BUD7_YEAST
ID BUD7_YEAST Reviewed; 746 AA.
AC Q08754; D6W2Z9;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Bud site selection protein 7;
GN Name=BUD7; OrderedLocusNames=YOR299W;
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=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(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=11452010; DOI=10.1091/mbc.12.7.2147;
RA Ni L., Snyder M.;
RT "A genomic study of the bipolar bud site selection pattern in Saccharomyces
RT cerevisiae.";
RL Mol. Biol. Cell 12:2147-2170(2001).
RN [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [5]
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 [6]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH ARF1; BCH1; BCH2; CHS3;
RP CHS5 AND CHS6, AND DOMAIN.
RX PubMed=16498409; DOI=10.1038/sj.emboj.7601007;
RA Trautwein M., Schindler C., Gauss R., Dengjel J., Hartmann E., Spang A.;
RT "Arf1p, Chs5p and the ChAPs are required for export of specialized cargo
RT from the Golgi.";
RL EMBO J. 25:943-954(2006).
RN [7]
RP FUNCTION, IDENTIFICATION IN THE CHS5/6 COMPLEX, INTERACTION WITH ARF1, AND
RP SUBCELLULAR LOCATION.
RX PubMed=17000877; DOI=10.1083/jcb.200605106;
RA Wang C.-W., Hamamoto S., Orci L., Schekman R.;
RT "Exomer: a coat complex for transport of select membrane proteins from the
RT trans-Golgi network to the plasma membrane in yeast.";
RL J. Cell Biol. 174:973-983(2006).
RN [8]
RP FUNCTION, IDENTIFICATION IN THE CHS5/6 COMPLEX, AND INTERACTION WITH CHS3.
RX PubMed=16855022; DOI=10.1091/mbc.e06-03-0210;
RA Sanchatjate S., Schekman R.;
RT "Chs5/6 complex: a multiprotein complex that interacts with and conveys
RT chitin synthase III from the trans-Golgi network to the cell surface.";
RL Mol. Biol. Cell 17:4157-4166(2006).
RN [9]
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: Member of the CHS5-ARF1P-binding proteins (CHAPS) which
CC mediates export of specific cargo proteins, including chitin synthase
CC CHS3. May be involved in positioning the proximal bud pole signal.
CC {ECO:0000269|PubMed:11452010, ECO:0000269|PubMed:16498409,
CC ECO:0000269|PubMed:16855022, ECO:0000269|PubMed:17000877}.
CC -!- SUBUNIT: Component of the CHS5/6 complex composed of the 4 CHAPS
CC proteins BCH1, BCH2v, BUD7, and CHS6 as well as at least CHS5 and GTP-
CC bound ARF1. The complex interacts with the cargo protein CHS3.
CC {ECO:0000269|PubMed:16498409, ECO:0000269|PubMed:16855022,
CC ECO:0000269|PubMed:17000877}.
CC -!- INTERACTION:
CC Q08754; P11076: ARF1; NbExp=2; IntAct=EBI-32770, EBI-2816;
CC Q08754; Q05029: BCH1; NbExp=5; IntAct=EBI-32770, EBI-27508;
CC Q08754; Q12114: CHS5; NbExp=10; IntAct=EBI-32770, EBI-4640;
CC Q08754; P40955: CHS6; NbExp=2; IntAct=EBI-32770, EBI-4649;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16498409,
CC ECO:0000269|PubMed:17000877}; Peripheral membrane protein
CC {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16498409,
CC ECO:0000269|PubMed:17000877}. Note=Trans-Golgi network location
CC requires interaction with CHS5 and with myristoylated GTP-bound ARF1
CC for the recruitment to the membranes.
CC -!- MISCELLANEOUS: Present with 2070 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the CHAPS family. {ECO:0000305}.
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DR EMBL; Z75207; CAA99528.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA11065.1; -; Genomic_DNA.
DR PIR; S67203; S67203.
DR RefSeq; NP_014943.1; NM_001183718.1.
