Q8VCC1 (PGDH_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
15-hydroxyprostaglandin dehydrogenase [NAD(+)]
Short name=15-PGDH
EC=1.1.1.141

Alternative name(s):
Prostaglandin dehydrogenase 1

Gene names

Name:	Hpgd
Synonyms:	Pgdh1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	269 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Prostaglandin inactivation. Contributes to the regulation of events that are under the control of prostaglandin levels. Catalyzes the NAD-dependent dehydrogenation of lipoxin A4 to form 15-oxo-lipoxin A4 By similarity. Ref.1
Catalytic activity	(5Z,13E,15S)-11-alpha,15-dihydroxy-9-oxoprost-5,13-dienoate + NAD+ = (5Z,13E)-11-alpha-hydroxy-9,15-dioxoprost-5,13-dienoate + NADH.
Subunit structure	Homodimer By similarity.
Subcellular location	Cytoplasm By similarity.
Tissue specificity	Expressed in lung, intestine, stomach and liver. Ref.1
Sequence similarities	Belongs to the short-chain dehydrogenases/reductases (SDR) family.
Sequence caution	The sequence AAB41825.1 differs from that shown. Reason: Frameshift at position 267.

Ontologies

Keywords
Biological process	Fatty acid metabolism Lipid metabolism Prostaglandin metabolism
Cellular component	Cytoplasm
Disease	Tumor suppressor
Ligand	NAD
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	ductus arteriosus closure Inferred from mutant phenotype PubMed 11821873. Source: UniProtKB female pregnancy Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of cell cycle Inferred from sequence or structural similarity. Source: UniProtKB ovulation Inferred from sequence or structural similarity. Source: UniProtKB parturition Inferred from sequence or structural similarity. Source: UniProtKB prostaglandin metabolic process Inferred from sequence or structural similarity. Source: UniProtKB thrombin receptor signaling pathway Inferred from sequence or structural similarity. Source: UniProtKB transforming growth factor beta receptor signaling pathway Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: Compara
Molecular_function	15-hydroxyprostaglandin dehydrogenase (NAD+) activity Inferred from sequence or structural similarity. Source: UniProtKB NAD+ binding Inferred from sequence or structural similarity. Source: UniProtKB prostaglandin E receptor activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 269	269	15-hydroxyprostaglandin dehydrogenase [NAD(+)]		PRO_0000253626
Regions
	Nucleotide binding	12 – 20	9	NAD By similarity
	Nucleotide binding	36 – 37	2	NAD By similarity
	Nucleotide binding	63 – 65	3	NAD By similarity
	Nucleotide binding	151 – 155	5	NAD By similarity
	Nucleotide binding	186 – 188	3	NAD By similarity
Sites
	Active site	151	1	Proton acceptor By similarity
	Binding site	91	1	NAD; via carbonyl oxygen By similarity
	Binding site	138	1	Substrate By similarity
	Binding site	148	1	Substrate By similarity
Experimental info
	Sequence conflict	113	1	S → G in AAB41825. Ref.1
	Sequence conflict	153	1	A → S in AAB41825. Ref.1
	Sequence conflict	205	1	E → G in AAB41825. Ref.1
	Sequence conflict	224	1	T → A in AAB41825. Ref.1
	Sequence conflict	231	1	N → D in AAB41825. Ref.1
	Sequence conflict	241	1	A → P in AAB41825. Ref.1
	Sequence conflict	246	1	T → S in AAB41825. Ref.1
	Sequence conflict	249	1	K → E in AAB41825. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q8VCC1 [UniParc]. Last modified March 1, 2002. Version 1. Checksum: 10E879A7E31A8E34	FASTA	269	29,181
	10 20 30 40 50 60 MHVNGKVALV TGAAQGIGKA FAEALLLHGA KVALVDWNLE AGVKCKAALD EQFEPQKTLF 70 80 90 100 110 120 VQCDVADQKQ LRDTFRKVVD HFGRLDILVN NAGVNNEKNW EQTLQINLVS VISGTYLGLD 130 140 150 160 170 180 YMSKQNGGEG GIIINMSSLA GLMPVAQQPV YCASKHGIIG FTRSAAMAAN LMKSGVRLNV 190 200 210 220 230 240 ICPGFVDTPI LESIEKEENM GQYIEYKDQI KAMMKFYGVL HPSTIANGLI NLIEDDALNG 250 260 AIMKITASKG IHFQDYDISP LLVKAPLTS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and expression of the cDNA for mouse NAD(+)-dependent 15-hydroxyprostaglandin dehydrogenase." Matsuo M., Ensor C.M., Tai H.H. Biochim. Biophys. Acta 1309:21-24(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY. Tissue: Lung.
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Placenta.
[3]	"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]. Strain: FVB/N. Tissue: Colon.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U44389 mRNA. Translation: AAB41825.1. Frameshift. AK146038 mRNA. Translation: BAE26850.1. BC021157 mRNA. Translation: AAH21157.1.
IPI	IPI00310903.
RefSeq	NP_032304.2. NM_008278.2.
UniGene	Mm.18832.
3D structure databases
ProteinModelPortal	Q8VCC1.
SMR	Q8VCC1. Positions 3-256.
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-1855369.
PTM databases
PhosphoSite	Q8VCC1.
Proteomic databases
PaxDb	Q8VCC1.
PRIDE	Q8VCC1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000034026; ENSMUSP00000034026; ENSMUSG00000031613.
GeneID	15446.
KEGG	mmu:15446.
UCSC	uc009lso.1. mouse.
Organism-specific databases
CTD	3248.
MGI	MGI:108085. Hpgd.
Phylogenomic databases
eggNOG	COG1028.
GeneTree	ENSGT00700000104319.
HOVERGEN	HBG107379.
InParanoid	Q8VCC1.
KO	K00069.
OMA	IEYTDHI.
OrthoDB	EOG4R23VH.
Gene expression databases
Bgee	Q8VCC1.
CleanEx	MM_HPGD.
Genevestigator	Q8VCC1.
GermOnline	ENSMUSG00000031613. Mus musculus.
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. IPR020904. Sc_DH/Rdtase_CS. [Graphical view]
Pfam	PF00106. adh_short. 1 hit. [Graphical view]
PRINTS	PR00081. GDHRDH. PR00080. SDRFAMILY.
PROSITE	PS00061. ADH_SHORT. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	HPGD. mouse.
NextBio	288244.
SOURCE	Search...

Entry information

Entry name

PGDH_MOUSE

Accession

Primary (citable) accession number: Q8VCC1
Secondary accession number(s): Q61106

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 17, 2006
Last sequence update:	March 1, 2002
Last modified:	May 29, 2013
This is version 92 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program