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Protein BNI1 (Pointed projection formation protein 3) (Sensitive to high expression protein 5) (Synthetic lethal 39)

 BNI1_YEAST              Reviewed;        1953 AA.
P41832; D6W0S3; O13450;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
21-SEP-2011, sequence version 3.
22-NOV-2017, entry version 177.
RecName: Full=Protein BNI1;
AltName: Full=Pointed projection formation protein 3;
AltName: Full=Sensitive to high expression protein 5;
AltName: Full=Synthetic lethal 39;
Name=BNI1; Synonyms=PPF3, SHE5; OrderedLocusNames=YNL271C;
ORFNames=N0646;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Fares H.F., Pringle J.R.;
"Synthetic lethals of CDC12.";
Submitted (APR-1994) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 26109 / X2180;
PubMed=7941743; DOI=10.1002/yea.320100503;
Yorihuzi T., Ohsumi Y.;
"Saccharomyces cerevisiae MATa mutant cells defective in pointed
projection formation in response to alpha-factor at high
concentrations.";
Yeast 10:579-594(1994).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169873;
Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F.,
Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M.,
Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N.,
Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D.,
Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A.,
Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A.,
Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C.,
Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M.,
Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J.,
Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L.,
Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M.,
Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P.,
Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A.,
Wambutt R., Wedler H., Zollner A., Hani J.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV
and its evolutionary implications.";
Nature 387:93-98(1997).
[4]
GENOME REANNOTATION, AND SEQUENCE REVISION TO 938.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-1553.
STRAIN=ATCC 96604 / S288c / FY1679;
PubMed=8740425;
DOI=10.1002/(SICI)1097-0061(199604)12:5<505::AID-YEA932>3.0.CO;2-F;
Sen-Gupta M., Lyck R., Fleig U., Niedenthal R.K., Hegemann J.H.;
"The sequence of a 24,152 bp segment from the left arm of chromosome
XIV from Saccharomyces cerevisiae between the BNI1 and the POL2
genes.";
Yeast 12:505-514(1996).
[6]
FUNCTION.
PubMed=10085293; DOI=10.1083/jcb.144.5.947;
Lee L., Klee S.K., Evangelista M., Boone C., Pellman D.;
"Control of mitotic spindle position by the Saccharomyces cerevisiae
formin Bni1p.";
J. Cell Biol. 144:947-961(1999).
[7]
FUNCTION, AND TETRAMERIZATION.
PubMed=14561409; DOI=10.1016/j.cub.2003.09.057;
Zigmond S.H., Evangelista M., Boone C., Yang C., Dar A.C., Sicheri F.,
Forkey J., Pring M.;
"Formin leaky cap allows elongation in the presence of tight capping
proteins.";
Curr. Biol. 13:1820-1823(2003).
[8]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-311; SER-1170; SER-1338
AND SER-1344, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
STRAIN=ADR376;
PubMed=17330950; DOI=10.1021/pr060559j;
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
Elias J.E., Gygi S.P.;
"Large-scale phosphorylation analysis of alpha-factor-arrested
Saccharomyces cerevisiae.";
J. Proteome Res. 6:1190-1197(2007).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-311 AND SER-1170, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-325; SER-1085; SER-1170
AND THR-1918, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides
insights into evolution.";
Science 325:1682-1686(2009).
[12]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1350-1760, AND DIMERIZATION.
PubMed=15006353; DOI=10.1016/S0092-8674(04)00210-7;
Xu Y., Moseley J.B., Sagot I., Poy F., Pellman D., Goode B.L.,
Eck M.J.;
"Crystal structures of a formin homology-2 domain reveal a tethered
dimer architecture.";
Cell 116:711-723(2004).
[13]
X-RAY CRYSTALLOGRAPHY (3.05 ANGSTROMS) OF 1327-1769 IN COMPLEX WITH
ATP AND ACTIN.
PubMed=15635372; DOI=10.1038/nature03251;
Otomo T., Tomchick D.R., Otomo C., Panchal S.C., Machius M.,
Rosen M.K.;
"Structural basis of actin filament nucleation and processive capping
by a formin homology 2 domain.";
Nature 433:488-494(2005).
-!- 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. Potential target of the RHO
family members. {ECO:0000269|PubMed:10085293,
ECO:0000269|PubMed:14561409}.
-!- SUBUNIT: Homodimer, and possibly also homotetramer. Interacts with
PFY1 via the FH1 domain and with actin via the FH2 domain.
{ECO:0000269|PubMed:15635372}.
