ID DHRSX_HUMAN Reviewed; 330 AA.
AC Q8N5I4; Q6UWC7; Q8WUS4; Q96GR8; Q9NTF6;
DT 03-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 27-MAR-2024, entry version 170.
DE RecName: Full=Dehydrogenase/reductase SDR family member on chromosome X;
DE EC=1.1.-.-;
DE AltName: Full=DHRSXY;
DE AltName: Full=Short chain dehydrogenase/reductase family 46C member 1;
DE AltName: Full=Short chain dehydrogenase/reductase family 7C member 6;
GN Name=DHRSX; Synonyms=CXorf11, DHRS5X, SDR46C1, SDR7C6;
GN ORFNames=UNQ6508/PRO21433;
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], TISSUE SPECIFICITY, AND VARIANTS LEU-247 AND
RP ARG-292.
RC TISSUE=Teratocarcinoma;
RX PubMed=11731500; DOI=10.1101/gr.197001;
RA Gianfrancesco F., Sanges R., Esposito T., Tempesta S., Rao E., Rappold G.,
RA Archidiacono N., Graves J.A.M., Forabosco A., D'Urso M.;
RT "Differential divergence of three human pseudoautosomal genes and their
RT mouse homologs: implications for sex chromosome evolution.";
RL Genome Res. 11:2095-2100(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS ARG-292 AND LYS-297.
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., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS LEU-247; ARG-292 AND
RP LYS-297.
RC TISSUE=Brain, Duodenum, and Ovary;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 127-330, AND VARIANTS LEU-247 AND
RP ARG-292.
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP PROTEIN SEQUENCE OF 2-11, FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=25076851; DOI=10.7150/ijms.9529;
RA Zhang G., Luo Y., Li G., Wang L., Na D., Wu X., Zhang Y., Mo X., Wang L.;
RT "DHRSX, a novel non-classical secretory protein associated with starvation
RT induced autophagy.";
RL Int. J. Med. Sci. 11:962-970(2014).
CC -!- FUNCTION: Involved in the positive regulation of starvation-induced
CC autophagy (PubMed:25076851). {ECO:0000269|PubMed:25076851}.
CC -!- INTERACTION:
CC Q8N5I4; P02654: APOC1; NbExp=3; IntAct=EBI-3923585, EBI-1220105;
CC Q8N5I4; Q13520: AQP6; NbExp=3; IntAct=EBI-3923585, EBI-13059134;
CC Q8N5I4; Q12797-6: ASPH; NbExp=3; IntAct=EBI-3923585, EBI-12092171;
CC Q8N5I4; Q9UHD4: CIDEB; NbExp=3; IntAct=EBI-3923585, EBI-7062247;
CC Q8N5I4; Q96DZ9-2: CMTM5; NbExp=3; IntAct=EBI-3923585, EBI-11522780;
CC Q8N5I4; Q9Y5Q0: FADS3; NbExp=3; IntAct=EBI-3923585, EBI-17548630;
CC Q8N5I4; Q8NBQ5: HSD17B11; NbExp=3; IntAct=EBI-3923585, EBI-1052304;
CC Q8N5I4; O15173: PGRMC2; NbExp=3; IntAct=EBI-3923585, EBI-1050125;
CC Q8N5I4; P57054: PIGP; NbExp=3; IntAct=EBI-3923585, EBI-17630288;
CC Q8N5I4; Q86VR2: RETREG3; NbExp=3; IntAct=EBI-3923585, EBI-10192441;
CC Q8N5I4; Q96GQ5: RUSF1; NbExp=3; IntAct=EBI-3923585, EBI-8636004;
CC Q8N5I4; Q96MV1: TLCD4; NbExp=3; IntAct=EBI-3923585, EBI-12947623;
CC Q8N5I4; Q96AN5: TMEM143; NbExp=3; IntAct=EBI-3923585, EBI-13342951;
CC Q8N5I4; Q9NUH8: TMEM14B; NbExp=3; IntAct=EBI-3923585, EBI-8638294;
CC Q8N5I4; Q8N661: TMEM86B; NbExp=3; IntAct=EBI-3923585, EBI-2548832;
CC Q8N5I4; Q96MV8: ZDHHC15; NbExp=3; IntAct=EBI-3923585, EBI-12837904;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:25076851}.
CC Note=Secreted in a non-classical form. A signal peptide sequence at
CC position 1-31 is predicted.
CC -!- TISSUE SPECIFICITY: Widely expressed. Highly expressed in the pancreas.
CC {ECO:0000269|PubMed:11731500, ECO:0000269|PubMed:25076851}.
CC -!- MISCELLANEOUS: The gene coding for this protein is located in the
CC pseudoautosomal region 1 (PAR1) of X and Y chromosomes.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; AJ293620; CAC82170.1; -; mRNA.
DR EMBL; AY358849; AAQ89208.1; -; mRNA.
DR EMBL; AC079176; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX119919; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX649443; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR381696; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR856018; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC019696; AAH19696.2; ALT_SEQ; mRNA.
DR EMBL; BC032340; AAH32340.1; -; mRNA.
DR EMBL; AL137300; CAB70685.1; -; mRNA.
DR CCDS; CCDS35195.1; -.
DR PIR; T46363; T46363.
DR RefSeq; NP_660160.2; NM_145177.2.
DR AlphaFoldDB; Q8N5I4; -.
