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Protein

GPI-anchor transamidase

Gene

Pigk

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

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).By similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei164 – 1641By similarity
Active sitei206 – 2061By similarity

GO - Molecular functioni

  1. cysteine-type endopeptidase activity Source: InterPro
  2. GPI-anchor transamidase activity Source: UniProtKB

GO - Biological processi

  1. attachment of GPI anchor to protein Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Keywords - Biological processi

GPI-anchor biosynthesis

Enzyme and pathway databases

ReactomeiREACT_236590. Attachment of GPI anchor to uPAR.
UniPathwayiUPA00196.

Protein family/group databases

MEROPSiC13.005.

Names & Taxonomyi

Protein namesi
Recommended name:
GPI-anchor transamidase (EC:3.-.-.-)
Short name:
GPI transamidase
Alternative name(s):
Phosphatidylinositol-glycan biosynthesis class K protein
Short name:
PIG-K
Gene namesi
Name:Pigk
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 3

Organism-specific databases

MGIiMGI:1913863. Pigk.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini28 – 367340LumenalSequence AnalysisAdd
BLAST
Transmembranei368 – 38821HelicalSequence AnalysisAdd
BLAST
Topological domaini389 – 3957CytoplasmicSequence Analysis

GO - Cellular componenti

  1. GPI-anchor transamidase complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2727By similarityAdd
BLAST
Chaini28 – 395368GPI-anchor transamidasePRO_0000026530Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi92 – 92Interchain (with C-186 in PIGT)By similarity

Post-translational modificationi

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

Keywords - PTMi

Disulfide bond

Proteomic databases

MaxQBiQ9CXY9.
PaxDbiQ9CXY9.
PRIDEiQ9CXY9.

PTM databases

PhosphoSiteiQ9CXY9.

Expressioni

Gene expression databases

BgeeiQ9CXY9.
ExpressionAtlasiQ9CXY9. baseline and differential.
GenevestigatoriQ9CXY9.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

IntActiQ9CXY9. 1 interaction.
STRINGi10090.ENSMUSP00000045351.

Structurei

3D structure databases

ProteinModelPortaliQ9CXY9.
SMRiQ9CXY9. Positions 45-255.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni311 – 32111Essential for GPI attachmentBy similarityAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase C13 family.Curated

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG5206.
GeneTreeiENSGT00530000063391.
HOGENOMiHOG000204398.
HOVERGENiHBG027488.
InParanoidiQ9CXY9.
KOiK05290.
OrthoDBiEOG70W3DZ.

Family and domain databases

InterProiIPR028361. GPI_transamidase.
IPR001096. Peptidase_C13.
[Graphical view]
PANTHERiPTHR12000. PTHR12000. 1 hit.
PfamiPF01650. Peptidase_C13. 1 hit.
[Graphical view]
PIRSFiPIRSF500138. GPI8. 1 hit.
PIRSF019663. Legumain. 1 hit.
PRINTSiPR00776. HEMOGLOBNASE.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9CXY9-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAAPCFLTLR VATLAALALL SLGSSAAGHI EDQAEQFFRS GHTNNWAVLV
60 70 80 90 100
CTSRFWFNYR HVANTLSVYR SVKRLGIPDS HIVLMLADDM ACNARNPKPA
110 120 130 140 150
TVFSHKNMEL NVYGDDVEVD YRSYEVTVEN FLRVLTGRVP PSTPRSKRLL
160 170 180 190 200
SDDRSNILIY MTGHGGNGFL KFQDSEEITN IELADAFEQM WQKRRYNELL
210 220 230 240 250
FIIDTCQGAS MYERFYSPNI MALASSQVGE DSLSHQPDPA IGVHLMDRYT
260 270 280 290 300
FYVLEFLEEI NPASQTNMND LFQVCPKSLC VSTPGHRTDL FQRDPKNVLI
310 320 330 340 350
TDFFGSVRKV EITTEKISLQ WDSQVVDSSS KEDGTAEERM GPLKYAEQLP
360 370 380 390
VAQIIHQKPK PRDWHPPGGF ILGLWALIIM VFFKTYGIKH MKFIF
Length:395
Mass (Da):44,895
Last modified:August 16, 2004 - v2
Checksum:i4765ADDF4D46E386
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti125 – 1262EV → RG in BAB29018. (PubMed:16141072)Curated
Sequence conflicti138 – 1381R → E in BAB29018. (PubMed:16141072)Curated
Sequence conflicti154 – 1541R → K in BAB29018. (PubMed:16141072)Curated
Sequence conflicti257 – 2582LE → WK in BAB29018. (PubMed:16141072)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK013853 mRNA. Translation: BAB29018.1.
AK077893 mRNA. Translation: BAC37051.1.
AK082806 mRNA. Translation: BAC38629.1.
BC060175 mRNA. Translation: AAH60175.1.
CCDSiCCDS17919.1.
RefSeqiNP_079938.1. NM_025662.5.
NP_821135.1. NM_178016.3.
UniGeneiMm.331447.