-!- INTERACTION:
Self; NbExp=3; IntAct=EBI-3692, EBI-3692;
P68139:ACTA1 (xeno); NbExp=2; IntAct=EBI-3692, EBI-3058728;
P36006:MYO3; NbExp=3; IntAct=EBI-3692, EBI-11670;
-!- SUBCELLULAR LOCATION: Cell membrane. Cell projection, ruffle
membrane. Cytoplasm, cytoskeleton.
-!- 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}.
-!- MISCELLANEOUS: Each FH2 dimer contains binding sites for 4 actin
molecules.
-!- MISCELLANEOUS: Present with 166 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the formin homology family. BNI1 subfamily.
{ECO:0000305}.
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EMBL; L31766; AAA34455.1; -; Genomic_DNA.
EMBL; D38411; BAA22512.1; -; Genomic_DNA.
EMBL; Z71546; CAA96178.1; -; Genomic_DNA.
EMBL; Z71547; CAA96179.1; -; Genomic_DNA.
EMBL; X92494; CAA63225.1; -; Genomic_DNA.
EMBL; BK006947; DAA10289.2; -; Genomic_DNA.
PIR; S63244; S63244.
RefSeq; NP_014128.2; NM_001183109.2.
PDB; 1UX4; X-ray; 3.30 A; A/B=1352-1765.
PDB; 1UX5; X-ray; 2.50 A; A=1350-1760.
PDB; 1Y64; X-ray; 3.05 A; B=1327-1769.
PDBsum; 1UX4; -.
PDBsum; 1UX5; -.
PDBsum; 1Y64; -.
ProteinModelPortal; P41832; -.
SMR; P41832; -.
BioGrid; 35569; 433.
DIP; DIP-974N; -.
IntAct; P41832; 29.
MINT; MINT-582139; -.
STRING; 4932.YNL271C; -.
iPTMnet; P41832; -.
MaxQB; P41832; -.
PRIDE; P41832; -.
EnsemblFungi; YNL271C; YNL271C; YNL271C.
GeneID; 855450; -.
KEGG; sce:YNL271C; -.
EuPathDB; FungiDB:YNL271C; -.
SGD; S000005215; BNI1.
GeneTree; ENSGT00710000107854; -.
HOGENOM; HOG000095244; -.
InParanoid; P41832; -.
KO; K11238; -.
OMA; NDANKQA; -.
OrthoDB; EOG092C03J2; -.
BioCyc; YEAST:G3O-33265-MONOMER; -.
EvolutionaryTrace; P41832; -.
PRO; PR:P41832; -.
Proteomes; UP000002311; Chromosome XIV.
GO; GO:0005884; C:actin filament; IDA:SGD.
GO; GO:0032153; C:cell division site; IDA:SGD.
GO; GO:0005935; C:cellular bud neck; IDA:SGD.
GO; GO:0005934; C:cellular bud tip; IDA:SGD.
GO; GO:0000131; C:incipient cellular bud site; IDA:SGD.
GO; GO:0043332; C:mating projection tip; IDA:SGD.
GO; GO:0000133; C:polarisome; IDA:SGD.
GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0005522; F:profilin binding; IDA:SGD.
GO; GO:0017048; F:Rho GTPase binding; IEA:InterPro.
GO; GO:0051017; P:actin filament bundle assembly; IMP:SGD.
GO; GO:0045010; P:actin nucleation; IDA:SGD.
GO; GO:0071519; P:actomyosin contractile ring actin filament bundle assembly; IMP:SGD.
GO; GO:0051016; P:barbed-end actin filament capping; IDA:SGD.
GO; GO:0007118; P:budding cell apical bud growth; IMP:SGD.
GO; GO:0000132; P:establishment of mitotic spindle orientation; IMP:SGD.
GO; GO:0070649; P:formin-nucleated actin cable assembly; IDA:SGD.
GO; GO:2000251; P:positive regulation of actin cytoskeleton reorganization; IMP:SGD.
GO; GO:0032880; P:regulation of protein localization; IMP:SGD.
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; 3.
PROSITE; PS51231; DAD; 1.
PROSITE; PS51444; FH2; 1.
PROSITE; PS51232; GBD_FH3; 1.
1: Evidence at protein level;
3D-structure; Actin-binding; Cell membrane; Cell projection;
Coiled coil; Complete proteome; Cytoplasm; Cytoskeleton; Membrane;
Phosphoprotein; Reference proteome.
CHAIN 1 1953 Protein BNI1.
/FTId=PRO_0000194899.
DOMAIN 174 696 GBD/FH3. {ECO:0000255|PROSITE-
ProRule:PRU00579}.
DOMAIN 1053 1337 FH1.
DOMAIN 1348 1766 FH2. {ECO:0000255|PROSITE-
ProRule:PRU00774}.
