IMT1_SCHPO
ID IMT1_SCHPO Reviewed; 319 AA.
AC O14084; Q9UT90;
DT 13-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 13-DEC-2002, sequence version 2.
DT 25-MAY-2022, entry version 120.
DE RecName: Full=Inositol phosphoceramide mannosyltransferase 1;
DE EC=2.4.-.-;
DE AltName: Full=IPC mannosyltransferase 1;
GN Name=imt1; ORFNames=SPAC2F3.01, SPAC323.09;
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 SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=20388730; DOI=10.1242/jcs.059139;
RA Nakase M., Tani M., Morita T., Kitamoto H.K., Kashiwazaki J., Nakamura T.,
RA Hosomi A., Tanaka N., Takegawa K.;
RT "Mannosylinositol phosphorylceramide is a major sphingolipid component and
RT is required for proper localization of plasma-membrane proteins in
RT Schizosaccharomyces pombe.";
RL J. Cell Sci. 123:1578-1587(2010).
CC -!- FUNCTION: With imt2 and imt3, is required for the synthesis of mannosyl
CC phosphorylinositol ceramide (MIPC). Catalyzes the addition of mannosyl
CC to phosphorylinositol ceramide (IPC). MIPC is essential for cell
CC morphology, cell-surface distribution of ergosterol, localization for
CC plasma-membrane transporters, and lipid-raft-mediated endocytosis of
CC plasma membrane proteins to the vacuole. {ECO:0000269|PubMed:20388730}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network membrane;
CC Multi-pass membrane protein. Golgi apparatus, trans-Golgi network
CC membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 32 family.
CC {ECO:0000305}.
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DR EMBL; CU329670; CAB53412.1; -; Genomic_DNA.
DR PIR; T38646; T38533.
DR RefSeq; XP_001713095.1; XM_001713043.2.
DR AlphaFoldDB; O14084; -.
DR SMR; O14084; -.
DR BioGRID; 280508; 1.
DR STRING; 4896.SPAC2F3.01.1; -.
DR CAZy; GT32; Glycosyltransferase Family 32.
DR MaxQB; O14084; -.
DR PaxDb; O14084; -.
DR EnsemblFungi; SPAC2F3.01.1; SPAC2F3.01.1:pep; SPAC2F3.01.
DR PomBase; SPAC2F3.01; imt1.
DR VEuPathDB; FungiDB:SPAC2F3.01; -.
DR eggNOG; ENOG502QS3D; Eukaryota.
DR HOGENOM; CLU_036369_4_0_1; -.
DR InParanoid; O14084; -.
DR OMA; GTRPWTW; -.
DR PhylomeDB; O14084; -.
DR PRO; PR:O14084; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0033106; C:cis-Golgi network membrane; IDA:PomBase.
DR GO; GO:0005794; C:Golgi apparatus; HDA:PomBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0032588; C:trans-Golgi network membrane; IDA:PomBase.
DR GO; GO:0005537; F:mannose binding; ISM:PomBase.
DR GO; GO:0000030; F:mannosyltransferase activity; ISO:PomBase.
DR GO; GO:0051999; P:mannosyl-inositol phosphorylceramide biosynthetic process; IGI:PomBase.
DR InterPro; IPR007577; GlycoTrfase_DXD_sugar-bd_CS.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR Pfam; PF04488; Gly_transf_sug; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 3: Inferred from homology;
KW Glycoprotein; Glycosyltransferase; Golgi apparatus; Membrane;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..319
FT /note="Inositol phosphoceramide mannosyltransferase 1"
FT /id="PRO_0000014199"
FT TRANSMEM 8..28
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 211..231
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 279..299
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 115
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 198
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 319 AA; 37130 MW; E524ED667A9E5139 CRC64;
MGRKCRKLLL KGIPICGVIL LILWGYSLYN TLRFMVPGKA TEPFTLSLSD VSDDTSAPGE
MEKIPRVIHQ LWKDENIPER WSNTVNSCRR QHPDENGWQF ILWTDEKIMS FMNENYSWFM
PVFHSYPYNI QKFDAARYFI LYHYGGVYMD LDIGCKKPMD PLLSKATFIL PSTEPIGYSN
DWFAATPKHP FLYQAIHNLS KFNHRYFTKY PTVFLSAGPL FLSYQFCKYL LTPHEPVRVL
PALLYGNGPN SFFSHVTGDS WHGTDAKVFI WIDRNSKSVL FFAFLAAFAI LFLCLRVVFK
RRRKRGIAAS HSQIQELYP
