PALA_YEAST
ID PALA_YEAST Reviewed; 661 AA.
AC Q12033; D6W2X5;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=pH-response regulator protein palA/RIM20;
DE AltName: Full=Regulator of IME2 protein 20;
GN Name=RIM20; OrderedLocusNames=YOR275C;
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].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8896271;
RX DOI=10.1002/(sici)1097-0061(199609)12:10b%3c1059::aid-yea994%3e3.0.co;2-7;
RA Cheret G., Bernardi A., Sor F.J.;
RT "DNA sequence analysis of the VPH1-SNF2 region on chromosome XV of
RT Saccharomyces cerevisiae.";
RL Yeast 12:1059-1064(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(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, INTERACTION WITH RIM101, AND MUTAGENESIS OF 292-ASP-ASN-293.
RX PubMed=11698381; DOI=10.1128/jb.183.23.6917-6923.2001;
RA Xu W., Mitchell A.P.;
RT "Yeast PalA/AIP1/Alix homolog Rim20p associates with a PEST-like region and
RT is required for its proteolytic cleavage.";
RL J. Bacteriol. 183:6917-6923(2001).
RN [5]
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 [6]
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 [7]
RP INTERACTION WITH SNF7.
RX PubMed=15371534; DOI=10.1091/mbc.e04-08-0666;
RA Xu W., Smith F.J. Jr., Subaran R., Mitchell A.P.;
RT "Multivesicular body-ESCRT components function in pH response regulation in
RT Saccharomyces cerevisiae and Candida albicans.";
RL Mol. Biol. Cell 15:5528-5537(2004).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(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. May act as a scaffold protein that
CC recruits the calpain-like protease RIM13 via SNF7 to its substrate
CC RIM101. {ECO:0000269|PubMed:11698381}.
CC -!- SUBUNIT: Interacts with SNF7 with its BRO1 domain. Interacts with
CC RIM101 with its C-terminal domain, probably binding to its two YPX[LI]
CC motifs. {ECO:0000269|PubMed:11698381, ECO:0000269|PubMed:15371534}.
CC -!- INTERACTION:
CC Q12033; P33400: RIM101; NbExp=3; IntAct=EBI-38947, EBI-14422;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 2881 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the palA/RIM20 family. {ECO:0000305}.
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DR EMBL; X89633; CAA61781.1; -; Genomic_DNA.
DR EMBL; Z75183; CAA99500.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA11041.1; -; Genomic_DNA.
DR PIR; S67177; S67177.
DR RefSeq; NP_014918.1; NM_001183694.1.
DR AlphaFoldDB; Q12033; -.
DR SMR; Q12033; -.
DR BioGRID; 34664; 516.
DR DIP; DIP-998N; -.
DR IntAct; Q12033; 2.
DR STRING; 4932.YOR275C; -.
DR TCDB; 3.A.31.1.1; the endosomal sorting complexes required for transport iii (escrt-iii) family.
DR iPTMnet; Q12033; -.
DR MaxQB; Q12033; -.
DR PaxDb; Q12033; -.
DR PRIDE; Q12033; -.
DR EnsemblFungi; YOR275C_mRNA; YOR275C; YOR275C.
DR GeneID; 854449; -.
DR KEGG; sce:YOR275C; -.
DR SGD; S000005801; RIM20.
DR VEuPathDB; FungiDB:YOR275C; -.
DR eggNOG; KOG2220; Eukaryota.
DR GeneTree; ENSGT00940000163083; -.
DR HOGENOM; CLU_007181_3_1_1; -.
DR InParanoid; Q12033; -.
DR OMA; SAKHIDD; -.
DR BioCyc; YEAST:G3O-33764-MON; -.
DR PRO; PR:Q12033; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q12033; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR GO; GO:0001403; P:invasive growth in response to glucose limitation; IMP:SGD.
DR GO; GO:0071985; P:multivesicular body sorting pathway; IEA:InterPro.
DR GO; GO:0016485; P:protein processing; IDA:SGD.
DR GO; GO:0006508; P:proteolysis; IMP:SGD.
DR GO; GO:0009268; P:response to pH; IMP:SGD.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IMP:SGD.
DR Gene3D; 1.25.40.280; -; 1.
DR InterPro; IPR025304; ALIX_V_dom.
DR InterPro; IPR045251; BRO1-like.
DR InterPro; IPR004328; BRO1_dom.
DR InterPro; IPR038499; BRO1_sf.
DR PANTHER; PTHR23030; PTHR23030; 1.
DR Pfam; PF13949; ALIX_LYPXL_bnd; 2.
DR Pfam; PF03097; BRO1; 1.
DR SMART; SM01041; BRO1; 1.
DR PROSITE; PS51180; BRO1; 1.
PE 1: Evidence at protein level;
KW Acetylation; Coiled coil; Cytoplasm; Nucleus; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..661
FT /note="pH-response regulator protein palA/RIM20"
FT /id="PRO_0000218885"
FT DOMAIN 3..371
FT /note="BRO1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00526"
FT COILED 388..422
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MUTAGEN 292..293
FT /note="DN->AA: In RIM20-292; prevents cleavage of RIM101."
FT /evidence="ECO:0000269|PubMed:11698381"
SQ SEQUENCE 661 AA; 75947 MW; A1EF91ACE2AA3570 CRC64;
MSELLAIPLK RTLEVDFATE LSKLIDTTSF QTASFFQSDI LKVVDARNNA IAPDISIDGL
SALKEYYVIL LQLEKKFPNN QIEFTWFQTL SQKSRGTSQY SLQWEKLTII YNIGCMYSLL
ALNSNNDAAE SLKTSCLYFQ NAAGCFKHVL DHQKNLETIP VVDDATLNAL TSLMLAQAQE
CFWFKAVQDK HKDSLIAKLS QQIVDFYCEA INDAQRGKLI RSDWINHLKA KKAYFSAVTY
YRIALSFNEK KQFGNVVKAL QMGLQFINES TLSSQAKFKT VVESSLKEAQ RDNEFIYLQE
VPSELPSIKP ALMVKPSSSA TLLPSIKKDE TLFKDLIPIE VMEYCTAYNE RQDEYVEQRV
TNPLASLNKL LKESLTTFQI PQGLTKVSEA ELSHYQASLN NLLINNKNVQ VQLDNIEQIL
NEEAFTDNQL RLKHGTLNWT LPESSTTNTA YYEKLKKLRG YLDEGSAIDK QTNELFQSID
KNLIGSEIRL PESNDPLTNK IKMIIQERND YIDRTRRKSS EYRILPKIIT SYKKNGTVDF
EPIFIGHLKY FDEDLRYVNS TKEENIKLIE EVNLSKKNNP GRSGIEPKKM VRIDPRELYI
EDLRYSFKLL DEVKENLSAG TAFYENLITS TSNLYNEVQE YDTARRAEKA RLDKSLTFED
Q
