GPAA1_MOUSE
ID GPAA1_MOUSE Reviewed; 621 AA.
AC Q9WTK3; Q3TNU9; Q9R1U8;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Glycosylphosphatidylinositol anchor attachment 1 protein;
DE Short=GPI anchor attachment protein 1;
DE AltName: Full=GAA1 protein homolog;
DE Short=mGAA1;
GN Name=Gpaa1; Synonyms=Gaa1;
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 [GENOMIC DNA / MRNA].
RC STRAIN=129/SvJ, and C57BL/6J;
RX PubMed=10393431; DOI=10.1159/000015258;
RA Inoue N., Ohishi K., Endo Y., Fujita T., Takeda J., Kinoshita T.;
RT "Human and mouse GPAA1 (glycosylphosphatidylinositol anchor attachment 1)
RT genes: genomic structures, chromosome loci and the presence of a minor
RT class intron.";
RL Cytogenet. Cell Genet. 84:199-205(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Heart;
RX PubMed=10898732; DOI=10.1152/ajpcell.2000.279.1.c205;
RA Hiroi Y., Chen R., Sawa H., Hosoda T., Kudoh S., Kobayashi Y.,
RA Aburatani H., Nagashima K., Nagai R., Yazaki Y., Medof M.E., Komuro I.;
RT "Cloning of murine glycosyl phosphatidylinositol anchor attachment protein,
RT GPAA1.";
RL Am. J. Physiol. 279:C205-C212(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Eye;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary tumor;
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 [5]
RP FUNCTION, AND SUBUNIT.
RX PubMed=10793132; DOI=10.1091/mbc.11.5.1523;
RA Ohishi K., Inoue N., Maeda Y., Takeda J., Riezman H., Kinoshita T.;
RT "Gaa1p and gpi8p are components of a glycosylphosphatidylinositol (GPI)
RT transamidase that mediates attachment of GPI to proteins.";
RL Mol. Biol. Cell 11:1523-1533(2000).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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: Essential for GPI-anchoring of precursor proteins but not for
CC GPI synthesis. Acts before or during formation of the carbonyl
CC intermediate. {ECO:0000269|PubMed:10793132,
CC ECO:0000269|PubMed:10898732}.
CC -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor
CC biosynthesis.
CC -!- SUBUNIT: Forms a complex with PIGK/GPI8, PIGT, PIGU and PIGS.
CC {ECO:0000269|PubMed:10793132}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed in fetal and adult tissues.
CC Expressed at higher levels in fetal tissues than adult tissues. In
CC embryos abundant in the choroid plexus, skeletal muscle,.
CC {ECO:0000269|PubMed:10898732}.
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DR EMBL; AB002136; BAA82589.1; -; mRNA.
DR EMBL; AB002138; BAA82591.1; -; Genomic_DNA.
DR EMBL; AB006970; BAB03274.1; -; mRNA.
DR EMBL; AB006971; BAB03275.1; -; Genomic_DNA.
DR EMBL; AB017266; BAA82586.1; -; Genomic_DNA.
DR EMBL; AK077518; BAC36840.1; -; mRNA.
DR EMBL; AK164219; BAE37686.1; -; mRNA.
DR EMBL; AK164978; BAE37988.1; -; mRNA.
DR EMBL; BC006697; AAH06697.1; -; mRNA.
DR CCDS; CCDS37120.1; -.
DR RefSeq; NP_034461.1; NM_010331.2.
DR AlphaFoldDB; Q9WTK3; -.
DR SMR; Q9WTK3; -.
DR BioGRID; 200010; 2.
DR STRING; 10090.ENSMUSP00000023221; -.
DR GlyGen; Q9WTK3; 1 site.
DR PhosphoSitePlus; Q9WTK3; -.
DR EPD; Q9WTK3; -.
DR MaxQB; Q9WTK3; -.
DR PaxDb; Q9WTK3; -.
DR PeptideAtlas; Q9WTK3; -.
DR PRIDE; Q9WTK3; -.
DR ProteomicsDB; 271139; -.
DR Antibodypedia; 28266; 156 antibodies from 24 providers.
