RV167_YEAST
ID RV167_YEAST Reviewed; 482 AA.
AC P39743; D6VT22;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 197.
DE RecName: Full=Reduced viability upon starvation protein 167;
GN Name=RVS167; OrderedLocusNames=YDR388W; ORFNames=D9509.8;
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 26109 / X2180;
RX PubMed=8336735; DOI=10.1128/mcb.13.8.5070-5084.1993;
RA Bauer F., Urdaci M., Aigle M., Crouzet M.;
RT "Alteration of a yeast SH3 protein leads to conditional viability with
RT defects in cytoskeletal and budding patterns.";
RL Mol. Cell. Biol. 13:5070-5084(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(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 INTERACTION WITH ACTIN.
RX PubMed=7719850; DOI=10.1038/nsb0195-28;
RA Amberg D.C., Basart E., Botstein D.;
RT "Defining protein interactions with yeast actin in vivo.";
RL Nat. Struct. Biol. 2:28-35(1995).
RN [5]
RP INTERACTION WITH ABP1.
RX PubMed=10388809; DOI=10.1093/genetics/152.3.881;
RA Colwill K., Field D., Moore L., Friesen J., Andrews B.;
RT "In vivo analysis of the domains of yeast Rvs167p suggests Rvs167p function
RT is mediated through multiple protein interactions.";
RL Genetics 152:881-893(1999).
RN [6]
RP PHOSPHORYLATION, AND INTERACTION WITH PCL2.
RX PubMed=9843683; DOI=10.1016/s0960-9822(07)00561-1;
RA Lee J., Colwill K., Aneliunas V., Tennyson C.N., Moore L., Ho Y.,
RA Andrews B.J.;
RT "Interaction of yeast Rvs167 and Pho85 cyclin-dependent kinase complexes
RT may link the cell cycle to the actin cytoskeleton.";
RL Curr. Biol. 8:1310-1321(1998).
RN [7]
RP PHOSPHORYLATION AT SER-299; SER-321 AND SER-379.
RX PubMed=12857883; DOI=10.1091/mbc.e02-09-0613;
RA Friesen H., Murphy K., Breitkreutz A., Tyers M., Andrews B.J.;
RT "Regulation of the yeast amphiphysin homologue Rvs167p by
RT phosphorylation.";
RL Mol. Biol. Cell 14:3027-3040(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 UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-481, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=SUB592;
RX PubMed=12872131; DOI=10.1038/nbt849;
RA Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D., Marsischky G.,
RA Roelofs J., Finley D., Gygi S.P.;
RT "A proteomics approach to understanding protein ubiquitination.";
RL Nat. Biotechnol. 21:921-926(2003).
RN [10]
RP FUNCTION, AND INTERACTION WITH GYL1 AND GYP5.
RX PubMed=15802519; DOI=10.1534/genetics.104.040063;
RA Friesen H., Colwill K., Robertson K., Schub O., Andrews B.;
RT "Interaction of the Saccharomyces cerevisiae cortical actin patch protein
RT Rvs167p with proteins involved in ER to Golgi vesicle trafficking.";
RL Genetics 170:555-568(2005).
RN [11]
RP INTERACTION WITH YBR108W.
RX PubMed=15561700; DOI=10.1074/jbc.m412454200;
RA Germann M., Swain E., Bergman L., Nickels J.T. Jr.;
RT "Characterizing the sphingolipid signaling pathway that remediates defects
RT associated with loss of the yeast amphiphysin-like orthologs, Rvs161p and
RT Rvs167p.";
RL J. Biol. Chem. 280:4270-4278(2005).
RN [12]
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 [13]
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).
RN [14]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-242 AND LYS-481, AND
RP IDENTIFICATION BY 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: Component of a cytoskeletal structure that is required for
CC the formation of endocytic vesicles at the plasma membrane level. Could
CC be implicated in cytoskeletal reorganization in response to
CC environmental stresses and could act in the budding site selection
CC mechanism. {ECO:0000269|PubMed:15802519}.
