ID HSDL1_HUMAN Reviewed; 330 AA. AC Q3SXM5; B4DSL2; D3DUL4; Q3SXM4; Q8NC98; Q9BY22; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 30-NOV-2010, sequence version 3. DT 27-MAR-2024, entry version 156. DE RecName: Full=Inactive hydroxysteroid dehydrogenase-like protein 1; DE AltName: Full=Short chain dehydrogenase/reductase family 12C member 3; GN Name=HSDL1; Synonyms=SDR12C3; 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] (ISOFORM 1), AND TISSUE SPECIFICITY. RC TISSUE=Fetal brain; RX PubMed=12153137; DOI=10.1023/a:1015726217890; RA Huang Y., Tang R., Dai J., Gu S., Zhao W., Cheng C., Xu M., Zhou Z., RA Ying K., Xi Y., Mao Y.; RT "A novel human hydroxysteroid dehydrogenase like 1 gene (HSDL1) is highly RT expressed in reproductive tissues."; RL Mol. Biol. Rep. 28:185-191(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT RP CYS-327. RC TISSUE=Brain; 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]. RX PubMed=15616553; DOI=10.1038/nature03187; RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M., RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., RA Myers R.M., Rubin E.M., Pennacchio L.A.; RT "The sequence and analysis of duplication-rich human chromosome 16."; RL Nature 432:988-994(2004). RN [4] 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). 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 [6] RP PROTEIN SEQUENCE OF 2-12 AND 91-99, CLEAVAGE OF INITIATOR METHIONINE, RP ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Chronic myeloid leukemia cell; RA Bienvenut W.V., Preisinger C., Kolch W.; RL Submitted (JUL-2008) to UniProtKB. RN [7] RP LACK OF ENZYME ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, RP MUTAGENESIS OF PHE-218, AND INTERACTION WITH STYXL1. RX PubMed=19026618; DOI=10.1016/j.cbi.2008.10.036; RA Meier M., Tokarz J., Haller F., Mindnich R., Adamski J.; RT "Human and zebrafish hydroxysteroid dehydrogenase like 1 (HSDL1) proteins RT are inactive enzymes but conserved among species."; RL Chem. Biol. Interact. 178:197-205(2009). RN [8] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). CC -!- SUBUNIT: Interacts with STYXL1. {ECO:0000269|PubMed:19026618}. CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:19026618}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q3SXM5-1; Sequence=Displayed; CC Name=2; CC IsoId=Q3SXM5-2; Sequence=VSP_042823; CC -!- TISSUE SPECIFICITY: Highly expressed in testis and ovary. Also detected CC in thyroid, spinal cord, adrenal gland, heart, placenta, skeletal CC muscle, small intestine, colon, spleen, prostate and pancreas. CC {ECO:0000269|PubMed:12153137, ECO:0000269|PubMed:19026618}. CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) CC family. 17-beta-HSD 3 subfamily. {ECO:0000305}. CC -!- CAUTION: Although it belongs to the SDR family, Phe-218 is present CC instead of the conserved Tyr which is an active site residue. It is CC therefore expected that this protein lacks oxidoreductase activity. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAK15047.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAK16927.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF237684; AAK15047.1; ALT_INIT; mRNA. DR EMBL; AY028377; AAK16927.1; ALT_INIT; mRNA. DR EMBL; AK074878; BAC11262.1; -; mRNA. DR EMBL; AK299798; BAG61674.1; -; mRNA. DR EMBL; AC040169; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471114; EAW95502.1; -; Genomic_DNA. DR EMBL; CH471114; EAW95503.1; -; Genomic_DNA. DR EMBL; CH471114; EAW95504.1; -; Genomic_DNA. DR EMBL; BC104219; AAI04220.1; -; mRNA. DR EMBL; BC106917; AAI06918.1; -; mRNA. DR EMBL; BC104218; AAI04219.1; -; mRNA. DR CCDS; CCDS10942.1; -. [Q3SXM5-1] DR CCDS; CCDS54046.1; -. [Q3SXM5-2] DR RefSeq; NP_001139523.1; NM_001146051.1. [Q3SXM5-2] DR RefSeq; NP_113651.4; NM_031463.4. [Q3SXM5-1] DR RefSeq; XP_005256246.1; XM_005256189.2. [Q3SXM5-1] DR AlphaFoldDB; Q3SXM5; -. DR SMR; Q3SXM5; -. DR BioGRID; 123727; 74. DR IntAct; Q3SXM5; 24. DR MINT; Q3SXM5; -. DR STRING; 9606.ENSP00000219439; -. DR