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Reviewed, UniProtKB/Swiss-Prot Q9CXR4 (PIGC_MOUSE)

Last modified January 19, 2010. Version 59. 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 · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Phosphatidylinositol N-acetylglucosaminyltransferase subunit C
    EC=2.4.1.198
Alternative name(s):
    Phosphatidylinositol-glycan biosynthesis class C protein
      Short name=PIG-C
Gene names
Name: Pigc
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 length297 AA.
Sequence statusComplete.
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, PIGH, PIGP, PIGQ and DPM2. The latter is not essential for activity By similarity.

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein Potential.

Sequence similarities

Belongs to the PIGC family.

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Ontologies

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

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentendoplasmic reticulum

Inferred from electronic annotation. Source: UniProtKB-KW

integral 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 – 297297Phosphatidylinositol N-acetylglucosaminyltransferase subunit C
PRO_0000058432

Regions

Transmembrane67 – 8721 Potential
Transmembrane88 – 10821 Potential
Transmembrane153 – 17321 Potential
Transmembrane239 – 25921 Potential

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Sequences

Sequence LengthMass (Da)Tools
Q9CXR4-1 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 3116EF0B412E58BC

FASTA29733,724
        10         20         30         40         50         60 
MCAQRVTDTP EVKWQKVLYE RQPFPDNYVD QRFLEELRKN IYARKYQYWA VVFESSVVIQ 

        70         80         90        100        110        120 
QLCSVCVFVV IWWYMDEGLL APQWLFGTGL ASSLVGYVLF DLIDGGDGRK KSGRTRWADL 

       130        140        150        160        170        180 
KSTLVFITFT YGFSPVLKTL TESVSTDTIY AMAVFMLLGH LIFFDYGANA AIVSSTLSLN 

       190        200        210        220        230        240 
MAIFASVCLA SRLPRSLHAF IMVTFAIQIF ALWPMLQKKL KAYTPRSYVG VTLLFAFSAF 

       250        260        270        280        290 
GGLLSISAVG AILFALLLFS ISCLCPYYLI HLQLFKENIH GPWDEAEIKE DLSRFLS

« Hide

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References

[1]"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.
Tissue: Bone marrow and Embryonic head.
[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].
Strain: 129.
Tissue: Mammary tumor.
+Additional computationally mapped references.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AK014096 mRNA. Translation: BAB29152.1.
AK152660 mRNA. Translation: BAE31396.1.
BC006938 mRNA. Translation: AAH06938.1.
IPIIPI00110669.
RefSeqNP_001034134.1.
NP_080354.1.
UniGeneMm.45106

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ9CXR4.

Proteomic databases

PRIDEQ9CXR4.

Genome annotation databases

EnsemblENSMUST00000028021; ENSMUSP00000028021; ENSMUSG00000026698; Mus musculus. [Genome view]
ENSMUST00000111594; ENSMUSP00000107221; ENSMUSG00000026698; Mus musculus. [Genome view]
GeneID67292.
KEGGmmu:67292.
UCSCuc007dfx.1. mouse.

Organism-specific databases

CTD67292.
MGIMGI:1914542. Pigc.

Phylogenomic databases

HOGENOMHBG714597.
HOVERGENQ9CXR4.
InParanoidQ9CXR4.
OMAIQQLCSV.
OrthoDBEOG93JFR1.
PhylomeDBQ9CXR4.

Enzyme and pathway databases

BRENDA2.4.1.198. 244.

Gene expression databases

ArrayExpressQ9CXR4.
BgeeQ9CXR4.
GenevestigatorQ9CXR4.
GermOnlineENSMUSG00000026698. Mus musculus.

Family and domain databases

InterProIPR009450. Plno_GlcNAc_GPI2.
[Graphical view]
PANTHERPTHR12982. GPI2. 1 hit.
PfamPF06432. GPI2. 1 hit.
[Graphical view]
PIRSFPIRSF016104. GPI2. 1 hit.
ProtoNetSearch...

Other Resources

NextBio324140.
SOURCESearch...

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Entry information

Entry namePIGC_MOUSE
AccessionPrimary (citable) accession number: Q9CXR4
Secondary accession number(s): Q3U7H3
Entry history
Integrated into UniProtKB/Swiss-Prot: April 12, 2005
Last sequence update: June 1, 2001
Last modified: January 19, 2010
This is version 59 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 · Cross-references · Entry information · Relevant documents