RV167_CANAL
ID RV167_CANAL Reviewed; 440 AA.
AC Q59LF3; A0A1D8PQB3;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 2.
DT 25-MAY-2022, entry version 96.
DE RecName: Full=Regulator of cytoskeleton and endocytosis RVS167 {ECO:0000305};
GN Name=RVS167; OrderedLocusNames=CAALFM_C604040CA;
GN ORFNames=CaO19.1220, CaO19.8807;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=15470256; DOI=10.1128/ec.3.5.1272-1286.2004;
RA Oberholzer U., Iouk T.L., Thomas D.Y., Whiteway M.;
RT "Functional characterization of myosin I tail regions in Candida
RT albicans.";
RL Eukaryot. Cell 3:1272-1286(2004).
RN [5]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=19596778; DOI=10.1128/iai.00683-09;
RA Douglas L.M., Martin S.W., Konopka J.B.;
RT "BAR domain proteins Rvs161 and Rvs167 contribute to Candida albicans
RT endocytosis, morphogenesis, and virulence.";
RL Infect. Immun. 77:4150-4160(2009).
RN [6]
RP DISRUPTION PHENOTYPE.
RX PubMed=20402797; DOI=10.1111/j.1567-1364.2010.00624.x;
RA Reijnst P., Walther A., Wendland J.;
RT "Functional analysis of Candida albicans genes encoding SH3-domain-
RT containing proteins.";
RL FEMS Yeast Res. 10:452-461(2010).
CC -!- FUNCTION: Component of a cytoskeletal structure that is required for
CC the formation of endocytic vesicles at the plasma membrane level. Plays
CC an important role in virulence. {ECO:0000269|PubMed:19596778}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:P39743, ECO:0000303|PubMed:15470256}.
CC -!- DISRUPTION PHENOTYPE: Leads to defects in actin polarization,
CC endocytosis, bud morphogenesis, as well as altered abundance and
CC distribution of the cortical actin patches and increased sensitivity to
CC calcofluor white and Congo red. Shows also attenuated virulence.
CC {ECO:0000269|PubMed:19596778, ECO:0000269|PubMed:20402797}.
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DR EMBL; CP017628; AOW30325.1; -; Genomic_DNA.
DR RefSeq; XP_710570.2; XM_705478.2.
DR AlphaFoldDB; Q59LF3; -.
DR SMR; Q59LF3; -.
DR BioGRID; 1230917; 2.
DR STRING; 237561.Q59LF3; -.
DR GeneID; 3647831; -.
DR KEGG; cal:CAALFM_C604040CA; -.
DR CGD; CAL0000200028; RVS167.
DR VEuPathDB; FungiDB:C6_04040C_A; -.
DR eggNOG; KOG3771; Eukaryota.
DR HOGENOM; CLU_025518_0_1_1; -.
DR InParanoid; Q59LF3; -.
DR OrthoDB; 1090526at2759; -.
DR PRO; PR:Q59LF3; -.
DR Proteomes; UP000000559; Chromosome 6.
DR GO; GO:0030479; C:actin cortical patch; IBA:GO_Central.
DR GO; GO:0005934; C:cellular bud tip; IEA:EnsemblFungi.
DR GO; GO:0043332; C:mating projection tip; IBA:GO_Central.
DR GO; GO:0031097; C:medial cortex; IBA:GO_Central.
DR GO; GO:1990528; C:Rvs161p-Rvs167p complex; IBA:GO_Central.
DR GO; GO:0005516; F:calmodulin binding; IEA:EnsemblFungi.
DR GO; GO:0008092; F:cytoskeletal protein binding; IEA:EnsemblFungi.
DR GO; GO:0008289; F:lipid binding; IEA:EnsemblFungi.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:EnsemblFungi.
DR GO; GO:0051666; P:actin cortical patch localization; IBA:GO_Central.
DR GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR GO; GO:0060988; P:lipid tube assembly; IEA:EnsemblFungi.
DR GO; GO:1903475; P:mitotic actomyosin contractile ring assembly; IEA:EnsemblFungi.
DR GO; GO:0097320; P:plasma membrane tubulation; IBA:GO_Central.
DR GO; GO:0072741; P:protein localization to cell division site; IEA:EnsemblFungi.
DR GO; GO:0030100; P:regulation of endocytosis; IEA:EnsemblFungi.
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 3: Inferred from homology;
KW Cytoplasm; Cytoskeleton; Endocytosis; Reference proteome; SH3 domain;
KW Virulence.
FT CHAIN 1..440
FT /note="Regulator of cytoskeleton and endocytosis RVS167"
FT /id="PRO_0000430558"
FT DOMAIN 17..254
FT /note="BAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00361"
FT DOMAIN 382..440
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 286..380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..311
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 328..368
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 440 AA; 49220 MW; B1BB044AD0C6FAA2 CRC64;
MSFKGFKKGV LRAPQTMRQK FNMGEITQDA VYLDAERRFK EIEMETKKLS EESKKYFNAV
NGMLDEQIDF AKAVAEIYKP ISGRLSDPSA TVPEDNPQGI EASESYQAVV KDLKDTLKPD
LELIEKRIVE PAQELLKIIQ AIRKMSVKRD HKQLDLDRHK RNLSKYESKK ERTVKDEEKM
FSAQAEVEIA QQEYDYYNDL LKNELPVLFQ MQSDFIKPLF VSFYYMQLNI FYTLYTRMEE
LKIPYFDLST DIVEAYTAKK GNIEEQTDAI GITHFKVGHA KSKLEATKRR HAAMNSPPPT
GASSIASTGT GGELPAYSPG GYNQPYGDSK YQPPSSPATY QSPVVAATAQ SPATYQSPVA
TGQPPSYLPQ TPASAPPPQV GSGLPTCTAL YDYTAQAQGD LTFPAGAVIE IIQRTEDANG
WWTGKYNGQT GVFPGNYVQL