Genome annotation databases

EnsembliENSMUST00000159899; ENSMUSP00000123772; ENSMUSG00000039047.
GeneIDi329777.
KEGGimmu:329777.
UCSCiuc012czo.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK013853 mRNA. Translation: BAB29018.1.
AK077893 mRNA. Translation: BAC37051.1.
AK082806 mRNA. Translation: BAC38629.1.
BC060175 mRNA. Translation: AAH60175.1.
CCDSiCCDS17919.1.
RefSeqiNP_079938.1. NM_025662.5.
NP_821135.1. NM_178016.3.
UniGeneiMm.331447.

3D structure databases

ProteinModelPortaliQ9CXY9.
SMRiQ9CXY9. Positions 45-255.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9CXY9. 1 interaction.
STRINGi10090.ENSMUSP00000045351.

Protein family/group databases

MEROPSiC13.005.

PTM databases

PhosphoSiteiQ9CXY9.

Proteomic databases

MaxQBiQ9CXY9.
PaxDbiQ9CXY9.
PRIDEiQ9CXY9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000159899; ENSMUSP00000123772; ENSMUSG00000039047.
GeneIDi329777.
KEGGimmu:329777.
UCSCiuc012czo.1. mouse.

Organism-specific databases

CTDi10026.
MGIiMGI:1913863. Pigk.

Phylogenomic databases

eggNOGiCOG5206.
GeneTreeiENSGT00530000063391.
HOGENOMiHOG000204398.
HOVERGENiHBG027488.
InParanoidiQ9CXY9.
KOiK05290.
OrthoDBiEOG70W3DZ.

Enzyme and pathway databases

UniPathwayiUPA00196.
ReactomeiREACT_236590. Attachment of GPI anchor to uPAR.

Miscellaneous databases

NextBioi398962.
PROiQ9CXY9.
SOURCEiSearch...

Gene expression databases

BgeeiQ9CXY9.
ExpressionAtlasiQ9CXY9. baseline and differential.
GenevestigatoriQ9CXY9.

Family and domain databases

InterProiIPR028361. GPI_transamidase.
IPR001096. Peptidase_C13.
[Graphical view]
PANTHERiPTHR12000. PTHR12000. 1 hit.
PfamiPF01650. Peptidase_C13. 1 hit.
[Graphical view]
PIRSFiPIRSF500138. GPI8. 1 hit.
PIRSF019663. Legumain. 1 hit.
PRINTSiPR00776. HEMOGLOBNASE.
ProtoNetiSearch...

Publicationsi

  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.
    , 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.

Entry informationi

Entry nameiGPI8_MOUSE
AccessioniPrimary (citable) accession number: Q9CXY9
Secondary accession number(s): Q8BH63
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2002
Last sequence update: August 16, 2004
Last modified: January 7, 2015
This is version 98 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. Peptidase families
    Classification of peptidase families and list of entries
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.