BNR1_CANAL
ID BNR1_CANAL Reviewed; 1485 AA.
AC Q5AAF4; A0A1D8PRL0;
DT 11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Formin BNR1;
GN Name=BNR1; Synonyms=BNI1; OrderedLocusNames=CAALFM_CR00070WA;
GN ORFNames=CaO19.7537;
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 FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=16215178; DOI=10.1128/ec.4.10.1712-1724.2005;
RA Martin R., Walther A., Wendland J.;
RT "Ras1-induced hyphal development in Candida albicans requires the formin
RT Bni1.";
RL Eukaryot. Cell 4:1712-1724(2005).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=15914538; DOI=10.1242/jcs.02393;
RA Li C.R., Wang Y.M., De Zheng X., Liang H.Y., Tang J.C., Wang Y.;
RT "The formin family protein CaBni1p has a role in cell polarity control
RT during both yeast and hyphal growth in Candida albicans.";
RL J. Cell Sci. 118:2637-2648(2005).
RN [6]
RP SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=17351079; DOI=10.1128/ec.00201-06;
RA Dunkler A., Wendland J.;
RT "Candida albicans Rho-type GTPase-encoding genes required for polarized
RT cell growth and cell separation.";
RL Eukaryot. Cell 6:844-854(2007).
RN [7]
RP FUNCTION.
RX PubMed=17715368; DOI=10.1128/ec.00188-07;
RA Wolyniak M.J., Sundstrom P.;
RT "Role of actin cytoskeletal dynamics in activation of the cyclic AMP
RT pathway and HWP1 gene expression in Candida albicans.";
RL Eukaryot. Cell 6:1824-1840(2007).
RN [8]
RP INTERACTION WITH IQG1.
RX PubMed=18923418; DOI=10.1038/emboj.2008.219;
RA Li C.R., Wang Y.M., Wang Y.;
RT "The IQGAP Iqg1 is a regulatory target of CDK for cytokinesis in Candida
RT albicans.";
RL EMBO J. 27:2998-3010(2008).
CC -!- FUNCTION: May organize microtubules by mediating spindle positioning
CC and movement in the budding process. Required for cytokinesis and the
CC maintenance of polarized hyphal growth. {ECO:0000269|PubMed:16215178,
CC ECO:0000269|PubMed:17715368}.
CC -!- SUBUNIT: Interacts with IQG1. {ECO:0000269|PubMed:18923418}.
CC -!- SUBCELLULAR LOCATION: Bud neck. Cell septum. Note=Localizes only at
CC septal sites in both yeast and hyphal stages.
CC -!- DISRUPTION PHENOTYPE: Lead to a cell separation defect.
CC {ECO:0000269|PubMed:16215178, ECO:0000269|PubMed:17351079}.
CC -!- SIMILARITY: Belongs to the formin homology family. BNI1 subfamily.
CC {ECO:0000305}.
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DR EMBL; CP017630; AOW30778.1; -; Genomic_DNA.
DR RefSeq; XP_718693.1; XM_713600.1.
DR AlphaFoldDB; Q5AAF4; -.
DR SMR; Q5AAF4; -.
DR BioGRID; 1222766; 1.
DR IntAct; Q5AAF4; 1.
DR MINT; Q5AAF4; -.
DR STRING; 237561.Q5AAF4; -.
DR PRIDE; Q5AAF4; -.
DR GeneID; 3639672; -.
DR KEGG; cal:CAALFM_CR00070WA; -.
DR CGD; CAL0000190952; BNR1.
DR VEuPathDB; FungiDB:CR_00070W_A; -.
DR eggNOG; KOG1922; Eukaryota.
DR HOGENOM; CLU_002339_0_0_1; -.
DR InParanoid; Q5AAF4; -.
DR OMA; LHMFANL; -.
DR OrthoDB; 1204639at2759; -.
DR Proteomes; UP000000559; Chromosome R.
DR GO; GO:0032153; C:cell division site; IBA:GO_Central.
DR GO; GO:0030428; C:cell septum; IDA:CGD.
DR GO; GO:0005935; C:cellular bud neck; IDA:CGD.
DR GO; GO:0000142; C:cellular bud neck contractile ring; IDA:CGD.
DR GO; GO:0032177; C:cellular bud neck split septin rings; IDA:CGD.
DR GO; GO:0001411; C:hyphal tip; IDA:CGD.
DR GO; GO:0043332; C:mating projection tip; IBA:GO_Central.
DR GO; GO:0003779; F:actin binding; IEA:InterPro.
DR GO; GO:0008092; F:cytoskeletal protein binding; IDA:CGD.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0051017; P:actin filament bundle assembly; IBA:GO_Central.
DR GO; GO:0051016; P:barbed-end actin filament capping; IBA:GO_Central.
DR GO; GO:1903475; P:mitotic actomyosin contractile ring assembly; IBA:GO_Central.
DR GO; GO:0000920; P:septum digestion after cytokinesis; IMP:CGD.
DR Gene3D; 1.20.58.2220; -; 1.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR015425; FH2_Formin.
