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Database: UniProt
Entry: C5MI96_CANTT
LinkDB: C5MI96_CANTT
Original site: C5MI96_CANTT 
ID   C5MI96_CANTT            Unreviewed;       427 AA.
AC   C5MI96;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   24-JAN-2024, entry version 59.
DE   RecName: Full=Reduced viability upon starvation protein 167 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=CTRG_05789 {ECO:0000313|EMBL:EER30390.1};
OS   Candida tropicalis (strain ATCC MYA-3404 / T1) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=294747 {ECO:0000313|EMBL:EER30390.1, ECO:0000313|Proteomes:UP000002037};
RN   [1] {ECO:0000313|EMBL:EER30390.1, ECO:0000313|Proteomes:UP000002037}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-3404 / T1 {ECO:0000313|Proteomes:UP000002037};
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA   Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA   Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA   Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA   Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA   Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA   Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA   Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA   Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(2009).
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DR   EMBL; GG692404; EER30390.1; -; Genomic_DNA.
DR   RefSeq; XP_002546311.1; XM_002546265.1.
DR   AlphaFoldDB; C5MI96; -.
DR   STRING; 294747.C5MI96; -.
DR   EnsemblFungi; CTRG_05789-t43_1; CTRG_05789-t43_1-p1; CTRG_05789.
DR   GeneID; 8296713; -.
DR   KEGG; ctp:CTRG_05789; -.
DR   VEuPathDB; FungiDB:CTRG_05789; -.
DR   eggNOG; KOG3771; Eukaryota.
DR   HOGENOM; CLU_025518_0_1_1; -.
DR   OrthoDB; 2972088at2759; -.
DR   Proteomes; UP000002037; Unassembled WGS sequence.
DR   GO; GO:0030479; C:actin cortical patch; IEA:EnsemblFungi.
DR   GO; GO:0005934; C:cellular bud tip; IEA:EnsemblFungi.
DR   GO; GO:0043332; C:mating projection tip; IEA:EnsemblFungi.
DR   GO; GO:0031097; C:medial cortex; IEA:EnsemblFungi.
DR   GO; GO:0110085; C:mitotic actomyosin contractile ring; IEA:EnsemblFungi.
DR   GO; GO:1990528; C:Rvs161p-Rvs167p complex; IEA:EnsemblFungi.
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; IEA:EnsemblFungi.
DR   GO; GO:0006974; P:DNA damage response; IEA:EnsemblFungi.
DR   GO; GO:0006897; P:endocytosis; IEA:EnsemblFungi.
DR   GO; GO:0007163; P:establishment or maintenance of cell polarity; IEA:EnsemblFungi.
DR   GO; GO:0030447; P:filamentous growth; IEA:UniProt.
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; IEA:EnsemblFungi.
DR   GO; GO:0072741; P:protein localization to cell division site; IEA:EnsemblFungi.
DR   GO; GO:0030100; P:regulation of endocytosis; IEA:EnsemblFungi.
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   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002037};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}.
FT   DOMAIN          17..254
FT                   /note="BAR"
FT                   /evidence="ECO:0000259|PROSITE:PS51021"
FT   DOMAIN          369..427
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   COILED          156..193
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   427 AA;  47386 MW;  8B9FBDB6BE1C227B CRC64;
     MSFKGIKKGI LRTPQTIRQK FNMGEITHDA VYEDAERRFK EIEIETKKLS DESKKYFNAV
     NGMLDNQIEF AKAVAEIYKP ISGRLSDPNA TVPEDNPDGI TASEQYQDVV KELKETLKPD
     LELIDKRIVQ PAQELLTIVA SIRKTSKKRD HKQLDLDRHK RTFTKYESKA ERTAKEEEKM
     YAAQAELEIA EQEYEYYNQT LKDELPILFQ MQSQFIKPLF ESLYFMQLSI FYTLYIRMEE
     LKIPYFDLTS DILEAYNLKK GNIEEQTDAI GITHFKVGHA KAKLEATRRR HAAMNSPPPS
     AAAGAGVATA GVATAGSAQE LPAYTQGGYT QPVGDNKYQA PGTPASATPP AYSPVGGAPV
     GAPAAAVAAP AQTCTALYDY TAQAQGDLTF PAGAVIEIVE RTADANGWWT GRYNGQVGVF
     PGNYVQL
//
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