CC -!- SUBUNIT: Binds to actin. Interacts with ABP1, GYL1, GYP5, PCL2 and
CC YBR108W. {ECO:0000269|PubMed:10388809, ECO:0000269|PubMed:15561700,
CC ECO:0000269|PubMed:15802519, ECO:0000269|PubMed:7719850,
CC ECO:0000269|PubMed:9843683}.
CC -!- INTERACTION:
CC P39743; P15891: ABP1; NbExp=6; IntAct=EBI-14500, EBI-2036;
CC P39743; Q12168: ACF2; NbExp=9; IntAct=EBI-14500, EBI-32973;
CC P39743; P47129: ACF4; NbExp=5; IntAct=EBI-14500, EBI-25556;
CC P39743; P60010: ACT1; NbExp=4; IntAct=EBI-14500, EBI-2169;
CC P39743; P38266: AIM3; NbExp=6; IntAct=EBI-14500, EBI-21584;
CC P39743; P53933: APP1; NbExp=9; IntAct=EBI-14500, EBI-28798;
CC P39743; Q06604: BSP1; NbExp=5; IntAct=EBI-14500, EBI-37047;
CC P39743; P38140: ERT1; NbExp=4; IntAct=EBI-14500, EBI-21048;
CC P39743; P40956: GTS1; NbExp=4; IntAct=EBI-14500, EBI-7968;
CC P39743; Q04322: GYL1; NbExp=8; IntAct=EBI-14500, EBI-27427;
CC P39743; Q12344: GYP5; NbExp=6; IntAct=EBI-14500, EBI-38508;
CC P39743; Q12446: LAS17; NbExp=14; IntAct=EBI-14500, EBI-10022;
CC P39743; Q04439: MYO5; NbExp=3; IntAct=EBI-14500, EBI-11687;
CC P39743; Q06833: NVJ2; NbExp=3; IntAct=EBI-14500, EBI-37290;
CC P39743; P25343: RVS161; NbExp=16; IntAct=EBI-14500, EBI-14490;
CC P39743; P39743: RVS167; NbExp=3; IntAct=EBI-14500, EBI-14500;
CC P39743; P32855: SEC8; NbExp=2; IntAct=EBI-14500, EBI-16896;
CC P39743; P37370: VRP1; NbExp=3; IntAct=EBI-14500, EBI-20502;
CC P39743; Q03780: YDR239C; NbExp=2; IntAct=EBI-14500, EBI-30094;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC -!- PTM: Phosphorylated redundantly by cyclin-dependent kinase PHO85 in
CC association with PCL1,2-type cyclins or by MAP kinase FUS3.
CC Phosphorylation inhibits interaction with complexes involved in actin
CC cytoskeleton function. {ECO:0000269|PubMed:12857883,
CC ECO:0000269|PubMed:9843683}.
CC -!- MISCELLANEOUS: Present with 14600 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
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DR EMBL; M92092; AAA35051.1; -; Genomic_DNA.
DR EMBL; U32274; AAB64830.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12232.1; -; Genomic_DNA.
DR PIR; S40887; S40887.
DR RefSeq; NP_010676.1; NM_001180696.1.
DR AlphaFoldDB; P39743; -.
DR SMR; P39743; -.
DR BioGRID; 32449; 1007.
DR ComplexPortal; CPX-1335; RVS161-RVS167 amphiphysin complex.
DR DIP; DIP-770N; -.
DR IntAct; P39743; 146.
DR MINT; P39743; -.
DR STRING; 4932.YDR388W; -.
DR MoonDB; P39743; Predicted.
DR iPTMnet; P39743; -.
DR MaxQB; P39743; -.
DR PaxDb; P39743; -.
DR PRIDE; P39743; -.
DR EnsemblFungi; YDR388W_mRNA; YDR388W; YDR388W.
DR GeneID; 851996; -.
DR KEGG; sce:YDR388W; -.
DR SGD; S000002796; RVS167.
DR VEuPathDB; FungiDB:YDR388W; -.
DR eggNOG; KOG3771; Eukaryota.
DR GeneTree; ENSGT00950000182882; -.
DR HOGENOM; CLU_025518_0_1_1; -.