DR InterPro; IPR042201; FH2_Formin_sf.
DR InterPro; IPR010472; FH3_dom.
DR InterPro; IPR014768; GBD/FH3_dom.
DR InterPro; IPR010473; GTPase-bd.
DR Pfam; PF06367; Drf_FH3; 1.
DR Pfam; PF06371; Drf_GBD; 1.
DR Pfam; PF02181; FH2; 1.
DR SMART; SM01139; Drf_FH3; 1.
DR SMART; SM01140; Drf_GBD; 1.
DR SMART; SM00498; FH2; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS51444; FH2; 1.
DR PROSITE; PS51232; GBD_FH3; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Coiled coil; Reference proteome.
FT CHAIN 1..1485
FT /note="Formin BNR1"
FT /id="PRO_0000424602"
FT DOMAIN 110..636
FT /note="GBD/FH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00579"
FT DOMAIN 953..1368
FT /note="FH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00774"
FT REGION 65..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 226..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 549..575
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 746..874
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1447..1471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 660..734
FT /evidence="ECO:0000255"
FT COILED 1240..1312
FT /evidence="ECO:0000255"
FT COILED 1351..1382
FT /evidence="ECO:0000255"
FT COMPBIAS 73..88
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 746..761
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 826..874
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1447..1462
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1485 AA; 168566 MW; 266E3711C135B1AB CRC64;
MNEPPPKRQS VFAKGMKKLQ RSKSLLNFAE QAKPPTPENF SSLDPKSNLN SIGLSLVGYG
LSSDHLPPPR LDTDSESVSS RTSSPTLHVT TKFNPKQRVE SFQTATNFKN QIPPEEIVDQ
LFEKLLSIRV FPDEAVYSLK KQPVERKWEL LLREHETNHH FDLKKLSEQA TDKFLTNRDR
FQEHEFLIMS RSTTQEPKPK LKPLRIVSGG EDYDDEETPT VTKLVHDDSS TSKLSIESGG
SSGAPTETES LLGLVNKKLK IRDGSPDWYV SRIMANKLSL KDCKKLERKL VENNVVKNSG
VTWTQGFINA QGETALSVVL TKINKKSIKS NEEFDKEYLI VKCLKHINSE KRDETSSLKE
KVYVVKALVF LLVSPRLTTR ILVTEVLVML MLLRDKTLWK SALDGLSSLQ DRNGDYVIFQ
PWLNAFEETI IKYSWSQNKA GELSNLKNYA TITLILINSM VDMCSSLKRR ISIRRDFGNA
RILNIFEKLA QIEDTRIDNE IEKYEMYAEE DYNEYVEGKK KRNSKQLPNI PQSKLKLLQV
SDFVTTPEAN TSLEEDELTP ELEDNLSGTE SSFDEKSFMT KLKEAEDIES DGAMKSVLQR
LMKLKQSERS TEDVHKMLVL VDSMLQHVTN ESRVIGTDAH SVLNITIQKL MDRLSTEDMA
RRAVAESKML SRQLELVKEE KELLEKELET NKIETIRELK KENYYQAELI ATQERQLSKL
QQKIEQLQSP NNTALPVVDV GQQGFGNGTV ASLKDTSSSS PSKRPPTPPG LYSMQKGSLR
GGISAPPMLD FKDARPVSDL QDSRPVSDLQ DAPRLVESSA PPLPESKDPV AQPPPPESKD
SVAPPPPPVP DFIKSAAPPP PPLPGFMNAS APPPPPVPEF IKSSAPPPPP LPGFITTTPP
PPPPLPGFIT TTPPPPPMPG MLQPGKVKEL GTLFKEKHKQ EPQKGITKTK ADVVPSIRPK
NKLKQMHWDK LENIEKTFWN NLEDSVLSNK LIEQGVLGEV EQVFAAKTAT IKKKTAVESQ
QQPTKKSFLS RDLSQQFGIN LHMFANLSEE KLVLKVLRCN SEILENHSVL EFFNNEALVE
LSDSLFRNLA PYSTDPRTRK KPMKNPEELE RADRIFLELC YNLRHYWRSR SRALLFSQTY
KKDYIDLMRK LNIVDEANAA LKKSESLQNV LGIIRTVGNF MNDDAKQALG FKLDTLQRLK
FMKDDQNSMT FLHYIEKIVR HSFPEYGSFV DDLNVLSTLH NISIEQLETD CEEMSRSVKN
ITDSLERGKL SNKKDLHPED RILTTISSPM LNAKNKNAML QSHLKRTAGE LNSLMTFFGE
NPKDATARNT FFYKFVTFIT EYKKAHVENI QREEEQRTYE IRKKILEDKI AKKEKLKEES
AEPEAVVDTA EESSAVIDSL LEKLKSSTPI TTNRAKTKNR RSKALSFYSE NPLEIVADTK
YESVNNLKRR MTTRKRTTDG ETSPKSEQFM SRAQAMLHQL RNKEE