DR AlphaFoldDB; Q08754; -.
DR SMR; Q08754; -.
DR BioGRID; 34688; 95.
DR ComplexPortal; CPX-1719; Exomer complex.
DR DIP; DIP-2692N; -.
DR IntAct; Q08754; 19.
DR MINT; Q08754; -.
DR STRING; 4932.YOR299W; -.
DR iPTMnet; Q08754; -.
DR MaxQB; Q08754; -.
DR PaxDb; Q08754; -.
DR PRIDE; Q08754; -.
DR EnsemblFungi; YOR299W_mRNA; YOR299W; YOR299W.
DR GeneID; 854475; -.
DR KEGG; sce:YOR299W; -.
DR SGD; S000005825; BUD7.
DR VEuPathDB; FungiDB:YOR299W; -.
DR eggNOG; ENOG502QSKI; Eukaryota.
DR GeneTree; ENSGT00940000176338; -.
DR HOGENOM; CLU_019711_0_0_1; -.
DR InParanoid; Q08754; -.
DR OMA; WNAFRRC; -.
DR BioCyc; YEAST:G3O-33784-MON; -.
DR PRO; PR:Q08754; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q08754; protein.
DR GO; GO:0034044; C:exomer complex; IDA:SGD.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000282; P:cellular bud site selection; IMP:SGD.
DR GO; GO:0034221; P:fungal-type cell wall chitin biosynthetic process; IPI:SGD.
DR GO; GO:0006893; P:Golgi to plasma membrane transport; IGI:SGD.
DR GO; GO:0015031; P:protein transport; IC:ComplexPortal.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR015374; ChAPs.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR31975; PTHR31975; 2.
DR Pfam; PF09295; ChAPs; 1.
DR SUPFAM; SSF48452; SSF48452; 1.
PE 1: Evidence at protein level;
KW Golgi apparatus; Membrane; Protein transport; Reference proteome;
KW Transport.
FT CHAIN 1..746
FT /note="Bud site selection protein 7"
FT /id="PRO_0000065019"
FT REGION 733..746
FT /note="CHS5-binding"
SQ SEQUENCE 746 AA; 84830 MW; 93E6DF36F5A5C1F2 CRC64;
MITQNSIPEV KEDFIGYALH ERRIRLPQFQ DLGPADLVTL TKYLPTSSNT NAINSTSRNG
AAIIQSPAAV VADDSAASMA TNGDASDTAV TTNYTNASIY SSSRNANDGA PMVAELHPLD
KLKDEVGTFF YSMGVDTSGP TSIAIFLKEI SEVISEKPQV WFGRKKTFNV ARISFSTWNA
FRRCDINVVV HIPGSIQNFI VDCNGESQNI EMCADYDLIW AETFVSGVVR SIMLMKENAE
EGELQNLVET LILNPFTAGQ IDDVPEMFID LFPIVYHKGP LLGAPYYITN VTNTNNYLVE
TLVEIVKLTR NVSRAEIMLK NLATDNPEAI IILIKIFLVC DQELDAIKLT YDMLSQDKII
NNTNNRMDYK SELLCLQAQF LIDKRQDYSL AQNIAQEAVN CSPSEFRPWY LLSKVYVKLN
DIENALLILN SCPMSPLKEK YVLKRVAPLP SNNSLHLPLP IDVVLDEVTS LNPQDVQNEH
RSADPMLVNL AASNLKSTFQ LAYRLLTEIV QITGWENLLK YRSNIFVMEE EYQKSSSSLP
KDVNKQEEQP LRAKRLCERW LDNLFMLLYE DLKMYTLWQT EQLYMDAQNN NHNKLTFEWE
LFGLCARRLG HFPEAAKAFQ NGLSQRFSSR CARKLLEYCI NERQRVKNFI NSPNSHDMVP
EIVSSRIREL DNSIIDLCVK ICCWNHRWYT EFSISLLDCL SVVIQDMSLT KVSNEISSRY
PETVLNLVQE NLLNFFTTCT IGCYDA
