CSH1_YEAST
ID CSH1_YEAST Reviewed; 376 AA.
AC P38287; D6VQF6;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Mannosyl phosphorylinositol ceramide synthase CSH1 {ECO:0000303|PubMed:12954640};
DE EC=2.4.1.370 {ECO:0000269|PubMed:12954640};
DE AltName: Full=CSG1/SUR1 homolog 1 {ECO:0000303|PubMed:12954640};
GN Name=CSH1 {ECO:0000303|PubMed:12954640}; OrderedLocusNames=YBR161W;
GN ORFNames=YBR1212;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7597849; DOI=10.1002/yea.320110508;
RA Baur S., Becker J., Li Z., Niegemann E., Wehner E., Wolter R., Brendel M.;
RT "Sequence analysis of a 5.6 kb fragment of chromosome II from Saccharomyces
RT cerevisiae reveals two new open reading frames next to CDC28.";
RL Yeast 11:455-458(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP FUNCTION, SUBUNIT, DISRUPTION PHENOTYPE, AND CATALYTIC ACTIVITY.
RX PubMed=12954640; DOI=10.1074/jbc.m305498200;
RA Uemura S., Kihara A., Inokuchi J., Igarashi Y.;
RT "Csg1p and newly identified Csh1p function in mannosylinositol
RT phosphorylceramide synthesis by interacting with Csg2p.";
RL J. Biol. Chem. 278:45049-45055(2003).
RN [6]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [7]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-354, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
CC -!- FUNCTION: Involved in the synthesis of mannosyl phosphorylinositol
CC ceramide (PubMed:12954640). Catalyzes the addition of mannosyl to
CC phosphorylinositol ceramide (PubMed:12954640).
CC {ECO:0000269|PubMed:12954640}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1D-myo-inositol-1-phospho-N-[(R)-2-hydroxy-very-long-chain
CC fatty acyl]-(R)-4-hydroxysphingoid base + GDP-alpha-D-mannose = an
CC alpha-D-mannosyl-(1<->6)-1D-myo-inositol-1-phospho-N-[(R)-2-hydroxy-
CC very-long-chain fatty acyl]-(R)-4-hydroxysphingoid base + GDP + H(+);
CC Xref=Rhea:RHEA:64596, ChEBI:CHEBI:15378, ChEBI:CHEBI:57527,
CC ChEBI:CHEBI:58189, ChEBI:CHEBI:155885, ChEBI:CHEBI:155926;
CC EC=2.4.1.370; Evidence={ECO:0000269|PubMed:12954640};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64597;
CC Evidence={ECO:0000269|PubMed:12954640};
CC -!- SUBUNIT: Heterodimer of CSH1 and CSG2. {ECO:0000269|PubMed:12954640}.
CC -!- INTERACTION:
CC P38287; P35206: CSG2; NbExp=2; IntAct=EBI-20861, EBI-2051140;
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:14562095};
CC Multi-pass membrane protein {ECO:0000269|PubMed:14562095}.
CC -!- DISRUPTION PHENOTYPE: Exhibits a reduction in the synthesis of
CC mannosylated sphingolipids. {ECO:0000269|PubMed:12954640}.
CC -!- MISCELLANEOUS: Present with 195 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 32 family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X80224; CAA56510.1; -; Genomic_DNA.
DR EMBL; Z36030; CAA85120.1; -; Genomic_DNA.
DR EMBL; AY692764; AAT92783.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07276.1; -; Genomic_DNA.
DR PIR; S46032; S46032.
DR RefSeq; NP_009719.3; NM_001178509.3.
DR AlphaFoldDB; P38287; -.
DR SMR; P38287; -.
DR BioGRID; 32860; 206.
DR ComplexPortal; CPX-1740; Mannosyl phosphorylinositol ceramide synthase CSH1-CSG2.
DR DIP; DIP-5144N; -.
DR IntAct; P38287; 3.
DR MINT; P38287; -.
DR STRING; 4932.YBR161W; -.
DR CAZy; GT32; Glycosyltransferase Family 32.
DR iPTMnet; P38287; -.
DR MaxQB; P38287; -.
DR PaxDb; P38287; -.
DR PRIDE; P38287; -.
DR EnsemblFungi; YBR161W_mRNA; YBR161W; YBR161W.
DR GeneID; 852458; -.
DR KEGG; sce:YBR161W; -.
DR SGD; S000000365; CSH1.
DR VEuPathDB; FungiDB:YBR161W; -.
DR eggNOG; ENOG502QS3D; Eukaryota.
DR GeneTree; ENSGT00940000176781; -.
DR HOGENOM; CLU_036369_3_2_1; -.
DR InParanoid; P38287; -.
DR OMA; HHLGNSW; -.
DR BioCyc; MetaCyc:G3O-29111-MON; -.
DR BioCyc; YEAST:G3O-29111-MON; -.
DR BRENDA; 2.4.1.370; 984.
DR PRO; PR:P38287; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P38287; protein.
DR GO; GO:0000324; C:fungal-type vacuole; HDA:SGD.
DR GO; GO:0005794; C:Golgi apparatus; IDA:ComplexPortal.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031501; C:mannosyltransferase complex; IPI:ComplexPortal.
DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0103064; F:inositol phosphorylceramide mannosyltransferase activity; IEA:RHEA.
DR GO; GO:0000030; F:mannosyltransferase activity; IMP:SGD.
DR GO; GO:0006688; P:glycosphingolipid biosynthetic process; IMP:SGD.
DR GO; GO:0006676; P:mannosyl diphosphorylinositol ceramide metabolic process; IDA:ComplexPortal.
DR GO; GO:0051999; P:mannosyl-inositol phosphorylceramide biosynthetic process; IBA:GO_Central.
DR GO; GO:0030148; P:sphingolipid biosynthetic process; IMP:SGD.
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 1: Evidence at protein level;
KW Membrane; Phosphoprotein; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix; Vacuole.
FT CHAIN 1..376
FT /note="Mannosyl phosphorylinositol ceramide synthase CSH1"
FT /id="PRO_0000079395"
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 274..294
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 331..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 354
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
SQ SEQUENCE 376 AA; 44382 MW; 34D992039DA0B796 CRC64;
MKKELKILII ANIALLISII HYTFDLLTLC IDDTSKDALT DEQLNPPNGF NSTFYESPPQ
LIPKIIHQTY KTNDIPEQWV KGRQKCIDLH PDYTYILWTD EMSDTFIKQE YPWFLDTFRS
YEYPIERADA IRYFILSHYG GIYIDLDDGC ERRLDPLLKV PAFLRKTSPT GVSNDVMGSV
PRHPFFLKVI KSLKHYKKNW YIPYMTIMGS TGPLFISVVW KQYKRWSNTA ENGAVRILQP
ADYKMHNNSF FSISKGSSWH TGDANFMKTL ENHILSCVVT GFIFGFFILY GEFTFYTWLC
SGPFNNKRYY IQWLSDKFKL HKWKLTSSYK NKEKRRNPTR HEYNSRGKRL RKDSNIPYDS
VFLDIEKNHA KFTDLT
