PIGU_MOUSE
ID PIGU_MOUSE Reviewed; 434 AA.
AC Q8K358; Q921E1;
DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Phosphatidylinositol glycan anchor biosynthesis class U protein;
DE AltName: Full=Cell division cycle protein 91-like 1;
DE Short=Protein CDC91-like 1;
DE AltName: Full=GPI transamidase component PIG-U;
GN Name=Pigu; Synonyms=Cdc91l1;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 285-434.
RC TISSUE=Mammary cancer;
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=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. May be involved in
CC the recognition of either the GPI attachment signal or the lipid
CC portion of GPI (By similarity). {ECO:0000250}.
CC -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor
CC biosynthesis.
CC -!- SUBUNIT: Forms a complex with PIGK/GPI8, PIGS, PIGT and GPAA1/GAA1.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305};
CC Multi-pass membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the PIGU family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH28278.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AL845325; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL929588; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC028278; AAH28278.1; ALT_INIT; mRNA.
DR AlphaFoldDB; Q8K358; -.
DR SMR; Q8K358; -.
DR STRING; 10090.ENSMUSP00000076816; -.
DR iPTMnet; Q8K358; -.
DR PhosphoSitePlus; Q8K358; -.
DR EPD; Q8K358; -.
DR MaxQB; Q8K358; -.
DR PaxDb; Q8K358; -.
DR PRIDE; Q8K358; -.
DR ProteomicsDB; 288159; -.
DR Antibodypedia; 60375; 32 antibodies from 11 providers.
DR Ensembl; ENSMUST00000165234; ENSMUSP00000126236; ENSMUSG00000038383.
DR MGI; MGI:3039607; Pigu.
DR VEuPathDB; HostDB:ENSMUSG00000038383; -.
DR eggNOG; KOG2552; Eukaryota.
DR GeneTree; ENSGT00390000014941; -.
DR InParanoid; Q8K358; -.
DR Reactome; R-MMU-162791; Attachment of GPI anchor to uPAR.
DR UniPathway; UPA00196; -.
DR ChiTaRS; Pigu; mouse.
DR PRO; PR:Q8K358; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q8K358; protein.
DR Bgee; ENSMUSG00000038383; Expressed in external carotid artery and 256 other tissues.
DR ExpressionAtlas; Q8K358; baseline and differential.
DR Genevisible; Q8K358; MM.
DR GO; GO:0042765; C:GPI-anchor transamidase complex; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0034235; F:GPI anchor binding; ISO:MGI.
DR GO; GO:0016255; P:attachment of GPI anchor to protein; ISO:MGI.
DR GO; GO:0006506; P:GPI anchor biosynthetic process; ISO:MGI.
DR GO; GO:0034394; P:protein localization to cell surface; IBA:GO_Central.
DR GO; GO:0046425; P:regulation of receptor signaling pathway via JAK-STAT; ISO:MGI.
DR InterPro; IPR009600; PIG-U.
DR PANTHER; PTHR13121; PTHR13121; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; GPI-anchor biosynthesis; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..434
FT /note="Phosphatidylinositol glycan anchor biosynthesis
FT class U protein"
FT /id="PRO_0000121395"
FT TRANSMEM 66..86
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 165..185
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 187..207
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 236..256
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 258..278
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 285..305
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 312..332
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 354..374
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 385..405
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 268..288
FT /note="May be involved in recognition of long-chain fatty
FT acids in GPI"
FT /evidence="ECO:0000250"
SQ SEQUENCE 434 AA; 49804 MW; 901451A5A73C5515 CRC64;
MAAPLALVLV VAVTVRAALF RSSLAEFISE RVEVVSPLSS WKRVVEGLAL LDLGVSPYSG
AVFHETPLII YLFHFLIDYA ELVFMITDAL TAIALYFAIQ DFNKVVFKKQ KLLLELDQYA
PDVAELIRTP MEMRYIPLKV ALYLLNPYTI LSCVAKSTCA INNTLIAFFI LTTIKGSVFL
SAVFLALATY QSLYPVTLFA PGLLYLLQRQ YIPVKVKSKA FWIFSWEYAM MYTGSLVVIV
CLSFFLLSSW DFIPAVYGFI LSVPDLTPNI GLFWYFFAEM FEHFSLFFVC VFQINVFFYT
VPLAIKLKEH PIFFMFIQIA IISIFKSYPT VGDVALYMAF FPVWNHLYRF LRNIFVLTCI
IIVCSLLFPV LWHLWIYAGS ANSNFFYAIT LTFNVGQILL ISDYFYAFLR REYYLTHGLY
LTAKDGTEAM LVLK
