PIGM_PONAB
ID PIGM_PONAB Reviewed; 423 AA.
AC Q5RAH7; Q5R958;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 60.
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;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RG The German cDNA consortium;
RL Submitted (NOV-2004) 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; CR859038; CAH91233.1; -; mRNA.
DR EMBL; CR859536; CAH91702.1; -; mRNA.
DR RefSeq; NP_001125728.1; NM_001132256.1.
DR AlphaFoldDB; Q5RAH7; -.
DR SMR; Q5RAH7; -.
DR STRING; 9601.ENSPPYP00000000753; -.
DR CAZy; GT50; Glycosyltransferase Family 50.
DR GeneID; 100172653; -.
DR CTD; 93183; -.
DR eggNOG; KOG3893; Eukaryota.
DR InParanoid; Q5RAH7; -.
DR UniPathway; UPA00196; -.
DR Proteomes; UP000001595; 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_0000246216"
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..314
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 315..337
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 338
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 339..350
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 351..357
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 358..378
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 379..384
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 385..405
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 406..423
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CONFLICT 151
FT /note="A -> S (in Ref. 1; CAH91702)"
FT /evidence="ECO:0000305"
FT CONFLICT 214
FT /note="C -> R (in Ref. 1; CAH91702)"
FT /evidence="ECO:0000305"
FT CONFLICT 233
FT /note="V -> I (in Ref. 1; CAH91702)"
FT /evidence="ECO:0000305"
FT CONFLICT 263
FT /note="T -> I (in Ref. 1; CAH91702)"
FT /evidence="ECO:0000305"
FT CONFLICT 338
FT /note="W -> R (in Ref. 1; CAH91702)"
FT /evidence="ECO:0000305"
FT CONFLICT 357
FT /note="A -> T (in Ref. 1; CAH91702)"
FT /evidence="ECO:0000305"
FT CONFLICT 370
FT /note="M -> I (in Ref. 1; CAH91702)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 423 AA; 49460 MW; E17DCD8252E28EF0 CRC64;
MGSTKHWGEW LLNLKVAPAG VFGVAFLARV ALVFYGVFQD RTLHVRYTDI DYQVFTDAAR
FVTEGRSPYL RATYRYTPLL GWLLTPNIYL SELFGKFLFI SCDLLTAFLL YRLLLLKGLG
RRQACGYCVF WLLNPLPMAV SSRGNADSIV ASLVLMVLYL IKKRLVACAA VFYGFAVHMK
IYPVTYILPI TLHLLPDRDN DKSLRQFRYT FQACLYELLK RLCNRAVLLF VAVAGLTFFA
LSFGFYYEYG WEFLEHTYFY HLTRRDIRHN FSPYFYMLYL TAESKWSFSL GIAAFLPQLI
LLSAVSFAYY RDLVFCCFLH TSIFVTFNKV CTSQYFLWYL CLLPLVMPLV RMPWKRAVVL
LMLWFIGQAM WLAPAYVLEF QGKNTFLFIW LAGLFFLLIN CSILIQIISH YKEEPLTERI
KYD
