CHS7_PHANO
ID CHS7_PHANO Reviewed; 332 AA.
AC Q0UDX8;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 25-MAY-2022, entry version 69.
DE RecName: Full=Chitin synthase export chaperone;
GN Name=CHS7; ORFNames=SNOG_10036;
OS Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS blotch fungus) (Parastagonospora nodorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC Parastagonospora.
OX NCBI_TaxID=321614;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173;
RX PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L.,
RA Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E.,
RA Torriani S.F.F., McDonald B.A., Oliver R.P.;
RT "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT analysis of the wheat pathogen Stagonospora nodorum.";
RL Plant Cell 19:3347-3368(2007).
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; CH445340; EAT82371.1; -; Genomic_DNA.
DR RefSeq; XP_001800319.1; XM_001800267.1.
DR AlphaFoldDB; Q0UDX8; -.
DR STRING; 13684.SNOT_10036; -.
DR EnsemblFungi; SNOT_10036; SNOT_10036; SNOG_10036.
DR GeneID; 5977225; -.
DR KEGG; pno:SNOG_10036; -.
DR eggNOG; ENOG502QRVH; Eukaryota.
DR HOGENOM; CLU_050424_1_1_1; -.
DR InParanoid; Q0UDX8; -.
DR OMA; SKATVWE; -.
DR OrthoDB; 1163040at2759; -.
DR Proteomes; UP000001055; 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..332
FT /note="Chitin synthase export chaperone"
FT /id="PRO_0000280582"
FT TRANSMEM 51..71
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 86..106
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 121..141
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 149..169
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 182..202
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 218..238
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 248..268
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 332 AA; 36999 MW; 10499DDC3B40FE7B CRC64;
MGFGDFSTIC TKAAIPLCAL VGEQQINGGA GIQTNCYSRT IEIANTLIFQ CANDFMHILA
MVMTVIMIIH VRSKFTAVGR KEITSVFYIY LLLTIISLIL DAGVTAPGSA PYPYFAAVQN
GLVSALCTCL LINGFVGFQL YEDGTTLSVW LLRLCSLAMF VVSGAVSLLT FKNWAGLSSK
NPIGIMIVTY IVNAIFLFVY VVSQIILVVG TLEDRWPLGD ISFGVFFFVI GQVILYVFSD
TICDNVQHYI DGLFFATICN LLAVMMVYKY WDSITREDLE FSVGVKQHNW EVKELLPDED
KRGTVYQDSD YTPSLYQQQY NGRHSHYSNL GH
