ID   PIGM_MACFA              Reviewed;         423 AA.
AC   Q4R4E1;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 56.
DE   RecName: Full=GPI mannosyltransferase 1;
DE            EC=2.4.1.-;
DE   AltName: Full=GPI mannosyltransferase I;
DE            Short=GPI-MT-I;
DE   AltName: Full=Phosphatidylinositol-glycan biosynthesis class M protein;
DE            Short=PIG-M;
GN   Name=PIGM; ORFNames=QtsA-10615, QtsA-10624;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RG   International consortium for macaque cDNA sequencing and analysis;
RT   "DNA sequences of macaque genes expressed in brain or testis and its
RT   evolutionary implications.";
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Mannosyltransferase involved in glycosylphosphatidylinositol-
CC       anchor biosynthesis. Transfers the first alpha-1,4-mannose to GlcN-
CC       acyl-PI during GPI precursor assembly (By similarity). {ECO:0000250}.
CC   -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor
CC       biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC       Multi-pass membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the PIGM family. {ECO:0000305}.
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DR   EMBL; AB178972; BAE02023.1; -; mRNA.
DR   EMBL; AB178973; BAE02024.1; -; mRNA.
DR   RefSeq; NP_001271052.1; NM_001284123.1.
DR   AlphaFoldDB; Q4R4E1; -.
DR   STRING; 9541.XP_005541340.1; -.
DR   CAZy; GT50; Glycosyltransferase Family 50.
DR   GeneID; 101867401; -.
DR   CTD; 93183; -.
DR   eggNOG; KOG3893; Eukaryota.
DR   OrthoDB; 1003258at2759; -.
DR   UniPathway; UPA00196; -.
DR   Proteomes; UP000233100; 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:0051751; F:alpha-1,4-mannosyltransferase activity; IEA:InterPro.
DR   GO; GO:0004376; F:glycolipid mannosyltransferase activity; IEA:InterPro.
DR   GO; GO:0006506; P:GPI anchor biosynthetic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR007704; PIG-M.
DR   PANTHER; PTHR12886; PTHR12886; 1.
DR   Pfam; PF05007; Mannosyl_trans; 1.
PE   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Glycosyltransferase; GPI-anchor biosynthesis;
KW   Membrane; Reference proteome; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..423
FT                   /note="GPI mannosyltransferase 1"
FT                   /id="PRO_0000246214"
FT   TOPO_DOM        1..17
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        18..38
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        39..79
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        80..100
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        101..138
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        139..161
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        162..169
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        170..190
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        191..225
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        226..246
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        247..287
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        288..308
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        309..329
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        330..350
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        351..357
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        358..378
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        379..384
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        385..405
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        406..423
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   423 AA;  49451 MW;  2D80BEDB4EA05BAC CRC64;
     MGSTKHWGEW LLNLKLAPAG VFGVAFLARV ALVFYGVFQD RTLHVRYTDI DYQVFTDAAR
     FVAEGRSPYL RATYRYTPLL GWLLTPNIYL SELFGKFLFI SCDLLTAFLL YRLLLLKGLA
     RRQACGYCVF WLLNPLPMAV SSRGNADSIV ASLVLMVLYL IRKRVVACAA VFYGFAVHMK
     IYPVTYILPI TLHLLPDRDN DKSLRQSRYT FQAHLYELLK RLCDRAVLLF VAVAGLTFFA
     LSFGFYYEYG WEFLEHTYFY HLTRRDIRHN FSPYFYMLYL TAESKWSFSL GIAAFLPQFI
     LLSAVSFAYY RDLVFCCFLH TSIFVTFNKV CTSQYFLWYL CLLPLVMPLV RMTWKRAVVL
     LMLWFIGQAL WLAPAYVLEF QGKNTFLFIW LAGLFFLLIN SSILIQIISH YKEEPLTERI
     KYD