Full text data of RDH14
RDH14
(PAN2)
[Confidence: low (only semi-automatic identification from reviews)]
Retinol dehydrogenase 14; 1.1.1.- (Alcohol dehydrogenase PAN2)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Retinol dehydrogenase 14; 1.1.1.- (Alcohol dehydrogenase PAN2)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9HBH5
ID RDH14_HUMAN Reviewed; 336 AA.
AC Q9HBH5;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAR-2001, sequence version 1.
DT 22-JAN-2014, entry version 104.
DE RecName: Full=Retinol dehydrogenase 14;
DE EC=1.1.1.-;
DE AltName: Full=Alcohol dehydrogenase PAN2;
GN Name=RDH14; Synonyms=PAN2; ORFNames=UNQ529/PRO1072;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lung;
RA Brereton P.S., Li K.X., Krozowski Z.S.;
RT "Pan2, a novel member of the SCAD superfamily.";
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S.,
RA Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
RA Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
RA Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
RA Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
RA Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
RA Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale
RT effort to identify novel human secreted and transmembrane proteins: a
RT bioinformatics assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=B-cell;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP FUNCTION.
RX PubMed=12226107; DOI=10.1074/jbc.M208882200;
RA Haeseleer F., Jang G.-F., Imanishi Y., Driessen C.A.G.G.,
RA Matsumura M., Nelson P.S., Palczewski K.;
RT "Dual-substrate specificity short chain retinol dehydrogenases from
RT the vertebrate retina.";
RL J. Biol. Chem. 277:45537-45546(2002).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-5, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Exhibits an oxidoreductive catalytic activity towards
CC retinoids. Most efficient as an NADPH-dependent retinal reductase.
CC Displays high activity toward 9-cis and all-trans-retinol. No
CC steroid dehydrogenase activity detected.
CC -!- TISSUE SPECIFICITY: Expressed in brain, kidney, pancreas and
CC placenta.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases
CC (SDR) family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF237952; AAG12190.1; -; mRNA.
DR EMBL; AY358511; AAQ88875.1; -; mRNA.
DR EMBL; BC009830; AAH09830.1; -; mRNA.
DR RefSeq; NP_065956.1; NM_020905.3.
DR UniGene; Hs.120319; -.
DR ProteinModelPortal; Q9HBH5; -.
DR SMR; Q9HBH5; 44-329.
DR MINT; MINT-4723605; -.
DR STRING; 9606.ENSP00000370648; -.
DR DrugBank; DB00162; Vitamin A.
DR PhosphoSite; Q9HBH5; -.
DR DMDM; 34395826; -.
DR PaxDb; Q9HBH5; -.
DR PeptideAtlas; Q9HBH5; -.
DR PRIDE; Q9HBH5; -.
DR DNASU; 57665; -.
DR Ensembl; ENST00000381249; ENSP00000370648; ENSG00000240857.
DR GeneID; 57665; -.
DR KEGG; hsa:57665; -.
DR UCSC; uc002rcx.4; human.
DR CTD; 57665; -.
DR GeneCards; GC02M018735; -.
DR HGNC; HGNC:19979; RDH14.
DR neXtProt; NX_Q9HBH5; -.
DR PharmGKB; PA134872714; -.
DR eggNOG; COG1028; -.
DR HOVERGEN; HBG078800; -.
DR KO; K11162; -.
DR OMA; RAFCQEM; -.
DR OrthoDB; EOG73Z2TK; -.
DR BRENDA; 1.1.1.105; 2681.
DR GeneWiki; RDH14; -.
DR GenomeRNAi; 57665; -.
DR NextBio; 64446; -.
DR PRO; PR:Q9HBH5; -.
DR ArrayExpress; Q9HBH5; -.
DR Bgee; Q9HBH5; -.
DR CleanEx; HS_PAN2; -.
DR CleanEx; HS_RDH14; -.
DR Genevestigator; Q9HBH5; -.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:LIFEdb.
DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.720; -; 1.
DR InterPro; IPR002198; DH_sc/Rdtase_SDR.
DR InterPro; IPR002347; Glc/ribitol_DH.
DR InterPro; IPR016040; NAD(P)-bd_dom.
DR Pfam; PF00106; adh_short; 1.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR PROSITE; PS00061; ADH_SHORT; FALSE_NEG.
PE 1: Evidence at protein level;
KW Complete proteome; NADP; Oxidoreductase; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1 336 Retinol dehydrogenase 14.
FT /FTId=PRO_0000054770.
FT NP_BIND 50 56 NADP (By similarity).
FT ACT_SITE 217 217 Proton acceptor (By similarity).
FT BINDING 192 192 Substrate (By similarity).
FT MOD_RES 5 5 Phosphothreonine.
SQ SEQUENCE 336 AA; 36865 MW; BCC17B3CD6B70DED CRC64;
MAVATAAAVL AALGGALWLA ARRFVGPRVQ RLRRGGDPGL MHGKTVLITG ANSGLGRATA
AELLRLGARV IMGCRDRARA EEAAGQLRRE LRQAAECGPE PGVSGVGELI VRELDLASLR
SVRAFCQEML QEEPRLDVLI NNAGIFQCPY MKTEDGFEMQ FGVNHLGHFL LTNLLLGLLK
SSAPSRIVVV SSKLYKYGDI NFDDLNSEQS YNKSFCYSRS KLANILFTRE LARRLEGTNV
TVNVLHPGIV RTNLGRHIHI PLLVKPLFNL VSWAFFKTPV EGAQTSIYLA SSPEVEGVSG
RYFGDCKEEE LLPKAMDESV ARKLWDISEV MVGLLK
//
ID RDH14_HUMAN Reviewed; 336 AA.
