RGC1_YEAST
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 03-AUG-2022, entry version 145.
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; 100.
DR DIP; DIP-1970N; -.
DR IntAct; Q06108; 32.
DR MINT; Q06108; -.
DR STRING; 4932.YPR115W; -.
DR iPTMnet; Q06108; -.
DR MaxQB; Q06108; -.
DR PaxDb; Q06108; -.
DR PRIDE; Q06108; -.
DR EnsemblFungi; YPR115W_mRNA; YPR115W; YPR115W.
DR GeneID; 856231; -.
DR KEGG; sce:YPR115W; -.
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 BioCyc; YEAST:G3O-34254-MON; -.
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; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR SMART; SM00233; PH; 1.
DR SUPFAM; SSF103657; SSF103657; 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
