ID DHI1L_HUMAN Reviewed; 315 AA. AC Q7Z5J1; Q05D45; Q52LF4; Q7Z5I9; Q7Z5J0; Q7Z5P5; Q7Z5P6; Q7Z5P7; Q7Z5P8; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2003, sequence version 1. DT 27-MAR-2024, entry version 143. DE RecName: Full=Hydroxysteroid 11-beta-dehydrogenase 1-like protein; DE EC=1.1.1.-; DE AltName: Full=11-beta-hydroxysteroid dehydrogenase type 3; DE Short=11-DH3; DE Short=11-beta-HSD3; DE AltName: Full=Short chain dehydrogenase/reductase family 26C member 2; DE AltName: Full=Short-chain dehydrogenase/reductase 10; DE Flags: Precursor; GN Name=HSD11B1L; Synonyms=HSD3, SCDR10, SDR26C2; 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] (ISOFORMS 1; 2; 3; 4; 5; 6 AND 7). RA Huang C.Q., Wu S.L., Chen Z., Xiao P.J.; RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15057824; DOI=10.1038/nature02399; RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A., RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., RA Rubin E.M., Lucas S.M.; RT "The DNA sequence and biology of human chromosome 19."; RL Nature 428:529-535(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 (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 7 AND 8), AND NUCLEOTIDE RP SEQUENCE [LARGE SCALE MRNA] OF 106-315 (ISOFORM 5). RC TISSUE=Brain, 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). CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=8; CC Name=1; CC IsoId=Q7Z5J1-1; Sequence=Displayed; CC Name=2; Synonyms=B; CC IsoId=Q7Z5J1-2; Sequence=VSP_030796, VSP_030797; CC Name=3; Synonyms=G; CC IsoId=Q7Z5J1-3; Sequence=VSP_030793; CC Name=4; Synonyms=F; CC IsoId=Q7Z5J1-4; Sequence=VSP_030791; CC Name=5; Synonyms=C; CC IsoId=Q7Z5J1-5; Sequence=VSP_030792, VSP_030796, VSP_030797; CC Name=6; Synonyms=A; CC IsoId=Q7Z5J1-6; Sequence=VSP_030793, VSP_030796, VSP_030797; CC Name=7; Synonyms=D; CC IsoId=Q7Z5J1-7; Sequence=VSP_030791, VSP_030796, VSP_030797; CC Name=8; CC IsoId=Q7Z5J1-8; Sequence=VSP_030794, VSP_030795; CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) CC family. {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; AY268351; AAP42285.1; -; mRNA. DR EMBL; AY268352; AAP42286.1; -; mRNA. DR EMBL; AY268353; AAP42287.1; -; mRNA. DR EMBL; AY268354; AAP42288.1; -; mRNA. DR EMBL; AY313894; AAP83166.1; -; mRNA. DR EMBL; AY313895; AAP83167.1; -; mRNA. DR EMBL; AY313896; AAP83168.1; -; mRNA. DR EMBL; AC011499; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471139; EAW69156.1; -; Genomic_DNA. DR EMBL; CH471139; EAW69157.1; -; Genomic_DNA. DR EMBL; BC053546; AAH53546.1; -; mRNA. DR EMBL; BC072434; AAH72434.1; -; mRNA. DR EMBL; BC093950; AAH93950.1; -; mRNA. DR EMBL; BC112187; AAI12188.1; -; mRNA. DR EMBL; BC018336; AAH18336.1; -; mRNA. DR CCDS; CCDS12144.1; -. [Q7Z5J1-6] DR CCDS; CCDS12145.1; -. [Q7Z5J1-2] DR CCDS; CCDS12146.1; -. [Q7Z5J1-5] DR CCDS; CCDS45931.1; -. [Q7Z5J1-1] DR