CHS4_MAGO7
ID CHS4_MAGO7 Reviewed; 1229 AA.
AC O13353; A4R0F5; G4MRN7;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Chitin synthase 4;
DE EC=2.4.1.16;
DE AltName: Full=Chitin-UDP acetyl-glucosaminyl transferase 4;
DE AltName: Full=Class-IV chitin synthase 4;
GN Name=CHS4; ORFNames=MGG_09962;
OS Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS fungus) (Pyricularia oryzae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX NCBI_TaxID=242507;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Guyane 11;
RA Specht C.A.;
RL Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX PubMed=15846337; DOI=10.1038/nature03449;
RA Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL Nature 434:980-986(2005).
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. Class IV subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB71411.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF020528; AAB71411.1; ALT_FRAME; Genomic_DNA.
DR EMBL; CM001231; EHA57460.1; -; Genomic_DNA.
DR EMBL; CM001231; EHA57461.1; -; Genomic_DNA.
DR RefSeq; XP_003710072.1; XM_003710024.1.
DR RefSeq; XP_003710073.1; XM_003710025.1.
DR AlphaFoldDB; O13353; -.
DR STRING; 318829.MGG_09962T0; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR PRIDE; O13353; -.
DR EnsemblFungi; MGG_09962T0; MGG_09962T0; MGG_09962.
DR EnsemblFungi; MGG_09962T1; MGG_09962T1; MGG_09962.
DR GeneID; 2680870; -.
DR KEGG; mgr:MGG_09962; -.
DR VEuPathDB; FungiDB:MGG_09962; -.
DR eggNOG; KOG2571; Eukaryota.
DR HOGENOM; CLU_002572_1_0_1; -.
DR InParanoid; O13353; -.
DR OMA; DIMGLCG; -.
DR OrthoDB; 134286at2759; -.
DR Proteomes; UP000009058; Chromosome 1.
DR GO; GO:0005935; C:cellular bud neck; IEA:EnsemblFungi.
DR GO; GO:0045009; C:chitosome; IEA:EnsemblFungi.
DR GO; GO:0000131; C:incipient cellular bud site; IEA:EnsemblFungi.
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:0005628; C:prospore membrane; IEA:EnsemblFungi.
DR GO; GO:0004100; F:chitin synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0030476; P:ascospore wall assembly; IEA:EnsemblFungi.
DR GO; GO:0048315; P:conidium formation; IEA:UniProt.
DR GO; GO:0034221; P:fungal-type cell wall chitin biosynthetic process; IEA:EnsemblFungi.
DR GO; GO:0097271; P:protein localization to bud neck; IEA:EnsemblFungi.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR004835; Chitin_synth.
DR InterPro; IPR001199; Cyt_B5-like_heme/steroid-bd.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR22914; PTHR22914; 1.
DR SMART; SM01117; Cyt-b5; 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..1229
FT /note="Chitin synthase 4"
FT /id="PRO_0000193700"
FT TOPO_DOM 1..202
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 203..223
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 224..240
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 241..261
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 262..495
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 496..516
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 517..1054
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1055..1075
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1076..1088
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1089..1109
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1110..1114
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1115..1135
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1136..1229
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 1..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 539..589
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 601..648
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1210..1229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..80
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..109
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..151
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 154..196
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 539..560
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 573..589
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 601..647
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 608
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 635
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1030
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT VARIANT 545..546
FT /note="KR -> NG (in strain: Guyane 11)"
SQ SEQUENCE 1229 AA; 137828 MW; 388030A667144D55 CRC64;
MSLPERPGAK ASYEQRNSYR KSPSRRNRPN DIEASGYYPV TGGQHQRGPS VNSFAETIRS
PNSNIESAPL SPSAEQIEHG SDQPFQRKRS LIRPERNRID RDHPNYHYRK HAAKMNTLPS
STGNDPVLED VSGATESGPP SGSNSASGSG VREENIPRKS RKASGRETVA EKSDNTRRRV
STRNSKIVKE GKRKEKIPEQ LRPPSAWNVY CAVITFWSPD FIMKCCGMPA KAQRRAWREK
IGLISLILII MGVVGFLTFG FNQAVCGGPV LRLHINSVDR SYMIFHGTAY NLDGSHHPVA
EGIPKRLDGT GANVVYDLPE GYGGTDGSFM FQNVNGKCKG LITKAPNSDV PSEGDNLAWY
FPCHARNQDG SSQPNMTYPY YFGYACHTTP LARSTFYTQL DKSADVYFTW ADIRNNSRNL
FVYSGNVLDL DLLFWFNRDQ VNIPRRFEEL RDKNNAANRA IRGRDATRTF MASGDRQIAE
CFEDIIKVGT VDTDTVGCIA AKVVLYVSLA LILSVVGARF TLALIFQWFI SKNYAADKTS
QTSDKRKRNK QIEDWSEDIY RAPPRMPGDV GSSVAGASSS DHTSKRSSFL PTTSRFSTVY
GAERSARNKS MPTTMASQAS GGYMGPSSTA YRETNESRTS FLKSDPYATN TAPIEGPGPS
GFIHDSVVPQ PPSDWMPFGF PLAHTICLVT AYSEGELGLR TTLDSVAMTD YPNSHKVILV
ICDGIIKGKG ESKSTPEYVL DMMKDHTIPV EDVEAFSYVA VASGSKRHNM AKIYAGFYDY
GTQSNIPLDK QQRVPMMVVV KCGTPDEMVK SKPGNRGKRD SQIILMSFLQ KVMFDERMTE
LEYEMFNGLW KVTGISPDFY EIVLMVDADT KVFPDSLTHM ISAMVKDPEI MGLCGETKIA
NKRDSWVSAI QVFEYFISHH LAKSFESVFG GVTCLPGCFC MYRIKAPKGA QNYWVPILAN
PDVVEHYSEN VVDTLHKKNL LLLGEDRYLT TLMLRTFPKR KQVFVPQAVC KTTVPDSFMV
LLSQRRRWIN STIHNLMELV LVRDLCGTFC FSMQFVIFIE LIGTLVLPAA IAFTFYVVII
SIINQPPQII PLVLLGLILG LPAILIIITA HSWSYVLWML IYLLSLPVWN FVLPAYAFWK
FDDFSWGDTR KTAGEKTKKA GIEYEGEFDS SKITMKRWAE FERDRRARQS QYWGSRENVT
GGVRTASGVW ASAPPHHHQQ QYDEYYSDA
