BNR1_YEAST
ID BNR1_YEAST Reviewed; 1375 AA.
AC P40450; D6VVC7;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=BNI1-related protein 1;
GN Name=BNR1; OrderedLocusNames=YIL159W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169870;
RA Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
RA Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E.,
RA Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C.,
RA Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V.,
RA Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
RL Nature 387:84-87(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP FUNCTION.
RX PubMed=9184220; DOI=10.1093/emboj/16.10.2745;
RA Imamura H., Tanaka K., Hihara T., Umikawa M., Kamei T., Takahashi K.,
RA Sasaki T., Takai Y.;
RT "Bni1p and Bnr1p: downstream targets of the Rho family small G-proteins
RT which interact with profilin and regulate actin cytoskeleton in
RT Saccharomyces cerevisiae.";
RL EMBO J. 16:2745-2755(1997).
RN [4]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-621 AND SER-751, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: May organize microtubules by mediating spindle positioning
CC and movement in the budding process. Potential target of the RHO family
CC members (By similarity). {ECO:0000250, ECO:0000269|PubMed:9184220}.
CC -!- SUBUNIT: Interacts with profilin at the FH1 domain.
CC -!- INTERACTION:
CC P40450; P11710: FUS1; NbExp=5; IntAct=EBI-3711, EBI-7179;
CC P40450; Q05080: HOF1; NbExp=5; IntAct=EBI-3711, EBI-5412;
CC P40450; P36006: MYO3; NbExp=6; IntAct=EBI-3711, EBI-11670;
CC P40450; Q04439: MYO5; NbExp=7; IntAct=EBI-3711, EBI-11687;
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 -!- MISCELLANEOUS: Present with 259 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the formin homology family. BNI1 subfamily.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Z38059; CAA86119.1; -; Genomic_DNA.
DR EMBL; BK006942; DAA08393.1; -; Genomic_DNA.
DR PIR; S48375; S48375.
DR RefSeq; NP_012107.1; NM_001179507.1.
DR AlphaFoldDB; P40450; -.
DR SMR; P40450; -.
DR BioGRID; 34833; 197.
DR DIP; DIP-817N; -.
DR IntAct; P40450; 19.
DR MINT; P40450; -.
DR STRING; 4932.YIL159W; -.
DR iPTMnet; P40450; -.
DR MaxQB; P40450; -.
DR PaxDb; P40450; -.
DR PRIDE; P40450; -.
DR EnsemblFungi; YIL159W_mRNA; YIL159W; YIL159W.
DR GeneID; 854647; -.
DR KEGG; sce:YIL159W; -.
DR SGD; S000001421; BNR1.
DR VEuPathDB; FungiDB:YIL159W; -.
DR eggNOG; KOG1922; Eukaryota.
DR GeneTree; ENSGT00940000170414; -.
DR HOGENOM; CLU_002339_0_0_1; -.
DR InParanoid; P40450; -.
DR OMA; KQIHWEK; -.
DR BioCyc; YEAST:G3O-31407-MON; -.
DR PRO; PR:P40450; -.
DR Proteomes; UP000002311; Chromosome IX.
DR RNAct; P40450; protein.
DR GO; GO:0032153; C:cell division site; IDA:SGD.
DR GO; GO:0005935; C:cellular bud neck; IDA:SGD.
DR GO; GO:0043332; C:mating projection tip; IBA:GO_Central.
DR GO; GO:0003779; F:actin binding; IEA:InterPro.
DR GO; GO:0005522; F:profilin binding; IDA:SGD.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0051017; P:actin filament bundle assembly; IDA:SGD.
DR GO; GO:0045010; P:actin nucleation; IDA:SGD.
DR GO; GO:0051016; P:barbed-end actin filament capping; IDA:SGD.
DR GO; GO:0070649; P:formin-nucleated actin cable assembly; IDA:SGD.
DR GO; GO:1903475; P:mitotic actomyosin contractile ring assembly; IGI:SGD.
DR GO; GO:2000251; P:positive regulation of actin cytoskeleton reorganization; IGI:SGD.
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; IPR014768; GBD/FH3_dom.
DR InterPro; IPR010473; GTPase-bd.
