RCH1_YEAST
ID RCH1_YEAST Reviewed; 434 AA.
AC Q05131; D6VZK9;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Solute carrier RCH1 {ECO:0000303|PubMed:26832117};
DE AltName: Full=Regulator of calcium homeostasis 1 {ECO:0000303|PubMed:26832117};
GN Name=RCH1 {ECO:0000303|PubMed:26832117}; OrderedLocusNames=YMR034C;
GN ORFNames=YM9973.08C;
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=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(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 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 [4]
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-425, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [6]
RP FUNCTION, INDUCTION, AND SUBCELLULAR LOCATION.
RX PubMed=26832117; DOI=10.1016/j.ejcb.2016.01.001;
RA Zhao Y., Yan H., Happeck R., Peiter-Volk T., Xu H., Zhang Y., Peiter E.,
RA van Oostende Triplet C., Whiteway M., Jiang L.;
RT "The plasma membrane protein Rch1 is a negative regulator of cytosolic
RT calcium homeostasis and positively regulated by the calcium/calcineurin
RT signaling pathway in budding yeast.";
RL Eur. J. Cell Biol. 95:164-174(2016).
CC -!- FUNCTION: Solute carrier protein that negatively regulates the
CC cytosolic calcium homeostasis in response to high levels of
CC extracellular calcium. {ECO:0000269|PubMed:26832117}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26832117};
CC Multi-pass membrane protein {ECO:0000255}. Bud neck
CC {ECO:0000269|PubMed:26832117}. Note=Distributes as multiple foci in the
CC plasma membrane prior to cell division, moves toward and concentrates
CC at the bud neck as the bud grows in size, and disperses again along the
CC plasma membrane immediately prior to cytokinesis.
CC {ECO:0000269|PubMed:26832117}.
CC -!- INDUCTION: Expression is positively regulated by calcium/calcineurin
CC signaling through the sole CDRE element (5'-TTAGCCTC-3') in its
CC promoter. {ECO:0000269|PubMed:26832117}.
CC -!- SIMILARITY: Belongs to the bile acid:sodium symporter (BASS) (TC
CC 2.A.28) family. {ECO:0000305}.
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DR EMBL; Z49213; CAA89150.1; -; Genomic_DNA.
DR EMBL; AY692713; AAT92732.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA09933.1; -; Genomic_DNA.
DR PIR; S53951; S53951.
DR RefSeq; NP_013748.1; NM_001182531.1.
DR AlphaFoldDB; Q05131; -.
DR BioGRID; 35206; 87.
DR MINT; Q05131; -.
DR STRING; 4932.YMR034C; -.
DR iPTMnet; Q05131; -.
DR PaxDb; Q05131; -.
DR PRIDE; Q05131; -.
DR EnsemblFungi; YMR034C_mRNA; YMR034C; YMR034C.
DR GeneID; 855050; -.
DR KEGG; sce:YMR034C; -.
DR SGD; S000004637; RCH1.
DR VEuPathDB; FungiDB:YMR034C; -.
DR eggNOG; KOG4821; Eukaryota.
DR GeneTree; ENSGT00390000011932; -.
DR HOGENOM; CLU_039013_3_0_1; -.
DR InParanoid; Q05131; -.
DR OMA; FFFYGLK; -.
DR BioCyc; YEAST:G3O-32739-MON; -.
DR PRO; PR:Q05131; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; Q05131; protein.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
DR GO; GO:0005935; C:cellular bud neck; IDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR GO; GO:0008028; F:monocarboxylic acid transmembrane transporter activity; ISA:SGD.
DR GO; GO:0006816; P:calcium ion transport; IEA:UniProtKB-KW.
DR GO; GO:0051481; P:negative regulation of cytosolic calcium ion concentration; IGI:SGD.
DR Gene3D; 1.20.1530.20; -; 1.
DR InterPro; IPR038770; Na+/solute_symporter_sf.
DR InterPro; IPR016833; Put_Na-Bile_cotransptr.
DR PANTHER; PTHR18640; PTHR18640; 1.
DR Pfam; PF13593; SBF_like; 1.
DR PIRSF; PIRSF026166; UCP026166; 1.
PE 1: Evidence at protein level;
KW Calcium; Calcium transport; Cell membrane; Ion transport; Membrane;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..434
FT /note="Solute carrier RCH1"
FT /id="PRO_0000203274"
FT TOPO_DOM 1..15
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 16..36
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 37..50
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 51..71
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 72..87
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 88..108
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 109..118
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 119..139
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 140..149
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 150..170
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 171..199
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 200..220
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 221..234
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 235..255
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 256..264
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 265..285
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 286..327
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 328..348
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 349..362
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 363..383
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 384..434
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 425
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 434 AA; 48375 MW; 80922AC8D1BEE433 CRC64;
MKTQYSLIRK IWAHSVTEFL KSQWFFICLA ILIVIARFAP NFARDGGLIK GQYSIGYGCV
AWIFLQSGLG MKSRSLMANM LNWRAHATIL VLSFLITSSI VYGFCCAVKA ANDPKIDDWV
LIGLILTATC PTTVASNVIM TTNAGGNSLL CVCEVFIGNL LGAFITPALV QMFTNRAPFA
YGNPATGNGI GALYGRVMKQ VGLSVFVPLF VGQVIQNCFP KGTAYYLGFL KKYHIKIGSY
MLLLIMFSSF STAFYQDAFT SVSHVCIIFL CFFNLGIYIF FTGLSYLCAR PWFILKLFPH
EPIEGKSTRL YRYSYNIFRP FYYSKEDAIC IMFCGPAKTA ALGVSLITSQ YGDKKEHLGK
LLVPLVLYQV EQVMTANFFV SLFKRWIQKD AQADGSESSC ANENEEVDLE KIISIGTGEN
QSVLSNNVPY TQPR
