PIGU_RAT
ID PIGU_RAT Reviewed; 435 AA.
AC Q8CHJ1;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 109.
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;
DE AltName: Full=Liver regeneration-related protein LRRGT00059;
GN Name=Pigu; Synonyms=Cdc91l1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND SUBUNIT.
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RA Xu C.S., Chang C.F., Han H.P., Wang G.P., Chai L.Q., Yuan J.Y., Yang K.J.,
RA Zhao L.F., Ma H., Wang L., Wang S.F., Xing X.K., Shen G.M., Shi J.B.,
RA Rahman S., Wang Q.N., Zhang J.B.;
RT "Liver regeneration after PH.";
RL Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8CHJ1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8CHJ1-2; Sequence=VSP_009544, VSP_009545;
CC -!- SIMILARITY: Belongs to the PIGU family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAQ96272.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB086841; BAC53625.1; -; mRNA.
DR EMBL; AY383714; AAQ96272.1; ALT_INIT; mRNA.
DR RefSeq; NP_853668.1; NM_181637.1. [Q8CHJ1-1]
DR AlphaFoldDB; Q8CHJ1; -.
DR STRING; 10116.ENSRNOP00000032963; -.
DR jPOST; Q8CHJ1; -.
DR PaxDb; Q8CHJ1; -.
DR Ensembl; ENSRNOT00000034708; ENSRNOP00000032963; ENSRNOG00000025181. [Q8CHJ1-1]
DR Ensembl; ENSRNOT00000038809; ENSRNOP00000036137; ENSRNOG00000025181. [Q8CHJ1-2]
DR GeneID; 353304; -.
DR KEGG; rno:353304; -.
DR UCSC; RGD:727825; rat. [Q8CHJ1-1]
DR CTD; 128869; -.
DR RGD; 727825; Pigu.
DR eggNOG; KOG2552; Eukaryota.
DR GeneTree; ENSGT00390000014941; -.
DR HOGENOM; CLU_1708432_0_0_1; -.
DR InParanoid; Q8CHJ1; -.
DR OrthoDB; 1339553at2759; -.
DR PhylomeDB; Q8CHJ1; -.
DR Reactome; R-RNO-162791; Attachment of GPI anchor to uPAR.
DR UniPathway; UPA00196; -.
DR PRO; PR:Q8CHJ1; -.
DR Proteomes; UP000002494; Chromosome 3.
DR GO; GO:0042765; C:GPI-anchor transamidase complex; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0034235; F:GPI anchor binding; IEA:Ensembl.
DR GO; GO:0016255; P:attachment of GPI anchor to protein; ISO:RGD.
DR GO; GO:0006506; P:GPI anchor biosynthetic process; ISO:RGD.
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:RGD.
DR InterPro; IPR009600; PIG-U.
DR PANTHER; PTHR13121; PTHR13121; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Endoplasmic reticulum; GPI-anchor biosynthesis;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..435
FT /note="Phosphatidylinositol glycan anchor biosynthesis
FT class U protein"
FT /id="PRO_0000121396"
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 VAR_SEQ 44..107
FT /note="VVEGLALLDLGVSPYSGAVFHETPLIIYLFHFLIDYAELVFMITDALTAIAL
FT YFAIQDFNKVVF -> ALRGNSSPSAKDIKKILDSMGIKVGGDQLNKVVTPAAASAPTA
FT TEEKKEESEVLDDNMGFGLFD (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_009544"
FT VAR_SEQ 108..435
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_009545"
SQ SEQUENCE 435 AA; 49953 MW; 2A48ADFF2A758E61 CRC64;
MAAPLALVLV VAVTVRAALF RSSLAEFISE RVEVVSPLSS WKRVVEGLAL LDLGVSPYSG
AVFHETPLII YLFHFLIDYA ELVFMITDAL TAIALYFAIQ DFNKVVFKKQ KLLLELDQYA
PDVAELIRTP MEMRYIPLKV ALFYLLNPYT ILSCVAKSTC AINNTLIAFF ILTTIKGSVF
LSAIFLALAT YQSLYPITLF APGLLYLLQR QYIPVKVKSK AFWIFSWEYA MMYTGSLVVI
VCLSFFLLSS WDFIPAVYGF ILSVPDLTPN IGLFWYFFAE MFEHFSLFFV CVFQINVFFY
TVPLAIKLKE HPIFFMFIQI AIISIFKSYP TVGDVALYMA FFPVWSHLYR FLRNIFVLTC
IIIVCSLLFP VLWHLWIYAG SANSNFFYAI TLTFNVGQIL LISDYFYAFL RREYYLTHGL
YLTAKDGTEA MLVLK
