GENTAUR Molecular Products.

 BNI1_CANAL              Reviewed;        1732 AA.
 Q5AL52; A0A1D8PFJ4;
 11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
 26-APR-2005, sequence version 1.
 28-MAR-2018, entry version 94.
 RecName: Full=Formin BNI1;
 Name=BNI1; OrderedLocusNames=CAALFM_C112960CA;
 ORFNames=CaO19.12393, CaO19.4927;
 Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
 Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
 Saccharomycetes; Saccharomycetales; Debaryomycetaceae;
 Candida/Lodderomyces clade; Candida.
 NCBI_TaxID=237561;
 [1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
 STRAIN=SC5314 / ATCC MYA-2876;
 PubMed=15123810; DOI=10.1073/pnas.0401648101;
 Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S.,
 Magee B.B., Newport G., Thorstenson Y.R., Agabian N., Magee P.T.,
 Davis R.W., Scherer S.;
 "The diploid genome sequence of Candida albicans.";
 Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
 [2]
 GENOME REANNOTATION.
 STRAIN=SC5314 / ATCC MYA-2876;
 PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
 van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
 Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
 Chibana H., Nantel A., Magee P.T.;
 "Assembly of the Candida albicans genome into sixteen supercontigs
 aligned on the eight chromosomes.";
 Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
 [3]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME
 REANNOTATION.
 STRAIN=SC5314 / ATCC MYA-2876;
 PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
 Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
 "Assembly of a phased diploid Candida albicans genome facilitates
 allele-specific measurements and provides a simple model for repeat
 and indel structure.";
 Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
 [4]
 FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
 PubMed=16215178; DOI=10.1128/EC.4.10.1712-1724.2005;
 Martin R., Walther A., Wendland J.;
 "Ras1-induced hyphal development in Candida albicans requires the
 formin Bni1.";
 Eukaryot. Cell 4:1712-1724(2005).
 [5]
 FUNCTION, AND SUBCELLULAR LOCATION.
 PubMed=15914538; DOI=10.1242/jcs.02393;
 Li C.R., Wang Y.M., De Zheng X., Liang H.Y., Tang J.C., Wang Y.;
 "The formin family protein CaBni1p has a role in cell polarity control
 during both yeast and hyphal growth in Candida albicans.";
 J. Cell Sci. 118:2637-2648(2005).
 [6]
 SUBCELLULAR LOCATION.
 PubMed=15976451; DOI=10.1242/jcs.02414;
 Crampin H., Finley K., Gerami-Nejad M., Court H., Gale C., Berman J.,
 Sudbery P.;
 "Candida albicans hyphae have a Spitzenkorper that is distinct from
 the polarisome found in yeast and pseudohyphae.";
 J. Cell Sci. 118:2935-2947(2005).
 [7]
 FUNCTION.
 PubMed=16855023; DOI=10.1091/mbc.E06-02-0143;
 Rida P.C., Nishikawa A., Won G.Y., Dean N.;
 "Yeast-to-hyphal transition triggers formin-dependent Golgi
 localization to the growing tip in Candida albicans.";
 Mol. Biol. Cell 17:4364-4378(2006).
 [8]
 FUNCTION.
 PubMed=17715368; DOI=10.1128/EC.00188-07;
 Wolyniak M.J., Sundstrom P.;
 "Role of actin cytoskeletal dynamics in activation of the cyclic AMP
 pathway and HWP1 gene expression in Candida albicans.";
 Eukaryot. Cell 6:1824-1840(2007).
 [9]
 SUBCELLULAR LOCATION.
 PubMed=17504812; DOI=10.1242/jcs.002931;
 Li C.R., Lee R.T., Wang Y.M., Zheng X.D., Wang Y.;
 "Candida albicans hyphal morphogenesis occurs in Sec3p-independent and
 Sec3p-dependent phases separated by septin ring formation.";
 J. Cell Sci. 120:1898-1907(2007).
 [10]
 INTERACTION WITH IQG1.
