CSC1_YEAST
ID CSC1_YEAST Reviewed; 782 AA.
AC Q06538; D6VYN9;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Calcium permeable stress-gated cation channel 1;
DE Short=ScCSC1;
GN Name=CSC1; OrderedLocusNames=YLR241W;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
RN [2]
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 [3]
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).
RN [4]
RP FUNCTION, AND ACTIVITY REGULATION.
RX PubMed=24503647; DOI=10.1038/cr.2014.14;
RA Hou C., Tian W., Kleist T., He K., Garcia V., Bai F., Hao Y., Luan S.,
RA Li L.;
RT "DUF221 proteins are a family of osmosensitive calcium-permeable cation
RT channels conserved across eukaryotes.";
RL Cell Res. 24:632-635(2014).
CC -!- FUNCTION: Acts as an osmosensitive calcium-permeable cation channel.
CC {ECO:0000269|PubMed:24503647}.
CC -!- ACTIVITY REGULATION: Activated by hyperosmotic shock after mannitol
CC treatment. {ECO:0000269|PubMed:24503647}.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the CSC1 (TC 1.A.17) family. {ECO:0000305}.
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DR EMBL; U20865; AAB67395.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09555.1; -; Genomic_DNA.
DR PIR; S59387; S59387.
DR RefSeq; NP_013342.1; NM_001182128.1.
DR AlphaFoldDB; Q06538; -.
DR SMR; Q06538; -.
DR BioGRID; 31508; 47.
DR DIP; DIP-3791N; -.
DR IntAct; Q06538; 3.
DR MINT; Q06538; -.
DR STRING; 4932.YLR241W; -.
DR TCDB; 1.A.17.5.11; the calcium-dependent chloride channel (ca-clc) family.
DR iPTMnet; Q06538; -.
DR MaxQB; Q06538; -.
DR PaxDb; Q06538; -.
DR PRIDE; Q06538; -.
DR EnsemblFungi; YLR241W_mRNA; YLR241W; YLR241W.
DR GeneID; 850942; -.
DR KEGG; sce:YLR241W; -.
DR SGD; S000004231; CSC1.
DR VEuPathDB; FungiDB:YLR241W; -.
DR eggNOG; KOG1134; Eukaryota.
DR HOGENOM; CLU_002458_0_2_1; -.
DR InParanoid; Q06538; -.
DR OMA; QGIGMFP; -.
DR BioCyc; YEAST:G3O-32348-MON; -.
DR PRO; PR:Q06538; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q06538; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0000329; C:fungal-type vacuole membrane; HDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005227; F:calcium activated cation channel activity; IDA:UniProtKB.
DR GO; GO:0006812; P:cation transport; IDA:UniProtKB.
DR InterPro; IPR045122; Csc1-like.
DR InterPro; IPR032880; Csc1_N.
DR InterPro; IPR027815; PHM7_cyt.
DR InterPro; IPR003864; RSN1_7TM.
DR PANTHER; PTHR13018; PTHR13018; 1.
DR Pfam; PF14703; PHM7_cyt; 1.
DR Pfam; PF02714; RSN1_7TM; 1.
DR Pfam; PF13967; RSN1_TM; 1.
PE 1: Evidence at protein level;
KW Calcium; Glycoprotein; Ion channel; Ion transport; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..782
FT /note="Calcium permeable stress-gated cation channel 1"
FT /id="PRO_0000247173"
FT TOPO_DOM 1..34
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 35..55
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 56..116
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 117..139
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 140..181
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 182..202
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 203..440
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 441..461
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 462..485
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 486..506
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 507..530
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 531..551
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 552..578
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 579..599
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 600..621
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 622..642
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 643..648
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 649..669
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 670..681
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 682..702
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 703..709
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 710..730
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 731..782
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 171
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 782 AA; 89344 MW; 7DFD926B98FA15DA CRC64;
MTSYIERLKS AASYLDTVPD EHHDFRKPTA KVVTTQLTIA TSLGIFALLS FSILLKKWPR
LYASRRYKDD GNLRLPSWNQ SSLFGWLTVL YKIRDEQILE YAGLDAYVFL SFFKMCIKLL
SIFCFFSVCV ISPVRYHFTG KIDDGNDDDD SESSLIHLVK RIVEGSGDGD NHSAPERTNV
YLWMYVLFTY FFTFIAIKMA VAETKHVVST RQAYLGKQNT ITDRTIRLSG IPIELRDSEA
LKTRIEQLKI GTVSSITICR EWGPLNKLFH CRKKILKNLE LKYSECPREL RTRQPYSENY
HLLGNEQSGA VTHGENVPSS NNNDEDTILY SQISLGERPK MKIGYRGIFG KEVDAIEYLE
QQLKFIDAEI IEARKQHYSA TPTAFVTMDS VANAQMAAQA VLDPRVHYFI TRLAPAPHDI
KWDHVCLSRK DRLTKVYSTT VFIGLSSLFL VIPVSYLATL LNLKTLSKFW PSVGQLLKDH
QWAANIVTGL LPTYLFTLLN FGIPYFYEYL TSYQGLVSYS EEEISLVSKN FFYIFVNLFL
VFTLAGTASN YWAYLSDTTK IAYQLATSVK EFSLFYVDLI ILQGIGMFPF KLLLVGSLIG
FPLVKIKAKT PRQRNELYNP PIFNFGLQLP QPILILIITL IYSVMSTKIL TSGLAYFIIG
FYVYKYQLIF ATDHLPHSTG KVWPLIFRRI IVGLLLFQLT MTGTLAGFEG GWVLSSCLFP
LPVVTLCFLY DFEKNYLPLS KYIALSSIRE YERDNSTVNS ANEEESYAYP YAVSELEGPM
LD
