PIGM_MOUSE
ID PIGM_MOUSE Reviewed; 423 AA.
AC Q8C2R7; Q8C917; Q99J22; Q9D315;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 2.
DT 03-AUG-2022, entry version 120.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD;
RC TISSUE=Aorta, Cerebellum, Colon, Thymus, and Vein;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=NMRI; TISSUE=Eye, and Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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; AK018560; BAB31275.1; -; mRNA.
DR EMBL; AK040397; BAC30585.1; -; mRNA.
DR EMBL; AK043216; BAC31497.1; -; mRNA.
DR EMBL; AK080242; BAC37857.1; -; mRNA.
DR EMBL; AK088117; BAC40156.1; -; mRNA.
DR EMBL; BC005650; AAH05650.1; -; mRNA.
DR EMBL; BC083115; AAH83115.1; -; mRNA.
DR CCDS; CCDS15513.1; -.
DR RefSeq; NP_080510.1; NM_026234.4.
DR AlphaFoldDB; Q8C2R7; -.
DR SMR; Q8C2R7; -.
DR STRING; 10090.ENSMUSP00000052838; -.
DR CAZy; GT50; Glycosyltransferase Family 50.
DR iPTMnet; Q8C2R7; -.
DR PhosphoSitePlus; Q8C2R7; -.
DR EPD; Q8C2R7; -.
DR MaxQB; Q8C2R7; -.
DR PaxDb; Q8C2R7; -.
DR PeptideAtlas; Q8C2R7; -.
DR PRIDE; Q8C2R7; -.
DR ProteomicsDB; 288209; -.
DR Antibodypedia; 34265; 77 antibodies from 17 providers.
DR DNASU; 67556; -.
DR Ensembl; ENSMUST00000052455; ENSMUSP00000052838; ENSMUSG00000050229.
DR GeneID; 67556; -.
DR KEGG; mmu:67556; -.
DR UCSC; uc007dqk.2; mouse.
DR CTD; 93183; -.
DR MGI; MGI:1914806; Pigm.
DR VEuPathDB; HostDB:ENSMUSG00000050229; -.
DR eggNOG; KOG3893; Eukaryota.
DR GeneTree; ENSGT00390000017728; -.
DR HOGENOM; CLU_024220_3_1_1; -.
DR InParanoid; Q8C2R7; -.
DR OMA; VTSQYFI; -.
DR OrthoDB; 1003258at2759; -.
DR PhylomeDB; Q8C2R7; -.
DR TreeFam; TF314752; -.
DR Reactome; R-MMU-162710; Synthesis of glycosylphosphatidylinositol (GPI).
DR UniPathway; UPA00196; -.
DR BioGRID-ORCS; 67556; 10 hits in 73 CRISPR screens.
DR PRO; PR:Q8C2R7; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q8C2R7; protein.
DR Bgee; ENSMUSG00000050229; Expressed in metanephric cortical collecting duct and 184 other tissues.
DR Genevisible; Q8C2R7; MM.
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; ISO:MGI.
DR GO; GO:0006506; P:GPI anchor biosynthetic process; ISO:MGI.
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_0000246215"
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"
FT CONFLICT 206
FT /note="Q -> H (in Ref. 1; BAC40156 and 2; AAH05650)"
FT /evidence="ECO:0000305"
FT CONFLICT 347
FT /note="M -> I (in Ref. 1; BAC40156)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 423 AA; 49789 MW; 0862F05F69894FEE CRC64;
MSYPMHWGEW ILNFRVPPAG VFGVAFLARV ALVFYGVFQD RTLLVRYTDI DYHVFTDAAR
FVTEGRSPYL RATYRYTPLL SWLLTPNVYL SELFGKFLFI SCDLLTAFLL YRLLLLKGLG
RRQACGYCVF WLLNPLPMAV SSRGNADSIV ASLVLSTLYF IEKRLIACAA VFYGFAVHMK
MYPVTYILPI ALHLRPERDD DERLRQARFS FQARLYDFLR RLCSWAVLLF VAVAGLTFVA
LSFGFYYKYG WEFLEHTYFY HLTRRDIRHN FSPYFYMLYL TAESKWSFTL GIAAFLPQFI
LLSAASFAYY RDLVFCCFLH TSIFVTFNKV CTSQYFLWYL CLLPLVMPLV RMPWKRAVVL
LLFWFIGQAL WLAPAYVLEF QGKNTFLFIW LAGLFFLLIN CSILIQIISH YKEDRLTERI
KYD
