PIGM_TRYB2
ID PIGM_TRYB2 Reviewed; 430 AA.
AC Q9BPQ5; Q584X3;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 2.
DT 25-MAY-2022, entry version 83.
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;
DE AltName: Full=TbPIG-M;
GN Name=PIGM; ORFNames=Tb927.6.3300;
OS Trypanosoma brucei brucei (strain 927/4 GUTat10.1).
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX NCBI_TaxID=185431;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=927/4 GUTat10.1 {ECO:0000312|Proteomes:UP000008524};
RX PubMed=16020726; DOI=10.1126/science.1112642;
RA Berriman M., Ghedin E., Hertz-Fowler C., Blandin G., Renauld H.,
RA Bartholomeu D.C., Lennard N.J., Caler E., Hamlin N.E., Haas B., Bohme U.,
RA Hannick L., Aslett M.A., Shallom J., Marcello L., Hou L., Wickstead B.,
RA Alsmark U.C.M., Arrowsmith C., Atkin R.J., Barron A.J., Bringaud F.,
RA Brooks K., Carrington M., Cherevach I., Chillingworth T.J., Churcher C.,
RA Clark L.N., Corton C.H., Cronin A., Davies R.M., Doggett J., Djikeng A.,
RA Feldblyum T., Field M.C., Fraser A., Goodhead I., Hance Z., Harper D.,
RA Harris B.R., Hauser H., Hostetler J., Ivens A., Jagels K., Johnson D.,
RA Johnson J., Jones K., Kerhornou A.X., Koo H., Larke N., Landfear S.,
RA Larkin C., Leech V., Line A., Lord A., Macleod A., Mooney P.J., Moule S.,
RA Martin D.M., Morgan G.W., Mungall K., Norbertczak H., Ormond D., Pai G.,
RA Peacock C.S., Peterson J., Quail M.A., Rabbinowitsch E., Rajandream M.A.,
RA Reitter C., Salzberg S.L., Sanders M., Schobel S., Sharp S., Simmonds M.,
RA Simpson A.J., Tallon L., Turner C.M., Tait A., Tivey A.R., Van Aken S.,
RA Walker D., Wanless D., Wang S., White B., White O., Whitehead S.,
RA Woodward J., Wortman J., Adams M.D., Embley T.M., Gull K., Ullu E.,
RA Barry J.D., Fairlamb A.H., Opperdoes F., Barrell B.G., Donelson J.E.,
RA Hall N., Fraser C.M., Melville S.E., El-Sayed N.M.A.;
RT "The genome of the African trypanosome Trypanosoma brucei.";
RL Science 309:416-422(2005).
CC -!- FUNCTION: Mannosyltransferase involved in glycosylphosphatidylinositol-
CC anchor biosynthesis. Transfers the first alpha-1,4-mannose to GlcN-PI
CC 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 -!- MISCELLANEOUS: In T.brucei, PIGM has a different substrate specificity
CC compared to mammalian. Given that the protozoan parasite evades the
CC immune response of mammalian hosts and digestion in the gut of the
CC insect vector by means of its coat proteins tethered to the cell
CC surface via GPI-anchors, it may be a good candidate for chemotherapy
CC against African trypanosomiasis.
CC -!- SIMILARITY: Belongs to the PIGM family. {ECO:0000305}.
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DR EMBL; AB050105; BAB20994.1; -; mRNA.
DR EMBL; AC074258; AAX79949.1; -; Genomic_DNA.
DR RefSeq; XP_845451.1; XM_840358.1.
DR AlphaFoldDB; Q9BPQ5; -.
DR STRING; 5691.AAZ11892; -.
DR CAZy; GT50; Glycosyltransferase Family 50.
DR PaxDb; Q9BPQ5; -.
DR PRIDE; Q9BPQ5; -.
DR GeneID; 3657966; -.
DR KEGG; tbr:Tb927.6.3300; -.
DR VEuPathDB; TriTrypDB:Tb927.6.3300; -.
DR eggNOG; KOG3893; Eukaryota.
DR InParanoid; Q9BPQ5; -.
DR OMA; HESFIYH; -.
DR UniPathway; UPA00196; -.
DR Proteomes; UP000008524; Chromosome 6.
DR GO; GO:0005737; C:cytoplasm; IDA:GeneDB.
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:0005635; C:nuclear envelope; IDA:GeneDB.
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; IBA:GO_Central.
DR GO; GO:0006506; P:GPI anchor biosynthetic process; IBA:GO_Central.
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..430
FT /note="GPI mannosyltransferase 1"
FT /id="PRO_0000246221"
FT TOPO_DOM 1..11
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 33..72
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 73..93
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 94..115
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 116..136
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 137..163
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 164..184
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 185..206
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 207..227
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 228..360
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 361..381
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 382..388
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 389..409
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 410..430
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CONFLICT 284
FT /note="A -> V (in Ref. 1; BAB20994)"
FT /evidence="ECO:0000305"
FT CONFLICT 391
FT /note="Q -> K (in Ref. 1; BAB20994)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 430 AA; 48849 MW; B5AA67EB54A73FD6 CRC64;
MELQSLIDTV SLQKLLLLGA LLRLILIAYA FFHDQWFRVK YTDIDYMIVV DGARHMWNGG
SPFDRTTFRY TPLLAALVMP SIWIANPMGK LIFASSDLGA AWYCYGVLKS FAKERSAKWM
VSLFILFNPI VLSVSTRGNS DMLVTFMSLM VLSKFARRKC YQAAAVLGFA VHFKIYPIIY
ALPLTLGVWE QSVAASTNTW RRVVKTAVVV SICALMAAIS FAVPTVLCYM KYGQQYLNEA
FIYHVYREDH RHNFSPYWLL MYLNMARRHL GQGVDFSPRL VAFAPQAVVL SFVSYKLRRN
TAHACCVQTV LFVAFNKVCT VQYFVWFIPF LAFLFCEPKE VEDDESGGSG AFKFFSWVKA
LGVVLMWAAT IPLWVTTAVP LEFHGYSDFA QLWIVSCLFF LAMVVLASML ARIAYRVQCT
KCSAKSIKVA
