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UniProtKB/Swiss-Prot entry P56937


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name DHB7_HUMAN
Primary accession number P56937
Secondary accession numbers Q7Z4V9 Q8WWS2 Q9UF00
Integrated into Swiss-Prot on May 30, 2000
Sequence was last modified on May 30, 2000 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 84)
Name and origin of the protein
Protein name 3-keto-steroid reductase
Synonyms EC 1.1.1.270
Estradiol 17-beta-dehydrogenase 7
EC 1.1.1.62
17-beta-hydroxysteroid dehydrogenase 7
17-beta-HSD 7
Gene name
Name: HSD17B7
ORFNames: UNQ2563/PRO6243
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2).
DOI=10.1016/S0014-5793(99)01366-6; PubMed=10544267 [NCBI, ExPASy, EBI, Israel, Japan]
Krazeisen A., Breitling R., Imai K., Fritz S., Moeller G., Adamski J.;
"Determination of cDNA, gene structure and chromosomal localization of the novel human 17beta-hydroxysteroid dehydrogenase type 7.";
FEBS Lett. 460:373-379(1999).
[2]
NUCLEOTIDE SEQUENCE (ISOFORMS 1 AND 2).
TISSUE=Ovary;
Krazeisen A., Breitling R., Imai K., Fritz S., Moeller G., Adamski J.;
Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE (ISOFORM 1).
Zhou Y., Yu L., Zhao S.Y.;
"Cloning of a new human cDNA homologous to Rattus norvegicus ovarian-specific protein.";
Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE (ISOFORMS 1 AND 3).
TISSUE=Placenta;
DOI=10.1016/S0006-291X(03)00694-6; PubMed=12732193 [NCBI, ExPASy, EBI, Israel, Japan]
Toern S., Nokelainen P., Kurkela R., Pulkka A., Menjivar M., Ghosh S., Coca-Prados M., Peltoketo H., Isomaa V., Vihko P.;
"Production, purification, and functional analysis of recombinant human and mouse 17beta-hydroxysteroid dehydrogenase type 7.";
Biochem. Biophys. Res. Commun. 305:37-45(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
DOI=10.1101/gr.1293003; PubMed=12975309 [NCBI, ExPASy, EBI, Israel, Japan]
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment.";
Genome Res. 13:2265-2270(2003).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Skin, and Urinary bladder;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
CHARACTERIZATION, AND FUNCTION.
DOI=10.1210/me.2002-0436; PubMed=12829805 [NCBI, ExPASy, EBI, Israel, Japan]
Marijanovic Z., Laubner D., Moeller G., Gege C., Husen B., Adamski J., Breitling R.;
"Closing the gap: identification of human 3-ketosteroid reductase, the last unknown enzyme of mammalian cholesterol biosynthesis.";
Mol. Endocrinol. 17:1715-1725(2003).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF098786; AAF09266.2; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF162767; AAF14537.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF162759; AAF14537.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF162760; AAF14537.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF162761; AAF14537.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF162762; AAF14537.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF162763; AAF14537.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF162764; AAF14537.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF162765; AAF14537.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF162766; AAF14537.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF145023; AAP97275.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ249179; CAC20418.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ250550; CAC88111.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ250551; CAC88111.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ250552; CAC88111.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ250553; CAC88111.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ250554; CAC88111.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ250555; CAC88111.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ250556; CAC88111.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ250557; CAC88111.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ250558; CAC88111.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY358962; AAQ89321.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT007075; AAP35738.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC007068; AAH07068.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC065246; AAH65246.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_057455.1; -.
