Reviewed, UniProtKB/Swiss-Prot Q14914 (PTGR1_HUMAN)

Names and origin

Protein names

Recommended name:
    Prostaglandin reductase 1
      Short name=PRG-1
    EC=1.3.1.-
Alternative name(s):
    NADP-dependent leukotriene B4 12-hydroxydehydrogenase
    EC=1.3.1.74
    15-oxoprostaglandin 13-reductase
    EC=1.3.1.48

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.
Sequence processing	The displayed sequence is not processed.
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.
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
Gene Ontology (GO)
Biological process	leukotriene metabolic process Ref.3 Non-traceable author statement. Source: UniProtKB oxidation reduction Inferred from electronic annotation. Source: InterPro
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 activity Inferred from electronic annotation. Source: EC alcohol dehydrogenase activity Non-traceable author statement. Source: UniProtKB 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

149 – 166

18

NADP Potential

Compositional bias

250 – 257

8

Pro-rich

Sites

Binding site

178

1

NADP By similarity

Binding site

193

1

NADP By similarity

Binding site

217

1

NADP By similarity

Binding site

245

1

NADP By similarity

Binding site

321

1

NADP By similarity

Natural variations

Natural variant

27

1

A → S: dbSNP rs1053959.

VAR_023111

Experimental info

Sequence conflict

311

1

A → R in BAA08382. Ref.3

Secondary structure

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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)
	Q14914-1 [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]	"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].
[2]	"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.
[3]	"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.
[4]	"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.

Cross-references

Sequence databases

EMBLGenBankDDBJ

AL135787 Genomic DNA. Translation: CAC22151.1.
BC035228 mRNA. Translation: AAH35228.1.
D49387 mRNA. Translation: BAA08382.1.

RefSeq

NP_036344.1.

UniGene

Hs.584864

3D structure databases

PDBMSD

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

ModBase

Search...

PTM databases

PhosphoSite

Q14914.

Genome annotation databases

Ensembl

ENSG00000106853. Homo sapiens. [Contig view]

GeneID

22949.

KEGG

hsa:22949.

Organism-specific databases

HGNC

HGNC:18429. PTGR1.

MIM

601274. gene.

PharmGKB

PA134971979.

GenAtlas

Search...

GeneCards

Search...

Phylogenomic databases

HOGENOM

Q14914.

HOVERGEN

Q14914.

Gene expression databases

ArrayExpress

Q14914.

CleanEx

HS_PTGR1.

GermOnline

ENSG00000106853. Homo sapiens.

Family and domain databases

InterPro

IPR002085. AlcDHase_SF_Zn.
IPR013149. AlcDHase_Zn-bd.
IPR014190. B4_12hDHase.
IPR016040. NAD(P)-bd.
[Graphical view]

Gene3D

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

PANTHER

PTHR11695. ADH_Sf_Zn. 1 hit.

Pfam

PF00107. ADH_zinc_N. 1 hit.
[Graphical view]

TIGRFAMs

TIGR02825. B4_12hDH. 1 hit.

ProtoNet

Search...

Other Resources

LinkHub

Q14914.

NextBio

43715.

SOURCE

Search...

Entry information

Entry name

PTGR1_HUMAN

Accession

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

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	September 19, 2002
Last modified:	November 25, 2008
This is version 79 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)