GPI18_SCHPO
ID GPI18_SCHPO Reviewed; 464 AA.
AC Q09712;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2012, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=GPI mannosyltransferase 2;
DE EC=2.4.1.-;
DE AltName: Full=GPI mannosyltransferase II;
DE Short=GPI-MT-II;
DE AltName: Full=Glycosylphosphatidylinositol-anchor biosynthesis protein 18;
GN Name=gpi18; ORFNames=SPAC18B11.05;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [3]
RP REVISION OF GENE MODEL.
RX PubMed=21270388; DOI=10.1534/genetics.110.123497;
RA Bitton D.A., Wood V., Scutt P.J., Grallert A., Yates T., Smith D.L.,
RA Hagan I.M., Miller C.J.;
RT "Augmented annotation of the Schizosaccharomyces pombe genome reveals
RT additional genes required for growth and viability.";
RL Genetics 187:1207-1217(2011).
CC -!- FUNCTION: Mannosyltransferase involved in glycosylphosphatidylinositol-
CC anchor biosynthesis. Responsible for the transfer of the second mannose
CC to the glycosylphosphatidylinositol during GPI precursor assembly (By
CC similarity). {ECO:0000250}.
CC -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor
CC biosynthesis.
CC -!- SUBUNIT: Part of the GPI mannosyltransferase 2 complex composed of
CC gpi18 and C167.09. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the PIGV family. {ECO:0000305}.
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DR EMBL; CU329670; CAA90590.2; -; Genomic_DNA.
DR PIR; T37909; S58304.
DR RefSeq; NP_592878.2; NM_001018278.2.
DR AlphaFoldDB; Q09712; -.
DR STRING; 4896.SPAC18B11.05.1; -.
DR CAZy; GT76; Glycosyltransferase Family 76.
DR SwissPalm; Q09712; -.
DR MaxQB; Q09712; -.
DR PaxDb; Q09712; -.
DR PRIDE; Q09712; -.
DR EnsemblFungi; SPAC18B11.05.1; SPAC18B11.05.1:pep; SPAC18B11.05.
DR PomBase; SPAC18B11.05; gpi18.
DR VEuPathDB; FungiDB:SPAC18B11.05; -.
DR eggNOG; KOG2647; Eukaryota.
DR HOGENOM; CLU_029048_0_0_1; -.
DR InParanoid; Q09712; -.
DR OMA; EYFLHIA; -.
DR Reactome; R-SPO-162710; Synthesis of glycosylphosphatidylinositol (GPI).
DR UniPathway; UPA00196; -.
DR PRO; PR:Q09712; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0120097; C:glycosylphosphatidylinositol-mannosyltransferase II complex; ISO:PomBase.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISO:PomBase.
DR GO; GO:0031501; C:mannosyltransferase complex; IBA:GO_Central.
DR GO; GO:0000009; F:alpha-1,6-mannosyltransferase activity; IEA:InterPro.
DR GO; GO:0052926; F:dol-P-Man:Man(6)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferase activity; ISS:PomBase.
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; ISO:PomBase.
DR InterPro; IPR007315; PIG-V/Gpi18.
DR PANTHER; PTHR12468; PTHR12468; 1.
DR Pfam; PF04188; Mannosyl_trans2; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum; Glycoprotein; Glycosyltransferase;
KW GPI-anchor biosynthesis; Membrane; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..464
FT /note="GPI mannosyltransferase 2"
FT /id="PRO_0000116387"
FT TOPO_DOM 1..70
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 71..91
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 92..166
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 167..187
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 188..219
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 220..240
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 241..260
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 261..281
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 282..289
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 290..309
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 310..356
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 357..377
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 378..388
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 389..409
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 410..440
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 441..461
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 462..464
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 108
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 139
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 326
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 464 AA; 53608 MW; FB1FF78DC133D14D CRC64;
MYYIGHPSYY RKHIEHVCFQ HSGILKKRNY QKNQKKYIMK LNESAMKNAE KKSNSYLAIR
MTRSGYNYFK GICVCTFLLS TILYLGIAVI MSHLCVFDDT AMLYLRQNRS RLAESNIFRT
LFISWIRWDA IYFVDMAVNG SLFEQEWAFS SLWPKIISFL AFRSKDVVLL GIVSCFASIF
FHAIACYALY LLTKSIFSNQ KMTAYTVIFY CFSPSGIYMS VGYTESLFAA FSFLGLLLFI
KKQQYPAAFL WSLATLIRSN GIFWCIFFGM PAIGTLKISL ERLQLTFMQV SQLVGYGTKC
LIILVPFFYN QYLGFKLFCP GVAWCNKSLP LIYPAVQEKY WNVGFLRYWT LNNIPNFLFA
LLSIIPILFA LFYSISGSTL HSFRSIKSHL VLSALYLYIG CFHMHTQVLN RMSSALPLLY
WSMAHATLYA KSRNLKAFGH CILFVWIVYT VIQAGLYGSF LPPA