DR SMR; Q8N5I4; -.
DR BioGRID; 128508; 23.
DR IntAct; Q8N5I4; 19.
DR STRING; 9606.ENSP00000334113; -.
DR iPTMnet; Q8N5I4; -.
DR PhosphoSitePlus; Q8N5I4; -.
DR BioMuta; DHRSX; -.
DR DMDM; 229462837; -.
DR EPD; Q8N5I4; -.
DR jPOST; Q8N5I4; -.
DR MassIVE; Q8N5I4; -.
DR MaxQB; Q8N5I4; -.
DR PaxDb; 9606-ENSP00000334113; -.
DR PeptideAtlas; Q8N5I4; -.
DR ProteomicsDB; 72063; -.
DR Pumba; Q8N5I4; -.
DR Antibodypedia; 575; 115 antibodies from 21 providers.
DR DNASU; 207063; -.
DR Ensembl; ENST00000334651.11; ENSP00000334113.5; ENSG00000169084.15.
DR Ensembl; ENST00000711204.1; ENSP00000518604.1; ENSG00000292338.1.
DR GeneID; 207063; -.
DR KEGG; hsa:207063; -.
DR MANE-Select; ENST00000334651.11; ENSP00000334113.5; NM_145177.3; NP_660160.2.
DR UCSC; uc004cqf.5; human.
DR AGR; HGNC:18399; -.
DR CTD; 207063; -.
DR GeneCards; DHRSX; -.
DR HGNC; HGNC:18399; DHRSX.
DR HPA; ENSG00000169084; Low tissue specificity.
DR MIM; 301034; gene.
DR MIM; 400049; gene.
DR neXtProt; NX_Q8N5I4; -.
DR OpenTargets; ENSG00000169084; -.
DR PharmGKB; PA27330; -.
DR VEuPathDB; HostDB:ENSG00000169084; -.
DR eggNOG; KOG1208; Eukaryota.
DR GeneTree; ENSGT00940000162345; -.
DR HOGENOM; CLU_010194_44_5_1; -.
DR InParanoid; Q8N5I4; -.
DR OMA; AKTACIW; -.
DR OrthoDB; 2466675at2759; -.
DR PhylomeDB; Q8N5I4; -.
DR TreeFam; TF105429; -.
DR PathwayCommons; Q8N5I4; -.
DR SignaLink; Q8N5I4; -.
DR BioGRID-ORCS; 207063; 52 hits in 628 CRISPR screens.
DR ChiTaRS; DHRSX; human.
DR GeneWiki; DHRSX; -.
DR GenomeRNAi; 207063; -.
DR Pharos; Q8N5I4; Tdark.
DR PRO; PR:Q8N5I4; -.
DR Proteomes; UP000005640; Chromosome X.
DR Proteomes; UP000005640; Chromosome Y.
DR RNAct; Q8N5I4; Protein.
DR Bgee; ENSG00000169084; Expressed in stromal cell of endometrium and 137 other cell types or tissues.
DR ExpressionAtlas; Q8N5I4; baseline and differential.
DR Genevisible; Q8N5I4; HS.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0010508; P:positive regulation of autophagy; IMP:UniProtKB.
DR CDD; cd05327; retinol-DH_like_SDR_c_like; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR PANTHER; PTHR24320:SF251; DEHYDROGENASE_REDUCTASE SDR FAMILY MEMBER ON CHROMOSOME X; 1.
DR PANTHER; PTHR24320; RETINOL DEHYDROGENASE; 1.
DR Pfam; PF00106; adh_short; 1.
DR PRINTS; PR00081; GDHRDH.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Oxidoreductase; Reference proteome; Secreted.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:25076851"
FT CHAIN 2..330
FT /note="Dehydrogenase/reductase SDR family member on
FT chromosome X"
FT /id="PRO_0000031974"
FT ACT_SITE 208
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 47..71
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 183
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT VARIANT 247
FT /note="V -> L (in dbSNP:rs1127915)"
FT /evidence="ECO:0000269|PubMed:11731500,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:17974005"
FT /id="VAR_055354"
FT VARIANT 292
FT /note="H -> R (in dbSNP:rs3210910)"
FT /evidence="ECO:0000269|PubMed:11731500,
FT ECO:0000269|PubMed:12975309, ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:17974005"
FT /id="VAR_055355"
FT VARIANT 297
FT /note="E -> K (in dbSNP:rs12010)"
FT /evidence="ECO:0000269|PubMed:12975309,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_016100"
SQ SEQUENCE 330 AA; 36443 MW; 0191EC6B0B98F56F CRC64;
MSPLSAARAA LRVYAVGAAV ILAQLLRRCR GGFLEPVFPP RPDRVAIVTG GTDGIGYSTA
KHLARLGMHV IIAGNNDSKA KQVVSKIKEE TLNDKVEFLY CDLASMTSIR QFVQKFKMKK
IPLHVLINNA GVMMVPQRKT RDGFEEHFGL NYLGHFLLTN LLLDTLKESG SPGHSARVVT
VSSATHYVAE LNMDDLQSSA CYSPHAAYAQ SKLALVLFTY HLQRLLAAEG SHVTANVVDP
GVVNTDVYKH VFWATRLAKK LLGWLLFKTP DEGAWTSIYA AVTPELEGVG GHYLYNEKET
KSLHVTYNQK LQQQLWSKSC EMTGVLDVTL
//
