CHS7_USTMA
ID CHS7_USTMA Reviewed; 1273 AA.
AC Q4P333; A0A0D1DVE4;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 25-MAY-2022, entry version 96.
DE RecName: Full=Chitin synthase 7;
DE EC=2.4.1.16;
DE AltName: Full=Chitin-UDP acetyl-glucosaminyl transferase 7;
GN Name=CHS7; ORFNames=UMAG_05480;
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 FUNCTION, AND 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.
CC {ECO:0000269|PubMed:16314447}.
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:0000269|PubMed:16314447}. Cytoplasmic
CC vesicle membrane {ECO:0000269|PubMed:16314447}; Multi-pass membrane
CC protein {ECO:0000269|PubMed:16314447}. Note=A constitutive cytoplasmic
CC pool is present that localizes to intracellular microvesicles termed
CC chitosomes. Chitosomes constitute a separate secretory route distinct
CC from the typical secretory pathway and serve as a vehicle for
CC delivering the enzyme to the sites on the cell surface where
CC polysaccharide sythesis takes place (By similarity). Localizes to septa
CC of yeast-like cells and to the basal septum separating the living tip
CC cell from the vacuolated part in hyphae. Also localizes to the growing
CC bud tip in yeast-like cells and to the tip of the hyphae.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the chitin synthase family. Class IV subfamily.
CC {ECO:0000305}.
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DR EMBL; CM003157; KIS66485.1; -; Genomic_DNA.
DR RefSeq; XP_011391813.1; XM_011393511.1.
DR AlphaFoldDB; Q4P333; -.
DR STRING; 5270.UM05480P0; -.
DR PRIDE; Q4P333; -.
DR EnsemblFungi; KIS66485; KIS66485; UMAG_05480.
DR GeneID; 23565362; -.
DR KEGG; uma:UMAG_05480; -.
DR VEuPathDB; FungiDB:UMAG_05480; -.
DR eggNOG; KOG2571; Eukaryota.
DR HOGENOM; CLU_002572_0_0_1; -.
DR InParanoid; Q4P333; -.
DR OMA; KYLVNCM; -.
DR OrthoDB; 134286at2759; -.
DR BRENDA; 2.4.1.16; 6587.
DR PHI-base; PHI:1113; -.
DR Proteomes; UP000000561; Chromosome 18.
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; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR22914; PTHR22914; 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..1273
FT /note="Chitin synthase 7"
FT /id="PRO_0000270623"
FT TOPO_DOM 1..79
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 80..100
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 101..117
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 118..138
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 139..360
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 361..381
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 382..820
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 821..841
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 842..857
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 858..878
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 879..881
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 882..902
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 903..1273
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 1..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 415..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 966..1009
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1126..1273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..69
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 433..447
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1185..1215
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1216..1239
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 412
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 667
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 796
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 1273 AA; 140139 MW; 4CB36E1DB66DC706 CRC64;
MPAVERNAPF TKTFIRKPGQ RNDTSIPLHT EAPPPLRQPT RIARAKTLTR PERSQPQVPL
INPSSGGPGF SAASRSKHRF SWWTAFSLFV TFWAPSPLLS SCCGLKDKQS RQAWREKVSL
VFIAILLGGF IGFITMGLNA ALCPSASSHS PNTYSRIGTG GAILGVHGWA FDIAQAHHLP
EAPALFSLST SRPGSDISSL FARSTSDQSP ACRGTTAAYA ADASCVALNG TLLKDCPLGP
LSPATFAQYG MYNQTRKIGY GWEDVESANF SNFLVLDGVV LNMSPYLKAN PSPIAADVVD
LAIRQQLATS PHRGRDATIT FYTNPTTRNA IKCLTQKYVA GYIDKITPGC FISNLVLYCS
LVVILAIVLI RFFMAVWFAW FMAGRMSSPP RPSRRRRLAP NVLPEGAMIS LNSSGAAPWA
NKQRPPPSQP ARRRRDSAQS ATPSVPDSLS VHHIGDEPYV VCLVTAYSEN EEGISTTLTS
LSETHYSDQR KLLFVVADGM VTGSGESMST PDVCVSLLEA DPRFGTPIPM SFVSIASGKK
EHNMAMVYAG HYTRATGRRT PMVVVVKCGA PEEAADSKPG NRGKRDSQMI LMNFFQRVTY
NDRMTPLDYD LFRKVHTLMG VTPDFFELCL MVDADTMVYP KSMKTLTNCM MRDPMIMGAC
GETRIANKTQ SWVTMIQVYE YFISHHQAKA FESVFGGVTC LPGCFSMYRI KARKQTDDDW
VPIIVKPEVT REYSQSVVTT LHQKNLLLLG EDRFLTTTLL RTFPNRKMVF CPEARCKTEV
PHTFKMLLSQ RRRWINSTIH NLMELVLVRD LCGTFCFSMQ FVVFMDLLGT AVLPISIALT
YTLVVTYCLN PPHSFTEAIP LMLLVAVIGM PALLILLATR KVVYVLWMLI YLLALPVWNF
VLPVYSFWHF DDFSWGETRK VEGEAKQTGH GDEGGSATGN AVPLRRWEDW ERSRLRKKKR
EEKRRRELER QFGSGFHNDN ASDGDPDRKE AGMPLSRPGS DSFSDSVTVS DFDDDKWGNQ
IGGYDETLPP PVQIVRHSVW IGDQEVIIDT EDMEKMLETG WDDKAFRARN LSSASSTNAL
LQAQQPQYPS AVNRNRLSQM GAFATKRDAP AVPEIPARYS MYVQNNGGGR PANGHGNSNG
HYEPGSYEME RTPSPGEYAS LIRGGAPSPC SPGFGPAQPY GHSSAVSGGA GQYSTGSHAR
QRSGGANAAY NQPHQHPPQP SQPPQPPQPA QPTRPGGAPA APPRGAGSQG SGFAGARPSN
PTGRGRSYHD RFS
