BNI4_YEAST
ID BNI4_YEAST Reviewed; 892 AA.
AC P53858; D6W0V9;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Protein BNI4;
GN Name=BNI4; OrderedLocusNames=YNL233W; ORFNames=N1146;
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 [GENOMIC DNA].
RX PubMed=8896273;
RX DOI=10.1002/(sici)1097-0061(199609)12:10b<1071::aid-yea4>3.0.co;2-s;
RA Pandolfo D., de Antoni A., Lanfranchi G., Valle G.;
RT "The DNA sequence of cosmid 14-5 from chromosome XIV reveals 21 open
RT reading frames including a novel gene encoding a globin-like domain.";
RL Yeast 12:1071-1076(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [3]
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 [4]
RP IDENTIFICATION, AND SUBUNIT.
RX PubMed=9314530; DOI=10.1083/jcb.139.1.75;
RA DeMarini D.J., Adams A.E., Fares H., De Virgilio C., Valle G., Chuang J.S.,
RA Pringle J.R.;
RT "A septin-based hierarchy of proteins required for localized deposition of
RT chitin in the Saccharomyces cerevisiae cell wall.";
RL J. Cell Biol. 139:75-93(1997).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-618, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-364, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-476; SER-503; SER-618;
RP THR-703; SER-746 AND SER-825, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43; SER-133; SER-281;
RP SER-394; THR-410; SER-476; SER-500; SER-503 AND SER-618, AND IDENTIFICATION
RP 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).
RN [9]
RP DISRUPTION PHENOTYPE.
RX PubMed=28346351; DOI=10.3390/ijms18040702;
RA Gohlke S., Muthukrishnan S., Merzendorfer H.;
RT "In Vitro and In Vivo Studies on the Structural Organization of Chs3 from
RT Saccharomyces cerevisiae.";
RL Int. J. Mol. Sci. 18:0-0(2017).
CC -!- SUBUNIT: May interact with CHS3 and seems to be an adapter (along with
CC SKT5) to link CHS3 to septins. {ECO:0000269|PubMed:9314530}.
CC -!- INTERACTION:
CC P53858; P32598: GLC7; NbExp=4; IntAct=EBI-3704, EBI-13715;
CC P53858; P02829: HSP82; NbExp=2; IntAct=EBI-3704, EBI-8659;
CC -!- DISRUPTION PHENOTYPE: CHS3 abnormally localized to vacuole.
CC {ECO:0000269|PubMed:28346351}.
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DR EMBL; Z69381; CAA93365.1; -; Genomic_DNA.
DR EMBL; Z71509; CAA96138.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10325.1; -; Genomic_DNA.
DR PIR; S63199; S63199.
DR RefSeq; NP_014166.1; NM_001183071.1.
DR AlphaFoldDB; P53858; -.
DR SMR; P53858; -.
DR BioGRID; 35605; 153.
DR ComplexPortal; CPX-1230; BNI4-GLC7 phosphatase complex.
DR DIP; DIP-1338N; -.
DR IntAct; P53858; 11.
DR MINT; P53858; -.
DR STRING; 4932.YNL233W; -.
DR iPTMnet; P53858; -.
DR MaxQB; P53858; -.
DR PaxDb; P53858; -.
DR PRIDE; P53858; -.
DR EnsemblFungi; YNL233W_mRNA; YNL233W; YNL233W.
DR GeneID; 855488; -.
DR KEGG; sce:YNL233W; -.
DR SGD; S000005177; BNI4.
DR VEuPathDB; FungiDB:YNL233W; -.
DR eggNOG; KOG4339; Eukaryota.
DR GeneTree; ENSGT00940000168134; -.
DR HOGENOM; CLU_312616_0_0_1; -.
DR InParanoid; P53858; -.
DR OMA; SINYHED; -.
DR BioCyc; YEAST:G3O-33233-MON; -.
DR Reactome; R-SCE-114608; Platelet degranulation.
DR PRO; PR:P53858; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P53858; protein.
DR GO; GO:0005935; C:cellular bud neck; IDA:SGD.
DR GO; GO:0032174; C:cellular bud neck septin collar; IDA:SGD.
DR GO; GO:0000131; C:incipient cellular bud site; IDA:SGD.
DR GO; GO:0000164; C:protein phosphatase type 1 complex; IPI:ComplexPortal.
DR GO; GO:0005940; C:septin ring; IDA:SGD.
DR GO; GO:0003779; F:actin binding; IBA:GO_Central.
DR GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0006031; P:chitin biosynthetic process; IMP:SGD.
DR GO; GO:0000917; P:division septum assembly; IMP:SGD.
DR GO; GO:0034221; P:fungal-type cell wall chitin biosynthetic process; IDA:ComplexPortal.
PE 1: Evidence at protein level;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..892
FT /note="Protein BNI4"
FT /id="PRO_0000064959"
FT REGION 185..287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 305..387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 506..526
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 618..644
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 685..734
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..219
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..237
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..284
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..335
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 685..702
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 703..718
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 719..734
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 43
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 133
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 281
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 364
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 394
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 410
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 476
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 500
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 503
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 618
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 703
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 746
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 825
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
SQ SEQUENCE 892 AA; 100590 MW; 0DF61702AD47B46C CRC64;
MSDSISDSKS SELLNSTFYS STSINTLDHA RTFRNSLILK EISDQSLNSS IKPCESVLDR
DVESSVLQRS FGESNARDSE VQTVNMTTSP SLSALADILN ERSKYADQKT RKAQNIESSI
IEEEEEAEEQ NNSINYHEDI TGSRLSVREE ANENLAMTSP NLIDIDGSNS IQVAPLSLPS
FEEPDFLSTP RVKPDSQGPR SKVSTRRTIL ERDNNLPVKR EENTIINSET ESTTHSAPFL
KEDPKPSPPS SKLYNPKVRL NKAEARKYTD SSAQRTTSAG SVLEDTSMHK KKKSIFSFLK
KKEPKPVIGN NSVTNEKNKM SSSSTFSMNI QTSLKTPEKL KKKSHSSSSI FNSFLKGKIE
TSDSPRKEPM RQKKRTPKSK DKKQDTEQII DAASVLSTES PLLRKNHDDT PVKIDHVTRS
IDQRKPTPLN MDLILGGDKQ INTPLQEHVR EDDDAKNDLQ LPTKDNFLSL DYEAPSPAFS
KHDTGEVLFP KFLDNHEVDS IVSLERTRST KSNKRSSMNS QRRSLTDTLS IKAQSEGMFI
TEASSVVLST PDLTKSPASS ILKNGRFEYS DNFSREHSYE GTTNEDFLDI KDDSGPLKKD
DIFLESIEQK FDQLVMASDE EKTEVERDVP KPREEPLKKD SERQSVFADD DNELISDIME
FASFINFGDD DLNLDLDLGD TTASYATETP EPVGNDEVNR SGTFDTRNNK EDSYKERETQ
SYSAAGATTY GDERQGQLHT FEQDGSEIND NEFENEDFNK HIEQPIEVTP RNNAYLPEFE
PNRPVSMSFK GLKAPRMNTS FIDSMTPDSP VKSDLTSLGE VYVNSNNDQG VRFSSQIILY
DTYGEFEYDR HPEISTCNQL TPQLAQMIKL ELNELKSAME VHDDSRCYTH FY
