ID   PALF_YEAST              Reviewed;         542 AA.
AC   P53179; D6VU94; P53180; Q9URQ4;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   21-JUN-2005, sequence version 2.
DT   27-MAR-2024, entry version 166.
DE   RecName: Full=pH-response regulator protein palF/RIM8;
DE   AltName: Full=Regulator of IME2 protein 8;
GN   Name=RIM8; Synonyms=PAL3; OrderedLocusNames=YGL045W; ORFNames=YGL046W;
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], AND FUNCTION.
RX   PubMed=10821185; DOI=10.1007/s004380051195;
RA   Treton B., Blanchin-Roland S., Lambert M., Lepingle A., Gaillardin C.;
RT   "Ambient pH signalling in ascomycetous yeasts involves homologues of the
RT   Aspergillus nidulans genes palF and palH.";
RL   Mol. Gen. Genet. 263:505-513(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9234674;
RX   DOI=10.1002/(sici)1097-0061(199707)13:9<861::aid-yea125>3.0.co;2-9;
RA   Feuermann M., de Montigny J., Potier S., Souciet J.-L.;
RT   "The characterization of two new clusters of duplicated genes suggests a
RT   'Lego' organization of the yeast Saccharomyces cerevisiae chromosomes.";
RL   Yeast 13:861-869(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169869;
RA   Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA   Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA   Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA   Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA   Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA   Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA   Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA   Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA   Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA   Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA   Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA   Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA   Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA   Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA   Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA   Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA   Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA   Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA   Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA   Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA   Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA   Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL   Nature 387:81-84(1997).
RN   [4]
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   [5]
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   [6]
RP   FUNCTION.
RX   PubMed=9017390; DOI=10.1093/genetics/145.1.63;
RA   Li W., Mitchell A.P.;
RT   "Proteolytic activation of Rim1p, a positive regulator of yeast sporulation
RT   and invasive growth.";
RL   Genetics 145:63-73(1997).
RN   [7]
RP   INDUCTION.
RX   PubMed=12509465; DOI=10.1128/mcb.23.2.677-686.2003;
RA   Lamb T.M., Mitchell A.P.;
RT   "The transcription factor Rim101p governs ion tolerance and cell
RT   differentiation by direct repression of the regulatory genes NRG1 and SMP1
RT   in Saccharomyces cerevisiae.";
RL   Mol. Cell. Biol. 23:677-686(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).
RN   [9]
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).
RN   [10]
RP   UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-521, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22106047; DOI=10.1002/pmic.201100166;
RA   Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT   "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL   Proteomics 12:236-240(2012).
CC   -!- FUNCTION: Required for the proteolytic cleavage of the transcriptional
CC       repressor RIM101 in response to alkaline ambient pH, which is necessary
CC       for sporulation and invasive growth. {ECO:0000269|PubMed:10821185,
CC       ECO:0000269|PubMed:9017390}.
CC   -!- INDUCTION: Expressed under acidic conditions and repressed by the
CC       processed, active form of RIM101 under alkaline conditions.
CC       {ECO:0000269|PubMed:12509465}.
CC   -!- MISCELLANEOUS: Present with 784 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the arrestin family. PalF/RIM8 subfamily.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA96748.1; Type=Frameshift; Evidence={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; AJ238650; CAB59334.1; -; Genomic_DNA.
DR   EMBL; Z72567; CAA96747.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; Z72568; CAA96748.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; AY693085; AAT93104.1; -; Genomic_DNA.
DR   EMBL; BK006941; DAA08055.1; -; Genomic_DNA.
DR   PIR; S64049; S64049.
DR   PIR; S64050; S64050.
DR   RefSeq; NP_011470.4; NM_001180910.3.
DR   AlphaFoldDB; P53179; -.
DR   BioGRID; 33203; 484.
DR   DIP; DIP-5115N; -.
DR   MINT; P53179; -.
DR   STRING; 4932.YGL045W; -.
DR   iPTMnet; P53179; -.
DR   MaxQB; P53179; -.
