DR9C7_HUMAN
ID DR9C7_HUMAN Reviewed; 313 AA.
AC Q8NEX9; B3KVB4;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Short-chain dehydrogenase/reductase family 9C member 7;
DE EC=1.1.1.-;
DE AltName: Full=Orphan short-chain dehydrogenase/reductase;
DE Short=SDR-O;
DE AltName: Full=RDH-S;
GN Name=SDR9C7; Synonyms=RDHS, SDRO;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Fetal liver;
RX PubMed=12234675; DOI=10.1016/s0378-1119(02)00757-6;
RA Chen W., Song M.-S., Napoli J.L.;
RT "SDR-O: an orphan short-chain dehydrogenase/reductase localized at mouse
RT chromosome 10/human chromosome 12.";
RL Gene 294:141-146(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Esophagus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NOMENCLATURE.
RX PubMed=19027726; DOI=10.1016/j.cbi.2008.10.040;
RA Persson B., Kallberg Y., Bray J.E., Bruford E., Dellaporta S.L.,
RA Favia A.D., Duarte R.G., Joernvall H., Kavanagh K.L., Kedishvili N.,
RA Kisiela M., Maser E., Mindnich R., Orchard S., Penning T.M., Thornton J.M.,
RA Adamski J., Oppermann U.;
RT "The SDR (short-chain dehydrogenase/reductase and related enzymes)
RT nomenclature initiative.";
RL Chem. Biol. Interact. 178:94-98(2009).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=19703561; DOI=10.1016/j.jsbmb.2009.08.001;
RA Kowalik D., Haller F., Adamski J., Moeller G.;
RT "In search for function of two human orphan SDR enzymes: Hydroxysteroid
RT dehydrogenase like 2 (HSDL2) and short-chain dehydrogenase/reductase-orphan
RT (SDR-O).";
RL J. Steroid Biochem. Mol. Biol. 117:117-124(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-185, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [8]
RP VARIANTS ARCI13 TRP-72 AND THR-200, CHARACTERIZATION OF VARIANTS ARCI13
RP TRP-72 AND THR-200, INVOLVEMENT IN ARCI13, AND TISSUE SPECIFICITY.
RX PubMed=28173123; DOI=10.1093/hmg/ddw277;
RA Shigehara Y., Okuda S., Nemer G., Chedraoui A., Hayashi R., Bitar F.,
RA Nakai H., Abbas O., Daou L., Abe R., Sleiman M.B., Kibbi A.G., Kurban M.,
RA Shimomura Y.;
RT "Mutations in SDR9C7 gene encoding an enzyme for vitamin A metabolism
RT underlie autosomal recessive congenital ichthyosis.";
RL Hum. Mol. Genet. 25:4484-4493(2016).
CC -!- FUNCTION: Displays weak conversion of all-trans-retinal to all-trans-
CC retinol in the presence of NADH. Has apparently no steroid
CC dehydrogenase activity. {ECO:0000269|PubMed:19703561}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19703561}.
CC Note=Granular distribution in the whole cell.
CC -!- TISSUE SPECIFICITY: Expressed in the skin (PubMed:28173123). Expressed
CC in granular and cornified layers of the epidermis (at protein level)
CC (PubMed:28173123). Highly expressed in liver (PubMed:12234675).
CC {ECO:0000269|PubMed:12234675}.
CC -!- DISEASE: Ichthyosis, congenital, autosomal recessive 13 (ARCI13)
CC [MIM:617574]: A form of autosomal recessive congenital ichthyosis, a
CC disorder of keratinization with abnormal differentiation and
CC desquamation of the epidermis, resulting in abnormal skin scaling over
CC the whole body. The main skin phenotypes are lamellar ichthyosis (LI)
CC and non-bullous congenital ichthyosiform erythroderma (NCIE), although
CC phenotypic overlap within the same patient or among patients from the
CC same family can occur. Lamellar ichthyosis is a condition often
CC associated with an embedment in a collodion-like membrane at birth;
CC skin scales later develop, covering the entire body surface. Non-
CC bullous congenital ichthyosiform erythroderma characterized by fine
CC whitish scaling on an erythrodermal background; larger brownish scales
CC are present on the buttocks, neck and legs.
CC {ECO:0000269|PubMed:28173123}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; AY044434; AAK95856.1; -; mRNA.
DR EMBL; AK122782; BAG53726.1; -; mRNA.
DR EMBL; CH471054; EAW96967.1; -; Genomic_DNA.
DR EMBL; BC101551; AAI01552.1; -; mRNA.
DR EMBL; BC101553; AAI01554.1; -; mRNA.
DR CCDS; CCDS8926.1; -.
DR RefSeq; NP_683695.1; NM_148897.2.
DR AlphaFoldDB; Q8NEX9; -.
DR SMR; Q8NEX9; -.
DR BioGRID; 125711; 144.