CCDS; CCDS45932.1; -. [Q7Z5J1-4] DR CCDS; CCDS58641.1; -. [Q7Z5J1-3] DR CCDS; CCDS58642.1; -. [Q7Z5J1-7] DR RefSeq; NP_001254798.1; NM_001267869.1. [Q7Z5J1-7] DR RefSeq; NP_001254799.1; NM_001267870.1. DR RefSeq; NP_001254800.1; NM_001267871.1. [Q7Z5J1-3] DR RefSeq; NP_940935.1; NM_198533.2. [Q7Z5J1-1] DR RefSeq; NP_941993.1; NM_198704.2. [Q7Z5J1-4] DR RefSeq; NP_941994.1; NM_198705.2. [Q7Z5J1-6] DR RefSeq; NP_941995.1; NM_198706.2. [Q7Z5J1-2] DR RefSeq; NP_941996.1; NM_198707.2. [Q7Z5J1-5] DR RefSeq; NP_941997.1; NM_198708.2. [Q7Z5J1-7] DR AlphaFoldDB; Q7Z5J1; -. DR SMR; Q7Z5J1; -. DR BioGRID; 131927; 6. DR IntAct; Q7Z5J1; 2. DR MINT; Q7Z5J1; -. DR STRING; 9606.ENSP00000480443; -. DR iPTMnet; Q7Z5J1; -. DR PhosphoSitePlus; Q7Z5J1; -. DR BioMuta; HSD11B1L; -. DR DMDM; 74750135; -. DR MassIVE; Q7Z5J1; -. DR PaxDb; 9606-ENSP00000480443; -. DR PeptideAtlas; Q7Z5J1; -. DR Antibodypedia; 64961; 138 antibodies from 19 providers. DR DNASU; 374875; -. DR Ensembl; ENST00000301382.8; ENSP00000301382.4; ENSG00000167733.14. [Q7Z5J1-6] DR Ensembl; ENST00000339423.7; ENSP00000340436.2; ENSG00000167733.14. [Q7Z5J1-2] DR Ensembl; ENST00000342970.6; ENSP00000343451.2; ENSG00000167733.14. [Q7Z5J1-5] DR Ensembl; ENST00000411793.6; ENSP00000398955.2; ENSG00000167733.14. [Q7Z5J1-4] DR Ensembl; ENST00000422535.6; ENSP00000409592.2; ENSG00000167733.14. [Q7Z5J1-8] DR Ensembl; ENST00000423665.6; ENSP00000407154.2; ENSG00000167733.14. [Q7Z5J1-1] DR Ensembl; ENST00000577917.5; ENSP00000463073.1; ENSG00000167733.14. [Q7Z5J1-3] DR Ensembl; ENST00000581521.5; ENSP00000463794.1; ENSG00000167733.14. [Q7Z5J1-2] DR Ensembl; ENST00000581773.5; ENSP00000462975.1; ENSG00000167733.14. [Q7Z5J1-2] DR Ensembl; ENST00000581893.5; ENSP00000464454.1; ENSG00000167733.14. [Q7Z5J1-7] DR Ensembl; ENST00000583928.5; ENSP00000462586.1; ENSG00000167733.14. [Q7Z5J1-7] DR GeneID; 374875; -. DR KEGG; hsa:374875; -. DR MANE-Select; ENST00000339423.7; ENSP00000340436.2; NM_198706.3; NP_941995.1. [Q7Z5J1-2] DR UCSC; uc002mcj.6; human. [Q7Z5J1-1] DR AGR; HGNC:30419; -. DR CTD; 374875; -. DR DisGeNET; 374875; -. DR GeneCards; HSD11B1L; -. DR HGNC; HGNC:30419; HSD11B1L. DR HPA; ENSG00000167733; Tissue enriched (brain). DR neXtProt; NX_Q7Z5J1; -. DR OpenTargets; ENSG00000167733; -. DR PharmGKB; PA144596423; -. DR VEuPathDB; HostDB:ENSG00000167733; -. DR eggNOG; KOG1205; Eukaryota. DR GeneTree; ENSGT00940000162487; -. DR HOGENOM; CLU_1488559_0_0_1; -. DR InParanoid; Q7Z5J1; -. DR OMA; EYTRWLM; -. DR OrthoDB; 2904540at2759; -. DR PhylomeDB; Q7Z5J1; -. DR TreeFam; TF329114; -. DR PathwayCommons; Q7Z5J1; -. DR SignaLink; Q7Z5J1; -. DR BioGRID-ORCS; 374875; 72 hits in 1155 CRISPR screens. DR ChiTaRS; HSD11B1L; human. DR GenomeRNAi; 374875; -. DR Pharos; Q7Z5J1; Tbio. DR PRO; PR:Q7Z5J1; -. DR Proteomes; UP000005640; Chromosome 19. DR RNAct; Q7Z5J1; Protein. DR Bgee; ENSG00000167733; Expressed in cingulate cortex and 132 other cell types or tissues. DR ExpressionAtlas; Q7Z5J1; baseline and differential. