IMT2_SCHPO
ID IMT2_SCHPO Reviewed; 345 AA.
AC Q9UT67;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 113.
DE RecName: Full=Inositol phosphoceramide mannosyltransferase 2;
DE EC=2.4.-.-;
DE AltName: Full=IPC mannosyltransferase 2;
GN ORFNames=SPCC4F11.04c;
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 imt1 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; CU329672; CAB55770.1; -; Genomic_DNA.
DR PIR; T41355; T41355.
DR RefSeq; NP_588403.1; NM_001023394.2.
DR AlphaFoldDB; Q9UT67; -.
DR SMR; Q9UT67; -.
DR BioGRID; 275306; 1.
DR STRING; 4896.SPCC4F11.04c.1; -.
DR CAZy; GT32; Glycosyltransferase Family 32.
DR MaxQB; Q9UT67; -.
DR PaxDb; Q9UT67; -.
DR EnsemblFungi; SPCC4F11.04c.1; SPCC4F11.04c.1:pep; SPCC4F11.04c.
DR GeneID; 2538722; -.
DR KEGG; spo:SPCC4F11.04c; -.
DR PomBase; SPCC4F11.04c; -.
DR VEuPathDB; FungiDB:SPCC4F11.04c; -.
DR eggNOG; ENOG502QS3D; Eukaryota.
DR HOGENOM; CLU_036369_1_0_1; -.
DR InParanoid; Q9UT67; -.
DR OMA; WTDEMAY; -.
DR PhylomeDB; Q9UT67; -.
DR PRO; PR:Q9UT67; -.
DR Proteomes; UP000002485; Chromosome III.
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:0031501; C:mannosyltransferase complex; IC:PomBase.
DR GO; GO:0032588; C:trans-Golgi network membrane; IDA: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..345
FT /note="Inositol phosphoceramide mannosyltransferase 2"
FT /id="PRO_0000372336"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 220..240
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 296..316
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 55
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 269
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 345 AA; 40764 MW; BB18434B3E1F7ADF CRC64;
MVKVIYKFAV FAAVNFFLMS SIVLYFNNEF LMFADRCTKD IIPSEELRYL RQVLNDSIPS
KDEPLPTLKL DSLNDISGEP VIPKIIHQTW KTTEVPEGWK GAQQSCIDLH PDYEYILWTD
EMSRNFIADN YPWFLPYFDA YPFNVQRADV IRYFVLYHYG GNYIDLDDGC RQRLDSLLYY
PVWVRRTDPV GVSNDVMGSV PHHPYFELII QNLEKNAKSY WLPYLTIMLS TGPLSISFLW
EKYKRQLPNP PAFYDHIRVL LERDYKFSND SYFTFYEGSS WHNNDAGIIL WANRHLAYVI
VAGFCLYFIL SYMFFSKLLD SRYVQRFVTS KRKQPTLPLA LQEDV
