CHS3_USTMA
ID CHS3_USTMA Reviewed; 1029 AA.
AC Q99126; A0A0D1CGJ4; Q4PHD9;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Chitin synthase 3;
DE EC=2.4.1.16;
DE AltName: Full=Chitin synthase I;
DE AltName: Full=Chitin-UDP acetyl-glucosaminyl transferase 3;
GN Name=CHS3; Synonyms=CHS1; ORFNames=UMAG_10120;
OS Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX NCBI_TaxID=237631;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=521 / FGSC 9021;
RX PubMed=17080091; DOI=10.1038/nature05248;
RA Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J.,
RA Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H.,
RA Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G.,
RA Snetselaar K., McCann M., Perez-Martin J., Feldbruegge M., Basse C.W.,
RA Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L.,
RA Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L.,
RA Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N.,
RA Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B.,
RA Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J.,
RA Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P.,
RA Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G.,
RA Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A.,
RA Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M.,
RA Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M.,
RA Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E.,
RA Birren B.W.;
RT "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT maydis.";
RL Nature 444:97-101(2006).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=521 / FGSC 9021;
RA Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-891.
RC STRAIN=RK32 / A2B3;
RX PubMed=8932711; DOI=10.1099/13500872-142-2-377;
RA Xoconostle-Cazares B., Leon-Ramirez C., Ruiz-Herrera J.;
RT "Two chitin synthase genes from Ustilago maydis.";
RL Microbiology 142:377-387(1996).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=17042749; DOI=10.1111/j.1567-1364.2006.00133.x;
RA Ruiz-Herrera J., Xoconostle-Cazares B., Reynaga-Pena C.G., Leon-Ramirez C.,
RA Carabez-Trejo A.;
RT "Immunolocalization of chitin synthases in the phytopathogenic dimorphic
RT fungus Ustilago maydis.";
RL FEMS Yeast Res. 6:999-1009(2006).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=16314447; DOI=10.1105/tpc.105.037341;
RA Weber I., Assmann D., Thines E., Steinberg G.;
RT "Polar localizing class V myosin chitin synthases are essential during
RT early plant infection in the plant pathogenic fungus Ustilago maydis.";
RL Plant Cell 18:225-242(2006).
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:0000269|PubMed:16314447};
CC Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle membrane
CC {ECO:0000269|PubMed:17042749}; Multi-pass membrane protein
CC {ECO:0000255}. Note=A constitutive cytoplasmic pool is present that
CC localizes to intracellular microvesicles termed chitosomes. Chitosomes
CC constitute a separate secretory route distinct from the typical
CC secretory pathway and serve as a vehicle for delivering the enzyme to
CC the sites on the cell surface where polysaccharide sythesis takes
CC place. Localizes to septa of yeast-like cells and to the basal septum
CC separating the living tip cell from the vacuolated part in hyphae.
CC {ECO:0000269|PubMed:16314447, ECO:0000269|PubMed:17042749}.
CC -!- SIMILARITY: Belongs to the chitin synthase family. Class I subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA61027.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAA61027.1; Type=Miscellaneous discrepancy; Note=Internal deletion and contaminating sequence at the C-terminus from position 892 onwards.; Evidence={ECO:0000305};
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DR EMBL; CM003140; KIS72052.1; -; Genomic_DNA.
DR EMBL; X87748; CAA61027.1; ALT_SEQ; Genomic_DNA.
DR PIR; S55520; S55520.
DR RefSeq; XP_011386676.1; XM_011388374.1.
DR AlphaFoldDB; Q99126; -.
DR STRING; 5270.UM00474P0; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR EnsemblFungi; KIS72052; KIS72052; UMAG_10120.
DR GeneID; 23566189; -.
DR KEGG; uma:UMAG_10120; -.
DR VEuPathDB; FungiDB:UMAG_10120; -.
DR eggNOG; KOG2571; Eukaryota.
DR InParanoid; Q99126; -.
DR OrthoDB; 256142at2759; -.
DR BioCyc; MetaCyc:MON-17189; -.
DR BRENDA; 2.4.1.16; 6587.
DR PHI-base; PHI:1110; -.
DR Proteomes; UP000000561; Chromosome 1.
DR GO; GO:0071944; C:cell periphery; IBA:GO_Central.
