CHS6_YEAST
ID CHS6_YEAST Reviewed; 746 AA.
AC P40955; D6VW85;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Chitin biosynthesis protein CHS6;
DE AltName: Full=Protein CSD3;
GN Name=CHS6; Synonyms=CSD3; OrderedLocusNames=YJL099W; ORFNames=J0838;
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].
RA Osmond B.C.;
RL Submitted (OCT-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=7483851; DOI=10.1002/yea.320110909;
RA Rasmussen S.W.;
RT "A 37.5 kb region of yeast chromosome X includes the SME1, MEF2, GSH1 and
RT CSD3 genes, a TCP-1-related gene, an open reading frame similar to the
RT DAL80 gene, and a tRNA(Arg).";
RL Yeast 11:873-883(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
RN [4]
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 [5]
RP FUNCTION.
RX PubMed=1532231; DOI=10.1128/mcb.12.4.1764-1776.1992;
RA Bulawa C.E.;
RT "CSD2, CSD3, and CSD4, genes required for chitin synthesis in Saccharomyces
RT cerevisiae: the CSD2 gene product is related to chitin synthases and to
RT developmentally regulated proteins in Rhizobium species and Xenopus
RT laevis.";
RL Mol. Cell. Biol. 12:1764-1776(1992).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=9614194; DOI=10.1091/mbc.9.6.1565;
RA Ziman M., Chuang J.S., Tsung M., Hamamoto S., Schekman R.;
RT "Chs6p-dependent anterograde transport of Chs3p from the chitosome to the
RT plasma membrane in Saccharomyces cerevisiae.";
RL Mol. Biol. Cell 9:1565-1576(1998).
RN [7]
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 [8]
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 [9]
RP FUNCTION.
RX PubMed=15715908; DOI=10.1186/1471-2156-6-8;
RA Lesage G., Shapiro J., Specht C.A., Sdicu A.-M., Menard P., Hussein S.,
RA Tong A.H.Y., Boone C., Bussey H.;
RT "An interactional network of genes involved in chitin synthesis in
RT Saccharomyces cerevisiae.";
RL BMC Genet. 6:8-8(2005).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH ARF1; BCH1; BCH2; BUD7;
RP CHS3 AND CHS5, 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 [11]
RP FUNCTION.
RX PubMed=16818716; DOI=10.1083/jcb.200602049;
RA Lam K.K.Y., Davey M., Sun B., Roth A.F., Davis N.G., Conibear E.;
RT "Palmitoylation by the DHHC protein Pfa4 regulates the ER exit of Chs3.";
RL J. Cell Biol. 174:19-25(2006).
RN [12]
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 [13]
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 [14]
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 -!- 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:1532231, ECO:0000269|PubMed:15715908,
CC ECO:0000269|PubMed:16498409, ECO:0000269|PubMed:16818716,
CC ECO:0000269|PubMed:16855022, ECO:0000269|PubMed:17000877,
CC ECO:0000269|PubMed:9614194}.
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 P40955; P11076: ARF1; NbExp=3; IntAct=EBI-4649, EBI-2816;
CC P40955; Q05029: BCH1; NbExp=5; IntAct=EBI-4649, EBI-27508;
CC P40955; Q08754: BUD7; NbExp=2; IntAct=EBI-4649, EBI-32770;
CC P40955; Q12114: CHS5; NbExp=17; IntAct=EBI-4649, EBI-4640;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16498409,
CC ECO:0000269|PubMed:17000877, ECO:0000269|PubMed:9614194}; Peripheral
CC membrane protein {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:16498409, ECO:0000269|PubMed:17000877,
CC ECO:0000269|PubMed:9614194}. Note=Trans-Golgi network location requires
CC interaction with CHS5 and with myristoylated GTP-bound ARF1 for the
CC recruitment to the membranes.
CC -!- DISRUPTION PHENOTYPE: Abolishes CHS3 localization to the bud neck and
CC plasma membrane, with increased protein localization to the trans-Golgi
CC cisternae. {ECO:0000269|PubMed:28346351}.
CC -!- MISCELLANEOUS: Present with 1180 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; U15603; AAA50840.1; -; Genomic_DNA.
DR EMBL; X85021; CAA59395.1; -; Genomic_DNA.
DR EMBL; Z49374; CAA89394.1; -; Genomic_DNA.