DOMAIN 1792 1826 DAD. {ECO:0000255|PROSITE-
ProRule:PRU00577}.
COILED 712 807 {ECO:0000255}.
COILED 864 894 {ECO:0000255}.
COILED 928 981 {ECO:0000255}.
COILED 1732 1811 {ECO:0000255}.
COMPBIAS 64 67 Poly-Ser.
COMPBIAS 1053 1057 Poly-Ser.
COMPBIAS 1239 1250 Poly-Pro.
COMPBIAS 1278 1291 Poly-Pro.
COMPBIAS 1303 1309 Poly-Pro.
COMPBIAS 1751 1754 Poly-Glu.
MOD_RES 311 311 Phosphoserine.
{ECO:0000244|PubMed:17330950,
ECO:0000244|PubMed:18407956}.
MOD_RES 325 325 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 1085 1085 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 1170 1170 Phosphoserine.
{ECO:0000244|PubMed:17330950,
ECO:0000244|PubMed:18407956,
ECO:0000244|PubMed:19779198}.
MOD_RES 1338 1338 Phosphoserine.
{ECO:0000244|PubMed:17330950}.
MOD_RES 1344 1344 Phosphoserine.
{ECO:0000244|PubMed:17330950}.
MOD_RES 1918 1918 Phosphothreonine.
{ECO:0000244|PubMed:19779198}.
CONFLICT 938 938 A -> T (in Ref. 3; CAA96178/CAA96179 and
5; CAA63225). {ECO:0000305}.
CONFLICT 1430 1430 G -> C (in Ref. 1; AAA34455).
{ECO:0000305}.
STRAND 1371 1373 {ECO:0000244|PDB:1UX5}.
HELIX 1378 1388 {ECO:0000244|PDB:1UX5}.
HELIX 1391 1398 {ECO:0000244|PDB:1UX5}.
STRAND 1400 1402 {ECO:0000244|PDB:1UX5}.
HELIX 1405 1413 {ECO:0000244|PDB:1UX5}.
TURN 1414 1416 {ECO:0000244|PDB:1UX5}.
HELIX 1423 1432 {ECO:0000244|PDB:1UX5}.
HELIX 1434 1436 {ECO:0000244|PDB:1UX5}.
HELIX 1441 1449 {ECO:0000244|PDB:1UX5}.
TURN 1450 1452 {ECO:0000244|PDB:1UX5}.
HELIX 1453 1456 {ECO:0000244|PDB:1UX5}.
HELIX 1459 1464 {ECO:0000244|PDB:1UX5}.
HELIX 1468 1471 {ECO:0000244|PDB:1UX5}.
HELIX 1475 1480 {ECO:0000244|PDB:1UX5}.
HELIX 1482 1484 {ECO:0000244|PDB:1UX5}.
HELIX 1494 1496 {ECO:0000244|PDB:1UX5}.
HELIX 1504 1506 {ECO:0000244|PDB:1Y64}.
HELIX 1509 1516 {ECO:0000244|PDB:1UX5}.
TURN 1517 1524 {ECO:0000244|PDB:1UX5}.
HELIX 1525 1535 {ECO:0000244|PDB:1UX5}.
HELIX 1538 1560 {ECO:0000244|PDB:1UX5}.
HELIX 1563 1579 {ECO:0000244|PDB:1UX5}.
HELIX 1582 1584 {ECO:0000244|PDB:1UX5}.
HELIX 1591 1596 {ECO:0000244|PDB:1UX5}.
STRAND 1597 1599 {ECO:0000244|PDB:1UX5}.
STRAND 1603 1608 {ECO:0000244|PDB:1UX4}.
HELIX 1609 1620 {ECO:0000244|PDB:1UX5}.
HELIX 1622 1626 {ECO:0000244|PDB:1UX5}.
HELIX 1627 1630 {ECO:0000244|PDB:1UX5}.
HELIX 1632 1637 {ECO:0000244|PDB:1UX5}.
HELIX 1642 1665 {ECO:0000244|PDB:1UX5}.
TURN 1667 1669 {ECO:0000244|PDB:1UX5}.
TURN 1671 1673 {ECO:0000244|PDB:1Y64}.
HELIX 1680 1715 {ECO:0000244|PDB:1UX5}.
STRAND 1720 1722 {ECO:0000244|PDB:1Y64}.
HELIX 1723 1757 {ECO:0000244|PDB:1UX5}.
