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Q8VCC1 (PGDH_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length269 AA.
Sequence statusComplete.
Protein existenceEvidence 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 processFatty acid metabolism
Lipid metabolism
Prostaglandin metabolism
   Cellular componentCytoplasm
   DiseaseTumor suppressor
   LigandNAD
   Molecular functionOxidoreductase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processductus 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_componentbasolateral plasma membrane

Inferred from direct assay PubMed 20448048. Source: MGI

cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from electronic annotation. Source: Ensembl

   Molecular_function15-hydroxyprostaglandin dehydrogenase (NAD+) activity

Inferred from sequence or structural similarity. Source: UniProtKB

NAD binding

Inferred from sequence or structural similarity. Source: UniProtKB

NAD+ binding

Inferred from sequence or structural similarity. Source: UniProtKB

catalytic activity

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 26926915-hydroxyprostaglandin dehydrogenase [NAD(+)]
PRO_0000253626

Regions

Nucleotide binding12 – 209NAD By similarity
Nucleotide binding36 – 372NAD By similarity
Nucleotide binding63 – 653NAD By similarity
Nucleotide binding151 – 1555NAD By similarity
Nucleotide binding186 – 1883NAD By similarity

Sites

Active site1511Proton acceptor By similarity
Binding site911NAD; via carbonyl oxygen By similarity
Binding site1381Substrate By similarity
Binding site1481Substrate By similarity

Experimental info

Sequence conflict1131S → G in AAB41825. Ref.1
Sequence conflict1531A → S in AAB41825. Ref.1
Sequence conflict2051E → G in AAB41825. Ref.1
Sequence conflict2241T → A in AAB41825. Ref.1
Sequence conflict2311N → D in AAB41825. Ref.1
Sequence conflict2411A → P in AAB41825. Ref.1
Sequence conflict2461T → S in AAB41825. Ref.1
Sequence conflict2491K → E in AAB41825. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q8VCC1 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: 10E879A7E31A8E34

FASTA26929,181
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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.
CCDSCCDS40341.1.
RefSeqNP_032304.2. NM_008278.2.
UniGeneMm.18832.

3D structure databases

ProteinModelPortalQ8VCC1.
SMRQ8VCC1. Positions 3-256.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ8VCC1. 1 interaction.
MINTMINT-1855369.

PTM databases

PhosphoSiteQ8VCC1.

Proteomic databases

MaxQBQ8VCC1.
PaxDbQ8VCC1.
PRIDEQ8VCC1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000034026; ENSMUSP00000034026; ENSMUSG00000031613.
GeneID15446.
KEGGmmu:15446.
UCSCuc009lso.1. mouse.

Organism-specific databases

CTD3248.
MGIMGI:108085. Hpgd.

Phylogenomic databases

eggNOGCOG1028.
GeneTreeENSGT00710000106273.
HOVERGENHBG107379.
InParanoidQ8VCC1.
KOK00069.
OMAIHFQNYD.
OrthoDBEOG7966HT.
PhylomeDBQ8VCC1.
TreeFamTF324093.

Gene expression databases

BgeeQ8VCC1.
CleanExMM_HPGD.
GenevestigatorQ8VCC1.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
InterProIPR002198. DH_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
[Graphical view]
PfamPF00106. adh_short. 1 hit.
[Graphical view]
PRINTSPR00081. GDHRDH.
PR00080. SDRFAMILY.
PROSITEPS00061. ADH_SHORT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSHPGD. mouse.
NextBio288244.
PROQ8VCC1.
SOURCESearch...

Entry information

Entry namePGDH_MOUSE
AccessionPrimary (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: July 9, 2014
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot