ID   CSG2_YEAST              Reviewed;         410 AA.
AC   P35206; D6VQ36;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 2.
DT   02-SEP-2026, entry version 171.
DE   RecName: Full=Mannosyl phosphorylinositol ceramide synthase regulatory protein CSG2;
DE   Flags: Precursor;
GN   Name=CSG2; Synonyms=CLS2; OrderedLocusNames=YBR036C; ORFNames=YBR0404;
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 [MRNA].
RX   PubMed=8125941; DOI=10.1016/s0021-9258(17)37280-0;
RA   Beeler T.J., Gable K., Zhao C., Dunn T.;
RT   "A novel protein, CSG2p, is required for Ca2+ regulation in Saccharomyces
RT   cerevisiae.";
RL   J. Biol. Chem. 269:7279-7284(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SUBCELLULAR LOCATION.
RX   PubMed=7854312; DOI=10.1007/bf00288599;
RA   Takita Y., Ohya Y., Anraku Y.;
RT   "The CLS2 gene encodes a protein with multiple membrane-spanning domains
RT   that is important Ca2+ tolerance in yeast.";
RL   Mol. Gen. Genet. 246:269-281(1995).
RN   [3]
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   [4]
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   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 116-410.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8091864; DOI=10.1002/yea.320100010;
RA   Smits P.H.M., de Haan M., Maat C., Grivell L.A.;
RT   "The complete sequence of a 33 kb fragment on the right arm of chromosome
RT   II from Saccharomyces cerevisiae reveals 16 open reading frames, including
RT   ten new open reading frames, five previously identified genes and a
RT   homologue of the SCO1 gene.";
RL   Yeast 10:S75-S80(1994).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-92.
RX   PubMed=2543907; DOI=10.1007/bf00332228;
RA   Schulze M., Roedel G.;
RT   "Accumulation of the cytochrome c oxidase subunits I and II in yeast
RT   requires a mitochondrial membrane-associated protein, encoded by the
RT   nuclear SCO1 gene.";
RL   Mol. Gen. Genet. 216:37-43(1989).
RN   [7]
RP   FUNCTION, AND SUBUNIT.
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   [8]
RP   TOPOLOGY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 208353 / W303-1A;
RX   PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA   Kim H., Melen K., Oesterberg M., von Heijne G.;
RT   "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
CC   -!- FUNCTION: Required for calcium regulation. May regulate calcium
CC       accumulation by a non-vacuole organelle. Also regulates the activity of
CC       CSH1 and SUR1 during mannosyl phosphorylinositol ceramide synthesis.
CC       {ECO:0000269|PubMed:12954640}.
CC   -!- SUBUNIT: Heterodimer of CSH1 and CSG2, and SUR1 and CSG2.
CC       {ECO:0000269|PubMed:12954640}.
CC   -!- INTERACTION:
CC       P35206; P38287: CSH1; NbExp=2; IntAct=EBI-2051140, EBI-20861;
CC       P35206; Q02774: SHR3; NbExp=3; IntAct=EBI-2051140, EBI-17099;
CC       P35206; P33300: SUR1; NbExp=2; IntAct=EBI-2051140, EBI-18569;
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:7854312}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:7854312}.
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; L24113; AAA34533.1; -; mRNA.
DR   EMBL; D28120; BAA05666.1; -; Genomic_DNA.
DR   EMBL; Z35905; CAA84978.1; -; Genomic_DNA.
DR   EMBL; X76078; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; X17441; CAA35491.1; -; Genomic_DNA.
DR   EMBL; BK006936; DAA07156.1; -; Genomic_DNA.
DR   PIR; S45894; S45894.
DR   RefSeq; NP_009592.1; NM_001178384.1.
DR   AlphaFoldDB; P35206; -.
DR   BioGRID; 32737; 981.
DR   ComplexPortal; CPX-1739; Mannosyl phosphorylinositol ceramide synthase SUR1-CSG2.
DR   ComplexPortal; CPX-1740; Mannosyl phosphorylinositol ceramide synthase CSH1-CSG2.
DR   DIP; DIP-8095N; -.
DR   FunCoup; P35206; 86.
DR   IntAct; P35206; 39.
DR   MINT; P35206; -.
DR   STRING; 4932.YBR036C; -.