 PubMed=18923418; DOI=10.1038/emboj.2008.219;
 Li C.R., Wang Y.M., Wang Y.;
 "The IQGAP Iqg1 is a regulatory target of CDK for cytokinesis in
 Candida albicans.";
 EMBO J. 27:2998-3010(2008).
 -!- FUNCTION: Required for the assembly of F-actin structures, such as
     actin cables and stress fibers. Nucleates actin filaments. Binds
     to the barbed end of the actin filament and acts as leaky capper,
     slowing both polymerization and depolymerization. Protects the
     growing actin fiber from tight capping proteins and so increases
     the time of elongation and the total amount of F-actin. May
     organize microtubules by mediating spindle positioning and
     movement in the budding process. Required for the maintenance of
     polarized hyphal growth. BNI1-mediated actin cables are necessary
     for positioning the Golgi complex to a putative site of germ tube
     emergence and for coordinating the transport and deposition of
     membrane and cell wall material to a growing hypha. Plays a key
     role in virulence. {ECO:0000269|PubMed:15914538,
     ECO:0000269|PubMed:16215178, ECO:0000269|PubMed:16855023,
     ECO:0000269|PubMed:17715368}.
 -!- SUBUNIT: Homodimer, and possibly also homotetramer (By
     similarity). Interacts with actin via the FH2 domain (By
     similarity). Interacts with IQG1. {ECO:0000250,
     ECO:0000269|PubMed:18923418}.
 -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Bud neck. Bud tip.
     Cell septum. Note=Localizes to the presumptive budding site in G1
     cells, the bud tip of small to medium-budded cells and the bud
     neck of large-budded cells. During hyphal growth at least a
     fraction persistently localizes at the tips of germ tubes and
     hyphae independently of cell cycle progression. Localizes at the
     Spitzenkorper, a structure found in fungal hyphae which is the
     organizing center for hyphal growth and morphogenesis.
 -!- DOMAIN: The DAD domain regulates activation via by an
     autoinhibitory interaction with the GBD/FH3 domain. This
     autoinhibition is released upon competitive binding of an
     activated GTPase. The release of DAD allows the FH2 domain to then
     nucleate and elongate nonbranched actin filaments (By similarity).
     {ECO:0000250}.
 -!- DISRUPTION PHENOTYPE: Leads to swollen cells, increased random
     budding pattern, and severe defect in cytokinesis with enlarged
     bud necks. {ECO:0000269|PubMed:16215178}.
 -!- SIMILARITY: Belongs to the formin homology family. BNI1 subfamily.
     {ECO:0000305}.
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 EMBL; CP017623; AOW26910.1; -; Genomic_DNA.
 RefSeq; XP_722138.1; XM_717045.1.
 ProteinModelPortal; Q5AL52; -.
 SMR; Q5AL52; -.
 IntAct; Q5AL52; 1.
 MINT; Q5AL52; -.
 PRIDE; Q5AL52; -.
 EnsemblFungi; AOW26910; AOW26910; CAALFM_C112960CA.
 GeneID; 3636118; -.
 KEGG; cal:CAALFM_C112960CA; -.
 CGD; CAL0000188644; BNI1.
 InParanoid; Q5AL52; -.
 KO; K11238; -.
 OMA; QIYLYTA; -.
 OrthoDB; EOG092C03J2; -.
 PRO; PR:Q5AL52; -.
 Proteomes; UP000000559; Chromosome 1.
 GO; GO:0030428; C:cell septum; IDA:CGD.
 GO; GO:0005935; C:cellular bud neck; IDA:CGD.
 GO; GO:0000142; C:cellular bud neck contractile ring; IDA:CGD.
 GO; GO:0005934; C:cellular bud tip; IDA:CGD.
 GO; GO:0001411; C:hyphal tip; IDA:CGD.
 GO; GO:0000131; C:incipient cellular bud site; IDA:CGD.
 GO; GO:0031521; C:spitzenkorper; IDA:CGD.
 GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
 GO; GO:0008092; F:cytoskeletal protein binding; IDA:CGD.
 GO; GO:0017048; F:Rho GTPase binding; IEA:InterPro.
 GO; GO:0051666; P:actin cortical patch localization; IMP:CGD.
 GO; GO:0030036; P:actin cytoskeleton organization; IEA:InterPro.
 GO; GO:0000920; P:cell separation after cytokinesis; IMP:CGD.
 GO; GO:0000282; P:cellular bud site selection; IMP:CGD.
 GO; GO:0009267; P:cellular response to starvation; IMP:CGD.
 GO; GO:0007163; P:establishment or maintenance of cell polarity; IMP:CGD.
 GO; GO:0030447; P:filamentous growth; IMP:CGD.
 GO; GO:0044182; P:filamentous growth of a population of unicellular organisms; IMP:CGD.
 GO; GO:0036180; P:filamentous growth of a population of unicellular organisms in response to biotic stimulus; IMP:CGD.
 GO; GO:0036171; P:filamentous growth of a population of unicellular organisms in response to chemical stimulus; IMP:CGD.
 GO; GO:0036170; P:filamentous growth of a population of unicellular organisms in response to starvation; IMP:CGD.
 GO; GO:0051645; P:Golgi localization; IMP:CGD.
 GO; GO:0030448; P:hyphal growth; IMP:CGD.
 GO; GO:0030011; P:maintenance of cell polarity; IMP:CGD.
 GO; GO:0009405; P:pathogenesis; IMP:CGD.
 InterPro; IPR016024; ARM-type_fold.
 InterPro; IPR014767; DAD_dom.
 InterPro; IPR015425; FH2_Formin.
 InterPro; IPR010472; FH3_dom.
 InterPro; IPR014768; GBD/FH3_dom.
 InterPro; IPR010473; GTPase-bd.
 Pfam; PF06367; Drf_FH3; 1.
 Pfam; PF06371; Drf_GBD; 1.
 Pfam; PF02181; FH2; 1.
 SMART; SM01139; Drf_FH3; 1.
 SMART; SM01140; Drf_GBD; 1.
 SMART; SM00498; FH2; 1.
 SUPFAM; SSF48371; SSF48371; 2.
 PROSITE; PS51231; DAD; 1.
 PROSITE; PS51444; FH2; 1.
 PROSITE; PS51232; GBD_FH3; 1.
 1: Evidence at protein level;
 Actin-binding; Cell cycle; Cell division; Coiled coil;
 Complete proteome; Cytoplasm; Cytoskeleton; Reference proteome;
 Virulence.
 CHAIN         1   1732       Formin BNI1.
                              /FTId=PRO_0000424601.
 DOMAIN      111    557       GBD/FH3. {ECO:0000255|PROSITE-
                              ProRule:PRU00579}.
 DOMAIN     1128   1544       FH2. {ECO:0000255|PROSITE-
                              ProRule:PRU00774}.
 DOMAIN     1563   1595       DAD. {ECO:0000255|PROSITE-
                              ProRule:PRU00577}.
 COILED      578    672       {ECO:0000255}.
 COILED      724    747       {ECO:0000255}.
 COILED      773    924       {ECO:0000255}.
 COILED     1419   1442       {ECO:0000255}.
 COILED     1518   1544       {ECO:0000255}.
 COMPBIAS     13     91       Ser-rich.
 COMPBIAS    756    759       Poly-Glu.
 COMPBIAS    788    797       Poly-Glu.
 COMPBIAS   1051   1067       Poly-Pro.
 COMPBIAS   1078   1088       Poly-Pro.