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central. 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; PTHR44279; HYDROXYSTEROID (11-BETA) DEHYDROGENASE 1-LIKE B-RELATED; 1. DR PANTHER; PTHR44279:SF3; HYDROXYSTEROID 11-BETA-DEHYDROGENASE 1-LIKE PROTEIN; 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; Q7Z5J1; HS. PE 2: Evidence at transcript level; KW Alternative splicing; NADP; Oxidoreductase; Reference proteome; Secreted; KW Signal. FT SIGNAL 1..15 FT /evidence="ECO:0000255" FT CHAIN 16..315 FT /note="Hydroxysteroid 11-beta-dehydrogenase 1-like protein" FT /id="PRO_0000316816" FT REGION 221..286 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 178 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001" FT BINDING 36..62 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250" FT BINDING 87..88 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250" FT BINDING 114..116 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250" FT BINDING 165 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 178..182 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250" FT BINDING 211..217 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250" FT VAR_SEQ 1..134 FT /note="Missing (in isoform 4 and isoform 7)" FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.1" FT /id="VSP_030791" FT VAR_SEQ 1..87 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.1" FT /id="VSP_030792" FT VAR_SEQ 25..105 FT /note="Missing (in isoform 3 and isoform 6)" FT /evidence="ECO:0000303|Ref.1" FT /id="VSP_030793" FT VAR_SEQ 69..87 FT /note="VVGNCRKLGAPKVFYIAAD -> ARWLTLVVSTLGGRGKWIT (in FT isoform 8)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_030794" FT VAR_SEQ 88..315 FT /note="Missing (in isoform 8)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_030795" FT VAR_SEQ 223..234 FT /note="Missing (in isoform 2, isoform 5, isoform 6 and FT isoform 7)" FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.1" FT /id="VSP_030796" FT VAR_SEQ 238..315 FT /note="PLQSQTAMFLPPTVPGARTLTETPLRGWPQPKMKSSRQKSKTEKNDGHLEPV FT TAWEVQVPRVRRLCRGLARPHLFGHD -> TRVKAAPGPKAALAVIRGGATRAAGVFYP FT WRFRLLCLLRRWLPRPRAWFIRQELNVTAAAA (in isoform 2, isoform 5, FT isoform 6 and isoform 7)" FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.1" FT /id="VSP_030797" SQ SEQUENCE 315 AA; 34288 MW; F7C3A61476A1E48F CRC64; MKVLLLTGLG ALFFAYYWDD NFDPASLQGA RVLLTGANAG VGEELAYHYA RLGSHLVLTA HTEALLQKVV GNCRKLGAPK VFYIAADMAS PEAPESVVQF ALDKLGGLDY LVLNHIGGAP AGTRARSPQA TRWLMQVNFV SYVQLTSRAL PSLTDSKGSL VVVSSLLGRV PTSFSTPYSA AKFALDGFFG SLRRELDVQD VNVAITMCVL GLRDRASAAE AVRSSTSRPR QPEHRGVPLQ SQTAMFLPPT VPGARTLTET PLRGWPQPKM KSSRQKSKTE KNDGHLEPVT AWEVQVPRVR RLCRGLARPH LFGHD //