ID CHS5_USTMA Reviewed; 1609 AA.
AC O13394; A0A0D1DZZ4; Q4PBE4;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 16-SEP-2015, sequence version 3.
DT 24-JAN-2024, entry version 131.
DE RecName: Full=Chitin synthase 5;
DE EC=2.4.1.16;
DE AltName: Full=Chitin-UDP acetyl-glucosaminyl transferase 5;
DE AltName: Full=Class-IV chitin synthase 5;
GN Name=CHS5; ORFNames=UMAG_10277;
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 [GENOMIC DNA], AND FUNCTION.
RC STRAIN=518;
RX PubMed=9454647; DOI=10.1006/fgbi.1997.1014;
RA Xoconostle-Cazares B., Specht C.A., Robbins P.W., Liu Y., Leon C.,
RA Ruiz-Herrera J.;
RT "Umchs5, a gene coding for a class IV chitin synthase in Ustilago maydis.";
RL Fungal Genet. Biol. 22:199-208(1997).
RN [2]
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 [3]
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 [4]
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, ECO:0000269|PubMed:9454647}.
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 in a tip-ward gradient at the hyphal
CC apex. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the chitin synthase family. Class IV subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB84284.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAB84284.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF030553; AAB84284.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CM003145; KIS69221.1; -; Genomic_DNA.
DR PIR; T42020; T42020.
DR RefSeq; XP_011389165.1; XM_011390863.1.
DR AlphaFoldDB; O13394; -.
DR STRING; 237631.O13394; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR GlyCosmos; O13394; 3 sites, No reported glycans.
DR EnsemblFungi; KIS69221; KIS69221; UMAG_10277.
DR GeneID; 23566330; -.
DR KEGG; uma:UMAG_10277; -.
DR VEuPathDB; FungiDB:UMAG_10277; -.
DR eggNOG; KOG2571; Eukaryota.
DR InParanoid; O13394; -.
DR OrthoDB; 1331060at2759; -.
DR BRENDA; 2.4.1.16; 6587.
DR PHI-base; PHI:98; -.
DR Proteomes; UP000000561; Chromosome 6.
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: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 CDD; cd04190; Chitin_synth_C; 1.
DR InterPro; IPR004835; Chitin_synth.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR22914; CHITIN SYNTHASE; 1.
DR PANTHER; PTHR22914:SF16; CHITIN SYNTHASE 3; 1.
DR Pfam; PF03142; Chitin_synth_2; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 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..1609
FT /note="Chitin synthase 5"
FT /id="PRO_0000193723"
FT TOPO_DOM 1..326
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 327..347
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 348..364
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 365..385
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 386..624
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 625..645
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 646..1176
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1177..1197
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1198..1202
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1203..1223
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1224..1227
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1228..1248
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1249..1609
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 1..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 248..280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 294..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 729..767
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1354..1381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1399..1609
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..55
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..80
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..134
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..168
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..188
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..317
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 743..765
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1354..1377
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1435..1449
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1504..1518
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1526..1555
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1574..1593
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1594..1609
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 654
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1015
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1144
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CONFLICT 54
FT /note="I -> S (in Ref. 1; AAB84284)"
FT /evidence="ECO:0000305"
FT CONFLICT 75..76
FT /note="Missing (in Ref. 1; AAB84284)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1609 AA; 176298 MW; D37C3155BB515528 CRC64;
MNPFESLPDA ARPAQGTRPN RSDGPPPLPP LTIPGSTGRP QNPIFSPPPN LHHILPPGYL
PQQQQQQQQQ QQQQQQRSQQ PFFSPPPPDA MSPPLGSHQA YLNSTSSQPT QRLPGISFQE
PQRMPVQRSG PSRDSVKSYG DDKRSINDPN SSSTALTQVN SLDPESGFSA HNDTFRRKKS
LVRPDRERMD PSHRQWYYRN HAAHMDVMAA SGGRVGYMPS TTGHLPQHGA APHGSGMAGI
VGPGGGLSGL GVTGPTNVPP GGLGRAPPLR RGKSLLGRDE DQVETGINVL KRGVSLRRKQ
SKSGNKPSKE VPRDLGESKT SRIAPGPVGG WMIYCYILTI CCPGPFLRIF GIRTPEQQRA
WREKMGLIGI ITLIMAAVGF LTFGFTQTVC GQQPDRYTLG TIDVGSMTFN GYDYSFDGFI
HPQVGPFGAD TIYNRTNPIY SEPWSSGGQD GSLLFQKIGA ACTGIISNRA GGAQPERYFD
CTLVRQDGKG GYANSTMPMC HTGSIVDQFN DGAQPRNSVL KKRGQVSLQW NNVTDPARNL
AVYRGSVLDL NRLNNLTTGL SYPELYDTLK RRNDSWAGRD VTSAVMRQRL EREFQCLEQI
TRVGFIDSET IGCVASKVEL YLSLVFIIGV VAIKFFMAVM FGWFISWRLG NYANETYEQR
MKRAAEIEQW SDDIYRPAPA GYRPNARKHK SFLPAKSRFS VADPLSLKSG SRAPMPLSEK
RMTRASRLGV ASPLGGSPPG SPSVAGGRSS ASLAPAHSRR SSFSGSPAEG AMGVCPFPLH
NTIPQPGPDY RPFGFQLAHS ICLVTAYSES FEGLRTTLDS LATTDYPNSH KLLLVIADGI
VKGAGSDIST PDICLSMMKD LVIPAEEVEG NSYVAIADGY KRHNMCKIYA GFYDYDDETV
ERSKQQRVPM ILVAKCGTPL EADSAKPGNR GKRDSQVLLM AFMQKVMFDE RMTAFEYEFF
NSIWRVTGVS PDNYEIVLCV DADTKVFPDS LSRMVACMVE DPEIMGLCGE TKIANKSETW
VTMIQVFEYY ISHHQTKAFE ACFGGVTCLP GCFSAYRIKA PKGPHGYWVP ILANPDIVEH
YSENVVDTLH KKNLLLLGED RYLTTLMLKT FPKRKMMFVP QAVCKTIVPD TFRILLSQRR
RWINSTVHNL FELVMVNDLC GTFCFSMRFV VFMELTGTLV LPAAIAFTLY VVVQAFLPNV
PTPTIPLILL ALILGLPGIL IVVTSRKIAY VGWMLIYLLS LPIWNFVLPL YAYWHMDDFS
WGATRVVQGE NKKDNHGDAD GKFDPSHIVM KRWAEFERER RWKSGTHSRD STYDVVQRTG
SPERAGSTRY SVVSSDTFHS SPFGQHDQFG RALPNAMSSS SASQFGPDVS EVSHSKSPSG
ARARLDAVPL LELPAPLATD AKHRSGASPT GTVVVPRPRA TSPAPLPHNS GHPALGSVSA
FSPTQHSAGR LPTLPGAATY EAYPHTDAAD EERRPMIGST SSSPDPEPRR YIGPDAGVRH
GNVSTEQRYP TVSESAYPMQ AYTAEPETDG SASPTPAQQG FNAANSNQQT RPLTRGFSLV
DDGPVASAQG VRQVQRGARR SQMPNSAASP PPANRTGNLP PGAAPPSFD
//
