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   27-MAR-2024, entry version 204.
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; 1015.
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   TCDB; 8.A.34.2.2; the endophilin (endophilin) family.
DR   iPTMnet; P39743; -.
DR   MaxQB; P39743; -.
DR   PaxDb; 4932-YDR388W; -.
DR   PeptideAtlas; P39743; -.
DR   EnsemblFungi; YDR388W_mRNA; YDR388W; YDR388W.
DR   GeneID; 851996; -.
DR   KEGG; sce:YDR388W; -.
DR   AGR; SGD:S000002796; -.
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; QEYDYYN; -.
DR   OrthoDB; 2972088at2759; -.
DR   BioCyc; YEAST:G3O-29936-MONOMER; -.
DR   BioGRID-ORCS; 851996; 1 hit in 10 CRISPR screens.
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   CDD; cd07599; BAR_Rvs167p; 1.
DR   Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 1.
DR   InterPro; IPR027267; AH/BAR_dom_sf.
DR   InterPro; IPR004148; BAR_dom.
DR   InterPro; IPR046982; BIN3/RVS161-like.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   PANTHER; PTHR47174; BRIDGING INTEGRATOR 3; 1.
DR   PANTHER; PTHR47174:SF1; REDUCED VIABILITY UPON STARVATION PROTEIN 167; 1.
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; BAR/IMD domain-like; 1.
DR   SUPFAM; SSF50044; SH3-domain; 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
//