SEQUENCE 1953 AA; 219673 MW; 0C5A9D5280A5858F CRC64;
MLKNSGSKHS NSKESHSNSS SGIFQNLKRL ANSNATNSNT GSPTYASQQQ HSPVGNEVST
SPASSSSFRK LNAPSRSTST EARPLNKKST LNTQNLSQYM NGKLSGDVPV SSQHARSHSM
QSKYSYSKRN SSQASNKLTR QHTGQSHSAS SLLSQGSLTN LSKFTTPDGK IYLEMPSDPY
EVEVLFEDIM YKRNIFQSLS EDKQEALMGY SIEKKWLIVK QDLQNELKKM RANTTSSSTA
SRTSMASDHH PILTANSSLS SPKSVLMTSA SSPTSTVYSN SLNHSTTLSS VGTSTSKGKK
LVSGSLKKQP SLNNIYRGGA ENNTSASTLP GDRTNRPPIH YVQRILADKL TSDEMKDLWV
TLRTEQLDWV DAFIDHQGHI AMANVLMNSI YKTAPRENLT KELLEKENSF FKCFRVLSML
SQGLYEFSTH RLMTDTVAEG LFSTKLATRK MATEIFVCML EKKNKSRFEA VLTSLDKKFR
IGQNLHMIQN FKKMPQYFSH LTLESHLKII QAWLFAVEQT LDGRGKMGSL VGASDEFKNG
GGENAILEYC QWTMVFINHL CSCSDNINQR MLLRTKLENC GILRIMNKIK LLDYDKVIDQ
IELYDNNKLD DFNVKLEANN KAFNVDLHDP LSLLKNLWDI CKGTENEKLL VSLVQHLFLS
SSKLIEENQN SSKLTKQLKL MDSLVTNVSV ASTSDEETNM NMAIQRLYDA MQTDEVARRA
ILESRALTKK LEEIQAERDS LSEKLSKAEH GLVGQLEDEL HERDRILAKN QRVMQQLEAE
LEELKKKHLL EKHQQEVELR KMLTILNSRP EESFNKNEGT RGMNSSLNSS EKANIQKVLQ
DGLSRAKKDY KDDSKKFGMT LQPNKRLKML RMQMENIENE ARQLEMTNFA EFEKDRLEPP
IHIKKPKVKK MKNKDRKPLV KPQEADVNKL NDLRRALAEI QMESNDISKF NVEERVNELF
NEKKSLALKR LKELETKYKG FGIDFNVDEI MDSPKKNTGD VETEEDANYA SLDPKTYQKK
LDEINRITDQ LLDIQTQTEH EIQVEEDGES DLSSSSSDDE SEEIYQDASP TQELRSEHSE
LSSGSGPGSF LDALSQKYGT GQNVTASAAF GENNNGSGIG PLHSKVEKTF MNRLRKSTVS
SAPYLEELTQ KVNKVEPYEQ NEDEGLDKKS LPENSTASAA SAFDKAEKDM RQHVENGKQG
RVVNHEEDKT ADFSAVSKLN NTDGAEDLST QSSVLSSQPP PPPPPPPPVP AKLFGESLEK
EKKSEDDTVK QETTGDSPAP PPPPPPPPPP PMALFGKPKG ETPPPPPLPS VLSSSTDGVI
PPAPPMMPAS QIKSAVTSPL LPQSPSLFEK YPRPHKKLKQ LHWEKLDCTD NSIWGTGKAE
KFADDLYEKG VLADLEKAFA AREIKSLASK RKEDLQKITF LSRDISQQFG INLHMYSSLS
VADLVKKILN CDRDFLQTPS VVEFLSKSEI IEVSVNLARN YAPYSTDWEG VRNLEDAKPP
EKDPNDLQRA DQIYLQLMVN LESYWGSRMR ALTVVTSYER EYNELLAKLR KVDKAVSALQ
ESDNLRNVFN VILAVGNFMN DTSKQAQGFK LSTLQRLTFI KDTTNSMTFL NYVEKIVRLN
YPSFNDFLSE LEPVLDVVKV SIEQLVNDCK DFSQSIVNVE RSVEIGNLSD SSKFHPLDKV
LIKTLPVLPE ARKKGDLLED EVKLTIMEFE SLMHTYGEDS GDKFAKISFF KKFADFINEY
KKAQAQNLAA EEEERLYIKH KKIVEEQQKR AQEKEKQKEN SNSPSSEGNE EDEAEDRRAV
MDKLLEQLKN AGPAKSDPSS ARKRALVRKK YLSEKDNAPQ LLNDLDTEEG SILYSPEAMD
PTADTVIHAE SPTPLATRGV MNTSEDLPSP SKTSALEDQE EISDRARMLL KELRGSDTPV
KQNSILDEHL EKLRARKERS IGEASTGNRL SFK


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