CHS2_USTMA
ID CHS2_USTMA Reviewed; 1074 AA.
AC P30599; A0A0D1DVQ8; Q4P6H3;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 2.
DT 25-MAY-2022, entry version 125.
DE RecName: Full=Chitin synthase 2;
DE EC=2.4.1.16;
DE AltName: Full=Chitin-UDP acetyl-glucosaminyl transferase 2;
GN Name=CHS2; ORFNames=UMAG_04290;
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 405-590.
RX PubMed=1731323; DOI=10.1073/pnas.89.2.519;
RA Bowen A.R., Chen-Wu J.L.-P., Momany M., Young R., Szaniszlo P.J.,
RA Robbins P.W.;
RT "Classification of fungal chitin synthases.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:519-523(1992).
RN [4]
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: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. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the chitin synthase family. Class II subfamily.
CC {ECO:0000305}.
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DR EMBL; CM003151; KIS67796.1; -; Genomic_DNA.
DR EMBL; M82959; AAA34225.1; -; Genomic_DNA.
DR PIR; A45189; A45189.
DR RefSeq; XP_011390745.1; XM_011392443.1.
DR AlphaFoldDB; P30599; -.
DR STRING; 5270.UM04290P0; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR EnsemblFungi; KIS67796; KIS67796; UMAG_04290.
DR GeneID; 23564516; -.
DR KEGG; uma:UMAG_04290; -.
DR VEuPathDB; FungiDB:UMAG_04290; -.
DR eggNOG; KOG2571; Eukaryota.
DR HOGENOM; CLU_004760_3_0_1; -.
DR InParanoid; P30599; -.
DR OMA; QYLFLMP; -.
DR OrthoDB; 256142at2759; -.
DR BRENDA; 2.4.1.16; 6587.
DR PHI-base; PHI:1109; -.
DR Proteomes; UP000000561; Chromosome 12.
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; IPR001173; Glyco_trans_2-like.
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 Pfam; PF13632; Glyco_trans_2_3; 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..1074
FT /note="Chitin synthase 2"
FT /id="PRO_0000193722"
FT TRANSMEM 608..628
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 742..762
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 779..799
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 817..837
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 867..887
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 891..911
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1001..1021
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1048..1068
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 56..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 209..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..151
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 72
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 97
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 149
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 289
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1074 AA; 120446 MW; 1EDA92BD08837863 CRC64;
MSHYHRQGGP GQPHDSYEDQ QQPYYTDQAH SGYDHHSYHQ QQLYHAAYDA AQPEYQAAPV
KPQRQPSRIR SNSSGSRSVS HTPAAYTNQG IPPVPSNLSA ARQRSDPSQA LPPSSSSYAQ
DAFSRPSYSS HRNAPNAPNS NHPSRWDPNA SYDTAPTAPL YDPAPLPGSG QLDADPSQHS
IDLGVREPLY DDQVMQQHYP YGGAAAFQRS DSYQSGRPGA GGYHSIDDEK SIHSKHSNQP
PGAWNAGAPS MPYNNMPTSH STIQMAQPAY PPSPYGEYEM HATGMPEPNM SIAGLGAPGA
LIAAAPMPGM QHHDSTYSRE NRERIMRKRT VKRIPLQDGN LVLDIPVASS ISKSTTNNPE
FREMRYQACT SDPDRFIEEK YTLRPWLYGR ETEMAIVLTC YNEDDVLFAR TMGGVIKNIA
HLCSRTRSKT WGPDAWKKVV VIIVADGRKK ANERMLKALG LMGCYNEGVM KDHVLKKPVE
AHIFEYTTRV QITEKGEVKV TPCPIQVVFC LKEQNKKKLN SHRWYFNAFC QMLKPNVCIL
LDVGTKPTGT SIYELWKSFD KHHRVGGACG EICVDTGRGC TALFNPLVAS QNFEYKMSNI
LDKPTESVFG FISVLPGAFS AYRYKALLGR PLEMYFKGEK LHSGEGSNSI FEGNMYLAED
RILCFELVTK EREGWLLRYV KSAKAYTDVP DRVPEFISQR RRWLNGSLFA SYYAVWHWYR
IFTSGQPFLR KLWLLFQVIY NLVLLVFSWF GIANFFLAFY FLLSASTSTE GSDPFGGQGA
AIVEIFQNIF IAMVIVVLVC SLGNRPQGSN FAYTSAIIIF ALIMGLALYA AGYTIYLALD
AAGLTHTNGW RVDNLETLFK TSGFRDIVIS LAATYVMWLL CSLLHLEPWH MLTSFVQYLF
LTPTYVIILS MYSMCNTNDL SWGTKQSNGP ATDLGGATGC NSKQDGKGEM VDVKIPTSAA
DAEELWTHYR QTLSQPTVEV KQKRDKATRQ EDHAKNFRTN LVLIWMCTNA LVVIIFTSTW
WNKYVRNHIY AGAVRRGEPV INPYQSAIFW STAGLSAVRF VGSITFLLLR LFGH
