RAV1_YEAST
ID RAV1_YEAST Reviewed; 1357 AA.
AC P47104; D6VWK6;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Regulator of V-ATPase in vacuolar membrane protein 1;
DE AltName: Full=Suppression of the onset of impotence protein 3;
GN Name=RAV1; Synonyms=SOI3; OrderedLocusNames=YJR033C; ORFNames=J1590;
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=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-1016.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7668047; DOI=10.1002/yea.320110809;
RA Huang M.-E., Chuat J.-C., Galibert F.;
RT "Analysis of a 42.5 kb DNA sequence of chromosome X reveals three tRNA
RT genes and 14 new open reading frames including a gene most probably
RT belonging to the family of ubiquitin-protein ligases.";
RL Yeast 11:775-781(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 728-1357.
RX PubMed=8619316; DOI=10.1002/yea.320111208;
RA Zagulski M., Babinska B., Gromadka R., Migdalski A., Rytka J., Sulicka J.,
RA Herbert C.J.;
RT "The sequence of 24.3 kb from chromosome X reveals five complete open
RT reading frames, all of which correspond to new genes, and a tandem
RT insertion of a Ty1 transposon.";
RL Yeast 11:1179-1186(1995).
RN [5]
RP FUNCTION, IDENTIFICATION IN THE RAVE COMPLEX WITH RAV2 AND CBF3D, AND
RP INTERACTION WITH RAV2; CBF3D; VMA1; VMA2; VMA4 AND VMA8.
RX PubMed=11283612; DOI=10.1038/35070067;
RA Seol J.H., Shevchenko A., Shevchenko A., Deshaies R.J.;
RT "Skp1 forms multiple protein complexes, including RAVE, a regulator of V-
RT ATPase assembly.";
RL Nat. Cell Biol. 3:384-391(2001).
RN [6]
RP FUNCTION OF THE RAVE COMPLEX.
RX PubMed=11844802; DOI=10.1074/jbc.m200682200;
RA Smardon A.M., Tarsio M., Kane P.M.;
RT "The RAVE complex is essential for stable assembly of the yeast V-ATPase.";
RL J. Biol. Chem. 277:13831-13839(2002).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15090613; DOI=10.1091/mbc.e03-10-0755;
RA Sipos G., Brickner J.H., Brace E.J., Chen L., Rambourg A., Kepes F.,
RA Fuller R.S.;
RT "Soi3p/Rav1p functions at the early endosome to regulate endocytic
RT trafficking to the vacuole and localization of trans-Golgi network
RT transmembrane proteins.";
RL Mol. Biol. Cell 15:3196-3209(2004).
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1244, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=YAL6B;
RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA Jensen O.N.;
RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT pathway.";
RL Mol. Cell. Proteomics 4:310-327(2005).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1244 AND SER-1248, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1244 AND SER-1248, 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: Component of the RAVE complex, which is required for stable
CC assembly of the vacuolar ATPase complex V-ATPase under many conditions.
CC Required for transport between the early endosome and the late
CC endosome/prevacuolar compartment (PVC), suggesting that assembly of
CC vacuolar ATPase at the early endosome is required for transport from
CC the early endosome to the PVC. {ECO:0000269|PubMed:11283612,
CC ECO:0000269|PubMed:11844802, ECO:0000269|PubMed:15090613}.
CC -!- SUBUNIT: Component of the RAVE complex composed of RAV1, RAV2 and
CC CBF3D/SKP1. Within the complex, it interacts directly with RAV2 and
CC CBF3D. Interacts with the V-ATPase V1 subunits VMA1, VMA2 and VMA8.
CC {ECO:0000269|PubMed:11283612}.
CC -!- INTERACTION:
CC P47104; P52286: SKP1; NbExp=5; IntAct=EBI-25471, EBI-4090;
CC P47104; P17255: VMA1; NbExp=2; IntAct=EBI-25471, EBI-20245;
CC P47104; P16140: VMA2; NbExp=3; IntAct=EBI-25471, EBI-20254;
CC P47104; P22203: VMA4; NbExp=3; IntAct=EBI-25471, EBI-20268;
CC P47104; P32610: VMA8; NbExp=2; IntAct=EBI-25471, EBI-20264;
CC -!- SUBCELLULAR LOCATION: Endomembrane system
CC {ECO:0000269|PubMed:15090613}. Note=Probably membrane-associated,
CC associates with high density membrane compartment like early endosomes.
CC -!- MISCELLANEOUS: Present with 149 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; Z49533; CAA89560.1; -; Genomic_DNA.
DR EMBL; L36344; AAA88735.1; -; Genomic_DNA.
DR EMBL; X87297; CAA60726.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08822.1; -; Genomic_DNA.
DR PIR; S57052; S57052.
DR RefSeq; NP_012567.3; NM_001181691.3.
DR AlphaFoldDB; P47104; -.
DR BioGRID; 33786; 275.
DR ComplexPortal; CPX-1627; RAVE complex.
DR DIP; DIP-916N; -.
DR IntAct; P47104; 6.
DR MINT; P47104; -.
DR STRING; 4932.YJR033C; -.
DR CarbonylDB; P47104; -.
DR iPTMnet; P47104; -.
DR MaxQB; P47104; -.
DR PaxDb; P47104; -.
DR PRIDE; P47104; -.
DR TopDownProteomics; P47104; -.
DR EnsemblFungi; YJR033C_mRNA; YJR033C; YJR033C.
DR GeneID; 853490; -.
DR KEGG; sce:YJR033C; -.
