PIGU_CRIGR
ID PIGU_CRIGR Reviewed; 435 AA.
AC Q8CHJ0;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 68.
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 Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, AND MUTAGENESIS OF
RP 274-PHE-TRP-275.
RX PubMed=12802054; DOI=10.1091/mbc.e02-12-0794;
RA Hong Y., Ohishi K., Kang J.Y., Tanaka S., Inoue N., Nishimura J., Maeda Y.,
RA Kinoshita T.;
RT "Human PIG-U and yeast Cdc91p are the fifth subunit of GPI transamidase
RT that attaches GPI-anchors to proteins.";
RL Mol. Biol. Cell 14:1780-1789(2003).
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. {ECO:0000269|PubMed:12802054}.
CC -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor
CC biosynthesis.
CC -!- SUBUNIT: Forms a complex with PIGK/GPI8, PIGS, PIGT and GPAA1/GAA1.
CC {ECO:0000269|PubMed:12802054}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305};
CC Multi-pass membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the PIGU family. {ECO:0000305}.
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DR EMBL; AB086843; BAC53627.1; -; mRNA.
DR RefSeq; NP_001233736.1; NM_001246807.1.
DR AlphaFoldDB; Q8CHJ0; -.
DR STRING; 10029.NP_001233736.1; -.
DR Ensembl; ENSCGRT00001016898; ENSCGRP00001012663; ENSCGRG00001013977.
DR GeneID; 100689380; -.
DR KEGG; cge:100689380; -.
DR CTD; 128869; -.
DR eggNOG; KOG2552; Eukaryota.
DR GeneTree; ENSGT00390000014941; -.
DR OMA; ALWHLWI; -.
DR OrthoDB; 1339553at2759; -.
DR UniPathway; UPA00196; -.
DR GO; GO:0042765; C:GPI-anchor transamidase complex; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0034235; F:GPI anchor binding; IEA:Ensembl.
DR GO; GO:0016255; P:attachment of GPI anchor to protein; IEA:Ensembl.
DR GO; GO:0046425; P:regulation of receptor signaling pathway via JAK-STAT; IEA:Ensembl.
DR InterPro; IPR009600; PIG-U.
DR PANTHER; PTHR13121; PTHR13121; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; GPI-anchor biosynthesis; Membrane; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..435
FT /note="Phosphatidylinositol glycan anchor biosynthesis
FT class U protein"
FT /id="PRO_0000121393"
FT TRANSMEM 67..87
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 166..186
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 188..208
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 237..257
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 259..279
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 286..306
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 313..333
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 355..375
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 386..406
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 269..289
FT /note="May be involved in recognition of long-chain fatty
FT acids in GPI"
FT MUTAGEN 274..275
FT /note="FW->LL: Loss of function."
FT /evidence="ECO:0000269|PubMed:12802054"
SQ SEQUENCE 435 AA; 49980 MW; DFA76299E376A153 CRC64;
MAAPLALVLV VAVTVRAALF RSSLAEFISE RVEVVSPLSS WKRVVEGLSL LDLGVSPYSG
AVFHETPLII YLFHFLIDYA ELVFMITDAL TAIALYFAIQ DFNKVVFKKQ KLLLELDQYA
PDVAELIRTP MEMRYIPLKV ALFYLLNPYT ILSCVAKSTC AINNTLIAFF ILTTIKGSVF
LSAIFLALAT YQTLYPVTLF APGLLYLLQR QYIPVKVKSK AFWIFSWEYA MMYIGSLVVI
VCLSFFLLSS WDFIPAVYGF ILSVPDLTPN IGLFWYFFAE MFEHFSLFFV CVFQINVFFY
TVPLAIKLKE HPIFFMFIQI AIISIFKSYP TVGDVALYMA FFPVWNHLYR FLRNVFVLTC
IIVVCSLLFP VLWHLWIYAG SANSNFFYAI TLTFNVGQIL LISDYFYAFL RREYYLTHGL
YLTAKDGTEA MLVLK
