CHS4_USTMA
ID CHS4_USTMA Reviewed; 942 AA.
AC Q99127; A0A0D1ECR8; Q4PHF1;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 2.
DT 25-MAY-2022, entry version 124.
DE RecName: Full=Chitin synthase 4;
DE EC=2.4.1.16;
DE AltName: Full=Chitin synthase II;
DE AltName: Full=Chitin-UDP acetyl-glucosaminyl transferase 4;
GN Name=CHS4; Synonyms=CHS2; ORFNames=UMAG_10117;
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 113-604.
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=CAA61028.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence at the N-terminus and at the C-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CM003140; KIS72040.1; -; Genomic_DNA.
DR EMBL; X87749; CAA61028.1; ALT_SEQ; Genomic_DNA.
DR PIR; S55519; S55519.
DR RefSeq; XP_011386673.1; XM_011388371.1.
DR AlphaFoldDB; Q99127; -.
DR STRING; 5270.UM00462P0; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR EnsemblFungi; KIS72040; KIS72040; UMAG_10117.
DR GeneID; 23566186; -.
DR KEGG; uma:UMAG_10117; -.
DR VEuPathDB; FungiDB:UMAG_10117; -.
DR eggNOG; KOG2571; Eukaryota.
DR InParanoid; Q99127; -.
DR OrthoDB; 256142at2759; -.
DR BRENDA; 2.4.1.16; 6587.
DR PHI-base; PHI:1111; -.
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..942
FT /note="Chitin synthase 4"
FT /id="PRO_0000193720"
FT TRANSMEM 641..661
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 674..694
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 709..729
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 755..775
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 783..803
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 885..905
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 909..929
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..39
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..111
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 604
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 123..124
FT /note="PL -> RN (in Ref. 3; CAA61028)"
FT /evidence="ECO:0000305"
FT CONFLICT 126..132
FT /note="Missing (in Ref. 3; CAA61028)"
FT /evidence="ECO:0000305"
FT CONFLICT 152
FT /note="Y -> H (in Ref. 3; CAA61028)"
FT /evidence="ECO:0000305"
FT CONFLICT 360..362
FT /note="VGK -> GGQ (in Ref. 3; CAA61028)"
FT /evidence="ECO:0000305"
FT CONFLICT 394
FT /note="Missing (in Ref. 3; CAA61028)"
FT /evidence="ECO:0000305"
FT CONFLICT 460..462
FT /note="GGA -> AGS (in Ref. 3; CAA61028)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 942 AA; 104902 MW; E525728BCB8B16F6 CRC64;
MPPRYPFGGG AQSDEAHHQP LERRTTAEAQ GNSFTHGHTA YPTYDMGAEP HSPPHVSYDP
YLPPSTSGDH SGYEMPSANY NDHHRSSYPQ AIHSPPRMTN PYANSQPRQG SADPFDEHDG
DVPLLPRGGN YAYAPASHFD EHGNHVGPVD KYADGDDDVM DEDAVNGQAR GRLLHTQVPH
DDDYMPGGFD PNVLENGQAG GVRFGKIPQR VPRRYKTLKR VELYHGNLVL DCPVPSKLLD
KLNDRESREF THMRYTAATC DPDEFKTERY TLRQVLFDPP RRTELFIVLT MYNEDEELFT
RTMHGVMTNI AHLCTRERSK TWGKEGWKKV VVCIVSDGRL KINSRTLACL AAMGVYQEGV
GKNVVNGKPV TAHIYEYTAQ LSIDPSMHFK GREKGIMPVQ ILFCLKERNQ KKINSHRWFF
NAFGQILQPN ICVLLDVGTM PRPRSIYHLW KAFDINSNVG GACGEIVALK GKFWGALLNP
LVAAQNFEYK MSNILDKPLE SVFGYITVLP GAFSAYRYIA LQNDAHGQGP LCSYFKGETL
HGGQSDADVF TSNMYLAEDR ILCWELVSKR DSAWILHYVK SAQAVTDVPD QVPELISQRR
RWLNGSFFAG IHSIIKFGYI YRSSHSFGRK FALHIEIIYQ TIQLIFSWFG MANFFIAFFI
LTSAMSDKIH ALKVPNLVLS YIYVAFIIFC FLLSMGNRPA GSKAGYTLAM VVFALLTVYM
TGAAIYLAVD SILNATGPNG GGTDALVSNR TFVNIVISLA ATFGIWLIAS IMFLEPMHMV
TSIVQYLLMA PTFVNVISIY AFANINDISW GTKGSDKVMT DLGVVGGSGN NQVEVAIPTE
SKDINDAYDD AIHVLSNKAP KAGPGPVDKE QKQKDYYATV RTNVVLCWSL SNAALVVGIL
NISSIGTRTI YMGFLLYSVA GLALFRMMGS TIYLIKRLFS GE
