PALF_YEAST
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 03-AUG-2022, entry version 158.
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};
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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; 474.
DR DIP; DIP-5115N; -.
DR MINT; P53179; -.
DR STRING; 4932.YGL045W; -.
DR iPTMnet; P53179; -.
DR MaxQB; P53179; -.
DR PaxDb; P53179; -.
DR PRIDE; P53179; -.
DR EnsemblFungi; YGL045W_mRNA; YGL045W; YGL045W.
DR GeneID; 852837; -.
DR KEGG; sce:YGL045W; -.
DR SGD; S000003013; RIM8.
DR VEuPathDB; FungiDB:YGL045W; -.
DR eggNOG; ENOG502QTQN; Eukaryota.
DR HOGENOM; CLU_006001_1_0_1; -.
DR InParanoid; P53179; -.
DR OMA; YEDYYPK; -.
DR BioCyc; YEAST:G3O-30556-MON; -.
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:0001403; P:invasive growth in response to glucose limitation; IMP:SGD.
DR GO; GO:0051321; P:meiotic cell cycle; IMP:SGD.
DR GO; GO:0016485; P:protein processing; IMP:SGD.
DR GO; GO:0015031; P:protein transport; 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 Pfam; PF02752; Arrestin_C; 1.
DR Pfam; PF00339; Arrestin_N; 1.
DR SMART; SM01017; Arrestin_C; 1.
DR SUPFAM; SSF81296; SSF81296; 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
