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   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.
DR   Genevisible; Q8N5I4; HS.
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
//