DR   PaxDb; 4932-YGL045W; -.
DR   PeptideAtlas; P53179; -.
DR   EnsemblFungi; YGL045W_mRNA; YGL045W; YGL045W.
DR   GeneID; 852837; -.
DR   KEGG; sce:YGL045W; -.
DR   AGR; SGD:S000003013; -.
DR   SGD; S000003013; RIM8.
DR   VEuPathDB; FungiDB:YGL045W; -.
DR   eggNOG; ENOG502QTQN; Eukaryota.
DR   HOGENOM; CLU_006001_1_0_1; -.
DR   InParanoid; P53179; -.
DR   OMA; QYYIEVL; -.
DR   OrthoDB; 1944514at2759; -.
DR   BioCyc; YEAST:G3O-30556-MONOMER; -.
DR   BioGRID-ORCS; 852837; 0 hits in 10 CRISPR screens.
DR   PRO; PR:P53179; -.
DR   Proteomes; UP000002311; Chromosome VII.
DR   RNAct; P53179; Protein.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0009898; C:cytoplasmic side of plasma membrane; IDA:SGD.
DR   GO; GO:0005829; C:cytosol; HDA:SGD.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0030674; F:protein-macromolecule adaptor activity; IBA:GO_Central.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IBA:GO_Central.
DR   GO; GO:0070086; P:ubiquitin-dependent endocytosis; IMP:SGD.
DR   Gene3D; 2.60.40.640; -; 2.
DR   InterPro; IPR014752; Arrestin-like_C.
DR   InterPro; IPR011021; Arrestin-like_N.
DR   InterPro; IPR011022; Arrestin_C-like.
DR   InterPro; IPR014756; Ig_E-set.
DR   PANTHER; PTHR11188; ARRESTIN DOMAIN CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR11188:SF161; PH-RESPONSE REGULATOR PROTEIN PALF_RIM8; 1.
DR   Pfam; PF02752; Arrestin_C; 1.
DR   Pfam; PF00339; Arrestin_N; 1.
DR   SMART; SM01017; Arrestin_C; 1.
DR   SUPFAM; SSF81296; E set domains; 1.
PE   1: Evidence at protein level;
KW   Isopeptide bond; Reference proteome; Ubl conjugation.
FT   CHAIN           1..542
FT                   /note="pH-response regulator protein palF/RIM8"
FT                   /id="PRO_0000058194"
FT   REGION          214..258
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          460..542
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        230..258
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        460..490
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        514..530
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CROSSLNK        521
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0007744|PubMed:22106047"
SQ   SEQUENCE   542 AA;  60864 MW;  5639227A1225ACC2 CRC64;
     MSLLRLWNKE SRAPSKIKSH GIVGSYGNSM LAHNNVKQFR IDIDEPHRVW KPNESITGEA
     VIDIKRDITN VAIKLSLVCE VRVKTGNSPT SKNKRIEKTL EKSTFLYGQD YVKTAFSAKE
     KKPHVDKTTI LNGLSKGEHR FPFRIRIPRG RGMLSSIKFE RGSITYFLSC TLESLNNING
     LKKPEARCER EFAVIVPLDV SRLPKPKTKT VVLQSASMVQ NKKNKSTEDE SSSYTQLTQK
     STTSNSSSSS VNSKTSPLPN KTVTISVDIP QAGFMIGEII PIDVKIDHYK PFYAPAGLTT
     TLVRICRVGG AGKDDPMETF RKDICQSISP IYINPETLQF QSRVYLKVPL DAFSTLTTVG
     KFFSFQYYIE VMVNLSKKNV VYTESNRIIG TPIGEQNGLG VENNINRIQR KMLRMVNPET
     LENDSEGYES SIFFKDMVNV EKLKRLRNVT GMSIETVIGT TRSEQQQSDA SIPSQSSITA
     PQNSPSNLRD WLAPLNAYDS DDVPVPKYSP NDKVSVPSED KQELEQKRLQ QLESDPPPCD
     DY
//