DHI1L_HUMAN
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 03-AUG-2022, entry version 135.
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; 3.
DR IntAct; Q7Z5J1; 1.
DR STRING; 9606.ENSP00000480443; -.
DR iPTMnet; Q7Z5J1; -.
DR PhosphoSitePlus; Q7Z5J1; -.
DR BioMuta; HSD11B1L; -.
DR DMDM; 74750135; -.
DR MassIVE; Q7Z5J1; -.
DR PaxDb; Q7Z5J1; -.
DR PeptideAtlas; Q7Z5J1; -.
DR PRIDE; Q7Z5J1; -.
DR Antibodypedia; 64961; 124 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 CTD; 374875; -.
DR DisGeNET; 374875; -.
DR GeneCards; HSD11B1L; -.
DR HGNC; HGNC:30419; HSD11B1L.
DR HPA; ENSG00000167733; Tissue enhanced (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; ITKDWFP; -.
DR PhylomeDB; Q7Z5J1; -.
DR TreeFam; TF329114; -.
DR PathwayCommons; Q7Z5J1; -.
DR SignaLink; Q7Z5J1; -.
DR BioGRID-ORCS; 374875; 69 hits in 1077 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 130 other tissues.
DR ExpressionAtlas; Q7Z5J1; baseline and differential.
DR Genevisible; Q7Z5J1; HS.
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 InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR Pfam; PF00106; adh_short; 1.
DR PRINTS; PR00081; GDHRDH.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
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
