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   24-JAN-2024, entry version 144.
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: Component of the GPI transamidase complex, necessary for
CC       transfer of GPI to proteins (By similarity). Mediates GPI anchoring in
CC       the endoplasmic reticulum, by replacing a protein's C-terminal GPI
CC       attachment signal peptide with a pre-assembled GPI. During this
CC       transamidation reaction, the GPI transamidase forms a carbonyl
CC       intermediate with the substrate protein (By similarity).
CC       {ECO:0000250|UniProtKB:Q92643}.
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; 6.
DR   STRING; 10090.ENSMUSP00000045351; -.
DR   MEROPS; C13.005; -.
DR   GlyGen; Q9CXY9; 1 site, 1 O-linked glycan (1 site).
DR   PhosphoSitePlus; Q9CXY9; -.
DR   SwissPalm; Q9CXY9; -.
DR   EPD; Q9CXY9; -.
DR   jPOST; Q9CXY9; -.
DR   MaxQB; Q9CXY9; -.
DR   PeptideAtlas; Q9CXY9; -.
DR   ProteomicsDB; 267760; -.
DR   Pumba; Q9CXY9; -.
DR   Antibodypedia; 33483; 193 antibodies from 23 providers.
DR   DNASU; 329777; -.
DR   Ensembl; ENSMUST00000159899.8; ENSMUSP00000123772.2; ENSMUSG00000039047.18.
DR   GeneID; 329777; -.
DR   KEGG; mmu:329777; -.
DR   UCSC; uc012czo.1; mouse.
DR   AGR; MGI:1913863; -.
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; 1122658at2759; -.
DR   Reactome; R-MMU-162791; Attachment of GPI anchor to uPAR.
DR   UniPathway; UPA00196; -.
DR   BioGRID-ORCS; 329777; 13 hits in 79 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 262 other cell types or tissues.
DR   ExpressionAtlas; Q9CXY9; baseline and differential.
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:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1460; -; 1.
DR   InterPro; IPR028361; GPI_transamidase.
DR   InterPro; IPR001096; Peptidase_C13.
DR   PANTHER; PTHR48067; GPI-ANCHOR TRANSAMIDASE; 1.
DR   PANTHER; PTHR48067:SF1; GPI-ANCHOR TRANSAMIDASE; 1.
DR   Pfam; PF01650; Peptidase_C13; 1.
DR   PIRSF; PIRSF500138; GPI8; 1.
DR   PIRSF; PIRSF019663; Legumain; 1.
DR   PRINTS; PR00776; HEMOGLOBNASE.
DR   Genevisible; Q9CXY9; MM.
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
//