DR Pfam; PF02181; FH2; 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 Coiled coil; Phosphoprotein; Reference proteome.
FT CHAIN 1..1375
FT /note="BNI1-related protein 1"
FT /id="PRO_0000194900"
FT DOMAIN 94..490
FT /note="GBD/FH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00579"
FT DOMAIN 659..851
FT /note="FH1"
FT DOMAIN 868..1290
FT /note="FH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00774"
FT DOMAIN 1302..1336
FT /note="DAD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00577"
FT REGION 661..684
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 764..785
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 817..839
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1285..1309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 520..601
FT /evidence="ECO:0000255"
FT COMPBIAS 764..783
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 817..831
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 621
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 751
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 1375 AA; 156852 MW; B16B04A33C9D2F08 CRC64;
MDSSPNKKTY RYPRRSLSLH ARDRVSEARK LEELNLNDGL VAAGLQLVGV ALEKQGTGSH
IYMKQKNFSA NDVSSSPMVS EEVNGSEMDF NPKCMPQDAS LVERMFDELL KDGTFFWGAA
YKNLQNISLR RKWLLICKIR SSNHWGKKKV TSSTTYSTHL ATNELAENAH FLDGLVRNLS
TGGMKLSKAL YKLEKFLRKQ SFLQLFLKDE IYLTTLIEKT LPLISKELQF VYLRCFKILM
NNPLARIRAL HSEPLIRWFT ELLTDQNSNL KCQLLSMELL LLLTYVEGST GCELIWDQLS
ILFTDWLEWF DKILADDIAI HSSLYLNWNQ LKIDYSTTFL LLINSILQGF NNKTALEILN
FLKKNNIHNT ITFLELAYKD DPNSVVIMEQ IKQFKSKESA IFDSMIKTTN DTNSLHPTKD
IARIESEPLC LENCLLLKAK DSPVEAPINE IIQSLWKILD SQKPYSESIK LLKLINSLLF
YLIDSFQVST NPSFDETLES AENVDYVFQD SVNKLLDSLQ SDEIARRAVT EIDDLNAKIS
HLNEKLNLVE NHDKDHLIAK LDESESLISL KTKEIENLKL QLKATKKRLD QITTHQRLYD
QPPSLASSNL SIAGSIIKNN SHGNIIFQNL AKKQQQQQKI SLPKRSTSLL KSKRVTSLSS
YLTDANNENE SQNESEDKSK DSLFQRSTST INFNIPSMKN ITNMQNVSLN SILSELEFSN
SLGTQPNYQS SPVLSSVSSS PKLFPRLSSD SLDNGIQLVP EVVKLPQLPP PPPPPPPPPL
PQSLLTEAEA KPDGVSCIAA PAPPPLPDLF KTKTCGAVPP PPPPPPLPES LSMNKGPSNH
DLVTPPAPPL PNGLLSSSSV SINPTTTDLK PPPTEKRLKQ IHWDKVEDIK DTLWEDTFQR
QETIKELQTD GIFSQIEDIF KMKSPTKIAN KRNAESSIAL SSNNGKSSNE LKKISFLSRD
LAQQFGINLH MFSQLSDMEF VMKVLNCDND IVQNVNILKF FCKEELVNIP KSMLNKYEPY
SQGKDGKAVS DLQRADRIFL ELCINLRFYW NARSKSLLTL STYERDYYDL IFKLQKIDDA
ISHLNRSPKF KSLMFIITEI GNHMNKRIVK GIKLKSLTKL AFVRSSIDQN VSFLHFIEKV
IRIKYPDIYG FVDDLKNIED LGKISLEHVE SECHEFHKKI EDLVTQFQVG KLSKEENLDP
RDQIIKKVKF KINRAKTKSE LLIGQCKLTL IDLNKLMKYY GEDPKDKESK NEFFQPFIEF
LAMFKKCAKE NIEKEEMERV YEQRKSLLDM RTSSNKKSNG SDENDGEKVN RDAVDLLISK
LREVKKDPEP LRRRKSTKLN EIAINVHEGD VKTRKDEDHV LLERTHAMLN DIQNI
