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Reviewed, UniProtKB/Swiss-Prot Q9JHG1 (PIGP_MOUSE)

Last modified October 13, 2009. Version 57. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Phosphatidylinositol N-acetylglucosaminyltransferase subunit P
    EC=2.4.1.198
Alternative name(s):
    Phosphatidylinositol-glycan biosynthesis class P protein
      Short name=PIG-P
    Down syndrome critical region protein 5 homolog
Gene names
Name: Pigp
Synonyms: Dcrc, Dscr5
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

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Protein attributes

Sequence length132 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

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General annotation (Comments)

Function

Part of the complex catalyzing the transfer of N-acetylglucosamine from UDP-N-acetylglucosamine to phosphatidylinositol, the first step of GPI biosynthesis By similarity.

Catalytic activity

UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol = UDP + 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol.

Pathway

Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.

Subunit structure

Associates with PIGA, PIGC, PIGH, PIGQ and DPM2. The latter is not essential for activity By similarity.

Subcellular location

Membrane; Multi-pass membrane protein Potential.

Tissue specificity

Expressed in tongue. Ref.1

Sequence similarities

Belongs to the PIGP family.

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Ontologies

Keywords
   Biological processGPI-anchor biosynthesis
   Cellular componentMembrane
   DomainTransmembrane
   Molecular functionGlycosyltransferase
Transferase
Gene Ontology (GO)
   Biological processGPI anchor biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentintegral to membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionphosphatidylinositol N-acetylglucosaminyltransferase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 132132Phosphatidylinositol N-acetylglucosaminyltransferase subunit P
PRO_0000191784

Regions

Transmembrane16 – 3621 Potential
Transmembrane56 – 7621 Potential

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Sequences

Sequence LengthMass (Da)Tools
Q9JHG1-1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: D21472651F850F9D

FASTA13215,101
        10         20         30         40         50         60 
MVENSPSPLP ERAIYGFVLF LSSQFGFILY LVWAFVPESW LNSLGLTYWP QKYWAVALPV 

        70         80         90        100        110        120 
YLLITVVIGY VLLFGINMMS TSPLDSIHTI TDNYAKNQQR KNYQEDAIPA LRDVPISEVN 

       130 
KMFFLGAKEL NT

« Hide

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References

« Hide 'large scale' references
[1]"Molecular cloning and characterization of a gene expressed in mouse developing tongue, mDscr5 gene, a homolog of human DSCR5 (Down syndrome critical region gene 5)."
Choi D.K., Suzuki Y., Yoshimura S., Togashi T., Hida M., Taylor T.D., Wang Y., Sugano S., Hattori M., Sakaki Y.
Mamm. Genome 12:347-351(2001) [PubMed: 11331941] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
[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: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
[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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J and FVB/N.
Tissue: Brain, Salivary gland and Thymus.
+Additional computationally mapped references.

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Cross-references

Sequence databases

AF216306 mRNA. Translation: AAF32294.1.
AF216307 mRNA. Translation: AAF32295.1.
AF216308 mRNA. Translation: AAF32296.1.
AF216309 mRNA. Translation: AAF32297.1.
AK004169 mRNA. Translation: BAB23204.1.
BC038252 mRNA. Translation: AAH38252.1.
BC061116 mRNA. Translation: AAH61116.1.
BC096569 mRNA. Translation: AAH96569.1.
IPIIPI00119343.
RefSeqNP_001153088.1.
NP_001153089.1.
NP_001153090.1.
NP_001153091.1.
NP_062416.1.
UniGeneMm.474449

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ9JHG1.

Proteomic databases

PRIDEQ9JHG1.

Genome annotation databases

EnsemblENSMUST00000062865; ENSMUSP00000058031; ENSMUSG00000022940; Mus musculus. [Genome view]
ENSMUST00000113905; ENSMUSP00000109538; ENSMUSG00000022940; Mus musculus. [Genome view]
ENSMUST00000113906; ENSMUSP00000109539; ENSMUSG00000022940; Mus musculus. [Genome view]
ENSMUST00000113910; ENSMUSP00000109543; ENSMUSG00000022940; Mus musculus. [Genome view]
ENSMUST00000113914; ENSMUSP00000109547; ENSMUSG00000022940; Mus musculus. [Genome view]
GeneID56176.
KEGGmmu:56176.
UCSCuc008aan.1. mouse.

Organism-specific databases

CTD56176.
MGIMGI:1860433. Pigp.

Phylogenomic databases

HOGENOMQ9JHG1.
HOVERGENQ9JHG1.

Enzyme and pathway databases

BRENDA2.4.1.198. 244.

Gene expression databases

BgeeQ9JHG1.
GenevestigatorQ9JHG1.
GermOnlineENSMUSG00000022940. Mus musculus.

Family and domain databases

InterProIPR013717. PIG-P.
IPR016542. PIG-P_GPI19.
[Graphical view]
PfamPF08510. PIG-P. 1 hit.
[Graphical view]
PIRSFPIRSF008765. PIG-P_GPI19. 1 hit.
ProtoNetSearch...

Other Resources

NextBio311948.
SOURCESearch...

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Entry information

Entry namePIGP_MOUSE
AccessionPrimary (citable) accession number: Q9JHG1
Entry history
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: October 1, 2000
Last modified: October 13, 2009
This is version 57 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

MGD cross-references

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents