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Formin BNI1

 BNI1_CANAL              Reviewed;        1732 AA.
Q5AL52; A0A1D8PFJ4;
11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
26-APR-2005, sequence version 1.
07-JUN-2017, entry version 91.
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; MINT-7295678; -.
PRIDE; Q5AL52; -.
GeneID; 3636118; -.
KEGG; cal:CAALFM_C112960CA; -.
CGD; CAL0000188644; BNI1.
InParanoid; Q5AL52; -.
KO; K11238; -.
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.
Gene3D; 1.25.10.10; -; 1.
InterPro; IPR011989; ARM-like.
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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