BNI1_CANAL
ID BNI1_CANAL Reviewed; 1732 AA.
AC Q5AL52; A0A1D8PFJ4;
DT 11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 25-MAY-2022, entry version 116.
DE RecName: Full=Formin BNI1;
GN Name=BNI1; OrderedLocusNames=CAALFM_C112960CA;
GN ORFNames=CaO19.12393, CaO19.4927;
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 FUNCTION, AND 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.
RX PubMed=15976451; DOI=10.1242/jcs.02414;
RA Crampin H., Finley K., Gerami-Nejad M., Court H., Gale C., Berman J.,
RA Sudbery P.;
RT "Candida albicans hyphae have a Spitzenkorper that is distinct from the
RT polarisome found in yeast and pseudohyphae.";
RL J. Cell Sci. 118:2935-2947(2005).
RN [7]
RP FUNCTION.
RX PubMed=16855023; DOI=10.1091/mbc.e06-02-0143;
RA Rida P.C., Nishikawa A., Won G.Y., Dean N.;
RT "Yeast-to-hyphal transition triggers formin-dependent Golgi localization to
RT the growing tip in Candida albicans.";
RL Mol. Biol. Cell 17:4364-4378(2006).
RN [8]
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 [9]
RP SUBCELLULAR LOCATION.
RX PubMed=17504812; DOI=10.1242/jcs.002931;
RA Li C.R., Lee R.T., Wang Y.M., Zheng X.D., Wang Y.;
RT "Candida albicans hyphal morphogenesis occurs in Sec3p-independent and
RT Sec3p-dependent phases separated by septin ring formation.";
RL J. Cell Sci. 120:1898-1907(2007).
RN [10]
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: Required for the assembly of F-actin structures, such as
CC actin cables and stress fibers. Nucleates actin filaments. Binds to the
CC barbed end of the actin filament and acts as leaky capper, slowing both
CC polymerization and depolymerization. Protects the growing actin fiber
CC from tight capping proteins and so increases the time of elongation and
CC the total amount of F-actin. May organize microtubules by mediating
CC spindle positioning and movement in the budding process. Required for
CC the maintenance of polarized hyphal growth. BNI1-mediated actin cables
CC are necessary for positioning the Golgi complex to a putative site of
CC germ tube emergence and for coordinating the transport and deposition
CC of membrane and cell wall material to a growing hypha. Plays a key role
CC in virulence. {ECO:0000269|PubMed:15914538,
CC ECO:0000269|PubMed:16215178, ECO:0000269|PubMed:16855023,
CC ECO:0000269|PubMed:17715368}.
CC -!- SUBUNIT: Homodimer, and possibly also homotetramer (By similarity).
CC Interacts with actin via the FH2 domain (By similarity). Interacts with
CC IQG1. {ECO:0000250, ECO:0000269|PubMed:18923418}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Bud neck. Bud tip. Cell
CC septum. Note=Localizes to the presumptive budding site in G1 cells, the
CC bud tip of small to medium-budded cells and the bud neck of large-
CC budded cells. During hyphal growth at least a fraction persistently
CC localizes at the tips of germ tubes and hyphae independently of cell
CC cycle progression. Localizes at the Spitzenkorper, a structure found in
CC fungal hyphae which is the organizing center for hyphal growth and
CC morphogenesis.
CC -!- DOMAIN: The DAD domain regulates activation via by an autoinhibitory
CC interaction with the GBD/FH3 domain. This autoinhibition is released
CC upon competitive binding of an activated GTPase. The release of DAD
CC allows the FH2 domain to then nucleate and elongate nonbranched actin
CC filaments (By similarity). {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Leads to swollen cells, increased random budding
CC pattern, and severe defect in cytokinesis with enlarged bud necks.
CC {ECO:0000269|PubMed:16215178}.
CC -!- SIMILARITY: Belongs to the formin homology family. BNI1 subfamily.
