ID   PIGX_RAT                Reviewed;         252 AA.
AC   Q60GF7;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 2.
DT   25-MAY-2022, entry version 82.
DE   RecName: Full=Phosphatidylinositol-glycan biosynthesis class X protein;
DE            Short=PIG-X;
DE   Flags: Precursor;
GN   Name=Pigx;
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], PROTEIN SEQUENCE OF 23-27, FUNCTION,
RP   SUBCELLULAR LOCATION, TOPOLOGY, GLYCOSYLATION, AND INITIATION CODON CTG.
RX   PubMed=15635094; DOI=10.1091/mbc.e04-09-0802;
RA   Ashida H., Hong Y., Murakami Y., Shishioh N., Sugimoto N., Kim Y.U.,
RA   Maeda Y., Kinoshita T.;
RT   "Mammalian PIG-X and yeast Pbn1p are the essential components of
RT   glycosylphosphatidylinositol-mannosyltransferase I.";
RL   Mol. Biol. Cell 16:1439-1448(2005).
CC   -!- FUNCTION: Essential component of glycosylphosphatidylinositol-
CC       mannosyltransferase 1 which transfers the first of the 4 mannoses in
CC       the GPI-anchor precursors during GPI-anchor biosynthesis. Probably acts
CC       by stabilizing the mannosyltransferase PIGM.
CC       {ECO:0000269|PubMed:15635094}.
CC   -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor
CC       biosynthesis.
CC   -!- SUBUNIT: Interacts with PIGM.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:15635094}; Single-pass type I membrane protein
CC       {ECO:0000269|PubMed:15635094}.
CC   -!- PTM: N-glycosylated. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the PIGX family. {ECO:0000305}.
CC   -!- CAUTION: PubMed:15635094 reported that the initiator methionine is
CC       coded by an unusual start codon, CTG. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD61008.1; Type=Miscellaneous discrepancy; Note=Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.; Evidence={ECO:0000305};
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DR   EMBL; AB177393; BAD61008.1; ALT_SEQ; mRNA.
DR   RefSeq; NP_001094121.1; NM_001100651.1.
DR   AlphaFoldDB; Q60GF7; -.
DR   STRING; 10116.ENSRNOP00000042305; -.
DR   GlyGen; Q60GF7; 2 sites.
DR   PaxDb; Q60GF7; -.
DR   GeneID; 288041; -.
DR   KEGG; rno:288041; -.
DR   UCSC; RGD:1307289; rat.
DR   CTD; 54965; -.
DR   RGD; 1307289; Pigx.
DR   eggNOG; ENOG502S32M; Eukaryota.
DR   InParanoid; Q60GF7; -.
DR   OrthoDB; 1537024at2759; -.
DR   PhylomeDB; Q60GF7; -.
DR   Reactome; R-RNO-162710; Synthesis of glycosylphosphatidylinositol (GPI).
DR   UniPathway; UPA00196; -.
DR   PRO; PR:Q60GF7; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0006506; P:GPI anchor biosynthetic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR013233; PIG-X/PBN1.
DR   InterPro; IPR040039; PIGX.
DR   PANTHER; PTHR28650; PTHR28650; 1.
DR   Pfam; PF08320; PIG-X; 1.
DR   SMART; SM00780; PIG-X; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Endoplasmic reticulum; Glycoprotein;
KW   GPI-anchor biosynthesis; Membrane; Reference proteome; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000269|PubMed:15635094"
FT   CHAIN           23..252
FT                   /note="Phosphatidylinositol-glycan biosynthesis class X
FT                   protein"
FT                   /id="PRO_0000246297"
FT   TRANSMEM        225..245
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        97
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        209
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   252 AA;  28423 MW;  28AE1E78438A3A85 CRC64;
     MAASALAWLL LWAAGLVGRL AADISDARFS DGVRATCSEI ILRQEFLKDG FHRDLLIKVK
     FGESIEDLQT CRLLIKHYIP TGLFVDPYEL ASLRERNITE AVMVSESFNL EAPNYLSTES
     AVLIYARQDA QCIDCFQAFL PVHYRYHRPH KKDGDTLIVV NNPDLLMHCD QEFPILKCWA
     QSEVAAPCSL KSEEICQWKN MQYKSILKNL TVQVPVGLTI HTSLVCSVTL LITVLCSTLI
     LLAVFKYGHF SL