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Q9CXY9 (GPI8_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 22, 2014. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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:
GPI-anchor transamidase

Short name=GPI transamidase
EC=3.-.-.-
Alternative name(s):
Phosphatidylinositol-glycan biosynthesis class K protein
Short name=PIG-K
Gene names
Name:Pigk
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length395 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Mediates GPI anchoring in the endoplasmic reticulum, by replacing a protein's C-terminal GPI attachment signal peptide with a pre-assembled GPI. During this transamidation reaction, the GPI transamidase forms a carbonyl intermediate with the substrate protein By similarity.

Pathway

Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.

Subunit structure

Forms a complex with PIGT, PIGS, PIGU and GAA1 By similarity.

Subcellular location

Endoplasmic reticulum membrane; Single-pass type I membrane protein By similarity.

Post-translational modification

The disulfide bond between PIGK/GPI8 and PIGT is important for normal enzyme activity By similarity.

Sequence similarities

Belongs to the peptidase C13 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727 By similarity
Chain28 – 395368GPI-anchor transamidase
PRO_0000026530

Regions

Topological domain28 – 367340Lumenal Potential
Transmembrane368 – 38821Helical; Potential
Topological domain389 – 3957Cytoplasmic Potential
Region311 – 32111Essential for GPI attachment By similarity

Sites

Active site1641 By similarity
Active site2061 By similarity

Amino acid modifications

Disulfide bond92Interchain (with C-186 in PIGT) By similarity

Experimental info

Sequence conflict125 – 1262EV → RG in BAB29018. Ref.1
Sequence conflict1381R → E in BAB29018. Ref.1
Sequence conflict1541R → K in BAB29018. Ref.1
Sequence conflict257 – 2582LE → WK in BAB29018. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9CXY9 [UniParc].

Last modified August 16, 2004. Version 2.
Checksum: 4765ADDF4D46E386

FASTA39544,895
        10         20         30         40         50         60 
MAAPCFLTLR VATLAALALL SLGSSAAGHI EDQAEQFFRS GHTNNWAVLV CTSRFWFNYR 

        70         80         90        100        110        120 
HVANTLSVYR SVKRLGIPDS HIVLMLADDM ACNARNPKPA TVFSHKNMEL NVYGDDVEVD 

       130        140        150        160        170        180 
YRSYEVTVEN FLRVLTGRVP PSTPRSKRLL SDDRSNILIY MTGHGGNGFL KFQDSEEITN 

       190        200        210        220        230        240 
IELADAFEQM WQKRRYNELL FIIDTCQGAS MYERFYSPNI MALASSQVGE DSLSHQPDPA 

       250        260        270        280        290        300 
IGVHLMDRYT FYVLEFLEEI NPASQTNMND LFQVCPKSLC VSTPGHRTDL FQRDPKNVLI 

       310        320        330        340        350        360 
TDFFGSVRKV EITTEKISLQ WDSQVVDSSS KEDGTAEERM GPLKYAEQLP VAQIIHQKPK 

       370        380        390 
PRDWHPPGGF ILGLWALIIM VFFKTYGIKH MKFIF 

« Hide

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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Embryonic head and Testis.
[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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6.
Tissue: Brain.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK013853 mRNA. Translation: BAB29018.1.
AK077893 mRNA. Translation: BAC37051.1.
AK082806 mRNA. Translation: BAC38629.1.
BC060175 mRNA. Translation: AAH60175.1.
RefSeqNP_079938.1. NM_025662.5.
NP_821135.1. NM_178016.3.
UniGeneMm.331447.

3D structure databases

ProteinModelPortalQ9CXY9.
SMRQ9CXY9. Positions 43-308.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ9CXY9. 1 interaction.
STRING10090.ENSMUSP00000045351.

Protein family/group databases

MEROPSC13.005.

PTM databases

PhosphoSiteQ9CXY9.

Proteomic databases

PaxDbQ9CXY9.
PRIDEQ9CXY9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000159899; ENSMUSP00000123772; ENSMUSG00000039047.
GeneID329777.
KEGGmmu:329777.
UCSCuc012czo.1. mouse.

Organism-specific databases

CTD10026.
MGIMGI:1913863. Pigk.

Phylogenomic databases

eggNOGCOG5206.
GeneTreeENSGT00530000063391.
HOGENOMHOG000204398.
HOVERGENHBG027488.
KOK05290.
OrthoDBEOG70W3DZ.

Enzyme and pathway databases

UniPathwayUPA00196.

Gene expression databases

ArrayExpressQ9CXY9.
BgeeQ9CXY9.
GenevestigatorQ9CXY9.

Family and domain databases

InterProIPR028361. GPI_transamidase.
IPR001096. Peptidase_C13.
[Graphical view]
PANTHERPTHR12000. PTHR12000. 1 hit.
PfamPF01650. Peptidase_C13. 1 hit.
[Graphical view]
PIRSFPIRSF500138. GPI8. 1 hit.
PIRSF019663. Legumain. 1 hit.
PRINTSPR00776. HEMOGLOBNASE.
ProtoNetSearch...

Other

NextBio398962.
PROQ9CXY9.
SOURCESearch...

Entry information

Entry nameGPI8_MOUSE
AccessionPrimary (citable) accession number: Q9CXY9
Secondary accession number(s): Q8BH63
Entry history
Integrated into UniProtKB/Swiss-Prot: July 11, 2002
Last sequence update: August 16, 2004
Last modified: January 22, 2014
This is version 92 of the entry and version 2 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

Peptidase families

Classification of peptidase families and list of entries

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

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