RIC1_YEAST
ID RIC1_YEAST Reviewed; 1056 AA.
AC P40395; D6VY42;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Guanine nucleotide exchange factor subunit RIC1 {ECO:0000305};
DE AltName: Full=Protein RIC1;
DE AltName: Full=Ribosome control protein 1;
DE Short=Ric1p {ECO:0000303|PubMed:10990452};
GN Name=RIC1 {ECO:0000312|SGD:S000004029}; OrderedLocusNames=YLR039C;
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 [GENOMIC DNA].
RA Mizuta K.;
RL Submitted (DEC-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
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 [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH RGP1.
RX PubMed=10990452; DOI=10.1093/emboj/19.18.4885;
RA Siniossoglou S., Peak-Chew S.Y., Pelham H.R.B.;
RT "Ric1p and Rgp1p form a complex that catalyses nucleotide exchange on
RT Ypt6p.";
RL EMBO J. 19:4885-4894(2000).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11689439; DOI=10.1093/emboj/20.21.5991;
RA Siniossoglou S., Pelham H.R.B.;
RT "An effector of Ypt6p binds the SNARE Tlg1p and mediates selective fusion
RT of vesicles with late Golgi membranes.";
RL EMBO J. 20:5991-5998(2001).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11160819; DOI=10.1091/mbc.12.1.13;
RA Bensen E.S., Yeung B.G., Payne G.S.;
RT "Ric1p and the Ypt6p GTPase function in a common pathway required for
RT localization of trans-Golgi network membrane proteins.";
RL Mol. Biol. Cell 12:13-26(2001).
RN [7]
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 [8]
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).
CC -!- FUNCTION: The RIC1-RGP1 complex acts as a guanine nucleotide exchange
CC factor (GEF), which activates YPT6 by exchanging bound GDP for free
CC GTP. It is thereby required for efficient fusion of endosome-derived
CC vesicles with the Golgi. The RIC1-RGP1 participates in the recycling of
CC SNC1, presumably by mediating fusion of endosomal vesicles with the
CC Golgi compartment. May also be indirectly involved in the transcription
CC of both ribosomal protein genes and ribosomal RNA.
CC {ECO:0000269|PubMed:10990452, ECO:0000269|PubMed:11160819,
CC ECO:0000269|PubMed:11689439}.
CC -!- SUBUNIT: Forms a complex with RGP1. {ECO:0000269|PubMed:10990452}.
CC -!- INTERACTION:
CC P40395; P16664: RGP1; NbExp=4; IntAct=EBI-15183, EBI-15080;
CC P40395; Q99260: YPT6; NbExp=3; IntAct=EBI-15183, EBI-29503;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:10990452, ECO:0000269|PubMed:11160819,
CC ECO:0000269|PubMed:11689439, ECO:0000269|PubMed:14562095}; Peripheral
CC membrane protein {ECO:0000269|PubMed:10990452,
CC ECO:0000269|PubMed:11160819, ECO:0000269|PubMed:11689439,
CC ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 78 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the RIC1 family. Highly divergent.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D43895; BAA07866.1; -; Genomic_DNA.
DR EMBL; Z73211; CAA97567.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09358.1; -; Genomic_DNA.
DR PIR; S56039; S56039.
DR RefSeq; NP_013140.1; NM_001181926.1.
DR AlphaFoldDB; P40395; -.
DR BioGRID; 31315; 1049.
DR ComplexPortal; CPX-3078; Ric1-Rgp1 guanyl-nucleotide exchange factor complex.
DR DIP; DIP-2564N; -.
DR IntAct; P40395; 11.
DR MINT; P40395; -.
DR STRING; 4932.YLR039C; -.
DR iPTMnet; P40395; -.
DR MaxQB; P40395; -.
DR PaxDb; P40395; -.
DR PRIDE; P40395; -.
DR EnsemblFungi; YLR039C_mRNA; YLR039C; YLR039C.
DR GeneID; 850728; -.
DR KEGG; sce:YLR039C; -.
DR SGD; S000004029; RIC1.
DR VEuPathDB; FungiDB:YLR039C; -.
DR eggNOG; KOG2006; Eukaryota.
DR HOGENOM; CLU_325467_0_0_1; -.
