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GPI10_SCHPO
ID   GPI10_SCHPO             Reviewed;         506 AA.
AC   Q9USN0;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 112.
DE   RecName: Full=GPI mannosyltransferase 3;
DE            EC=2.4.1.-;
DE   AltName: Full=GPI mannosyltransferase III;
DE            Short=GPI-MT-III;
DE   AltName: Full=Glycosylphosphatidylinositol-anchor biosynthesis protein 10;
GN   Name=gpi10; ORFNames=SPCC16A11.06c;
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).
CC   -!- FUNCTION: Mannosyltransferase involved in glycosylphosphatidylinositol-
CC       anchor biosynthesis. Transfers the third mannose to Man2-GlcN-acyl-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   -!- SIMILARITY: Belongs to the glycosyltransferase 22 family. PIGB
CC       subfamily. {ECO:0000305}.
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DR   EMBL; CU329672; CAB53078.1; -; Genomic_DNA.
DR   PIR; T41079; T41079.
DR   RefSeq; NP_587993.1; NM_001022984.2.
DR   AlphaFoldDB; Q9USN0; -.
DR   BioGRID; 275724; 2.
DR   STRING; 4896.SPCC16A11.06c.1; -.
DR   CAZy; GT22; Glycosyltransferase Family 22.
DR   PaxDb; Q9USN0; -.
DR   EnsemblFungi; SPCC16A11.06c.1; SPCC16A11.06c.1:pep; SPCC16A11.06c.
DR   GeneID; 2539152; -.
DR   KEGG; spo:SPCC16A11.06c; -.
DR   PomBase; SPCC16A11.06c; gpi10.
DR   VEuPathDB; FungiDB:SPCC16A11.06c; -.
DR   eggNOG; KOG1771; Eukaryota.
DR   HOGENOM; CLU_012353_2_0_1; -.
DR   InParanoid; Q9USN0; -.
DR   OMA; HHMVFNN; -.
DR   PhylomeDB; Q9USN0; -.
DR   Reactome; R-SPO-162710; Synthesis of glycosylphosphatidylinositol (GPI).
DR   UniPathway; UPA00196; -.
DR   PRO; PR:Q9USN0; -.
DR   Proteomes; UP000002485; Chromosome III.
DR   GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR   GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISM:PomBase.
DR   GO; GO:0000026; F:alpha-1,2-mannosyltransferase activity; ISO: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; IPR005599; GPI_mannosylTrfase.
DR   InterPro; IPR039521; PIG-B/GPI10.
DR   PANTHER; PTHR22760; PTHR22760; 1.
DR   PANTHER; PTHR22760:SF4; PTHR22760:SF4; 1.
DR   Pfam; PF03901; Glyco_transf_22; 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..506
FT                   /note="GPI mannosyltransferase 3"
FT                   /id="PRO_0000246266"
FT   TRANSMEM        180..200
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        229..249
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        257..277
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        285..305
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        330..350
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        358..378
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        115
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        395
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   506 AA;  59222 MW;  24466D3CE6878F91 CRC64;
     MRIWFWLAIL VFRWWNALWV KTFFQPDEFY QSLEVAHHFI FRYGFLTWEW TSAIRSALHP
     LIFAALYRVL QVLKLDSSYF VFTNAPKLLQ GTFAAILDYG TYKFALVRYG SKTANWTLAC
     SLVSIMNAYV GVRTFSNSLE TTLTSIGFYY FSYYLKYENS SPEQRKKAYS SLLGFISVAA
     FACFIRPTNI LVWIFPLLFW NKNPQTPIKD LLSFSNVFNR FRFLYALGYG RLFGIFVLCV
     SLFLVNIIAD RILYGRFVFP IISFFQFNVT SGLSSLYGLN AWHYYLSQAL PLICGGFLPF
     VLLTMDLQTA GTILCVFFPY SLIGHKELRF VYPISPILLT LAGKFFSSFS SWKRAARFFF
     LIGLGHALVI TFLCRFHQFG VMEVMPLIHS LAEKNQTGLI LAPCHTTPWQ SHIHSPFAEN
     GWKFLTCEPF EKPFDETDRF YENMPTFLDK IKEWPDYLIF FEERFYSLYS YLDSRGLKYE
     EVQRYYNSLI PESRERAGAL LVYKKL
 
 
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