Q14914 (PTGR1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Prostaglandin reductase 1
Short name=PRG-1
EC=1.3.1.-

Alternative name(s):
15-oxoprostaglandin 13-reductase
EC=1.3.1.48
NADP-dependent leukotriene B4 12-hydroxydehydrogenase
EC=1.3.1.74

Gene names

Name:	PTGR1
Synonyms:	LTB4DH

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	329 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Functions as 15-oxo-prostaglandin 13-reductase and acts on 15-oxo-PGE1, 15-oxo-PGE2 and 15-oxo-PGE2-alpha. Has no activity towards PGE1, PGE2 and PGE2-alpha By similarity. Catalyzes the conversion of leukotriene B4 into its biologically less active metabolite, 12-oxo-leukotriene B4. This is an initial and key step of metabolic inactivation of leukotriene B4.
Catalytic activity	n-alkanal + NAD(P)+ = alk-2-enal + NAD(P)H. 11-alpha-hydroxy-9,15-dioxoprost-5-enoate + NAD(P)+ = (5Z)-(13E)-11-alpha-hydroxy-9,15-dioxoprosta-5,13-dienoate + NAD(P)H.
Subunit structure	Monomer or homodimer By similarity.
Subcellular location	Cytoplasm.
Tissue specificity	High expression in the kidney, liver, and intestine but not in leukocytes. Ref.5
Sequence similarities	Belongs to the NADP-dependent oxidoreductase L4BD family.

Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Polymorphism
Ligand	NADP
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	leukotriene metabolic process Non-traceable author statement Ref.5. Source: UniProtKB
Cellular component	cytoplasm Non-traceable author statement. Source: UniProtKB
Molecular function	15-oxoprostaglandin 13-oxidase activity Inferred from electronic annotation. Source: EC 2-alkenal reductase [NAD(P)] activity Inferred from electronic annotation. Source: EC alcohol dehydrogenase (NAD) activity Non-traceable author statement. Source: UniProtKB nucleotide binding Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 329

329

Prostaglandin reductase 1

PRO_0000218065

Regions

Nucleotide binding

152 – 155

4

NADP

Nucleotide binding

239 – 245

7

NADP

Nucleotide binding

270 – 272

3

NADP

Compositional bias

250 – 257

8

Pro-rich

Sites

Binding site

178

1

NADP

Binding site

193

1

NADP

Binding site

217

1

NADP

Binding site

321

1

NADP

Natural variations

Natural variant

27

1

A → S. Ref.1 Ref.3 Ref.4
Corresponds to variant rs1053959 [ dbSNP | Ensembl ].

VAR_023111

Experimental info

Sequence conflict

311

1

A → R in BAA08382. Ref.5

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

329

Helix Strand Turn

Details...

