DHI1B_XENLA
ID DHI1B_XENLA Reviewed; 291 AA.
AC Q7SYS6;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Hydroxysteroid 11-beta-dehydrogenase 1-like protein B;
DE EC=1.1.1.-;
DE AltName: Full=11-beta-hydroxysteroid dehydrogenase type 3-B;
DE Short=11-DH3-B;
DE Short=11-beta-HSD3-B;
DE Flags: Precursor;
GN Name=hsd11b1l-b; Synonyms=hsd3-b;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Tadpole;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; BC054284; AAH54284.1; -; mRNA.
DR RefSeq; NP_001079804.1; NM_001086335.1.
DR AlphaFoldDB; Q7SYS6; -.
DR SMR; Q7SYS6; -.
DR DNASU; 379494; -.
DR GeneID; 379494; -.
DR KEGG; xla:379494; -.
DR CTD; 379494; -.
DR Xenbase; XB-GENE-5834075; hsd11b1l.2.L.
DR OrthoDB; 906746at2759; -.
DR Proteomes; UP000186698; Chromosome 1L.
DR Bgee; 379494; Expressed in intestine and 5 other tissues.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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 NADP; Oxidoreductase; Reference proteome; Secreted; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..291
FT /note="Hydroxysteroid 11-beta-dehydrogenase 1-like protein
FT B"
FT /id="PRO_0000316821"
FT ACT_SITE 183
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 40..66
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 91..92
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 118..120
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 170
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 183..187
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 216..222
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
SQ SEQUENCE 291 AA; 31596 MW; 91F137C4CA6D08F5 CRC64;
MAGVILLLLS LCVGYIAYYF FRTESMNKES VRGKRVLITG SSTGLGEQIA YEFARMGAHI
MITARRLQQL QEVASQCMKL GAASAHYVAS DMGNLESAQS VAQEAVVKLG GLDYLVLNHI
GGSGGFGFFK GDMDPVVGST TVNFLSYVQL TSSALSALQE SQGSIVVISS MSGRIGAPFT
TSYCASKFAL EGFYSSLRRE FALQNSKMSV TVAVLGYIDT ENAVKKVGNK VSMTASSKED
CAREVVKAAV LQQPEIFYPY WGIKPFVLLR DWFPGLVAKI LDKCYILENI Q