iPTMnet; Q3SXM5; -. DR PhosphoSitePlus; Q3SXM5; -. DR SwissPalm; Q3SXM5; -. DR BioMuta; HSDL1; -. DR DMDM; 313104226; -. DR EPD; Q3SXM5; -. DR jPOST; Q3SXM5; -. DR MassIVE; Q3SXM5; -. DR MaxQB; Q3SXM5; -. DR PaxDb; 9606-ENSP00000219439; -. DR PeptideAtlas; Q3SXM5; -. DR ProteomicsDB; 61817; -. [Q3SXM5-1] DR ProteomicsDB; 61818; -. [Q3SXM5-2] DR Pumba; Q3SXM5; -. DR Antibodypedia; 30543; 71 antibodies from 21 providers. DR DNASU; 83693; -. DR Ensembl; ENST00000219439.9; ENSP00000219439.4; ENSG00000103160.12. [Q3SXM5-1] DR Ensembl; ENST00000434463.7; ENSP00000407437.3; ENSG00000103160.12. [Q3SXM5-2] DR GeneID; 83693; -. DR KEGG; hsa:83693; -. DR MANE-Select; ENST00000219439.9; ENSP00000219439.4; NM_031463.5; NP_113651.4. DR UCSC; uc002fhk.3; human. [Q3SXM5-1] DR AGR; HGNC:16475; -. DR CTD; 83693; -. DR DisGeNET; 83693; -. DR GeneCards; HSDL1; -. DR HGNC; HGNC:16475; HSDL1. DR HPA; ENSG00000103160; Low tissue specificity. DR MIM; 619067; gene. DR neXtProt; NX_Q3SXM5; -. DR OpenTargets; ENSG00000103160; -. DR PharmGKB; PA134988345; -. DR VEuPathDB; HostDB:ENSG00000103160; -. DR eggNOG; KOG1014; Eukaryota. DR GeneTree; ENSGT00940000160053; -. DR HOGENOM; CLU_010194_38_0_1; -. DR InParanoid; Q3SXM5; -. DR OMA; QYGLMKC; -. DR OrthoDB; 6845at2759; -. DR PhylomeDB; Q3SXM5; -. DR TreeFam; TF314591; -. DR PathwayCommons; Q3SXM5; -. DR SignaLink; Q3SXM5; -. DR BioGRID-ORCS; 83693; 12 hits in 1155 CRISPR screens. DR ChiTaRS; HSDL1; human. DR GenomeRNAi; 83693; -. DR Pharos; Q3SXM5; Tbio. DR PRO; PR:Q3SXM5; -. DR Proteomes; UP000005640; Chromosome 16. DR RNAct; Q3SXM5; Protein. DR Bgee; ENSG00000103160; Expressed in cortical plate and 173 other cell types or tissues. DR ExpressionAtlas; Q3SXM5; baseline and differential. DR GO; GO:0045111; C:intermediate filament cytoskeleton; IDA:HPA. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA. DR GO; GO:0005739; C:mitochondrion; IDA:HPA. DR CDD; cd05356; 17beta-HSD1_like_SDR_c; 1. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR InterPro; IPR002347; SDR_fam. DR PANTHER; PTHR44889; INACTIVE HYDROXYSTEROID DEHYDROGENASE-LIKE PROTEIN 1; 1. DR PANTHER; PTHR44889:SF1; INACTIVE HYDROXYSTEROID DEHYDROGENASE-LIKE PROTEIN 1; 1. DR Pfam; PF00106; adh_short; 1. DR PIRSF; PIRSF000126; 11-beta-HSD1; 1. DR PRINTS; PR00081; GDHRDH. DR PRINTS; PR00080; SDRFAMILY. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. DR Genevisible; Q3SXM5; HS. PE 1: Evidence at protein level; KW Acetylation; Alternative splicing; Direct protein sequencing; KW Mitochondrion; NADP; Reference proteome. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|Ref.6" FT CHAIN 2..330 FT /note="Inactive hydroxysteroid dehydrogenase-like protein FT 1" FT /id="PRO_0000313671" FT REGION 2..82 FT /note="Required for mitochondria translocation" FT BINDING 74..80 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250" FT BINDING 125 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250" FT BINDING 222 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000269|Ref.6" FT VAR_SEQ 105..159 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_042823" FT VARIANT 248 FT /note="P -> S (in dbSNP:rs11540436)" FT /id="VAR_037693" FT VARIANT 327 FT /note="S -> C (in dbSNP:rs4378600)" FT /evidence="ECO:0000269|PubMed:14702039" FT /id="VAR_037694" FT MUTAGEN 218 FT /note="F->Y: Restores the oxidoreductase activity." FT /evidence="ECO:0000269|PubMed:19026618" FT CONFLICT 1 FT /note="M -> V (in Ref. 1; AAK15047/AAK16927)" FT /evidence="ECO:0000305" FT CONFLICT 222 FT /note="K -> R (in Ref. 5; AAI04220/AAI06918)" FT /evidence="ECO:0000305" SQ SEQUENCE 330 AA; 37002 MW; 6203476EE4E6151B CRC64; MAAVDSFYLL YREIARSCNC YMEALALVGA WYTARKSITV ICDFYSLIRL HFIPRLGSRA DLIKQYGRWA VVSGATDGIG KAYAEELASR GLNIILISRN EEKLQVVAKD IADTYKVETD IIVADFSSGR EIYLPIREAL KDKDVGILVN NVGVFYPYPQ YFTQLSEDKL WDIINVNIAA ASLMVHVVLP GMVERKKGAI VTISSGSCCK PTPQLAAFSA SKAYLDHFSR ALQYEYASKG IFVQSLIPFY VATSMTAPSN FLHRCSWLVP SPKVYAHHAV STLGISKRTT GYWSHSIQFL FAQYMPEWLW VWGANILNRS LRKEALSCTA //