RSN1_YEAST
ID RSN1_YEAST Reviewed; 953 AA.
AC Q03516; D6W092;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Uncharacterized protein RSN1;
DE AltName: Full=Rescuer of SRO7 at high Nacl protein 1;
GN Name=RSN1; OrderedLocusNames=YMR266W; ORFNames=YM8156.08;
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 GENE NAME.
RX PubMed=17005914; DOI=10.1091/mbc.e05-08-0798;
RA Wadskog I., Forsmark A., Rossi G., Konopka C., Oyen M., Goksor M.,
RA Ronne H., Brennwald P., Adler L.;
RT "The yeast tumor suppressor homologue Sro7p is required for targeting of
RT the sodium pumping ATPase to the cell surface.";
RL Mol. Biol. Cell 17:4988-5003(2006).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-949, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [5]
RP IDENTIFICATION BY 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).
CC -!- FUNCTION: Acts as an osmosensitive calcium-permeable cation channel.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the CSC1 (TC 1.A.17) family. {ECO:0000305}.
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DR EMBL; Z49260; CAA89249.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA10166.1; -; Genomic_DNA.
DR PIR; S54478; S54478.
DR RefSeq; NP_013993.1; NM_001182773.1.
DR AlphaFoldDB; Q03516; -.
DR SMR; Q03516; -.
DR BioGRID; 35444; 45.
DR DIP; DIP-6549N; -.
DR IntAct; Q03516; 4.
DR MINT; Q03516; -.
DR STRING; 4932.YMR266W; -.
DR iPTMnet; Q03516; -.
DR MaxQB; Q03516; -.
DR PaxDb; Q03516; -.
DR PRIDE; Q03516; -.
DR EnsemblFungi; YMR266W_mRNA; YMR266W; YMR266W.
DR GeneID; 855308; -.
DR KEGG; sce:YMR266W; -.
DR SGD; S000004879; RSN1.
DR VEuPathDB; FungiDB:YMR266W; -.
DR eggNOG; KOG1134; Eukaryota.
DR HOGENOM; CLU_002458_2_1_1; -.
DR InParanoid; Q03516; -.
DR OMA; TQVIWSN; -.
DR BioCyc; YEAST:G3O-32940-MON; -.
DR PRO; PR:Q03516; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; Q03516; protein.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
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:0016020; C:membrane; IDA:SGD.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005227; F:calcium activated cation channel activity; IBA:GO_Central.
DR InterPro; IPR045122; Csc1-like.
DR InterPro; IPR032880; Csc1_N.
DR InterPro; IPR027815; PHM7_cyt.
DR InterPro; IPR022257; PHM7_ext.
DR InterPro; IPR003864; RSN1_7TM.
DR PANTHER; PTHR13018; PTHR13018; 1.
DR Pfam; PF14703; PHM7_cyt; 1.
DR Pfam; PF12621; PHM7_ext; 1.
DR Pfam; PF02714; RSN1_7TM; 1.
DR Pfam; PF13967; RSN1_TM; 1.
PE 1: Evidence at protein level;
KW Calcium; Ion channel; Ion transport; Membrane; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..953
FT /note="Uncharacterized protein RSN1"
FT /id="PRO_0000203348"
FT TRANSMEM 23..43
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 103..123
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 148..168
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 392..412
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 435..455
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 481..501
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 540..560
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 575..595
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 599..619
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 642..662
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 666..686
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 910..953
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 939..953
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 949
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
SQ SEQUENCE 953 AA; 107673 MW; F6F7BA2B3F3AD44B CRC64;
MNSTNSTNST TTATSTNTST QQVVTSLVSN GTIFGVFVIA FLILRIKLKR IYEPKSSFNL
INEEKKPEPL PQGVWQWLKP LLKKSDNFVI QQAGLDGYFF LRYLFIIAIY CAVSMSYIFP
ILLSINASNG NHESGLNQLA YQNVKHRGRY FAHVFCGWIF FWGFLYIIYR ELYFYTSMKQ
AVLASPRYAK KLSSRTVLFQ TVPKQYLSEE EFSKLFDGVK RVWIARGSGS IEAMVKARDN
MAIQLEGAET KYLKAALKKI KKLNKKSPQL SVSDNIAEYV PDKKRPHHKI NKVAKFFFGK
KVDTISYIKE ELPKLNQKVK ALQEDHENSS PFNSVFVEFE SQYQAQVAAQ ITTYHAPLFM
TPVYIGIEPS DVVWFNLRMF WWERLGREVS AVSAIVALVI LWAFPVAFVG MISNITSLTN
EVKWLKFIYK LPKQLLGLLT SLAPTVALAV LMSFLPKFIR GMAITQGAPS KQNVEYFTQQ
AYFAFQVIQV FLVTTLSSAA TSTVTEIVKE PTKAMDLLAS NLPKASNFFM SYVILQGLSI
SSGALLQIVP LILFYVLGAF LDGTVRKKWN RFCGLSSMQW GTAFPVYTNL AVITFSYSII
SPLILLFAAV AFFLLYIAYL YNLTYVYQES PDARGIYYPR ALFQTIVGIY IGQICLLGLF
AVGKGWGPIV LQVIGICVTV LIHLHLSAAF DHLSKVIPVD TMKPLDGVSD TPSFKNIYKG
IESTKVKKNT FGANIDMDGI KELPEFPIKK YHKRSESVTE QQVENSIFSE NTFEYQFNPA
NEANADGHAI NAENLIEDVP LLADGDTMKI PPAPWWKRFL KPHIYYSYKA VKSRLPEIYG
LVDPDERVND FDISHAYDYP AVSAQCPELW IPRDPFGFSK LLISDVSGVV EMNDENATID
ENLKFTLRDV PPPYNDVKDE ANGEANGEFD TASKENNPFA DPKYKEEESR SAV
