PIGM_RAT
ID PIGM_RAT Reviewed; 423 AA.
AC Q9EQY6;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 103.
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 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].
RX PubMed=11226175; DOI=10.1093/emboj/20.1.250;
RA Maeda Y., Watanabe R., Harris C.L., Hong Y., Ohishi K., Kinoshita K.,
RA Kinoshita T.;
RT "PIG-M transfers the first mannose to glycosylphosphatidylinositol on the
RT lumenal side of the ER.";
RL EMBO J. 20:250-261(2001).
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; AB028126; BAB18566.1; -; mRNA.
DR RefSeq; NP_077058.1; NM_024144.1.
DR RefSeq; XP_008772129.1; XM_008773907.2.
DR AlphaFoldDB; Q9EQY6; -.
DR STRING; 10116.ENSRNOP00000010551; -.
DR CAZy; GT50; Glycosyltransferase Family 50.
DR PaxDb; Q9EQY6; -.
DR Ensembl; ENSRNOT00000010551; ENSRNOP00000010551; ENSRNOG00000007735.
DR GeneID; 79112; -.
DR KEGG; rno:79112; -.
DR UCSC; RGD:71041; rat.
DR CTD; 93183; -.
DR RGD; 71041; Pigm.
DR eggNOG; KOG3893; Eukaryota.
DR GeneTree; ENSGT00390000017728; -.
DR HOGENOM; CLU_024220_3_1_1; -.
DR InParanoid; Q9EQY6; -.
DR OMA; VTSQYFI; -.
DR OrthoDB; 1003258at2759; -.
DR PhylomeDB; Q9EQY6; -.
DR TreeFam; TF314752; -.
DR Reactome; R-RNO-162710; Synthesis of glycosylphosphatidylinositol (GPI).
DR UniPathway; UPA00196; -.
DR PRO; PR:Q9EQY6; -.
DR Proteomes; UP000002494; Chromosome 13.
DR Bgee; ENSRNOG00000007735; Expressed in thymus and 18 other tissues.
DR Genevisible; Q9EQY6; RN.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:1990529; C:glycosylphosphatidylinositol-mannosyltransferase I complex; IBA:GO_Central.
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:0000030; F:mannosyltransferase activity; IDA:RGD.
DR GO; GO:0006506; P:GPI anchor biosynthetic process; IDA:RGD.
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_0000246217"
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..89
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 90..110
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 111..169
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 170..190
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 191..224
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 225..245
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 246..287
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 288..308
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 309..329
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 330..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"
SQ SEQUENCE 423 AA; 49594 MW; 7FC172B5DF98992D CRC64;
MSYTKHWGEW FLNLRVPPAG VFGVAFLARV ALVFYGVFQD RTLLVRYTDI DYHVFTDAAR
FVTEGRSPYL RATYRYTPLL SWLLTPNVYL SELFGKFLFI SCDLLTAFLL YRLLLLKGLG
RRQACGYCVF WLLNPLPMAV SSRGNADSIV ASLVLTTLYL IEKRLIACAA VFYGFAVHMK
MYPVTYILPI ALHLRPERDS DEGLRLARYS FQARLYDFLK RLCSWAVLLF VAIAGLTFLA
LSFGFYYKYG WEFLEHTYLY HLTRRDIRHN FSPYFYMLYL TAESKWSFTL GIAAFLPQFI
LLSAASFAYY RDLVFCCFLH TSIFVTFNKV CTSQYFLWYL CLLPLVMPLV RMPWKRAVVL
LMLWFIGQAL WLAPAYVLEF QGKNTFLFIW LAGLFFLLIN CSILIQIISH YKEDRLTERI
KYD
