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CHS7_EMENI
ID   CHS7_EMENI              Reviewed;         331 AA.
AC   Q5BEG1; C8VTN7;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   25-MAY-2022, entry version 87.
DE   RecName: Full=Chitin synthase export chaperone;
GN   Name=chs7; ORFNames=AN1069;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS   M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA   Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA   Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA   Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA   Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA   Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA   Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA   Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA   Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA   Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA   Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA   Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA   Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA   van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA   Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA   Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA   Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA   Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA   Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA   van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA   Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA   Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT   effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
CC   -!- FUNCTION: Chaperone required for the export of the chitin synthase chs3
CC       from the endoplasmic reticulum. {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with chs3. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC       Multi-pass membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the CHS7 family. {ECO:0000305}.
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DR   EMBL; AACD01000016; EAA66187.1; -; Genomic_DNA.
DR   EMBL; BN001308; CBF88215.1; -; Genomic_DNA.
DR   RefSeq; XP_658673.1; XM_653581.1.
DR   AlphaFoldDB; Q5BEG1; -.
DR   STRING; 162425.CADANIAP00001570; -.
DR   EnsemblFungi; CBF88215; CBF88215; ANIA_01069.
DR   EnsemblFungi; EAA66187; EAA66187; AN1069.2.
DR   GeneID; 2876839; -.
DR   KEGG; ani:AN1069.2; -.
DR   VEuPathDB; FungiDB:AN1069; -.
DR   eggNOG; ENOG502QRVH; Eukaryota.
DR   HOGENOM; CLU_050424_1_1_1; -.
DR   InParanoid; Q5BEG1; -.
DR   OMA; SKATVWE; -.
DR   OrthoDB; 1163040at2759; -.
DR   Proteomes; UP000000560; Chromosome VIII.
DR   Proteomes; UP000005890; Unassembled WGS sequence.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0034221; P:fungal-type cell wall chitin biosynthetic process; IBA:GO_Central.
DR   GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   InterPro; IPR022057; Chs7.
DR   PANTHER; PTHR35329; PTHR35329; 1.
DR   Pfam; PF12271; Chs7; 1.
PE   3: Inferred from homology;
KW   Cell wall biogenesis/degradation; Endoplasmic reticulum; Membrane;
KW   Protein transport; Reference proteome; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..331
FT                   /note="Chitin synthase export chaperone"
FT                   /id="PRO_0000280577"
FT   TRANSMEM        52..72
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        84..104
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        113..133
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        150..170
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        184..204
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        219..239
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        249..269
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   331 AA;  36776 MW;  9505393750E2B05B CRC64;
     MGFGDFDEIC KKAALPLCSL VGPSSAISGS TGIIPNCYAR NIELANTIIF EGAASFLHII
     ALGMTVIMIL HIRSKFTAVG RKEIITFFYI YMALTVCSLV IDAGVVPPRS GPFPWFVAVQ
     NGLTSALCTS LLVNGFVGFQ LYEDGTALSV WLLRLTSTVM FAVSFLISIL TFKSWGGLSP
     TNTLAMFIVL YIINAICIAV YLVMQLLLVL NTLEDRWPLG HIAFGLLVFI AGQVIMYAFG
     DVICDNVQHY LDGLFFATFC NLLAVMMVYK FWDYITKEDL EFSVGIKPNN WEIKELLPDE
     DRRTTVYQDT NSEYAGSMYH HRASTYNGHG Y
 
 
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