UniGene Hs.492925
3D structure databases
ModBase P56937.
Enzyme and pathway databases
Reactome REACT_602; Lipid and lipoprotein metabolism.
Organism-specific databases
H-InvDB HIX0001267; -.
HIX0019166; -.
HGNC HGNC:5215; HSD17B7.
GenAtlas HSD17B7.
MIM 606756; gene. [NCBI / EBI]
PharmGKB PA29483; -.
GeneCards P56937.
Gene expression databases
ArrayExpress P56937; -.
CleanEx HS_HSD17B7; -.
GermOnline ENSG00000132196; Homo sapiens.
Ontologies
GO
GO:0005789; Cellular component: endoplasmic reticulum membrane (inferred from experiment from Reactome).
GO:0050576; Molecular function: 3-keto-steroid reductase activity (inferred from experiment from Reactome).
GO:0004303; Molecular function: estradiol 17-beta-dehydrogenase activity (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR002198; DHase_sc/Rdtase_SDR.
IPR002347; Glc/ribitol_DHase.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.720; NAD(P)-bd; 1.
PANTHER PTHR19410; ADH_short_C2; 1.
Pfam PF00106; adh_short; 1.
Pfam graphical view of domain structure.
PRINTS PR00081; GDHRDH.
PROSITE PS00061; ADH_SHORT; FALSE_NEG.
BLOCKS P56937.
ProtoNet P56937.
Genome annotation databases
Ensembl ENSG00000132196; Homo sapiens. [Contig view]
GeneID 51478; -.
KEGG hsa:51478; -.
Phylogenomic databases
HOGENOM P56937; -.
HOVERGEN P56937; -.
Other
DrugBank DB00157; NADH.
LinkHub P56937; -.
NextBio 55124; -.
SOURCE HSD17B7; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Alternative splicing; Glycoprotein; Lipid synthesis; Membrane; NAD; NADP; Oxidoreductase; Steroid biosynthesis; Transmembrane.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   341  341     3-keto-steroid reductase. PRO_0000054586
TOPO_DOM   1   229  229     Extracellular (Potential). 
TRANSMEM   230   250  21     Potential. 
TOPO_DOM   251   341  91     Cytoplasmic (Potential). 
NP_BIND   8    15  8     NAD (Potential). 
ACT_SITE   193   193        Proton acceptor (By similarity). 
BINDING   171   171        Substrate (By similarity). 
CARBOHYD   37    37        N-linked (GlcNAc...) (Potential). 
CARBOHYD   178   178        N-linked (GlcNAc...) (Potential). 
CARBOHYD   229   229        N-linked (GlcNAc...) (Potential). 
VAR_SEQ   112   119        Missing (in isoform 2). VSP_006029
VAR_SEQ   215   249        Missing (in isoform 3). VSP_012766
CONFLICT   52    53        HP -> PT (in Ref. 1; AAF14537). 
CONFLICT   61    61        Q -> P (in Ref. 1; AAF14537). 
CONFLICT   86    86        C -> R (in Ref. 4; CAC88111). 
CONFLICT   105   105        F -> L (in Ref. 4; CAC88111). 
CONFLICT   135   135        L -> F (in Ref. 3; AAP97275). 
CONFLICT   273   276        HQKP -> PPKA (in Ref. 3; AAP97275). 
CONFLICT   288   295        ATTGFGRN -> GTTALEEI (in Ref. 3; AAP97275). 
Sequence information
Length: 341 AA [This is the length of the unprocessed precursor] Molecular weight: 38206 Da [This is the MW of the unprocessed precursor] CRC64: FE4892B2602F549B [This is a checksum on the sequence]
        10         20         30         40         50         60 
MRKVVLITGA SSGIGLALCK RLLAEDDELH LCLACRNMSK AEAVCAALLA SHPTAEVTIV 

        70         80         90        100        110        120 
QVDVSNLQSV FRASKELKQR FQRLDCIYLN AGIMPNPQLN IKALFFGLFS RKVIHMFSTA 

       130        140        150        160        170        180 
EGLLTQGDKI TADGLQEVFE TNVFGHFILI RELEPLLCHS DNPSQLIWTS SRSARKSNFS 

       190        200        210        220        230        240 
LEDFQHSKGK EPYSSSKYAT DLLSVALNRN FNQQGLYSNV ACPGTALTNL TYGILPPFIW 

       250        260        270        280        290        300 
TLLMPAILLL RFFANAFTLT PYNGTEALVW LFHQKPESLN PLIKYLSATT GFGRNYIMTQ 

       310        320        330        340 
KMDLDEDTAE KFYQKLLELE KHIRVTIQKT DNQARLSGSC L 

P56937 in FASTA format

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