DR IntAct; Q8NEX9; 13.
DR STRING; 9606.ENSP00000293502; -.
DR iPTMnet; Q8NEX9; -.
DR PhosphoSitePlus; Q8NEX9; -.
DR BioMuta; SDR9C7; -.
DR DMDM; 74751264; -.
DR jPOST; Q8NEX9; -.
DR MassIVE; Q8NEX9; -.
DR PaxDb; Q8NEX9; -.
DR PeptideAtlas; Q8NEX9; -.
DR PRIDE; Q8NEX9; -.
DR ProteomicsDB; 73229; -.
DR Antibodypedia; 43915; 229 antibodies from 16 providers.
DR DNASU; 121214; -.
DR Ensembl; ENST00000293502.2; ENSP00000293502.1; ENSG00000170426.2.
DR GeneID; 121214; -.
DR KEGG; hsa:121214; -.
DR MANE-Select; ENST00000293502.2; ENSP00000293502.1; NM_148897.3; NP_683695.1.
DR UCSC; uc010sqw.2; human.
DR CTD; 121214; -.
DR DisGeNET; 121214; -.
DR GeneCards; SDR9C7; -.
DR GeneReviews; SDR9C7; -.
DR HGNC; HGNC:29958; SDR9C7.
DR HPA; ENSG00000170426; Group enriched (esophagus, skin, vagina).
DR MalaCards; SDR9C7; -.
DR MIM; 609769; gene.
DR MIM; 617574; phenotype.
DR neXtProt; NX_Q8NEX9; -.
DR OpenTargets; ENSG00000170426; -.
DR Orphanet; 313; Lamellar ichthyosis.
DR PharmGKB; PA164725648; -.
DR VEuPathDB; HostDB:ENSG00000170426; -.
DR eggNOG; KOG1610; Eukaryota.
DR GeneTree; ENSGT00940000161764; -.
DR HOGENOM; CLU_010194_2_0_1; -.
DR InParanoid; Q8NEX9; -.
DR OMA; IRRELHF; -.
DR OrthoDB; 942985at2759; -.
DR PhylomeDB; Q8NEX9; -.
DR TreeFam; TF325617; -.
DR PathwayCommons; Q8NEX9; -.
DR Reactome; R-HSA-2453902; The canonical retinoid cycle in rods (twilight vision).
DR SignaLink; Q8NEX9; -.
DR BioGRID-ORCS; 121214; 6 hits in 1070 CRISPR screens.
DR GenomeRNAi; 121214; -.
DR Pharos; Q8NEX9; Tbio.
DR PRO; PR:Q8NEX9; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q8NEX9; protein.
DR Bgee; ENSG00000170426; Expressed in skin of leg and 75 other tissues.
DR Genevisible; Q8NEX9; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0004745; F:NAD-retinol dehydrogenase activity; IDA:UniProtKB.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0016229; F:steroid dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0042572; P:retinol metabolic process; IBA:GO_Central.
DR GO; GO:0008202; P:steroid metabolic process; IBA:GO_Central.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR032968; SDR_9C7.
DR InterPro; IPR002347; SDR_fam.
DR PANTHER; PTHR43313:SF5; PTHR43313:SF5; 1.
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 1: Evidence at protein level;
KW Cytoplasm; Disease variant; Ichthyosis; NADP; Oxidoreductase;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..313
FT /note="Short-chain dehydrogenase/reductase family 9C member
FT 7"
FT /id="PRO_0000316885"
FT ACT_SITE 172
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 29..53
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 160
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 185
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VARIANT 72
FT /note="R -> W (in ARCI13; decreased protein abundance;
FT dbSNP:rs530109812)"
FT /evidence="ECO:0000269|PubMed:28173123"
FT /id="VAR_079292"
FT VARIANT 200
FT /note="I -> T (in ARCI13; decreased protein abundance;
FT dbSNP:rs770729222)"
FT /evidence="ECO:0000269|PubMed:28173123"
FT /id="VAR_079293"
SQ SEQUENCE 313 AA; 35263 MW; C60949797F23D05E CRC64;
MAALTDLSFM YRWFKNCNLV GNLSEKYVFI TGCDSGFGNL LAKQLVDRGM QVLAACFTEE
GSQKLQRDTS YRLQTTLLDV TKSESIKAAA QWVRDKVGEQ GLWALVNNAG VGLPSGPNEW
LTKDDFVKVI NVNLVGLIEV TLHMLPMVKR ARGRVVNMSS SGGRVAVIGG GYCVSKFGVE
AFSDSIRREL YYFGVKVCII EPGNYRTAIL GKENLESRMR KLWERLPQET RDSYGEDYFR
IYTDKLKNIM QVAEPRVRDV INSMEHAIVS RSPRIRYNPG LDAKLLYIPL AKLPTPVTDF
ILSRYLPRPA DSV
