CHS1_ENCCU
ID CHS1_ENCCU Reviewed; 816 AA.
AC Q8SSI7;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 25-MAY-2022, entry version 93.
DE RecName: Full=Chitin synthase 1;
DE EC=2.4.1.16;
DE AltName: Full=Chitin-UDP acetyl-glucosaminyl transferase 1;
DE AltName: Full=Class-IV chitin synthase 1;
GN Name=CHS1; OrderedLocusNames=ECU01_1390;
OS Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC Encephalitozoon.
OX NCBI_TaxID=284813;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GB-M1;
RX PubMed=11157783; DOI=10.1101/gr.164301;
RA Peyret P., Katinka M.D., Duprat S., Duffieux F., Barbe V., Barbazanges M.,
RA Weissenbach J., Saurin W., Vivares C.P.;
RT "Sequence and analysis of chromosome I of the amitochondriate intracellular
RT parasite Encephalitozoon cuniculi (Microspora).";
RL Genome Res. 11:198-207(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GB-M1;
RX PubMed=11719806; DOI=10.1038/35106579;
RA Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA Vivares C.P.;
RT "Genome sequence and gene compaction of the eukaryote parasite
RT Encephalitozoon cuniculi.";
RL Nature 414:450-453(2001).
RN [3]
RP DEVELOPMENTAL STAGE.
RX PubMed=17169074; DOI=10.1111/j.1550-7408.2006.00179.x;
RA Roennebaeumer K., Wagener J., Gross U., Bohne W.;
RT "Identification of novel developmentally regulated genes in Encephalitozoon
RT cuniculi: an endochitinase, a chitin-synthase, and two subtilisin-like
RT proteases are induced during meront-to-sporont differentiation.";
RL J. Eukaryot. Microbiol. 53:S74-S76(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:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- DEVELOPMENTAL STAGE: Expression is low in meronts, but becomes induced
CC when meronts start to differentiate into sporonts.
CC {ECO:0000269|PubMed:17169074}.
CC -!- SIMILARITY: Belongs to the chitin synthase family. Class IV subfamily.
CC {ECO:0000305}.
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DR EMBL; AL391737; CAD25012.1; -; Genomic_DNA.
DR RefSeq; XP_965977.1; XM_960884.1.
DR AlphaFoldDB; Q8SSI7; -.
DR STRING; 284813.Q8SSI7; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR GeneID; 860318; -.
DR KEGG; ecu:ECU01_1390; -.
DR VEuPathDB; MicrosporidiaDB:ECU01_1390; -.
DR HOGENOM; CLU_002572_0_1_1; -.
DR InParanoid; Q8SSI7; -.
DR OMA; AFMSQPW; -.
DR OrthoDB; 134286at2759; -.
DR Proteomes; UP000000819; Chromosome I.
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; IEA:UniProtKB-EC.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR004835; Chitin_synth.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR22914; PTHR22914; 3.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Cell wall biogenesis/degradation; Glycoprotein;
KW Glycosyltransferase; Membrane; Reference proteome; Sporulation;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..816
FT /note="Chitin synthase 1"
FT /id="PRO_0000382935"
FT TOPO_DOM 1..32
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 33..53
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 54..63
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 64..84
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 85..240
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 241..261
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 262..697
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 698..718
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 719..720
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 721..741
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 742..745
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 746..766
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 767..816
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 319
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 664
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 816 AA; 93665 MW; C1E404326FE125F7 CRC64;
MLSQGEILRN PSRTRLQRPP KSRSERKGWW YRVTIFLTCL IPNFMLRCFG MTTPEVQHAW
REKVALCICI FFCWIILGFT TYGMNTIICK GSNQYVASRL KRDAFDGNTV IANGGIYYTD
DEYAFGENHT YAFEKKSGAC KLAFGRQLPS GDEDIDDLER INDIYWDWGD IMSKGMIVVG
NKVYDPSYCT EPLFEEFNRK YAGTEGKPDF DTDEWRCYED MFYAGKVATK TPGCLLADTM
FWITTISIFG LIITKFLLGF FYSWYAKRRP KPSPKITPCI LLVTCYSEGK DGIKNTLDSL
CKQDYGYDYK LIVVICDGNI TGSGNSMSTP DIVLGLSDVD RRAEPKGYIS LTHGTKRYNR
AKVHAGYYHV REEKKSRRYR CWPCFGRQAD SSEVENYKTR ILVINKCGNP SETFKAGNRG
KRDSQVILMS FFSKLIYGDR MTELDFEIYQ KMKFLMPHIE PEDFECILMV DADTIVKPDA
LSIMVNVFET DQKVIGMCGE TMILNKFESW VTMIQVFEYY ISHHLSKAFE SVFGGVTCLP
GCFCMYRIKI VTNQQGQLLS GPSKSRASVP RFSSMKSILS SSLEKSLCLP ILANPAIINA
YSVLEVKTLH QKNLLHLGED RYLTTLLLKT FYRRKLVFIP AAKCETYVPG EFSVLLSQRR
RWINSTIHNL FELVQVNNLC GAFCFSMQLV VVMELFGTLV LPAAIIFTFV MIAVSILIEP
AWVPLIMLVG IFGLPAVLIL ITTMEIQYVF WCLVYILSIP IWNFVLPTYA FWHFDNFSWG
DTRKVDGEGK EDEEGEFDHT KIRIRELEEF LSEANK