Beta strand

4 – 11

8

Beta strand

14 – 16

3

Helix

19 – 21

3

Beta strand

22 – 28

7

Beta strand

37 – 45

9

Helix

49 – 53

5

Helix

54 – 56

3

Beta strand

67 – 75

9

Beta strand

84 – 87

4

Beta strand

91 – 97

7

Helix

115 – 119

5

Turn

120 – 122

3

Helix

124 – 135

12

Beta strand

144 – 149

6

Helix

155 – 163

9

Turn

164 – 166

3

Beta strand

168 – 175

8

Helix

176 – 184

9

Beta strand

188 – 192

5

Turn

193 – 195

3

Helix

199 – 206

8

Beta strand

211 – 218

8

Helix

220 – 227

8

Beta strand

230 – 238

9

Helix

242 – 244

3

Helix

257 – 262

6

Beta strand

266 – 269

4

Helix

272 – 274

3

Helix

277 – 292

16

Beta strand

300 – 304

5

Helix

306 – 308

3

Helix

309 – 317

9

Sequences

	Sequence		Length	Mass (Da)
	Q14914 [UniParc]. Last modified September 19, 2002. Version 2. Checksum: E121ADB7C5BD9CF8	FASTA	329	35,870
	10 20 30 40 50 60 MVRTKTWTLK KHFVGYPTNS DFELKTAELP PLKNGEVLLE ALFLTVDPYM RVAAKRLKEG 70 80 90 100 110 120 DTMMGQQVAK VVESKNVALP KGTIVLASPG WTTHSISDGK DLEKLLTEWP DTIPLSLALG 130 140 150 160 170 180 TVGMPGLTAY FGLLEICGVK GGETVMVNAA AGAVGSVVGQ IAKLKGCKVV GAVGSDEKVA 190 200 210 220 230 240 YLQKLGFDVV FNYKTVESLE ETLKKASPDG YDCYFDNVGG EFSNTVIGQM KKFGRIAICG 250 260 270 280 290 300 AISTYNRTGP LPPGPPPEIV IYQELRMEAF VVYRWQGDAR QKALKDLLKW VLEGKIQYKE 310 320 YIIEGFENMP AAFMGMLKGD NLGKTIVKA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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], VARIANT SER-27. Tissue: Brain cortex.
[2]	"DNA sequence and analysis of human chromosome 9." Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I. Nature 429:369-374(2004) [PubMed: 15164053] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	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], VARIANT SER-27.
[4]	"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], VARIANT SER-27. Tissue: Cervix.
[5]	"cDNA cloning, expression, and mutagenesis study of leukotriene B4 12-hydroxydehydrogenase." Yokomizo T., Ogawa Y., Uozumi N., Kume K., Izumi T., Shimizu T. J. Biol. Chem. 271:2844-2850(1996) [PubMed: 8576264] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-311, TISSUE SPECIFICITY. Tissue: Kidney.
[6]	"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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[7]	"Crystal structure of human NADP-dependent leukotriene B4 12-hydroxydehydrogenase." Structural genomics consortium (SGC) Submitted (MAY-2005) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 4-239.
[8]	"Crystal structure of human leukotriene B4 12-hydroxydehydrogenase in complex with NADP and raloxifene." Structural genomics consortium (SGC) Submitted (JAN-2011) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 4-329 IN COMPLEX WITH NADP AND RALOXIFENE.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AK289597 mRNA. Translation: BAF82286.1.
AL135787 Genomic DNA. Translation: CAC22151.1.
CH471105 Genomic DNA. Translation: EAW59074.1.
BC035228 mRNA. Translation: AAH35228.1.
D49387 mRNA. Translation: BAA08382.1.

IPI

IPI00292657.

RefSeq

NP_001139580.1. NM_001146108.1.
NP_001139581.1. NM_001146109.1.
NP_036344.2. NM_012212.3.

UniGene

Hs.584864.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1ZSV	X-ray	2.30	A/B/C/D	4-329	[»]
2Y05	X-ray	2.20	A/B/C/D	4-329	[»]

ProteinModelPortal

Q14914.

SMR

Q14914. Positions 4-329.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q14914. 1 interaction.

STRING

Q14914.

PTM databases

PhosphoSite

Q14914.

Polymorphism databases

DMDM

23503081.

Proteomic databases

PRIDE

Q14914.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000309195; ENSP00000311572; ENSG00000106853.
ENST00000407693; ENSP00000385763; ENSG00000106853.

GeneID

22949.

KEGG

hsa:22949.

UCSC

uc004bfh.1. human.

Organism-specific databases

CTD

22949.

GeneCards

GC09M114324.

H-InvDB

HIX0008283.

HGNC

HGNC:18429. PTGR1.

HPA

HPA036724.
HPA036725.

MIM

601274. gene.

neXtProt

NX_Q14914.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

HBG753318.

HOVERGEN

HBG055024.

InParanoid

Q14914.

OMA

FPTGTIV.

OrthoDB

EOG4N5VXH.

PhylomeDB

Q14914.

Gene expression databases

ArrayExpress

Q14914.

Bgee

Q14914.

CleanEx

HS_PTGR1.

Genevestigator

Q14914.

GermOnline

ENSG00000106853. Homo sapiens.

Family and domain databases

InterPro

IPR013149. ADH_C.
IPR002085. ADH_SF_Zn-type.
IPR014190. B4_12hDH.
IPR011032. GroES-like.
IPR016040. NAD(P)-bd_dom.
[Graphical view]

Gene3D

G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.

KO

K13948.

PANTHER

PTHR11695. ADH_Sf_Zn. 1 hit.

Pfam

PF00107. ADH_zinc_N. 1 hit.
[Graphical view]

SUPFAM

SSF50129. GroES_like. 2 hits.

TIGRFAMs

TIGR02825. B4_12hDH. 1 hit.

ProtoNet

Search...

Other

NextBio

43715.

SOURCE

Search...

Entry information

Entry name

PTGR1_HUMAN

Accession

Primary (citable) accession number: Q14914
Secondary accession number(s): A8K0N2, Q8IYQ0, Q9H1X6

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	September 19, 2002
Last modified:	January 25, 2012
This is version 116 of the entry and version 2 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.