DR InParanoid; P39743; -.
DR OMA; AEIYKPI; -.
DR BioCyc; YEAST:G3O-29936-MON; -.
DR PRO; PR:P39743; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P39743; protein.
DR GO; GO:0030479; C:actin cortical patch; IDA:SGD.
DR GO; GO:0005934; C:cellular bud tip; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005829; C:cytosol; HDA:SGD.
DR GO; GO:0043332; C:mating projection tip; IDA:SGD.
DR GO; GO:0031097; C:medial cortex; IBA:GO_Central.
DR GO; GO:1990528; C:Rvs161p-Rvs167p complex; IPI:SGD.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0005516; F:calmodulin binding; IDA:SGD.
DR GO; GO:0008092; F:cytoskeletal protein binding; IPI:SGD.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:SGD.
DR GO; GO:0051666; P:actin cortical patch localization; IMP:SGD.
DR GO; GO:0006897; P:endocytosis; IMP:SGD.
DR GO; GO:0060988; P:lipid tube assembly; IDA:SGD.
DR GO; GO:1903475; P:mitotic actomyosin contractile ring assembly; IMP:SGD.
DR GO; GO:0097320; P:plasma membrane tubulation; IDA:SGD.
DR GO; GO:0072741; P:protein localization to cell division site; IGI:SGD.
DR GO; GO:0030100; P:regulation of endocytosis; IDA:ComplexPortal.
DR GO; GO:0016192; P:vesicle-mediated transport; IPI:SGD.
DR Gene3D; 1.20.1270.60; -; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR004148; BAR_dom.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR Pfam; PF03114; BAR; 1.
DR Pfam; PF00018; SH3_1; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00721; BAR; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF103657; SSF103657; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS51021; BAR; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW Acetylation; Actin-binding; Coiled coil; Cytoplasm; Cytoskeleton;
KW Isopeptide bond; Phosphoprotein; Reference proteome; SH3 domain;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..482
FT /note="Reduced viability upon starvation protein 167"
FT /id="PRO_0000192961"
FT DOMAIN 17..254
FT /note="BAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00361"
FT DOMAIN 421..482
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 382..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 31..64
FT /evidence="ECO:0000255"
FT COILED 174..204
FT /evidence="ECO:0000255"
FT COMPBIAS 382..396
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 299
FT /note="Phosphoserine; by FUS3 and PHO85"
FT /evidence="ECO:0000269|PubMed:12857883"
FT MOD_RES 321
FT /note="Phosphoserine; by FUS3 and PHO85"
FT /evidence="ECO:0000269|PubMed:12857883"
FT MOD_RES 379
FT /note="Phosphoserine; by FUS3 and PHO85"
FT /evidence="ECO:0000269|PubMed:12857883"
FT CROSSLNK 242
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 481
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
SQ SEQUENCE 482 AA; 52774 MW; 3F0AB53EBCC95A5B CRC64;
MSFKGFTKAV SRAPQSFRQK FKMGEQTEDP VYEDAERRFQ ELEQETKKLS EESKRYSTAV
NGMLTHQIGF AKSMEEIFKP ISGKMSDPNA TIPEDNPQGI EASEQYRAIV AELQETLKPD
LALVEEKIVT PCQELLKIIT YIRKMATKRN HKKLDLDRHL NTYNKHEKKK EPTAKDEERL
YKAQAQVEVA QQEYDYYNDL LKTQLPILFS LEAEFVKPLF VSFYFMQLNI FYTLYNRLQD
MKIPYFDLNS DIVESYIAKK GNVEEQTDAL TITHFKLGYS KAKLEMTRRK YGVATAEGSP
VSGASSGVGY GAGYDPATAT SPTPTGYGYG AAAPSYAAQP AAQYGTAAAV GTAAAVGTAA
GAAAGAVPGT YPQYAAAQSP PLTGLGFQQS PQQQQGPPPA YSNPLTSPVA GTPAAAVAAA
PGVETVTALY DYQAQAAGDL SFPAGAVIEI VQRTPDVNEW WTGRYNGQQG VFPGNYVQLN
KN
