ID   BUD4_YEAS7              Reviewed;        1447 AA.
AC   A6ZQ47;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 56.
DE   RecName: Full=Bud site selection protein 4;
GN   Name=BUD4; ORFNames=SCY_3008;
OS   Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=307796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJM789;
RX   PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA   Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA   Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA   Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA   Steinmetz L.M.;
RT   "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT   strain YJM789.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
CC   -!- FUNCTION: Required for establishment of the axial budding pattern in
CC       haploid cells. Cooperates with other bud site selection proteins to
CC       recognize a spatial landmark during mitosis and they subsequently
CC       become a landmark for downstream polarity establishment factors that
CC       coordinate axial budding and cytokinesis. Involved in the septin
CC       organization at the bud neck (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with AXL1, IQG1 and SEC3. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Bud neck. Note=Localizes to two distinct rings on
CC       either side of the mother-bud neck. The rings stay present in cells
CC       after cytokinesis and disappear before the next bud emergence. Requires
CC       IQG1 for proper localization (By similarity). {ECO:0000250}.
CC   -!- INDUCTION: Cell cycle-dependent with low levels at START and a peak in
CC       mitosis (at protein level). {ECO:0000250}.
CC   -!- PTM: Phosphorylated by CDC28. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the BUD4 family. {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; AAFW02000040; EDN63407.1; -; Genomic_DNA.
DR   AlphaFoldDB; A6ZQ47; -.
DR   PRIDE; A6ZQ47; -.
DR   EnsemblFungi; EDN63407; EDN63407; SCY_3008.
DR   HOGENOM; CLU_004727_0_0_1; -.
DR   Proteomes; UP000007060; Unassembled WGS sequence.
DR   GO; GO:0005935; C:cellular bud neck; IEA:UniProtKB-SubCell.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   Gene3D; 2.30.29.30; -; 1.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   Pfam; PF00169; PH; 1.
DR   SMART; SM00233; PH; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   3: Inferred from homology;
KW   Cell cycle; Cell division; Phosphoprotein.
FT   CHAIN           1..1447
FT                   /note="Bud site selection protein 4"
FT                   /id="PRO_0000330081"
FT   DOMAIN          1302..1413
FT                   /note="PH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT   REGION          1..37
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          57..76
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          272..316
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          444..588
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          649..672
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          768..879
FT                   /note="Interaction with IQG1"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        1..20
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        21..36
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        274..316
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        456..474
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        475..499
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        515..587
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        649..670
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         10
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P47136"
FT   MOD_RES         78
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P47136"
FT   MOD_RES         81
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P47136"
FT   MOD_RES         91
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P47136"
FT   MOD_RES         96
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P47136"
FT   MOD_RES         167
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P47136"
FT   MOD_RES         365
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P47136"
FT   MOD_RES         367
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P47136"
FT   MOD_RES         511
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P47136"
FT   MOD_RES         616
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P47136"
FT   MOD_RES         805
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P47136"
FT   MOD_RES         811
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P47136"
SQ   SEQUENCE   1447 AA;  164353 MW;  21AFAD838F7A6EB3 CRC64;
     MHDAESTVDS LLKEIDNEME QTKSNITQNG SEDTPHNWKL PLQEIGDDTM EMLVKHNTRS
     NATENSRGRS PSKMSTISNE SLNLGLLRVN SELEESPAAV HQERIKNSVA NGALGHANSP
     KVLNNLKNMA QDIDKLARDE EKPVKLSSSP LKFTLKSTQP LLSYPESPIH RSSIEIETNY
     DDEDEEEEDA YTCLTQSPQI LHSPSRIPIT NAVSINKLNL DFTLNPNESD KSLVSDTSVD
     STGRELDTKT IPELPFCMSS TPEMTPVDEK CNLPSKLLNT SNNSHSDSRS PTASVEDLNI
     STNLPGADSS QNNPVTTDAD ALIENDVVRD LQQNMEHIDD AFDEKKVLDE GCSNEPVTFL
     GENDTRSIVY SNKGTNANVQ EFSQEDSLAH SEPNFKDLNA TSDDVWNEDK ETDANISTST
     KSEESYIADY KVTRQEDWDT KKLHQESEHA NEQPAIIPQK DSSEETFTEL NNESEFQRNS
     KDGEEYRIVQ HEESLYGQRT KSSEENIING SEIGVDHGEA DEVNEPLAKT SAEEHDLSSS
     CEDQSVSEAR NKDSIEEKEV ETKDENIETE KDESEYHKVE ENEESEHVPL LPPLPRWEEI
     QFNEPFIDEN DTSNDSIDLT RSMKPSDYIS IWHIQEEEIK SNSPESIANS QFSQQSSITT
     ASTVDSKKDN GSTSFKFKPR IVSRSRIYNP KSRVSSLNYY DNEDYILSNS EWNALDPMRR
     NTLISKRIQD NIRTQKGHAP LIRPSVMKLN GEDSGFQNHF LEVEQPQEHE NIPLSTHLSE
     QDITTNVGLD EQKLPTNTQD EAEISIREIE SAGDITFNRG DLLSLSFDEE LGQDFANFLD
     ALDHDSTSFN HGPDDSSSFQ RDSSKKSFNS LWESSYELKP PPSIRKQPIA PDVLQKLLES
     DTKDDADLEK IREERITEPR TGLGIGMLKT PVKDVSIALA ASIKGYEASF SDTDSRPEGM
     NNSDAITLNM FDDFEEDKMT PSTPVRSISP IKRHVSSPFK VVKAGNKQEN NEINIKAEEE
     IEPMTQQETD GLKQDIPPLL AQTKDNVEAK EETITQLEEP QDVEQEFPDM GTLYLSIKAI
     STLALYGTKS HRATYAIVFD NGENVVQTPW ESLPYDGNIR INKEFELPID FKGKAETSSA
     SSERDSYKKC VITLKCKYEK PRHELVEIVD KVPVGKSFFG KTKYKFEKKY VQKKPKQDEW
     DYLFAQDGSF ARCEIEINEE FLKNVAFNTS HMHYNMINKW SRIADKIHGS KRLYELPRKA
     PHKVASLDVE ACFLERTSAF EQFPKQFSLV NKIVSKYKLQ QNIYKEGYLL QDGGDLKGKI
     ENRFFKLHGS QLSGYHEISR KAKIDINLLK VTKVLRNEDI QADNGGQRNF TDWVLFNECF
     QLVFDDGERI TFNAECSNEE KSDWYNKLQE VVELNVFHQP WVKKYCEKLA EEEKTRTTGH
     NLKQDFN