BCH1_YEAST
ID BCH1_YEAST Reviewed; 724 AA.
AC Q05029; D6W063;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Protein BCH1;
DE AltName: Full=BUD7 and CHS6 homolog 1;
GN Name=BCH1; OrderedLocusNames=YMR237W; ORFNames=YM9959.19;
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=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(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 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 [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 FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH ARF1; BCH2; BUD7; 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 [6]
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 [7]
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 [8]
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).
CC -!- FUNCTION: Member of the CHS5-ARF1P-binding proteins (CHAPS) which
CC mediates export of specific cargo proteins, including chitin synthase
CC CHS3. {ECO:0000269|PubMed:16498409, ECO:0000269|PubMed:16855022,
CC ECO:0000269|PubMed:17000877}.
CC -!- SUBUNIT: Component of the CHS5/6 complex composed of the 4 CHAPS
CC proteins BCH1, BCH2, 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 Q05029; P11076: ARF1; NbExp=3; IntAct=EBI-27508, EBI-2816;
CC Q05029; P36122: BCH2; NbExp=4; IntAct=EBI-27508, EBI-26374;
CC Q05029; Q08754: BUD7; NbExp=5; IntAct=EBI-27508, EBI-32770;
CC Q05029; Q12114: CHS5; NbExp=17; IntAct=EBI-27508, EBI-4640;
CC Q05029; P40955: CHS6; NbExp=5; IntAct=EBI-27508, 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 3460 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; Z49939; CAA90208.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA10137.1; -; Genomic_DNA.
DR PIR; S57604; S57604.
DR RefSeq; NP_013964.1; NM_001182744.1.
DR PDB; 4IN3; X-ray; 2.94 A; B/D=1-724.
DR PDB; 4Q66; X-ray; 3.35 A; B/E/H/K=1-724.
DR PDBsum; 4IN3; -.
DR PDBsum; 4Q66; -.
DR AlphaFoldDB; Q05029; -.
DR SMR; Q05029; -.
DR BioGRID; 35415; 129.
DR ComplexPortal; CPX-1719; Exomer complex.
DR DIP; DIP-2569N; -.
DR IntAct; Q05029; 31.
DR MINT; Q05029; -.
DR STRING; 4932.YMR237W; -.
DR iPTMnet; Q05029; -.
DR MaxQB; Q05029; -.
DR PaxDb; Q05029; -.
DR PRIDE; Q05029; -.
DR EnsemblFungi; YMR237W_mRNA; YMR237W; YMR237W.
DR GeneID; 855277; -.
DR KEGG; sce:YMR237W; -.
DR SGD; S000004850; BCH1.
DR VEuPathDB; FungiDB:YMR237W; -.
DR eggNOG; ENOG502QSKI; Eukaryota.
DR GeneTree; ENSGT00940000176338; -.
DR HOGENOM; CLU_019711_0_0_1; -.
DR InParanoid; Q05029; -.
DR OMA; HKVVSGI; -.
DR BioCyc; YEAST:G3O-32918-MON; -.
DR PRO; PR:Q05029; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; Q05029; protein.
DR GO; GO:0034044; C:exomer complex; IDA:SGD.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0031267; F:small GTPase binding; IPI: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.