DR InParanoid; P40395; -.
DR OMA; WDMCFQL; -.
DR BioCyc; YEAST:G3O-32197-MON; -.
DR Reactome; R-SCE-6811440; Retrograde transport at the Trans-Golgi-Network.
DR Reactome; R-SCE-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR PRO; PR:P40395; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; P40395; protein.
DR GO; GO:0005801; C:cis-Golgi network; IDA:SGD.
DR GO; GO:0005829; C:cytosol; HDA:SGD.
DR GO; GO:0005794; C:Golgi apparatus; IDA:ComplexPortal.
DR GO; GO:0000139; C:Golgi membrane; IDA:SGD.
DR GO; GO:0032045; C:guanyl-nucleotide exchange factor complex; IDA:SGD.
DR GO; GO:0034066; C:Ric1-Rgp1 guanyl-nucleotide exchange factor complex; IPI:SGD.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR GO; GO:0006886; P:intracellular protein transport; IMP:SGD.
DR GO; GO:0043087; P:regulation of GTPase activity; IDA:ComplexPortal.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IMP:SGD.
DR InterPro; IPR009771; Ribosome_control_1.
DR InterPro; IPR040096; Ric1.
DR PANTHER; PTHR22746; PTHR22746; 1.
DR Pfam; PF07064; RIC1; 1.
PE 1: Evidence at protein level;
KW Golgi apparatus; Guanine-nucleotide releasing factor; Membrane;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..1056
FT /note="Guanine nucleotide exchange factor subunit RIC1"
FT /id="PRO_0000097332"
SQ SEQUENCE 1056 AA; 121650 MW; 2368616B67AEAD31 CRC64;
MFIKQSEKNT PKCLYKKKGK VRVLLTGSCK KLNTWKMHLW PVSPPQLLRI PPRNAELGEG
TKIDDCNILQ SMTLPQANVL IMLTPTRVLI YNFKPMALVA SHERTMASLK EFGDNRSMKR
SAPYNDIIEG LISKKDSQYL LWHQGKLIFY VMTDKNFLLT YQILKNCTNE IIFKEYGIPV
IEPLLMSEEE ANSAEYDYNN DDDTLTVFDK NSSSRIIQNG FGITKEKGFL HFLSNQENID
ELPVKKLELR LKVVLKFDYE IIDMIGIKTF SKVGDGRYEE VLIVLFPHGL QILTISDFKV
SKSSLVEVKK GSKTIVCNKQ LMVLSHDSVE KQTIVSIIDI EKQAVEAIPL TDTPDELLTC
LEVNGYLVVV YKEKIICFDT RIKKVSHSWK PPFVIKLCDK INDKILLLVS EDSVNIHFYT
EFGNLLFATY FDEDDYNGDN NNDNSKDKNE KKAAEYKISD FVCLDKSLIT VSHSGKYQVW
KLWEEIKQTQ FDFRNPKCYV LTNTNNDVII YSPVTSSSIN NDNLQVIKLP TKTFNNHIAF
VKINSSLRLF ATYVSNKNIL LIHNLETNMW SSFADQNVLD LHWLGDNYLV CHMKNDDGST
NLKCLQIPLQ EANPDVELSD YVMWEYNVPE NTIVFSLHVN TLSRYKLLKM KSKNHNASEK
QPDALLKTAE IILVTDTQTI VFDVISTVHP CGLNIIKKFY QYLKINIPID VLPNKIEWII
NMKEGLLFFA DRKFIKLGKV DGGGWQTLTL LDNIEKIIDV IRDEIFVVQG HNYVVYSLED
LWDDKKPLVS IPIEEDLYPI STTPETATTH TLHCIFNARF SKLVVKHQIY LDQLILAKLE
DNTDLEDISH NYRFLKPYKF ALEKILSTKI LRSDSLDDIL KLIKMYDNTD PEHNISPPTH
SGMLEIISNC LRKIETKYWN HLFTNLKMTP RDLLALCIEE NEAKMLGVLL LVFLNYDEKD
LGDDLHFKKS DLGTEESKAL NDNSTKKSEK SVTNLLKDEE LMLKVLELLV TSAANATDPI
KATDSWDMCF QLIRLLKELD RENNTQLVQK ALERFK
