CSG2_YEAST
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 03-AUG-2022, entry version 157.
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 -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:7854312}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:7854312}.
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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; 973.
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 IntAct; P35206; 38.
DR MINT; P35206; -.
DR STRING; 4932.YBR036C; -.
DR TCDB; 2.A.7.27.1; the drug/metabolite transporter (dmt) superfamily.
DR iPTMnet; P35206; -.
DR PaxDb; P35206; -.
DR PRIDE; P35206; -.
DR EnsemblFungi; YBR036C_mRNA; YBR036C; YBR036C.
DR GeneID; 852324; -.
DR KEGG; sce:YBR036C; -.
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 BioCyc; MetaCyc:MON3O-695; -.
DR BioCyc; YEAST:MON3O-695; -.
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:0000324; C:fungal-type vacuole; HDA:SGD.
DR GO; GO:0005794; C:Golgi apparatus; IDA:ComplexPortal.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA:SGD.
DR GO; GO:0031501; C:mannosyltransferase complex; IDA:ComplexPortal.
DR GO; GO:0030234; F:enzyme regulator activity; IMP:SGD.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; 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 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