DR EMBL; Z49373; CAA89393.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08701.1; -; Genomic_DNA.
DR PIR; S50226; S50226.
DR RefSeq; NP_012436.1; NM_001181532.1.
DR PDB; 4WJW; X-ray; 2.59 A; B=1-746.
DR PDB; 4YG8; X-ray; 2.75 A; B=1-746.
DR PDBsum; 4WJW; -.
DR PDBsum; 4YG8; -.
DR AlphaFoldDB; P40955; -.
DR SMR; P40955; -.
DR BioGRID; 33658; 231.
DR ComplexPortal; CPX-1719; Exomer complex.
DR DIP; DIP-5682N; -.
DR IntAct; P40955; 12.
DR MINT; P40955; -.
DR STRING; 4932.YJL099W; -.
DR iPTMnet; P40955; -.
DR MaxQB; P40955; -.
DR PaxDb; P40955; -.
DR PRIDE; P40955; -.
DR EnsemblFungi; YJL099W_mRNA; YJL099W; YJL099W.
DR GeneID; 853346; -.
DR KEGG; sce:YJL099W; -.
DR SGD; S000003635; CHS6.
DR VEuPathDB; FungiDB:YJL099W; -.
DR eggNOG; ENOG502QRF3; Eukaryota.
DR GeneTree; ENSGT00940000176338; -.
DR HOGENOM; CLU_019711_0_0_1; -.
DR InParanoid; P40955; -.
DR OMA; CKFLPRC; -.
DR BioCyc; YEAST:G3O-31554-MON; -.
DR PRO; PR:P40955; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P40955; protein.
DR GO; GO:0005829; C:cytosol; HDA:SGD.
DR GO; GO:0034044; C:exomer complex; IDA:SGD.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0034221; P:fungal-type cell wall chitin biosynthetic process; IMP:SGD.
DR GO; GO:0006893; P:Golgi to plasma membrane transport; IMP: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.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Golgi apparatus; Membrane; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..746
FT /note="Chitin biosynthesis protein CHS6"
FT /id="PRO_0000089662"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 734..746
FT /note="CHS5-binding"
FT HELIX 32..40
FT /evidence="ECO:0007829|PDB:4WJW"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:4WJW"
FT HELIX 53..66
FT /evidence="ECO:0007829|PDB:4WJW"
FT STRAND 77..88
FT /evidence="ECO:0007829|PDB:4WJW"
FT STRAND 91..99
FT /evidence="ECO:0007829|PDB:4WJW"
FT STRAND 104..106
FT /evidence="ECO:0007829|PDB:4WJW"
FT HELIX 107..118
FT /evidence="ECO:0007829|PDB:4WJW"
FT STRAND 131..138
FT /evidence="ECO:0007829|PDB:4WJW"
FT TURN 139..142
FT /evidence="ECO:0007829|PDB:4WJW"
FT STRAND 143..149
FT /evidence="ECO:0007829|PDB:4WJW"
FT STRAND 155..164
FT /evidence="ECO:0007829|PDB:4WJW"
FT HELIX 173..191
FT /evidence="ECO:0007829|PDB:4WJW"
FT HELIX 194..196
FT /evidence="ECO:0007829|PDB:4WJW"
FT HELIX 212..225
FT /evidence="ECO:0007829|PDB:4WJW"
FT HELIX 227..232
FT /evidence="ECO:0007829|PDB:4WJW"
FT TURN 237..239
FT /evidence="ECO:0007829|PDB:4WJW"
FT STRAND 245..248
FT /evidence="ECO:0007829|PDB:4WJW"
FT HELIX 249..258
FT /evidence="ECO:0007829|PDB:4WJW"
FT HELIX 262..264
FT /evidence="ECO:0007829|PDB:4WJW"
