P56937 (DHB7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
3-keto-steroid reductase
EC=1.1.1.270

Alternative name(s):
17-beta-hydroxysteroid dehydrogenase 7
Short name=17-beta-HSD 7
Estradiol 17-beta-dehydrogenase 7
EC=1.1.1.62

Gene names

Name:	HSD17B7
ORF Names:	UNQ2563/PRO6243

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	341 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Responsible for the reduction of the keto group on the C-3 of sterols. Ref.11
Catalytic activity	A 3-beta-hydroxysteroid + NADP+ = a 3-oxosteroid + NADPH. 17-beta-estradiol + NAD(P)+ = estrone + NAD(P)H.
Pathway	Steroid biosynthesis; estrogen biosynthesis. Steroid biosynthesis; zymosterol biosynthesis; zymosterol from lanosterol: step 5/6.
Subcellular location	Cell membrane; Single-pass membrane protein.
Tissue specificity	Highly expressed in adrenal gland, liver, lung and thymus. Expressed in breast, ovaries, pituitary gland, pregnant uterus, prostate, kidney, lymph node, small intestine, spinal cord and trachea. Weakly expressed in all other tissues tested. Isoform 3 is expressed in eye ciliary epithelial cells and neuroendocrine cells.
Post-translational modification	Phosphorylated.
Sequence similarities	Belongs to the short-chain dehydrogenases/reductases (SDR) family. ERG27 subfamily.

Ontologies

Keywords
Biological process	Lipid biosynthesis Lipid metabolism Steroid biosynthesis
Cellular component	Cell membrane Membrane
Coding sequence diversity	Alternative splicing
Domain	Transmembrane Transmembrane helix
Ligand	NAD NADP
Molecular function	Oxidoreductase
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cholesterol biosynthetic process Traceable author statement. Source: Reactome estrogen biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	endoplasmic reticulum membrane Traceable author statement. Source: Reactome integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	3-keto sterol reductase activity Inferred from electronic annotation. Source: EC estradiol 17-beta-dehydrogenase activity Traceable author statement Ref.1. Source: ProtInc nucleotide binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P56937-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P56937-2)

The sequence of this isoform differs from the canonical sequence as follows:
     112-119: Missing.

Isoform 3 (identifier: P56937-3)