DR SGD; S000003794; RAV1.
DR VEuPathDB; FungiDB:YJR033C; -.
DR eggNOG; KOG1064; Eukaryota.
DR GeneTree; ENSGT00390000000096; -.
DR HOGENOM; CLU_000310_0_1_1; -.
DR InParanoid; P47104; -.
DR OMA; TIECVAT; -.
DR BioCyc; YEAST:G3O-31670-MON; -.
DR PRO; PR:P47104; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P47104; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0012505; C:endomembrane system; IC:ComplexPortal.
DR GO; GO:0019898; C:extrinsic component of membrane; IDA:SGD.
DR GO; GO:0043291; C:RAVE complex; IPI:SGD.
DR GO; GO:0045022; P:early endosome to late endosome transport; IMP:SGD.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0043254; P:regulation of protein-containing complex assembly; IMP:SGD.
DR GO; GO:0007035; P:vacuolar acidification; IMP:SGD.
DR GO; GO:0070072; P:vacuolar proton-transporting V-type ATPase complex assembly; IDA:ComplexPortal.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR022033; Rav1p_C.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF12234; Rav1p_C; 1.
DR SMART; SM00320; WD40; 5.
DR SUPFAM; SSF50978; SSF50978; 2.
PE 1: Evidence at protein level;
KW Membrane; Phosphoprotein; Protein transport; Reference proteome; Repeat;
KW Transport; WD repeat.
FT CHAIN 1..1357
FT /note="Regulator of V-ATPase in vacuolar membrane protein
FT 1"
FT /id="PRO_0000051183"
FT REPEAT 98..134
FT /note="WD 1"
FT REPEAT 142..182
FT /note="WD 2"
FT REPEAT 190..239
FT /note="WD 3"
FT REPEAT 384..423
FT /note="WD 4"
FT REPEAT 431..470
FT /note="WD 5"
FT REPEAT 595..636
FT /note="WD 6"
FT REPEAT 638..679
FT /note="WD 7"
FT REPEAT 898..939
FT /note="WD 8"
FT REGION 1243..1357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1265..1316
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1317..1340
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1244
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15665377,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 1248
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
SQ SEQUENCE 1357 AA; 154933 MW; 6B7270B6901274CF CRC64;
MSLNFLPGRP NATPQTACQA TWQNHTIFAY CSGNNLIILT NKFTRLQTIY TQSDCTAVDI
NSQNGFIALS FHNRVLIYKP IHQIMQNPKW TQCCQLFHDD TPVNCLRWSS DNELAIGSDF
LSFWKIKDNF GVYQPILQWN QKQPKPVYNV IISQDSQLIV SIGKYDCNAK LWKRVSIVGE
QAIFNLTMLP HPKPITAMRW KKEPDQVSKN NTASHALYTL CEDKVLRIWS CFEMEKNHTV
QIWGEVPLSP TQKFCVIIDN WIIRQTLSVK DSEIFDISDS DIVILGSMTG EMEVLALNNL
SQDPPKPMTK KTISHKKVKK ATMLNDTRYL YLPEIQPYDN VKGKLSFLVH DLQGVIRHLL
IDILQLINNK TEDLSAALEH KFTGHNKSVQ KLVRSSDGEA LLTTSRFSEN GVWYPQKLNH
GVSLRLQNTI QTESPIKFAV VHELGKQVIC LLENGALQAW ECPTNRKEDS EQKQSYLRVE
TRLKEEKKIH PIVMLNTPEP KHSHERHFTA LIFSDGSIKA FEVSLTRGIF EVKSDSLDID
GDDIYKISII DPVHQTFVSN RPLISLITKK GLTRTYKAIV NYNDRHVQWI KACEINTGIM
NCTCIRGSST GKLCIVNSTG KVMSLWDLNR GVLEYEETFH NPIEDIDWTS TEYGQSIVSI
GFTGYALLYT QLRYDYTNNT PSYLPIEKID ITAHTAHNIG DSVWMKNGTF VVASGNQFYI
KDKSLDLTDP FTYQSIGSRK ILSNDILHLS SVLNGPLPVY HPQFLIQAIY ANKLQLVKEL
LLRLFLALRK LDFESQDVSN LDSNLGMDPL KYFIAKDRDY PVESFPDPYP CFNKTVSLAL
TEQLTKTTLP YLTRHQQITL ITVIEAVDEV TKNENIVDYN GVRFLLGVKL FLSHKNIQKS
ILMRDVSWAL HSDNKEILLS SIDRHITSWN RAREYRIAYW IKEQDLVKKF EDIAKYEFSK
DDKRDPSRCA IFYLALKKKQ ILLSLWKMAI GHPEQQKMVR FISNDFTVPR WRTAALKNAF
VLLSKHRYMD AAVFFLLTDS LKDCVNVLCK QVHDMDLAIG VCRVYEGDNG PVLGELLTAQ
MLPETIKEND RWKASFIYWK LRKQEVAIKA LLTAPIDLEN NSSIVDKEVC VNRSFLVEDP
ALLYLYNHLR NRNLKYFIGS LNVEAKIECT LILRVTDILC RMGCNYLAVS LVKNWKFIER
NSIPVQKLLK SPTKDRAYSA IGAMASEPIS TARMRPSLFD KFGSPSASDI ESPNPKLPNS
LLDDFLQPPP NSTSSNSLAQ SSSSAPRSIL DEFVSPSYSQ HKENLTPKAP NDSVGETDNS
ENRKDKLSKD ILDDLSSQKP QKPKKSAITK NLLDDFV
