BCH2_YEAST
ID BCH2_YEAST Reviewed; 765 AA.
AC P36122; D6VX92;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Protein BCH2;
DE AltName: Full=BUD7 and CHS6 homolog 2;
GN Name=BCH2; Synonyms=FMP50; OrderedLocusNames=YKR027W;
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=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
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; BCH1; 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 P36122; P11076: ARF1; NbExp=2; IntAct=EBI-26374, EBI-2816;
CC P36122; Q05029: BCH1; NbExp=4; IntAct=EBI-26374, EBI-27508;
CC P36122; Q12114: CHS5; NbExp=7; IntAct=EBI-26374, EBI-4640;
CC P36122; P40073: SHO1; NbExp=2; IntAct=EBI-26374, EBI-18140;
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 2540 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; Z28252; CAA82099.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA09182.1; -; Genomic_DNA.
DR PIR; S38099; S38099.
DR RefSeq; NP_012952.3; NM_001179817.3.
DR AlphaFoldDB; P36122; -.
DR SMR; P36122; -.
DR BioGRID; 34160; 186.
DR ComplexPortal; CPX-1719; Exomer complex.
DR IntAct; P36122; 10.
DR MINT; P36122; -.
DR STRING; 4932.YKR027W; -.
DR iPTMnet; P36122; -.
DR MaxQB; P36122; -.
DR PaxDb; P36122; -.
DR PRIDE; P36122; -.
DR EnsemblFungi; YKR027W_mRNA; YKR027W; YKR027W.
DR GeneID; 853898; -.
DR KEGG; sce:YKR027W; -.
DR SGD; S000001735; BCH2.
DR VEuPathDB; FungiDB:YKR027W; -.
DR eggNOG; ENOG502QRF3; Eukaryota.
DR GeneTree; ENSGT00940000176338; -.
DR HOGENOM; CLU_019711_0_0_1; -.
DR InParanoid; P36122; -.
DR OMA; TSIMARF; -.
DR BioCyc; YEAST:G3O-32003-MON; -.
DR PRO; PR:P36122; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P36122; protein.
DR GO; GO:0034044; C:exomer complex; IDA:SGD.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005739; C:mitochondrion; HDA: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; 1.
DR Pfam; PF09295; ChAPs; 2.
DR SUPFAM; SSF48452; SSF48452; 1.
PE 1: Evidence at protein level;
KW Golgi apparatus; Membrane; Protein transport; Reference proteome;
KW Transport.
FT CHAIN 1..765
FT /note="Protein BCH2"
FT /id="PRO_0000203204"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 735..765
FT /note="CHS5-binding"
SQ SEQUENCE 765 AA; 88044 MW; 53A4A700682287E8 CRC64;
MSFLWGSTKS KKGKNKKAAG SLPSGVVPQQ RVKPTRKNVP IDYPRTLEKV HGESLIFRTS
LLSELVSTGK SGIGPPDLIH CTELDKFHDE KIGEFFYITG IDASSVSMPI AFLKLIKWND
GKKLKSASLK NDDITTYCTF NIFQKLDIRL RYESEDVYQV NIVDCLNGNN EIPLSDLIWE
ETFVSCCIRS VIINSDFERK IPGLVELPFV FENRCASDYK RVIDSLCKFL PRFLECGWDS
TKSVYATILN NYLTESLLVF LSITPEFITD YAIQVLDNLM TNDPSNSRYY AIVIISIMER
SNDRDVEMIK RIHEILDLLL PVLYGLPSDE PYISDLINCI TDVLSIQARF LLNNNDYELS
LSISTLATNL SSDNFESWYL LSKGYIFSQQ YDKALLSINS MPCLAEYDIV KQAQINAFKF
YMNYYKAPLC HSREHCTMTS HELNHLMNIM HYENELELKT IIFGRTVMPN ESKYGCIEEI
WNKSCLELGP ICGPQSDNLI NFVSQQEVNT VGDMLLLKRS KETRQESWFI KQVRLLLMEL
VARIGWNALL QLRSDVFVME SKFKMIESSD KLSTELRQKR LCQRWFDAMF LDVYEDLSIS
TSSQENKATA KYSGLEWELL GLTLLRVSDL PDAVACLRTS ILARFDPISC HHLLNFYLTM
DFNDEFMRRF DVDIILDLLV KLISFRIRFY DRFQIFSLQV LRKLEGQLGS EIIKNKIINS
PYGQAGITSV IDYMLECLSK NRNEACLAYE RPLPDLPSTI KPLAD
