CHS7_NEUCR
ID CHS7_NEUCR Reviewed; 358 AA.
AC Q7SB92;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 25-MAY-2022, entry version 84.
DE RecName: Full=Chitin synthase export chaperone;
DE AltName: Full=Chitin synthase chaperone 1;
GN Name=csc-1; Synonyms=chs7; ORFNames=NCU05720;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
CC -!- FUNCTION: Chaperone required for the export of the chitin synthase chs-
CC 3 from the endoplasmic reticulum. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with chs-3. {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; CM002238; EAA33670.3; -; Genomic_DNA.
DR RefSeq; XP_962906.3; XM_957813.3.
DR AlphaFoldDB; Q7SB92; -.
DR STRING; 5141.EFNCRP00000007629; -.
DR EnsemblFungi; EAA33670; EAA33670; NCU05720.
DR GeneID; 3879045; -.
DR KEGG; ncr:NCU05720; -.
DR VEuPathDB; FungiDB:NCU05720; -.
DR HOGENOM; CLU_050424_1_1_1; -.
DR InParanoid; Q7SB92; -.
DR Proteomes; UP000001805; Chromosome 3, Linkage Group III.
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..358
FT /note="Chitin synthase export chaperone"
FT /id="PRO_0000280581"
FT TRANSMEM 49..69
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 88..108
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 117..137
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 159..179
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 185..205
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 220..240
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 250..270
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 321..358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 358 AA; 39306 MW; 1BD369FA13CE5058 CRC64;
MGKFGDFSSI CRMAPIPLCA SVGPITSIAT GVGIEPDCYA RNIEVANTII FQGAASVMHI
VALVMTVVML LHVRGKFTAV GRKEITTFFY LYMILTFLSL CIDAGVIPPH SGSYPYFVAV
QAGLASALVT CLVINGFVGF QLYEDGTPLS LWMLRLCSFV AFVISFLVGL ATFKSWAGLG
PTNTVGIFVV LYFLNALQLL LYVVMQIILV TRTLQDRWPL GDIAFGLFFF IAGQVILYAF
SSPICEGISH YLDGLFFATT CNLLAVMMVY KYWDSITKED LEFSVGTRMN NWEVKELLPQ
GPEEDRRATV YADPIYEGHY ASGPGTGSGA SASGYEGGHH RRESHGYTPS PNRQSLRY