The sequence of this isoform differs from the canonical sequence as follows:
     215-249: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 341	341	3-keto-steroid reductase		PRO_0000054586
Regions
	Topological domain	1 – 229	229	Extracellular Potential
	Transmembrane	230 – 250	21	Helical; Potential
	Topological domain	251 – 341	91	Cytoplasmic Potential
	Nucleotide binding	8 – 15	8	NAD Potential
Sites
	Active site	193	1	Proton acceptor By similarity
	Binding site	171	1	Substrate By similarity
Amino acid modifications
	Glycosylation	37	1	N-linked (GlcNAc...) Potential
	Glycosylation	178	1	N-linked (GlcNAc...) Potential
	Glycosylation	229	1	N-linked (GlcNAc...) Potential
Natural variations
	Alternative sequence	112 – 119	8	Missing in isoform 2.		VSP_006029
	Alternative sequence	215 – 249	35	Missing in isoform 3.		VSP_012766
Experimental info
	Sequence conflict	52 – 53	2	HP → PT in AAF14537. Ref.1
	Sequence conflict	61	1	Q → P in AAF14537. Ref.1
	Sequence conflict	86	1	C → R in CAC88111. Ref.3
	Sequence conflict	105	1	F → L in CAC88111. Ref.3
	Sequence conflict	135	1	L → F in AAP97275. Ref.4
	Sequence conflict	273 – 276	4	HQKP → PPKA in AAP97275. Ref.4
	Sequence conflict	288 – 295	8	ATTGFGRN → GTTALEEI in AAP97275. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 30, 2000. Version 1. Checksum: FE4892B2602F549B	FASTA	341	38,206
	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
	Isoform 2 [UniParc]. Checksum: 187F2F8818D93869	FASTA	333	37,262
	10 20 30 40 50 60 MRKVVLITGA SSGIGLALCK RLLAEDDELH LCLACRNMSK AEAVCAALLA SHPTAEVTIV 70 80 90 100 110 120 QVDVSNLQSV FRASKELKQR FQRLDCIYLN AGIMPNPQLN IKALFFGLFS RAEGLLTQGD 130 140 150 160 170 180 KITADGLQEV FETNVFGHFI LIRELEPLLC HSDNPSQLIW TSSRSARKSN FSLEDFQHSK 190 200 210 220 230 240 GKEPYSSSKY ATDLLSVALN RNFNQQGLYS NVACPGTALT NLTYGILPPF IWTLLMPAIL 250 260 270 280 290 300 LLRFFANAFT LTPYNGTEAL VWLFHQKPES LNPLIKYLSA TTGFGRNYIM TQKMDLDEDT 310 320 330 AEKFYQKLLE LEKHIRVTIQ KTDNQARLSG SCL
	Isoform 3 [UniParc]. Checksum: 61F696BEDA3B9EAE	FASTA	306	34,476
	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 FNQQLRFFAN AFTLTPYNGT EALVWLFHQK 250 260 270 280 290 300 PESLNPLIKY LSATTGFGRN YIMTQKMDLD EDTAEKFYQK LLELEKHIRV TIQKTDNQAR LSGSCL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Determination of cDNA, gene structure and chromosomal localization of the novel human 17beta-hydroxysteroid dehydrogenase type 7." Krazeisen A., Breitling R., Imai K., Fritz S., Moeller G., Adamski J. FEBS Lett. 460:373-379(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2).
[2]	Krazeisen A., Breitling R., Imai K., Fritz S., Moeller G., Adamski J. Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION.
[3]	"Production, purification, and functional analysis of recombinant human and mouse 17beta-hydroxysteroid dehydrogenase type 7." Toern S., Nokelainen P., Kurkela R., Pulkka A., Menjivar M., Ghosh S., Coca-Prados M., Peltoketo H., Isomaa V., Vihko P. Biochem. Biophys. Res. Commun. 305:37-45(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 3). Tissue: Placenta.
[4]	"Cloning of a new human cDNA homologous to Rattus norvegicus ovarian-specific protein." Zhou Y., Yu L., Zhao S.Y. Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[5]	"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment." 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. Genome Res. 13:2265-2270(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[6]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[7]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." 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. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[8]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[10]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Skin and Urinary bladder.
[11]	"Closing the gap: identification of human 3-ketosteroid reductase, the last unknown enzyme of mammalian cholesterol biosynthesis." Marijanovic Z., Laubner D., Moeller G., Gege C., Husen B., Adamski J., Breitling R. Mol. Endocrinol. 17:1715-1725(2003) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION, FUNCTION.
[12]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF098786 mRNA. Translation: AAF09266.2. AF162767 , AF162759, AF162760, AF162761, AF162762, AF162763, AF162764, AF162765, AF162766 Genomic DNA. Translation: AAF14537.1. AJ249179 mRNA. Translation: CAC20418.1. AJ250550 , AJ250551, AJ250552, AJ250553, AJ250554, AJ250555, AJ250556, AJ250557, AJ250558 Genomic DNA. Translation: CAC88111.1. AF145023 mRNA. Translation: AAP97275.1. AY358962 mRNA. Translation: AAQ89321.1. AK290741 mRNA. Translation: BAF83430.1. BT007075 mRNA. Translation: AAP35738.1. AL392003, AL445197 Genomic DNA. Translation: CAI13457.1. AL445197, AL392003 Genomic DNA. Translation: CAI15947.1. CH471067 Genomic DNA. Translation: EAW90716.1. BC007068 mRNA. Translation: AAH07068.1. BC065246 mRNA. Translation: AAH65246.1.
IPI	IPI00011970. IPI00220886. IPI00807691.
RefSeq	NP_057455.1. NM_016371.2.
UniGene	Hs.492925.
3D structure databases
ProteinModelPortal	P56937.
ModBase	Search...
Protein-protein interaction databases
IntAct	P56937. 5 interactions.
STRING	9606.ENSP00000254521.
PTM databases
PhosphoSite	P56937.
Polymorphism databases
DMDM	8134404.
Proteomic databases
PaxDb	P56937.
PRIDE	P56937.
Protocols and materials databases
DNASU	51478.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000254521; ENSP00000254521; ENSG00000132196. ENST00000367917; ENSP00000356894; ENSG00000132196.
GeneID	51478.
KEGG	hsa:51478.
UCSC	uc001gci.3. human.
Organism-specific databases
CTD	51478.
GeneCards	GC01P162760.
HGNC	HGNC:5215. HSD17B7.
HPA	HPA047496.
MIM	606756. gene.
neXtProt	NX_P56937.
PharmGKB	PA29483.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG1028.
HOGENOM	HOG000253921.
HOVERGEN	HBG058236.
InParanoid	P56937.
KO	K13373.
OMA	CHSDNPS.
PhylomeDB	P56937.
Enzyme and pathway databases
BioCyc	MetaCyc:HS05604-MONOMER.
Reactome	REACT_111217. Metabolism.
SABIO-RK	P56937.
UniPathway	UPA00769. UPA00770; UER00758.
Gene expression databases
ArrayExpress	P56937.
Bgee	P56937.
CleanEx	HS_HSD17B7.
Genevestigator	P56937.
GermOnline	ENSG00000132196. Homo sapiens.
Family and domain databases
Gene3D	3.40.50.720. 1 hit.
InterPro	IPR002198. DH_sc/Rdtase_SDR. IPR002347. Glc/ribitol_DH. IPR016040. NAD(P)-bd_dom. [Graphical view]
Pfam	PF00106. adh_short. 1 hit. [Graphical view]
PRINTS	PR00081. GDHRDH.
PROSITE	PS00061. ADH_SHORT. False negative. [Graphical view]
ProtoNet	Search...
Other
BindingDB	P56937.
ChEMBL	CHEMBL5999.
DrugBank	DB00157. NADH.
GenomeRNAi	51478.
NextBio	55124.
SOURCE	Search...

Entry information

Entry name

DHB7_HUMAN

Accession

Primary (citable) accession number: P56937
Secondary accession number(s): Q5T246 , Q7Z4V9, Q8WWS2, Q9UF00

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	May 30, 2000
Last modified:	May 1, 2013
This is version 133 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.