DR GO; GO:0030428; C:cell septum; IBA:GO_Central.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
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 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; Cytoplasmic vesicle;
KW Glycoprotein; Glycosyltransferase; Membrane; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..1029
FT /note="Chitin synthase 3"
FT /id="PRO_0000193719"
FT TRANSMEM 723..743
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 760..780
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 796..816
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 830..850
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 860..880
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 963..983
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 998..1018
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 46..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 168..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..64
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..200
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 37
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 401
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 514
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 527
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 689
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 8
FT /note="A -> G (in Ref. 3; CAA61027)"
FT /evidence="ECO:0000305"
FT CONFLICT 12..13
FT /note="AA -> G (in Ref. 3; CAA61027)"
FT /evidence="ECO:0000305"
FT CONFLICT 29
FT /note="D -> A (in Ref. 3; CAA61027)"
FT /evidence="ECO:0000305"
FT CONFLICT 62
FT /note="A -> E (in Ref. 3; CAA61027)"
FT /evidence="ECO:0000305"
FT CONFLICT 121
FT /note="S -> T (in Ref. 3; CAA61027)"
FT /evidence="ECO:0000305"
FT CONFLICT 271..274
FT /note="MAGP -> YGWT (in Ref. 3; CAA61027)"
FT /evidence="ECO:0000305"
FT CONFLICT 293
FT /note="A -> R (in Ref. 3; CAA61027)"
FT /evidence="ECO:0000305"
FT CONFLICT 312
FT /note="G -> R (in Ref. 3; CAA61027)"
FT /evidence="ECO:0000305"
FT CONFLICT 349..354
FT /note="DDFASE -> TDLER (in Ref. 3; CAA61027)"
FT /evidence="ECO:0000305"
FT CONFLICT 520
FT /note="D -> E (in Ref. 3; CAA61027)"
FT /evidence="ECO:0000305"
FT CONFLICT 526..527
FT /note="EN -> GD (in Ref. 3; CAA61027)"
FT /evidence="ECO:0000305"
FT CONFLICT 539
FT /note="L -> V (in Ref. 3; CAA61027)"
FT /evidence="ECO:0000305"
FT CONFLICT 545..546
FT /note="GA -> AQ (in Ref. 3; CAA61027)"
FT /evidence="ECO:0000305"
FT CONFLICT 630
FT /note="A -> R (in Ref. 3; CAA61027)"
FT /evidence="ECO:0000305"
FT CONFLICT 692..747
FT /note="FFAAVYALYHTAQFVRSGHNVWRKSLLVFESFYSFVNMCFAWFGLANYYIFF
FT RILT -> SP (in Ref. 3; CAA61027)"
FT /evidence="ECO:0000305"
FT CONFLICT 882
FT /note="L -> W (in Ref. 3; CAA61027)"
FT /evidence="ECO:0000305"
FT CONFLICT 885
FT /note="F -> M (in Ref. 3; CAA61027)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1029 AA; 113242 MW; 73AFE99E52CF2F80 CRC64;
MAYYSRPASA GAARAQDDQD PYPYYPDPDL IVGSGANTSF VNPYEASGAA SSASHTSPFS
DAHAASASPA SILPLSHQQV SAHAPQQQHM SISVDPRDGQ QSRMPGLSES FYSQAAYALA
SPPPAAGALS PSAHLATLPE HSQAPLSGSV DGEYTYYSQS AAGHYSSLAH RHGQDDEDDD
DAETKYSPSS AHDEKYAYDR PDSAAAGTSP FGRAAGIAYL QSPYAQVARN DDDDEDEDAE
DPYRVLTRDS AFGGDNGQGY DPNSAYGGAG MAGPTGQFGD NHFDTQHFGP APARGAQLRR
HKTKKNVRLT KGNLILDCPV PTKLQTFLTR RAEDEFTTMR YSAVTCDPDD FASESFTLRP
ALYGRHTELF IAITMYNEDE VLFCRTFHGV MKNIAHLCSR NKSRTWGKDG WKKVVVAIIS
DGRKKIHPRV LDCLAALGVY QDGVAKNMVD GKEVRAHLYE YTTQLSIDSN LQFKGAERGL
VPMQIIFCLK EKNAKKINSH RWFFNAFCPI LQPNVTILLD VGTRPENKSI YYLWKSFDLN
SNVAGACGEI CAETKGKWGV GPLLLNPLVA AQNFEYKISN ILDKTTESVM GYISVLPGAF
SAYRYIALQN DEFGHGPLAS YFKGENLLGA DADVFTSNMY LAEDRILCFE LAAKRGHGWV
LKYVKSARGV TDVPEGLPEF ISQRRRWLNG SFFAAVYALY HTAQFVRSGH NVWRKSLLVF
ESFYSFVNMC FAWFGLANYY IFFRILTTSL EDPTFKLRGI GVFNVFMQYI YLGTVVSSFI
FAMGNRPQGS KWKYWAAVVV FALLTVYMMV AAVLCLSKVV ARVEHDAIYA QMVVSLLATY
GVYLISSLLA CDPLHLITSF LQYLLLAPTY INILNIYAFC NLHDFSWGTK GDTSISADLG
AVVSTSKGTV EITLPTAQAD IDTAYDDALN NLRTRPMIIR GDASNAEKEA RQMDYYKNIR
TNVVLAWALS NGVLAAFILN GDAAGTFSDT GGVTRTKVYM VLVLIFVAGM ACIRFIGSTL
YLTIRLING
