CHS1_NEUCR
ID CHS1_NEUCR Reviewed; 917 AA.
AC P29070; Q7RVD4; Q8X0I7;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Chitin synthase 1;
DE EC=2.4.1.16;
DE AltName: Full=Chitin-UDP acetyl-glucosaminyl transferase 1;
DE AltName: Full=Class-III chitin synthase 3;
GN Name=chs-1; ORFNames=B11H24.170, NCU03611;
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 [GENOMIC DNA], AND FUNCTION.
RX PubMed=1836444; DOI=10.1101/gad.5.12b.2420;
RA Yarden O., Yanofsky C.;
RT "Chitin synthase 1 plays a major role in cell wall biogenesis in Neurospora
RT crassa.";
RL Genes Dev. 5:2420-2430(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12655011; DOI=10.1093/nar/gkg293;
RA Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D.,
RA Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.;
RT "What's in the genome of a filamentous fungus? Analysis of the Neurospora
RT genome sequence.";
RL Nucleic Acids Res. 31:1944-1954(2003).
RN [3]
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: Polymerizes chitin, a structural polymer of the cell wall and
CC septum, by transferring the sugar moiety of UDP-GlcNAc to the non-
CC reducing end of the growing chitin polymer.
CC {ECO:0000269|PubMed:1836444}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[(1->4)-N-acetyl-beta-D-glucosaminyl](n) + UDP-N-acetyl-alpha-
CC D-glucosamine = [(1->4)-N-acetyl-beta-D-glucosaminyl](n+1) + H(+) +
CC UDP; Xref=Rhea:RHEA:16637, Rhea:RHEA-COMP:9593, Rhea:RHEA-COMP:9595,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17029, ChEBI:CHEBI:57705,
CC ChEBI:CHEBI:58223; EC=2.4.1.16;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the chitin synthase family. Class III subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA33568.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; M73437; AAA33568.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AL670005; CAD21286.1; -; Genomic_DNA.
DR EMBL; CM002240; EAA32102.2; -; Genomic_DNA.
DR PIR; A41638; A41638.
DR RefSeq; XP_961338.2; XM_956245.3.
DR AlphaFoldDB; P29070; -.
DR STRING; 5141.EFNCRP00000003325; -.
DR ChEMBL; CHEMBL5625; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR EnsemblFungi; EAA32102; EAA32102; NCU03611.
DR GeneID; 3877520; -.
DR KEGG; ncr:NCU03611; -.
DR VEuPathDB; FungiDB:NCU03611; -.
DR HOGENOM; CLU_004760_0_1_1; -.
DR InParanoid; P29070; -.
DR OMA; FWIFSNA; -.
DR BRENDA; 2.4.1.16; 3627.
DR PRO; PR:P29070; -.
DR Proteomes; UP000001805; Chromosome 2, Linkage Group V.
DR GO; GO:0071944; C:cell periphery; IBA:GO_Central.
DR GO; GO:0030428; C:cell septum; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004100; F:chitin synthase activity; IBA:GO_Central.
DR GO; GO:0006038; P:cell wall chitin biosynthetic process; IBA:GO_Central.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0048315; P:conidium formation; IEA:UniProt.
DR InterPro; IPR004835; Chitin_synth.
DR InterPro; IPR004834; Chitin_synth_fun.
DR InterPro; IPR013616; Chitin_synth_N.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR22914; PTHR22914; 1.
DR Pfam; PF01644; Chitin_synth_1; 1.
DR Pfam; PF08407; Chitin_synth_1N; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 3: Inferred from homology;
KW Cell membrane; Cell wall biogenesis/degradation; Glycoprotein;
KW Glycosyltransferase; Membrane; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..917
FT /note="Chitin synthase 1"
FT /id="PRO_0000193701"
FT TOPO_DOM 1..570
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 571..591
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 592..629
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 630..650
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 651..664
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 665..685
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 686..716
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 717..737
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 738..744
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 745..765
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 766..843
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 844..864
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 865..884
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 885..905
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 906..917
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 544
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 33
FT /note="A -> R (in Ref. 1; AAA33568)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 917 AA; 102692 MW; 903EBBF6BD95A69A CRC64;
MAYHGRGDGY DGHQLQDLPG GHNQGDQHDD AQAPFLSENP MPYDNDRLGT DTPPVRPVSA
YSLTESYAPG AGTTRAGVAV NPTPPPHGGY GGGGVSSGVD QGYNYGGDYA TDPAYRMSAI
DEDDSWLRRQ QPNAAPTGGL KRYATRKVKL VQGSVLSLDY PVPSAIRNAV QPKYRDEEGN
NEEFFKMRYT AATCDPNDFT LKNGYDLRPR MYNRHTELLI AITYYNEDKV LLSRTLHSVM
TNIRDIVNLK KSSFWNRGGP AWQKIVVCLV FDGLDKTDKN VLDVLATIGV YQDGVIKKDV
DGKETVAHIF EYTSQLSVTP NQALIRPVDD GPQTLPPVQF IFCLKQKNTK KINSHRWLFN
AFGRILNPEV CILLDAGTKP SPRSLLALWE GFYNDKDLGG ACGEIHAMLG KGGKKLLNPL
VAVQNFEYKI SNILDKPLES AFGYVSVLPG AFSAYRFRAI MGRPLEQYFH GDHTLSKLLG
KKGIEGMNIF KKNMFLAEDR ILCFELVAKA GQKWHLSYIK AAKGETDVPE GAPEFISQRR
RWLNGSFAAS LYSLMHFGRM YKSGHNIVRM FFFHVQLIYN IANVIFTWFS LASYWLTTTV
IMDLVGTPVT ASSSSAEHHG WPFGDTVTPF FNAVLKYIYL AFVILQFILA LGNRPKGSKW
TYITSFFVFS LIQSYILVLS GYLVARAFSV PLDQQLQLDN AKDAMASLFG GSGSAGVILV
ALVTIYGLYF LASFMYLDPW HMFHSFPYYM LLMSTYINIL MIYAFNNWHD VSWGTKGSDK
AEALPSANVS KGEKDEAVVE EIEKPQEDID QQFEATVRRA LAPYKEDETP EPKDLEDSYK
SFRTMLVVSW LFSNCLLAVV ITSDNFNTFG IGQTASARTA WFFKFLLFAT GALSVIRFIG
FCWFLGRTGI MCCFARR
