ID   RGC1_YEAST              Reviewed;        1083 AA.
AC   Q06108; D6W4B4;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 151.
DE   RecName: Full=Regulator of the glycerol channel 1;
GN   Name=RGC1; OrderedLocusNames=YPR115W;
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=9169875;
RA   Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA   Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA   Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA   Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA   DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA   Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA   Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA   Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA   Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA   Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA   Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA   Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA   Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA   Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA   Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA   Vo D.H., Hani J.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL   Nature 387:103-105(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   FUNCTION.
RX   PubMed=12829295; DOI=10.1016/s0378-1097(03)00384-7;
RA   Zettel M.F., Garza L.R., Cass A.M., Myhre R.A., Haizlip L.A., Osadebe S.N.,
RA   Sudimack D.W., Pathak R., Stone T.L., Polymenis M.;
RT   "The budding index of Saccharomyces cerevisiae deletion strains identifies
RT   genes important for cell cycle progression.";
RL   FEMS Microbiol. Lett. 223:253-258(2003).
RN   [4]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
RN   [5]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [6]
RP   SUBCELLULAR LOCATION.
RX   PubMed=15023338; DOI=10.1016/s1097-2765(04)00083-8;
RA   Yu J.W., Mendrola J.M., Audhya A., Singh S., Keleti D., DeWald D.B.,
RA   Murray D., Emr S.D., Lemmon M.A.;
RT   "Genome-wide analysis of membrane targeting by S.cerevisiae pleckstrin
RT   homology domains.";
RL   Mol. Cell 13:677-688(2004).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-481, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ADR376;
RX   PubMed=17330950; DOI=10.1021/pr060559j;
RA   Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA   Elias J.E., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of alpha-factor-arrested
RT   Saccharomyces cerevisiae.";
RL   J. Proteome Res. 6:1190-1197(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-481; SER-652; THR-817;
RP   SER-866; SER-918 AND SER-1059, AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth phosphoproteome
RT   analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
RN   [9]
RP   FUNCTION.
RX   PubMed=19956799; DOI=10.1371/journal.pgen.1000738;
RA   Beese S.E., Negishi T., Levin D.E.;
RT   "Identification of positive regulators of the yeast fps1 glycerol
RT   channel.";
RL   PLoS Genet. 5:E1000738-E1000738(2009).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-136; SER-249; SER-252;
RP   SER-481; SER-537; SER-652; SER-765; SER-813; THR-817; THR-857; SER-866;
RP   SER-879; SER-966; SER-969; SER-975; SER-1059; SER-1081 AND SER-1082, AND
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: Positive regulator of FPS1 glycerol channel required for the
CC       glycerol efflux. {ECO:0000269|PubMed:12829295,
CC       ECO:0000269|PubMed:19956799}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095,
CC       ECO:0000269|PubMed:15023338}.
CC   -!- MISCELLANEOUS: Present with 300 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- MISCELLANEOUS: Does not bind efficiently to phosphoinositides and does
CC       not associate with membranes.
CC   -!- SIMILARITY: Belongs to the RGC1 family. {ECO:0000305}.
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DR   EMBL; U32445; AAB68085.1; -; Genomic_DNA.
DR   EMBL; BK006949; DAA11530.1; -; Genomic_DNA.
DR   PIR; S59780; S59780.
DR   RefSeq; NP_015440.1; NM_001184212.1.
DR   AlphaFoldDB; Q06108; -.
DR   BioGRID; 36282; 120.
DR   DIP; DIP-1970N; -.
DR   IntAct; Q06108; 32.
DR   MINT; Q06108; -.
DR   STRING; 4932.YPR115W; -.
DR   GlyGen; Q06108; 7 sites, 1 O-linked glycan (7 sites).
DR   iPTMnet; Q06108; -.
DR   MaxQB; Q06108; -.
DR   PaxDb; 4932-YPR115W; -.
DR   PeptideAtlas; Q06108; -.
DR   EnsemblFungi; YPR115W_mRNA; YPR115W; YPR115W.
DR   GeneID; 856231; -.
DR   KEGG; sce:YPR115W; -.
DR   AGR; SGD:S000006319; -.
DR   SGD; S000006319; RGC1.
DR   VEuPathDB; FungiDB:YPR115W; -.
DR   eggNOG; ENOG502QU0Q; Eukaryota.
DR   GeneTree; ENSGT00940000176324; -.
DR   HOGENOM; CLU_008754_0_0_1; -.
DR   InParanoid; Q06108; -.
DR   OrthoDB; 2039746at2759; -.
DR   BioCyc; YEAST:G3O-34254-MONOMER; -.
