Reviewed, UniProtKB/Swiss-Prot P56937 (DHB7_HUMAN)

Names and origin

Protein names

Recommended name:
    3-keto-steroid reductase
    EC=1.1.1.270
Alternative name(s):
    Estradiol 17-beta-dehydrogenase 7
    EC=1.1.1.62
    17-beta-hydroxysteroid dehydrogenase 7
      Short name=17-beta-HSD 7

Gene names

Name:	HSD17B7
ORF Names:	UNQ2563/PRO6243

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	341 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Responsible for the reduction of the keto group on the C-3 of sterols.
Catalytic activity	4-alpha-methyl-5-alpha-cholest-7-en-3-beta-ol + NADP(+) = 4-alpha-methyl-5-alpha-cholest-7-en-3-one + NADPH. Estradiol-17-beta + NAD(P)(+) = estrone + NAD(P)H.
Pathway	Steroid biosynthesis; estrogen biosynthesis. Steroid biosynthesis; zymosterol biosynthesis; zymosterol from lanosterol: step 5/6.
Subcellular location	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 synthesis Steroid biosynthesis
Cellular component	Membrane
Coding sequence diversity	Alternative splicing
Domain	Transmembrane
Ligand	NAD NADP
Molecular function	Oxidoreductase
PTM	Glycoprotein
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW steroid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	endoplasmic reticulum membrane Inferred from Experiment. Source: Reactome integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	3-keto-steroid reductase activity Inferred from electronic annotation. Source: EC binding Inferred from electronic annotation. Source: InterPro estradiol 17-beta-dehydrogenase activity Ref.1 Traceable author statement. Source: ProtInc
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	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		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		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: 10544267] [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: 12732193] [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: 12975309] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[6]	"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).
[7]	"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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[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: 16710414] [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: 15489334] [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: 12829805] [Abstract] Cited for: CHARACTERIZATION, FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	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. BT007075 mRNA. Translation: AAP35738.1. AK290741 mRNA. Translation: BAF83430.1. 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.
RefSeq	NP_057455.1.
UniGene	Hs.492925
3D structure databases
ModBase	Search...
PTM databases
PhosphoSite	P56937.
Genome annotation databases
Ensembl	ENSG00000132196. Homo sapiens. [Contig view]
GeneID	51478.
KEGG	hsa:51478.
Organism-specific databases
H-InvDB	HIX0001267. HIX0019166.
HGNC	HGNC:5215. HSD17B7.
MIM	606756. gene.
PharmGKB	PA29483.
GenAtlas	Search...
GeneCards	Search...
Phylogenomic databases
HOGENOM	P56937.
HOVERGEN	P56937.
Enzyme and pathway databases
Reactome	REACT_602. Lipid and lipoprotein