GPI8_MOUSE
ID GPI8_MOUSE Reviewed; 395 AA.
AC Q9CXY9; Q8BH63;
DT 11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=GPI-anchor transamidase;
DE Short=GPI transamidase;
DE EC=3.-.-.-;
DE AltName: Full=Phosphatidylinositol-glycan biosynthesis class K protein;
DE Short=PIG-K;
DE Flags: Precursor;
GN Name=Pigk;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryonic head, and Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Mediates GPI anchoring in the endoplasmic reticulum, by
CC replacing a protein's C-terminal GPI attachment signal peptide with a
CC pre-assembled GPI. During this transamidation reaction, the GPI
CC transamidase forms a carbonyl intermediate with the substrate protein
CC (By similarity). {ECO:0000250}.
CC -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor
CC biosynthesis.
CC -!- SUBUNIT: Forms a complex with PIGT, PIGS, PIGU and GAA1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Single-pass type I membrane protein {ECO:0000250}.
CC -!- PTM: The disulfide bond between PIGK/GPI8 and PIGT is important for
CC normal enzyme activity. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase C13 family. {ECO:0000305}.
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DR EMBL; AK013853; BAB29018.1; -; mRNA.
DR EMBL; AK077893; BAC37051.1; -; mRNA.
DR EMBL; AK082806; BAC38629.1; -; mRNA.
DR EMBL; BC060175; AAH60175.1; -; mRNA.
DR CCDS; CCDS17919.1; -.
DR RefSeq; NP_079938.1; NM_025662.5.
DR RefSeq; NP_821135.1; NM_178016.3.
DR AlphaFoldDB; Q9CXY9; -.
DR SMR; Q9CXY9; -.
DR BioGRID; 236834; 5.
DR MEROPS; C13.005; -.
DR PhosphoSitePlus; Q9CXY9; -.
DR SwissPalm; Q9CXY9; -.
DR EPD; Q9CXY9; -.
DR jPOST; Q9CXY9; -.
DR MaxQB; Q9CXY9; -.
DR PeptideAtlas; Q9CXY9; -.
DR PRIDE; Q9CXY9; -.
DR ProteomicsDB; 267760; -.
DR Antibodypedia; 33483; 183 antibodies from 23 providers.
DR DNASU; 329777; -.
DR Ensembl; ENSMUST00000159899; ENSMUSP00000123772; ENSMUSG00000039047.
DR GeneID; 329777; -.
DR KEGG; mmu:329777; -.
DR UCSC; uc012czo.1; mouse.
DR CTD; 10026; -.
DR MGI; MGI:1913863; Pigk.
DR VEuPathDB; HostDB:ENSMUSG00000039047; -.
DR GeneTree; ENSGT00940000156273; -.
DR HOGENOM; CLU_044656_1_0_1; -.
DR InParanoid; Q9CXY9; -.
DR OrthoDB; 1259741at2759; -.
DR Reactome; R-MMU-162791; Attachment of GPI anchor to uPAR.
DR UniPathway; UPA00196; -.
DR BioGRID-ORCS; 329777; 12 hits in 74 CRISPR screens.
DR ChiTaRS; Pigk; mouse.
DR PRO; PR:Q9CXY9; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q9CXY9; protein.
DR Bgee; ENSMUSG00000039047; Expressed in spermatocyte and 258 other tissues.
DR ExpressionAtlas; Q9CXY9; baseline and differential.
DR Genevisible; Q9CXY9; MM.
DR GO; GO:0042765; C:GPI-anchor transamidase complex; ISS:UniProtKB.
DR GO; GO:0003923; F:GPI-anchor transamidase activity; ISS:UniProtKB.
DR GO; GO:0016255; P:attachment of GPI anchor to protein; IBA:GO_Central.
DR GO; GO:0034394; P:protein localization to cell surface; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR InterPro; IPR028361; GPI_transamidase.
DR InterPro; IPR001096; Peptidase_C13.
DR PANTHER; PTHR48067; PTHR48067; 1.
DR Pfam; PF01650; Peptidase_C13; 1.
DR PIRSF; PIRSF500138; GPI8; 1.
DR PIRSF; PIRSF019663; Legumain; 1.
DR PRINTS; PR00776; HEMOGLOBNASE.
PE 1: Evidence at protein level;
KW Disulfide bond; Endoplasmic reticulum; GPI-anchor biosynthesis; Hydrolase;
KW Membrane; Protease; Reference proteome; Signal; Thiol protease;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..27
FT /evidence="ECO:0000250"
FT CHAIN 28..395
FT /note="GPI-anchor transamidase"
FT /id="PRO_0000026530"
FT TOPO_DOM 28..367
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 368..388
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 389..395
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 311..321
FT /note="Essential for GPI attachment"
FT /evidence="ECO:0000250"
FT ACT_SITE 164
FT /evidence="ECO:0000250"
FT ACT_SITE 206
FT /evidence="ECO:0000250"
FT DISULFID 92
FT /note="Interchain (with C-186 in PIGT)"
FT /evidence="ECO:0000250"
FT CONFLICT 125..126
FT /note="EV -> RG (in Ref. 1; BAB29018)"
FT /evidence="ECO:0000305"
FT CONFLICT 138
FT /note="R -> E (in Ref. 1; BAB29018)"
FT /evidence="ECO:0000305"
FT CONFLICT 154
FT /note="R -> K (in Ref. 1; BAB29018)"
FT /evidence="ECO:0000305"
FT CONFLICT 257..258
FT /note="LE -> WK (in Ref. 1; BAB29018)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 395 AA; 44895 MW; 4765ADDF4D46E386 CRC64;
MAAPCFLTLR VATLAALALL SLGSSAAGHI EDQAEQFFRS GHTNNWAVLV CTSRFWFNYR
HVANTLSVYR SVKRLGIPDS HIVLMLADDM ACNARNPKPA TVFSHKNMEL NVYGDDVEVD
YRSYEVTVEN FLRVLTGRVP PSTPRSKRLL SDDRSNILIY MTGHGGNGFL KFQDSEEITN
IELADAFEQM WQKRRYNELL FIIDTCQGAS MYERFYSPNI MALASSQVGE DSLSHQPDPA
IGVHLMDRYT FYVLEFLEEI NPASQTNMND LFQVCPKSLC VSTPGHRTDL FQRDPKNVLI
TDFFGSVRKV EITTEKISLQ WDSQVVDSSS KEDGTAEERM GPLKYAEQLP VAQIIHQKPK
PRDWHPPGGF ILGLWALIIM VFFKTYGIKH MKFIF
