CHS3_NEUCR
ID CHS3_NEUCR Reviewed; 888 AA.
AC P30588; Q1K7J0; Q9C209; Q9UVU7;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 31-AUG-2004, sequence version 2.
DT 25-MAY-2022, entry version 132.
DE RecName: Full=Chitin synthase 3;
DE EC=2.4.1.16;
DE AltName: Full=Chitin-UDP acetyl-glucosaminyl transferase 3;
GN Name=chs-3; ORFNames=G65A3.040, NCU04251;
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].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RA Beth-Din A., Yarden O.;
RT "The Neurospora crassa chs-3 gene encodes an essential chitin synthase.";
RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
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).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 228-388.
RX PubMed=1731323; DOI=10.1073/pnas.89.2.519;
RA Bowen A.R., Chen-Wu J.L.-P., Momany M., Young R., Szaniszlo P.J.,
RA Robbins P.W.;
RT "Classification of fungal chitin synthases.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:519-523(1992).
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. {ECO:0000305}.
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. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAA32006.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF127086; AAF00101.1; -; Genomic_DNA.
DR EMBL; AL513411; CAC28596.1; -; Genomic_DNA.
DR EMBL; CM002240; EAA32006.2; ALT_SEQ; Genomic_DNA.
DR EMBL; M82950; AAA33581.1; -; Genomic_DNA.
DR PIR; E38192; E38192.
DR RefSeq; XP_961242.2; XM_956149.2.
DR AlphaFoldDB; P30588; -.
DR STRING; 5141.EFNCRP00000003823; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR EnsemblFungi; EAA32006; EAA32006; NCU04251.
DR GeneID; 3877405; -.
DR KEGG; ncr:NCU04251; -.
DR HOGENOM; CLU_004760_3_1_1; -.
DR InParanoid; P30588; -.
DR OMA; AWILHYV; -.
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 InterPro; IPR004835; Chitin_synth.
DR InterPro; IPR004834; Chitin_synth_fun.
DR InterPro; IPR013616; Chitin_synth_N.
DR PANTHER; PTHR22914; PTHR22914; 1.
DR Pfam; PF01644; Chitin_synth_1; 1.
DR Pfam; PF08407; Chitin_synth_1N; 1.
PE 3: Inferred from homology;
KW Cell membrane; Cell wall biogenesis/degradation; Glycosyltransferase;
KW Membrane; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..888
FT /note="Chitin synthase 3"
FT /id="PRO_0000193703"
FT TRANSMEM 532..551
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 572..594
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 607..629
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 642..664
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 684..706
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 814..836
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 860..882
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 91..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 121..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 751..771
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..135
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 94
FT /note="H -> Q (in Ref. 1; AAF00101)"
FT /evidence="ECO:0000305"
FT CONFLICT 372
FT /note="K -> E (in Ref. 4; AAA33581)"
FT /evidence="ECO:0000305"
FT CONFLICT 388
FT /note="E -> D (in Ref. 4; AAA33581)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 888 AA; 100390 MW; CD6D3F2D8A50DC0B CRC64;
MDPRMHTAPP AGHPIQPGYQ LEDNPYHHQQ GFDIPAGPGR YSPGDALHIQ TPQPIEGMGG
YNAPGQHYTP DYAVNPEEHH DAYYNQPYEP QVGHDPYAAA PTPPVAGYQA HDDQRPMLMH
TDSQVGQSDP YHDEPQPPTN NAPIKRWKTV KQVLLYRGNL VLDCPIPPKL LNQLPHGERD
EFTHMRYSAA TCDPSEFYEE NFTLRQKLFS KPRHTELFIV VTMYNEDEIL FARTMIGVFK
NIEYMCKRTE SKTWGKDAWK KIVVCVVSDG RAKINPRTRA LLAGMGVYQE GIAKQQVNGK
DVTAHIYEYT TQVGMTIKND VVQLIPKQQP VQMLFCLKEK NQKKINSHRW FFQAFGRVLD
PNICVLIDAG TKPGGSSIYH LWKAFDLEPM CAGACGEIKA MLGTGGKNLI NPLVATQNFE
YKMSNILDKP LESAFGFISV LPGAFSAYRY VALQNDKNGQ GPLEKYFAGE KLHGGDAGIF
TANMYLAEDR ILCFELVTKR NCHWILQYVK SATGETDVPA DLTELILQRR RWLNGSFFAA
IYAIVHFHQF FRSDHSFLRK IAFFIEFVFQ TVNMIFAWFA IGNFFLVFKI LTTGLGDEKL
LGTVGQILGV VFAWAYGVTL ITCFVLSMGN RPAGSPRLYM GMVVFWAIIF IYLMFAAIYI
AVVAIQTDVQ KGLSFTDLFR NELFYTLIVS VVSTYGIWLI ASLLMFDPWH MVTSMVQYML
LSPTYTNVLN VYAFCNTHDI SWGTKGDDKP DKLPSVNTKD GQGKTDLPDE GDLNASYERE
LQVFSRKYVK PVTAPTSAQL EEKQMDYYRG VRSMVVLVWM ITNFALCAVV LSTAGLERID
PEEGSQEQQT TKRATIYMSV VLWSVAVLSG FKFVGACWFL VVRMFRGV