DR   BioGRID-ORCS; 856231; 2 hits in 10 CRISPR screens.
DR   PRO; PR:Q06108; -.
DR   Proteomes; UP000002311; Chromosome XVI.
DR   RNAct; Q06108; Protein.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0016247; F:channel regulator activity; ISS:SGD.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0090372; P:positive regulation of glycerol transport; IMP:SGD.
DR   Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   InterPro; IPR027267; AH/BAR_dom_sf.
DR   InterPro; IPR046868; BAR_4.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR046869; SLM1/RGC1-like_PH.
DR   PANTHER; PTHR31941:SF1; ACTIVATOR OF SKN7 PROTEIN 10-RELATED; 1.
DR   PANTHER; PTHR31941; CYTOSKELETAL SIGNALING PROTEIN SLM1; 1.
DR   Pfam; PF20400; BAR_4; 1.
DR   Pfam; PF20399; PH_20; 1.
DR   SMART; SM00233; PH; 1.
DR   SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
PE   1: Evidence at protein level;
KW   Cell cycle; Cytoplasm; Phosphoprotein; Reference proteome.
FT   CHAIN           1..1083
FT                   /note="Regulator of the glycerol channel 1"
FT                   /id="PRO_0000242488"
FT   DOMAIN          495..606
FT                   /note="PH"
FT   REGION          1..46
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          69..89
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          534..582
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          979..1083
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..35
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        70..84
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        544..570
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        979..994
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1015..1029
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1044..1061
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1069..1083
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         136
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         249
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         252
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         481
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT   MOD_RES         537
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         652
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         765
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         813
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         817
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:18407956,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         857
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         866
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         879
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         918
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MOD_RES         966
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         969
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         975
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         1059
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         1081
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         1082
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
SQ   SEQUENCE   1083 AA;  120395 MW;  28D63D32843BFE08 CRC64;
     MSDYFTFPKQ ENGGISKQPA TPGSTRSSSR NLELPKNYRS FGGSSDELAS MYSADSQYLM
     DMIPDSLTLK NEPASGNTQM NGPDGKENKD IKLDEYILPK TDPRSPYYIN MPIPKKLPKS
     EGKARAKQKV NRADPSDLDV ENIYETSGEF VREYPTDILI DRFHKWKKIL KSLIAYFREA
     AYSQEQIARI NYQMKNAVKF AFLTDLEDET NKLVDPSISK LPTKKPQPVP LAAQKLDSKY
     DTDVEQPQSI QSVPSEEVAS ASSGFMKFGS GSIQDIQVIL KKYHLSLGSQ QYKISKEILA
     YIIPKLTDLR KDLTTKMKEI KELNGDFKTN IGEHIKITSR LLNKYIASVK LLDEASTSGD
     KQGEKLKPKH DPYLLKLQLD LQLKRQLLEE NYLREAFLNL QSAALQLEKI VYSKIQSALQ
     RYSALIDSEA RLMIKNLCHE LQQGILSRPP AVEWDNFVSH HPTCLMNLKS TDPPPQPRRL
     SDIVYPNMKS PLAKCIRVGY LLKKTESSKS FTKGYFVLTT NYLHEFKSSD FFLDSKSPRS
     KNKPVVEQSD ISRVNKDGTN AGSHPSSKGT QDPKLTKRRK GLSSSNLYPI SSLSLNDCSL
     KDSTDSTFVL QGYASYHSPE DTCTKESSTT SDLACPTKTL ASNKGKHQRT PSALSMVSVP
     KFLKSSSVPK EQKKAKEEAN INKKSICEKR VEWTFKIFSA SLEPTPEESK NFKKWVQDIK
     ALTSFNSTQE RSNFIEEKIL KSRNHNNGKS SQRSKNSTYI TPVDSFVNLS EKVTPSSSVT
     TLNTRKRANR PRYIDIPKSA NMNAGAMNSV YRSKVNTPAI DENGNLAIVG ETKNSAPQNG
     MSYTIRTPCK SPYSPYTGEG MLYNRSADNL MASSSRKASA PGEVPQIAVS NHGDEAIIPA
     SAYSDSSHKS SRASSVASIH NQRVDFYPSP LMNLPGVSPS CLALDGNANG YFGIPLNCNS
     EARRGSDLSP FEMESPLFEE NRTQNCSGSR KSSACHIPHQ CGPRKEGNDS RLIYGNEKGA
     SQSRLTLKEP LTSKGVEAPY SSLKKTYSAE NVPLTSTVSN DKSLHSRKEG STNTVPATSA
     SSK
//