DR   TCDB; 2.A.7.27.1; the drug/metabolite transporter (dmt) superfamily.
DR   GlyCosmos; P35206; 2 sites, No reported glycans.
DR   GlyGen; P35206; 2 sites.
DR   iPTMnet; P35206; -.
DR   PaxDb; 4932-YBR036C; -.
DR   PeptideAtlas; P35206; -.
DR   EnsemblFungi; YBR036C_mRNA; YBR036C; YBR036C.
DR   GeneID; 852324; -.
DR   KEGG; sce:YBR036C; -.
DR   AGR; SGD:S000000240; -.
DR   SGD; S000000240; CSG2.
DR   VEuPathDB; FungiDB:YBR036C; -.
DR   eggNOG; ENOG502QY2R; Eukaryota.
DR   HOGENOM; CLU_671228_0_0_1; -.
DR   InParanoid; P35206; -.
DR   OMA; WICEPTQ; -.
DR   OrthoDB; 4069151at2759; -.
DR   BioCyc; MetaCyc:MONOMER3O-695; -.
DR   BioCyc; YEAST:MONOMER3O-695; -.
DR   BioGRID-ORCS; 852324; 8 hits in 10 CRISPR screens.
DR   PRO; PR:P35206; -.
DR   Proteomes; UP000002311; Chromosome II.
DR   RNAct; P35206; protein.
DR   GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:SGD.
DR   GO; GO:0000324; C:fungal-type vacuole; HDA:SGD.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:ComplexPortal.
DR   GO; GO:0031501; C:mannosyltransferase complex; IDA:ComplexPortal.
DR   GO; GO:0030234; F:enzyme regulator activity; IMP:SGD.
DR   GO; GO:0015278; F:intracellularly gated calcium channel activity; IDA:SGD.
DR   GO; GO:0032469; P:endoplasmic reticulum calcium ion homeostasis; IMP:SGD.
DR   GO; GO:0006688; P:glycosphingolipid biosynthetic process; IMP:SGD.
DR   GO; GO:0006874; P:intracellular calcium ion homeostasis; IMP:SGD.
DR   GO; GO:0006676; P:mannosyl diphosphorylinositol ceramide metabolic process; IDA:ComplexPortal.
DR   GO; GO:1903514; P:release of sequestered calcium ion into cytosol by endoplasmic reticulum; IMP:SGD.
DR   InterPro; IPR031581; Csg2.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   Pfam; PF16965; CSG2; 1.
PE   1: Evidence at protein level;
KW   Endoplasmic reticulum; Glycoprotein; Membrane; Reference proteome; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..410
FT                   /note="Mannosyl phosphorylinositol ceramide synthase
FT                   regulatory protein CSG2"
FT                   /id="PRO_0000021012"
FT   TOPO_DOM        18..50
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        51..71
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        72..141
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        142..161
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        162..167
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        168..187
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        188..197
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        198..217
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        218..245
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        246..265
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        266..285
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        286..305
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        306..324
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        325..344
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        345..355
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        356..374
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        375..385
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        386..404
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        405..410
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        35
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        49
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        68
FT                   /note="L -> W (in Ref. 1; AAA34533)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   410 AA;  45442 MW;  15780FEBA54E4FD2 CRC64;
     MSTTLLWFSS VIGYVIQTKC LSNIQSKKEI SVGPNGTIAT PETNGDNGNS SSLTFYLTFM
     YFASWLLLVP ASRLWEKMRP MFVSDSDSNR NSQFDNNNSG SVTNEDVDTF SHVLDDPQPR
     IPAQQQKQKI ISVATFKYVA KLTVLALIMI VADLTYNMAL SLSPAFDVAL MQNTAIFEIV
     TLLYGVCGIS RKNYVFRNFL IMMNAVIGIL IISYTKATCD MLAGKLSVNP NTGELSDPFL
     FDRLKGALIC GLGALIMGPF AVLWNRWFCS NISKNENSAV VLVKQSTHMA LIGIIGMVIL
     LPFIPKFPSR ESVESISLFY NDKSFWFSLL GSIIFGSLPS LISILELNRK APAEYLTTCN
     LGAIIFMGLA EWVCEPTQTT IVRWEVIGYI MLTVSLLVLS VTLGEGKYHH
//