AC Q9HBH5;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAR-2001, sequence version 1.
DT 22-JAN-2014, entry version 104.
DE RecName: Full=Retinol dehydrogenase 14;
DE EC=1.1.1.-;
DE AltName: Full=Alcohol dehydrogenase PAN2;
GN Name=RDH14; Synonyms=PAN2; ORFNames=UNQ529/PRO1072;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lung;
RA Brereton P.S., Li K.X., Krozowski Z.S.;
RT "Pan2, a novel member of the SCAD superfamily.";
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S.,
RA Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
RA Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
RA Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
RA Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
RA Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
RA Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale
RT effort to identify novel human secreted and transmembrane proteins: a
RT bioinformatics assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=B-cell;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP FUNCTION.
RX PubMed=12226107; DOI=10.1074/jbc.M208882200;
RA Haeseleer F., Jang G.-F., Imanishi Y., Driessen C.A.G.G.,
RA Matsumura M., Nelson P.S., Palczewski K.;
RT "Dual-substrate specificity short chain retinol dehydrogenases from
RT the vertebrate retina.";
RL J. Biol. Chem. 277:45537-45546(2002).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-5, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Exhibits an oxidoreductive catalytic activity towards
CC retinoids. Most efficient as an NADPH-dependent retinal reductase.
CC Displays high activity toward 9-cis and all-trans-retinol. No
CC steroid dehydrogenase activity detected.
CC -!- TISSUE SPECIFICITY: Expressed in brain, kidney, pancreas and
CC placenta.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases
CC (SDR) family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF237952; AAG12190.1; -; mRNA.
DR EMBL; AY358511; AAQ88875.1; -; mRNA.
DR EMBL; BC009830; AAH09830.1; -; mRNA.
DR RefSeq; NP_065956.1; NM_020905.3.
DR UniGene; Hs.120319; -.
DR ProteinModelPortal; Q9HBH5; -.
DR SMR; Q9HBH5; 44-329.
DR MINT; MINT-4723605; -.
DR STRING; 9606.ENSP00000370648; -.
DR DrugBank; DB00162; Vitamin A.
DR PhosphoSite; Q9HBH5; -.
DR DMDM; 34395826; -.
DR PaxDb; Q9HBH5; -.
DR PeptideAtlas; Q9HBH5; -.
DR PRIDE; Q9HBH5; -.
DR DNASU; 57665; -.
DR Ensembl; ENST00000381249; ENSP00000370648; ENSG00000240857.
DR GeneID; 57665; -.
DR KEGG; hsa:57665; -.
DR UCSC; uc002rcx.4; human.
DR CTD; 57665; -.
DR GeneCards; GC02M018735; -.
DR HGNC; HGNC:19979; RDH14.
DR neXtProt; NX_Q9HBH5; -.
DR PharmGKB; PA134872714; -.
DR eggNOG; COG1028; -.
DR HOVERGEN; HBG078800; -.
DR KO; K11162; -.
DR OMA; RAFCQEM; -.
DR OrthoDB; EOG73Z2TK; -.
DR BRENDA; 1.1.1.105; 2681.
DR GeneWiki; RDH14; -.
DR GenomeRNAi; 57665; -.
DR NextBio; 64446; -.
DR PRO; PR:Q9HBH5; -.
DR ArrayExpress; Q9HBH5; -.
DR Bgee; Q9HBH5; -.
DR CleanEx; HS_PAN2; -.
DR CleanEx; HS_RDH14; -.
DR Genevestigator; Q9HBH5; -.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:LIFEdb.
DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.720; -; 1.
DR InterPro; IPR002198; DH_sc/Rdtase_SDR.
DR InterPro; IPR002347; Glc/ribitol_DH.
DR InterPro; IPR016040; NAD(P)-bd_dom.
DR Pfam; PF00106; adh_short; 1.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR PROSITE; PS00061; ADH_SHORT; FALSE_NEG.
PE 1: Evidence at protein level;
KW Complete proteome; NADP; Oxidoreductase; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1 336 Retinol dehydrogenase 14.
FT /FTId=PRO_0000054770.
FT NP_BIND 50 56 NADP (By similarity).
FT ACT_SITE 217 217 Proton acceptor (By similarity).
FT BINDING 192 192 Substrate (By similarity).
FT MOD_RES 5 5 Phosphothreonine.
SQ SEQUENCE 336 AA; 36865 MW; BCC17B3CD6B70DED CRC64;
MAVATAAAVL AALGGALWLA ARRFVGPRVQ RLRRGGDPGL MHGKTVLITG ANSGLGRATA
AELLRLGARV IMGCRDRARA EEAAGQLRRE LRQAAECGPE PGVSGVGELI VRELDLASLR
SVRAFCQEML QEEPRLDVLI NNAGIFQCPY MKTEDGFEMQ FGVNHLGHFL LTNLLLGLLK
SSAPSRIVVV SSKLYKYGDI NFDDLNSEQS YNKSFCYSRS KLANILFTRE LARRLEGTNV
TVNVLHPGIV RTNLGRHIHI PLLVKPLFNL VSWAFFKTPV EGAQTSIYLA SSPEVEGVSG
RYFGDCKEEE LLPKAMDESV ARKLWDISEV MVGLLK
//