 SEQUENCE   1732 AA;  196794 MW;  7A1FC5191FE5D2FA CRC64;
 MRRRHKDKHN TDSVSDMSSN DSASILSSAS QNSTHSRRSA SLQSLHSQSH QYPQGHNNSS
 HRQASTYSIS SLSPYDKGAS LSRKSTNISI SRPIKTNDSN VFPIKQSFQL ERPNSAFEIE
 RMFRELLEKL NFKSLPPQAT REMLNYDIDR KWMMIEQDAR AEYDRQQRYA RAQNIFSPEE
 YAKVLMSKQV STNQLSGLWL ALRSEPIDWV RRFVYDCQGD TLLSVYLTKL QQEMVSCNIT
 DIEDDIFDKE VNVLQSLKCL MNQRLGAERI KTDVDVFVNA VSGSLLSPRI ITRKLATDTL
 TFMISYNGNN DNGRYHKVLR ALDSINEKSR MEFDSPDNYS PRKLTRKPPQ PANFKRFELW
 LNVVEKTIDA RGKFRNSDVG ASDELKSAYA GTRGSVITTR NQLENHLVEY CIATMLLINV
 IVGNGTDYRV RIHLRAQFRA AGLDRIIHKF LELGNEELDN MITRHKIDAN NDEEELKYSA
 NFNNEDNEVD FNDPVNLVQS LWQSVKNSDA EGYFLSAIQH LFLNQSEKRG NPEEMNRSLR
 VLDGLIQNIS SVRTVSEDTA INVAINKLIS NMSTDDMYRK ALEDVKIYRR IAEEATAERD
 DMSRQLSMGA DGYINSLLND VKERDMVISR FRRINEDMKE ELEQMKTKYM QEKQESELEM
 RELLIMLNNS EIGANAVKKD GGKTTISIST SNEELAARLK KQIHRRRAEY KLDNRQLGTN
 VEPSSRLRAL RDQMGDIENM ARELEMTDFE TYADPEEEEN NNDQSPEKSE IDESRSSQES
 EAEIQSVEED EEEEEKEVVI PPLPVPSGPK RAVRNDDLVR LDHLRKKLAN LQSESNDIMK
 YNSSSMFNKQ KFLAMERLQE LENNFKDFNI DFAVSDPEDK YNFNSNAGSV DDSIKNKTKE
 VLAEAEQIRE ELRRQLAAAQ KIKSPSPKRN TVLERIENKY VKGQVKIDAP DVVSNSPRTQ
 KRAHRSTTLN AMDPKFLQEL SLKVGKAEPI QDANNKNQFG GPLSSSPEDV SQKHKTSGDS
 SDKDKVLSSP ISSNDIKSPE TGNSTTSSAA PPPPPPPPPP PPPPLPPILG GNNSSAAPPP
 PPPPPPPPAF LNGSGSVIPP APPLPPPSSG RSSRSVPSTV TKSSGSAFDK IPRPKKKLKQ
 LHWEKIDHSQ VGNSFWNDPN THTLVDDLMS KGIFDEIELI FAAKEAKKLA TKKKEDLDKV
 TFLARDISQQ FSINLHAFNS FSDEEFVLKV LRCDKDVLTN PAVLDFFGKE DIVEITNTLA
 RNFEPYSTDY KTEEITKPEK DPNELQRPDR IYLELMYNLQ HYWKSRTRAL NVVVNYDKDY
 VEYVKKLRLI DEAVDSIKNS KHLKGVFEII LAVGNYMNDS AKQAHGFKLS SLQRLSFMKD
 EKNSMTFLHY VEKVIRTQYP EFLEFINELS CCNEITKFSI ENINNDCKEY ARAIKNVQSS
 IDIGNLSDVS KFHPSDRVLK AVLPALPRAK RKAELLLDQA NYTMKEFDDL MKYFGEDPTD
 QFVKNSFISK FTDFMKDFKR VQAENIKREE ELRVYEQRKK LLEKPKSSNN GDSNASDQDG
 ESNEGDGGVM DSLLQRLKAA APTKGESASA RKKALMRKQI LESQRKRTTG SVGSPTNVSP
 TRNNESDSGV DNKDDTHGSS PLDEQFHDSI TTQEDRIRDD NRPPEGVADF SNVEDPENPD
 VGARAKNLLQ ELRGADESSS KLSDAQRYRQ ERLKKKSVQI DLDEVAKNNN SE

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