DR DNASU; 14731; -.
DR Ensembl; ENSMUST00000023221; ENSMUSP00000023221; ENSMUSG00000022561.
DR GeneID; 14731; -.
DR KEGG; mmu:14731; -.
DR UCSC; uc007wjq.1; mouse.
DR CTD; 8733; -.
DR MGI; MGI:1202392; Gpaa1.
DR VEuPathDB; HostDB:ENSMUSG00000022561; -.
DR eggNOG; KOG3566; Eukaryota.
DR GeneTree; ENSGT00390000013685; -.
DR HOGENOM; CLU_007442_2_1_1; -.
DR InParanoid; Q9WTK3; -.
DR OMA; MAIALWM; -.
DR OrthoDB; 1486030at2759; -.
DR PhylomeDB; Q9WTK3; -.
DR TreeFam; TF313030; -.
DR Reactome; R-MMU-162791; Attachment of GPI anchor to uPAR.
DR UniPathway; UPA00196; -.
DR BioGRID-ORCS; 14731; 19 hits in 76 CRISPR screens.
DR PRO; PR:Q9WTK3; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q9WTK3; protein.
DR Bgee; ENSMUSG00000022561; Expressed in right kidney and 212 other tissues.
DR ExpressionAtlas; Q9WTK3; baseline and differential.
DR Genevisible; Q9WTK3; MM.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0042765; C:GPI-anchor transamidase complex; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:MGI.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0034235; F:GPI anchor binding; ISO:MGI.
DR GO; GO:0003923; F:GPI-anchor transamidase activity; TAS:MGI.
DR GO; GO:0016255; P:attachment of GPI anchor to protein; IBA:GO_Central.
DR GO; GO:0006506; P:GPI anchor biosynthetic process; ISS:MGI.
DR GO; GO:0065003; P:protein-containing complex assembly; ISO:MGI.
DR InterPro; IPR007246; Gaa1.
DR PANTHER; PTHR13304; PTHR13304; 1.
DR Pfam; PF04114; Gaa1; 1.
DR PIRSF; PIRSF036762; GAA1; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Glycoprotein; GPI-anchor biosynthesis; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..621
FT /note="Glycosylphosphatidylinositol anchor attachment 1
FT protein"
FT /id="PRO_0000087555"
FT TOPO_DOM 1..23
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 24..44
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 45..367
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 368..388
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 389..426
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 427..447
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 448..457
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 458..478
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 479..499
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 500..520
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 521..542
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 543..563
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 564..598
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 599..619
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 620..621
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 203
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 621 AA; 67949 MW; 880F6E3856272C91 CRC64;
MGLLSDPVRR RALARIVLRL NTPLCVLSYV AGIAWFLALA FPPLTQRTYM SENAMGSTMV
EEQFVGGDRA RSFARDFAAH RKKPGALPVA WLERSMRSVG LEVYTQSFSR KLPFPDETHE
RYMVSGTNVY GILRAPRSAS TESLVLTVPC GPDATNSQAV GLLLALAAHF RGQIYWAKDI
IFLVTDHDLL GTEAWLEAYH DINVTGIQSS PLQGRAGAIQ AAVALELSSD VVTSLDVTVE
GLNGQLPNLD LLNLFQTFCQ KGGLLCTLQG KLQPQDWTSL EGPLQGLQTL LLMVLRQASG
RPHGPHGLFL RYGVEALTLR GINSFRQYKY DLATVGKALE GMFRKLNHLL ERLHQSFFFY
LLPALSRFVS IGLYMPATGF LLLVLGLKAL ELWMQLHQAG VNPEEAGKAP SPGTPLLPTQ
GVGLASLTAP LLISQAMGLA LYFLPVLGQH LATQHFPVAE AEAVVLTLLA IYVAGLALPH
NTHRVVNSQV PDRGWMALKL VALIYLALQL GCIALLNFSL GFLLAATMVP AAALAKPHGP
RTLYAALLVV TSPAVTLFGS LFLWRELLEV PLSLAEGWQL FLTALAQGVL EHYTYGALLF
PILALGLYPC WLLFWNVLFW K