FT HELIX 265..278
FT /evidence="ECO:0007829|PDB:4WJW"
FT HELIX 280..282
FT /evidence="ECO:0007829|PDB:4WJW"
FT HELIX 283..294
FT /evidence="ECO:0007829|PDB:4WJW"
FT HELIX 298..300
FT /evidence="ECO:0007829|PDB:4WJW"
FT HELIX 301..312
FT /evidence="ECO:0007829|PDB:4WJW"
FT HELIX 315..317
FT /evidence="ECO:0007829|PDB:4WJW"
FT STRAND 319..321
FT /evidence="ECO:0007829|PDB:4WJW"
FT HELIX 327..349
FT /evidence="ECO:0007829|PDB:4WJW"
FT HELIX 353..366
FT /evidence="ECO:0007829|PDB:4WJW"
FT HELIX 371..383
FT /evidence="ECO:0007829|PDB:4WJW"
FT HELIX 387..395
FT /evidence="ECO:0007829|PDB:4WJW"
FT TURN 424..427
FT /evidence="ECO:0007829|PDB:4WJW"
FT HELIX 435..444
FT /evidence="ECO:0007829|PDB:4WJW"
FT HELIX 450..455
FT /evidence="ECO:0007829|PDB:4WJW"
FT STRAND 459..462
FT /evidence="ECO:0007829|PDB:4WJW"
FT HELIX 473..476
FT /evidence="ECO:0007829|PDB:4WJW"
FT TURN 477..481
FT /evidence="ECO:0007829|PDB:4WJW"
FT HELIX 489..492
FT /evidence="ECO:0007829|PDB:4WJW"
FT TURN 495..497
FT /evidence="ECO:0007829|PDB:4WJW"
FT HELIX 500..504
FT /evidence="ECO:0007829|PDB:4WJW"
FT HELIX 509..513
FT /evidence="ECO:0007829|PDB:4WJW"
FT STRAND 517..519
FT /evidence="ECO:0007829|PDB:4WJW"
FT HELIX 522..552
FT /evidence="ECO:0007829|PDB:4WJW"
FT HELIX 585..599
FT /evidence="ECO:0007829|PDB:4WJW"
FT STRAND 605..608
FT /evidence="ECO:0007829|PDB:4YG8"
FT HELIX 613..625
FT /evidence="ECO:0007829|PDB:4WJW"
FT HELIX 629..642
FT /evidence="ECO:0007829|PDB:4WJW"
FT HELIX 646..657
FT /evidence="ECO:0007829|PDB:4WJW"
FT STRAND 663..665
FT /evidence="ECO:0007829|PDB:4WJW"
FT HELIX 671..687
FT /evidence="ECO:0007829|PDB:4WJW"
FT HELIX 694..707
FT /evidence="ECO:0007829|PDB:4WJW"
FT HELIX 709..718
FT /evidence="ECO:0007829|PDB:4WJW"
FT HELIX 724..740
FT /evidence="ECO:0007829|PDB:4WJW"
SQ SEQUENCE 746 AA; 86042 MW; BD92DADA3D5396BC CRC64;
MNLFWPSETK KQNEIPGGDY TPGNSPSVQK GYQFLNRDIF KSCPRIMERQ FGECLHNRTH
LIKDLISSGN VGLGPIEIVH MSYLNKHEKE EFGEYFYVTG IEVSGPAMPV EFLEVLKSSK
RISKNISNNI ILTYCCFNFF SNLDIRIRYD ADDTFQTTAI DCNKETTDLT MTEKMWEETF
ASSVIRAIIT NTNPELKPPG LVECPFYVGK DTISSCKKII ELLCRFLPRS LNCGWDSTKS
MQATIVNNYL MYSLKSFIAI TPSLVDFTID YLKGLTKKDP IHDIYYKTAM ITILDHIETK
ELDMITILNE TLDPLLSLLN DLPPRDADSA RLMNCMSDLL NIQTNFLLNR GDYELALGVS
NTSTELALDS FESWYNLARC HIKKEEYEKA LFAINSMPRL RKNDGHLETM YSRFLTSNYY
KKPLNGTREH YDLTAMEFTN LSGTLRNWKE DELKRQIFGR IAMINEKKIG YTKEIWDDIA
IKLGPICGPQ SVNLINYVSP QEVKNIKNIN LIARNTIGKQ LGWFSGKIYG LLMEIVNKIG
WNGLLNIRTE AFMMETEFYQ ASNNIIDENG HIPMESRKKR FCEGWLDDLF LDLYQDLKLS
KISLSNKDEK HSGLEWELLG LIMLRTWHWE DAVACLRTSI VARFDPVSCQ QLLKIYLQPP
KNIQEVTLLD TDTIISLLIK KISYDCRYYN YCQIFNLQLL EKLCNELGTH ILRNKILLQP
SIGDEIMVMI DAMLAWIADL DHTVQP