CC {ECO:0000305}.
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DR EMBL; CP017623; AOW26910.1; -; Genomic_DNA.
DR RefSeq; XP_722138.1; XM_717045.1.
DR AlphaFoldDB; Q5AL52; -.
DR SMR; Q5AL52; -.
DR BioGRID; 1219195; 3.
DR IntAct; Q5AL52; 1.
DR MINT; Q5AL52; -.
DR STRING; 237561.Q5AL52; -.
DR PRIDE; Q5AL52; -.
DR GeneID; 3636118; -.
DR KEGG; cal:CAALFM_C112960CA; -.
DR CGD; CAL0000188644; BNI1.
DR VEuPathDB; FungiDB:C1_12960C_A; -.
DR eggNOG; KOG1922; Eukaryota.
DR HOGENOM; CLU_001313_1_0_1; -.
DR InParanoid; Q5AL52; -.
DR OMA; KALHWEK; -.
DR OrthoDB; 1204639at2759; -.
DR PRO; PR:Q5AL52; -.
DR Proteomes; UP000000559; Chromosome 1.
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:0005934; C:cellular bud tip; IDA:CGD.
DR GO; GO:0001411; C:hyphal tip; IDA:CGD.
DR GO; GO:0000131; C:incipient cellular bud site; IDA:CGD.
DR GO; GO:0043332; C:mating projection tip; IBA:GO_Central.
DR GO; GO:0031521; C:spitzenkorper; IDA:CGD.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0008092; F:cytoskeletal protein binding; IDA:CGD.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0051666; P:actin cortical patch localization; IMP:CGD.
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:0000282; P:cellular bud site selection; IMP:CGD.
DR GO; GO:0009267; P:cellular response to starvation; IMP:CGD.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IMP:CGD.
DR GO; GO:0030447; P:filamentous growth; IMP:CGD.
DR GO; GO:0044182; P:filamentous growth of a population of unicellular organisms; IMP:CGD.
DR GO; GO:0036180; P:filamentous growth of a population of unicellular organisms in response to biotic stimulus; IMP:CGD.
DR GO; GO:0036171; P:filamentous growth of a population of unicellular organisms in response to chemical stimulus; IMP:CGD.
DR GO; GO:0036170; P:filamentous growth of a population of unicellular organisms in response to starvation; IMP:CGD.
DR GO; GO:0051645; P:Golgi localization; IMP:CGD.
DR GO; GO:0030448; P:hyphal growth; IMP:CGD.
DR GO; GO:0030011; P:maintenance of cell polarity; IMP:CGD.
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; IPR014767; DAD_dom.
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; PS51231; DAD; 1.
DR PROSITE; PS51444; FH2; 1.
DR PROSITE; PS51232; GBD_FH3; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Cell cycle; Cell division; Coiled coil; Cytoplasm;
KW Cytoskeleton; Reference proteome; Virulence.
FT CHAIN 1..1732
FT /note="Formin BNI1"
FT /id="PRO_0000424601"
FT DOMAIN 111..557
FT /note="GBD/FH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00579"
FT DOMAIN 1128..1544
FT /note="FH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00774"
FT DOMAIN 1563..1595
FT /note="DAD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00577"
FT REGION 1..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 331..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 754..814
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 948..974
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 992..1136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1541..1569
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1601..1714
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 578..672
FT /evidence="ECO:0000255"
FT COILED 724..747
FT /evidence="ECO:0000255"
FT COILED 773..924
FT /evidence="ECO:0000255"
FT COILED 1419..1442
FT /evidence="ECO:0000255"
FT COILED 1518..1544
FT /evidence="ECO:0000255"
FT COMPBIAS 15..81
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 762..779
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 783..797
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 953..974
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 992..1011
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1023..1047
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1048..1110
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1111..1126
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1547..1561
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1605..1626
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1627..1665
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1697..1714
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ 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