PE 1: Evidence at protein level;
KW 3D-structure; Golgi apparatus; Membrane; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..724
FT /note="Protein BCH1"
FT /id="PRO_0000203335"
FT REGION 51..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 711..724
FT /note="CHS5-binding"
FT HELIX 18..25
FT /evidence="ECO:0007829|PDB:4IN3"
FT HELIX 26..28
FT /evidence="ECO:0007829|PDB:4IN3"
FT STRAND 37..43
FT /evidence="ECO:0007829|PDB:4IN3"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:4Q66"
FT HELIX 102..115
FT /evidence="ECO:0007829|PDB:4IN3"
FT STRAND 123..125
FT /evidence="ECO:0007829|PDB:4Q66"
FT STRAND 131..134
FT /evidence="ECO:0007829|PDB:4IN3"
FT STRAND 136..141
FT /evidence="ECO:0007829|PDB:4IN3"
FT TURN 142..145
FT /evidence="ECO:0007829|PDB:4IN3"
FT STRAND 146..151
FT /evidence="ECO:0007829|PDB:4IN3"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:4IN3"
FT STRAND 159..163
FT /evidence="ECO:0007829|PDB:4IN3"
FT HELIX 190..206
FT /evidence="ECO:0007829|PDB:4IN3"
FT TURN 207..215
FT /evidence="ECO:0007829|PDB:4IN3"
FT STRAND 223..225
FT /evidence="ECO:0007829|PDB:4Q66"
FT HELIX 228..230
FT /evidence="ECO:0007829|PDB:4IN3"
FT STRAND 233..235
FT /evidence="ECO:0007829|PDB:4IN3"
FT HELIX 237..243
FT /evidence="ECO:0007829|PDB:4IN3"
FT HELIX 245..248
FT /evidence="ECO:0007829|PDB:4IN3"
FT HELIX 252..255
FT /evidence="ECO:0007829|PDB:4IN3"
FT STRAND 266..269
FT /evidence="ECO:0007829|PDB:4IN3"
FT HELIX 270..282
FT /evidence="ECO:0007829|PDB:4IN3"
FT HELIX 285..298
FT /evidence="ECO:0007829|PDB:4IN3"
FT HELIX 300..302
FT /evidence="ECO:0007829|PDB:4IN3"
FT HELIX 303..312
FT /evidence="ECO:0007829|PDB:4IN3"
FT HELIX 316..328
FT /evidence="ECO:0007829|PDB:4IN3"
FT HELIX 341..361
FT /evidence="ECO:0007829|PDB:4IN3"
FT HELIX 366..379
FT /evidence="ECO:0007829|PDB:4IN3"
FT HELIX 384..397
FT /evidence="ECO:0007829|PDB:4IN3"
FT HELIX 400..408
FT /evidence="ECO:0007829|PDB:4IN3"
FT HELIX 463..466
FT /evidence="ECO:0007829|PDB:4IN3"
FT TURN 469..472
FT /evidence="ECO:0007829|PDB:4IN3"
FT HELIX 475..491
FT /evidence="ECO:0007829|PDB:4IN3"
FT HELIX 493..503
FT /evidence="ECO:0007829|PDB:4IN3"
FT HELIX 539..564
FT /evidence="ECO:0007829|PDB:4IN3"
FT HELIX 575..588
FT /evidence="ECO:0007829|PDB:4IN3"
FT HELIX 592..601
FT /evidence="ECO:0007829|PDB:4IN3"
FT HELIX 608..630
FT /evidence="ECO:0007829|PDB:4IN3"
FT HELIX 638..665
FT /evidence="ECO:0007829|PDB:4IN3"
FT HELIX 672..684
FT /evidence="ECO:0007829|PDB:4IN3"
FT HELIX 687..697
FT /evidence="ECO:0007829|PDB:4IN3"
FT HELIX 700..709
FT /evidence="ECO:0007829|PDB:4IN3"
FT HELIX 711..716
FT /evidence="ECO:0007829|PDB:4IN3"
SQ SEQUENCE 724 AA; 82049 MW; 3D9B80FDE9CF202B CRC64;
MLSQTSIPEV KEDVIGYALH QRRARVGQFQ DLGPPDLITL IKSLPSSSST TTATASANDN
GATSNINGQD PTTIVTELHS HDKLKGQIGT FFYCMGIDTS DPTSITIFAK KITDLFLDTP
QIWFGKKKHF HVSKISISSW NAFRKYDVNI IVHIPGTVQT YIINSDGEQS QLPSVAEASS
GRNSQDLNVN MIWAETFMSG IVRDIMIMKD NRADGESQNL VETLIFNPFT SGELEDVANN
FIKLFPLVYE KGVYLDAPTH VLNPSLTNNY LVETLVEIVR LTKSLEACRK MLKKLIEIHP
EAVIILIRVY FACDLEIDAV DLINEQLNSP SSFLADDSKT SHIQLIFKSE LLSIQSEFLL
DVKRDYKLAK EVAMEAVNCA PNEFKTWYLL TRIYIKLNDM SNALLSLNAC PMSQVKEKYV
LRRIAPITSD ENLHLPLPLD ASIEEISSLN PMDVQLEQKS ADPNLVNLSA SSLKSTFQLA
YKLLTEIVQI TGWEQLLKYR SKIFVMEDEY QGSTSSIDEA EVRGNDISKM RSKRLCERWL
DNLFMLLYED LKTYTDWQSE QLYFDAQNSK YHKLTVEWEL FGLCAKRLGH LPEAAKAFQI
GLSQRFSPVC AKNLLQFYID EHKRIRRDSV SANSELTSSQ ILSSINDIDS SIIDLVVKIC
CWNHRWYIEF SIILIDALSV AVQDMGITKV HNEIASRFSD PVAQLIDDNI LNFLKNFTND
TFDN
