DR OrthoDB; 1076292at2759; -.
DR TreeFam; TF105429; -.
DR Proteomes; UP000009136; Chromosome 19.
DR Bgee; ENSBTAG00000013501; Expressed in retina and 97 other tissues.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005743; C:mitochondrial inner membrane; IBA:GO_Central.
DR GO; GO:0052650; F:NADP-retinol dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0042574; P:retinal metabolic process; IBA:GO_Central.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR002347; SDR_fam.
DR Pfam; PF00106; adh_short; 1.
DR PRINTS; PR00081; GDHRDH.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 2: Evidence at transcript level;
KW NAD; NADP; Oxidoreductase; Reference proteome; Secreted; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..377
FT /note="Dehydrogenase/reductase SDR family member 13"
FT /id="PRO_0000311919"
FT REGION 310..363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..363
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 197
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q99714"
FT BINDING 46
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q99714"
FT BINDING 48
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q99714"
FT BINDING 170
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q99714"
FT BINDING 197
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q99714"
FT BINDING 201
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q99714"
FT BINDING 232
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q99714"
SQ SEQUENCE 377 AA; 40861 MW; DFDE3FC67AE90850 CRC64;
MEALLLGVGL LLGAYVLVYY NLVKAPPCRG LASLRGRTAV VTGANSGIGK MTALELARRG
ARVVLACRSR ERGEAAAFDL RQESGNNEVI FMALDLASLA SVRAFATAFL SSEPRLDILI
HNAGISSCGR TREPFNLLLR VNHIGPFLLT HLLLPRLKTS APSRVVVVSS AAHRRGRLDF
TRLDHPVVGW QQELRAYANS KLANVLFARE LATQLEGTGV TCYAAHPGPV NSELFLRHVP
GWLRPLLRPL AWLVLRAPRG GAQTPLYCAL QEGIEPLSGR YFANCHVEEV PPAARDDRAA
HRLWEASRKL AGLGPGEDAE SDEDSQPEDP GTPSSPSSPH PEEPTVSELY PSPQSSTDRS
TVTCRIPVKA ELEPQAC