ID   CHS_MELAT               Reviewed;        1851 AA.
AC   Q8T5G8;
DT   28-FEB-2018, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   25-MAY-2022, entry version 44.
DE   RecName: Full=Chitin synthase {ECO:0000303|PubMed:11589574};
DE            EC=2.4.1.16 {ECO:0000305|PubMed:15777697};
DE   AltName: Full=Chitin-UDP acetyl-glucosaminyl transferase {ECO:0000305};
OS   Meloidogyne artiellia (British root-knot nematode).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Tylenchomorpha; Tylenchoidea; Meloidogynidae; Meloidogyninae;
OC   Meloidogyne.
OX   NCBI_TaxID=42426 {ECO:0000312|EMBL:AAG40111.1};
RN   [1] {ECO:0000312|EMBL:AAG40111.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DEVELOPMENTAL STAGE.
RX   PubMed=11589574; DOI=10.1007/s004380100513;
RA   Veronico P., Gray L.J., Jones J.T., Bazzicalupo P., Arbucci S.,
RA   Cortese M.R., Di Vito M., De Giorgi C.;
RT   "Nematode chitin synthases: gene structure, expression and function in
RT   Caenorhabditis elegans and the plant parasitic nematode Meloidogyne
RT   artiellia.";
RL   Mol. Genet. Genomics 266:28-34(2001).
RN   [2] {ECO:0000305}
RP   FUNCTION, CATALYTIC ACTIVITY, DEVELOPMENTAL STAGE, PROTEOLYTIC CLEAVAGE,
RP   AND DISRUPTION PHENOTYPE.
RX   PubMed=15777697; DOI=10.1016/j.gene.2004.11.045;
RA   Fanelli E., Di Vito M., Jones J.T., De Giorgi C.;
RT   "Analysis of chitin synthase function in a plant parasitic nematode,
RT   Meloidogyne artiellia, using RNAi.";
RL   Gene 349:87-95(2005).
CC   -!- FUNCTION: Required for the synthesis of chitin.
CC       {ECO:0000269|PubMed:15777697}.
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         Evidence={ECO:0000305|PubMed:15777697};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:15777697};
CC       Multi-pass membrane protein {ECO:0000255}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in eggs (PubMed:11589574,
CC       PubMed:15777697). Not expressed in hatched second-stage juveniles or in
CC       young females (PubMed:15777697). {ECO:0000269|PubMed:11589574,
CC       ECO:0000269|PubMed:15777697}.
CC   -!- PTM: May require proteolytic cleavage for activation.
CC       {ECO:0000305|PubMed:15777697}.
CC   -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown causes a delay in egg
CC       hatching. {ECO:0000269|PubMed:15777697}.
CC   -!- SIMILARITY: Belongs to the chitin synthase family. Class IV subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AY013285; AAG40111.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8T5G8; -.
DR   CAZy; GT2; Glycosyltransferase Family 2.
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; IDA:UniProtKB.
DR   GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:UniProtKB.
DR   Gene3D; 3.90.550.10; -; 1.
DR   InterPro; IPR004835; Chitin_synth.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   PANTHER; PTHR22914; PTHR22914; 1.
DR   SUPFAM; SSF53448; SSF53448; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Coiled coil; Glycoprotein; Glycosyltransferase; Membrane;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..1851
FT                   /note="Chitin synthase"
FT                   /id="PRO_0000443250"
FT   TOPO_DOM        1..108
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        109..129
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        130..168
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        169..189
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        190..208
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        209..229
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        230..234
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        235..255
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        256..261
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        262..282
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        283..291
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        292..312
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        313..337
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        338..358
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        359..544
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        545..565
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        566..573
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        574..594
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        595..631
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        632..652
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        653..1124
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        1125..1145
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1146..1154
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        1155..1175
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1176..1179
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        1180..1200
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1201..1209
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        1210..1230
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1231..1235
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        1236..1256
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1257..1461
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        1462..1482
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1483..1527
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        1528..1548
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1549..1851
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          432..522
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          693..718
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1350..1402
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1626..1658
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1765..1851
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1329..1383
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        436..451
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        466..482
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1350..1365
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1374..1402
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1777..1826
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        146
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        385
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        435
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        469
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        474
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        1274
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        1660
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   1851 AA;  210667 MW;  4B63A6DF9505E416 CRC64;
     MQYHQHQHQF PGPGPSHTSV YSSDGFSCSM ESIPLPEHLQ QRNPPMEEHY LQQTILPTRV
     PESTVAKARE IVLSHITSQE HLPWDTFRLL PPKADRHQKD TLYNGFLQVL KMITFVALFV
     TTLGSSILAK LSLLVMAAGL GQAGHNISIC PDKIPESPKN SVLISPKNAA KWAWALLLAI
     CIPELLCFAR SLHRSLFRKV RGPSFLQFLL VFTVESVHAF GLGALVFAIM PRGMVITMLQ
     LGNSLCLIPS LLLPLSRSRS RWLPLLLLLD GSAILAQSSA AIWRGSIPLE RFGFVFLCTS
     LISIAWWQNF VHPHSFLPAT RFFAHYAAKL RECRSKTFVV LSPWKCLIFT FCMFQFVPPQ
     IPFRELLQKD PFGEKLVTIN AYNLNQSQLN AFQERMENLE RKAFHQQHPH IVHPLKLNRK
     IVENIANGEA ALFRNGTRRP PKKEEVKKNK MDSKKKTKKL KKKKGGNNNA TSTNSSEKTP
     TKGGVLPTKR ERRTMAATGS NERVEADYSS NSDADEQEEE EENVAAYNIY DDRVELNQFT
     TANDALWLVF VQAGSVLLCQ LCAKFACKVV MQRVGLALPV VLSIPFGILF LAYSCRQKAT
     NPCHLSEWMS KELFWQCPTR PFHWQRFFRE QPNLLWLCWW LSQCWITIHL WLPRQERLAK
     SEKLFVLGYI DAPFPEHSIA LDRRRDDKIQ IRSEDIDTEE EANEGGGEQE DGNSSTHTCE
     SAASGLVVVE APFPKHPNVG RPTAASICSN GSLSSGSHRS DDGGLIRELP SSADSVCKIY
     VCATMWHESA LEMGCMLKSI FRLDKDQCAR RNAQRYLKVV DPDYYVFEAH IYIDDAFELD
     ENGNPHPNKF VHQLLEKMDE AASTKLQLRT PRICVTSYGG RISYVLPWRN RLSIHLKNKL
     LIRQRKRWSQ VMYLYFLLGF RLMLRVHEQK RRELLAENTF ILTLDGDVDF QPECVHLLVD
     LMRKNRRLGA ACGRIHPRGS GLMVWYQKFE YAVGHWLQKA TEHMIGCVLC SPGCFSLFRS
     SALIDDNVAR KYATKSEKPF HYVQYDQGED RWLCTLLLQR GYRVEYCAAS DALTFAPEGF
     SEFFNQRRRW IPSTMANVID LLRDYRNVVR VNDSVSIWYI AYQLVMLFSS VLGPGTIFLM
     IVGAISISFN IDTRLALLIV TTPVLCFCVC CLTCGTETQL LLAQVIGALF AMLMTAVIVG
     TSLQIQKDGL LSPHSIFLFT VLGSWSFSAL LHPLEFGCLL PCGLYFLAIP CMYMLLPVYS
     LCNLNTVSWG TRENASVSSS STGQFSGKRE ERGDILPHLQ KTEDGELSVG CGNFCRVVCC
     VRNPSSPPCA DETVEVRKLD ENFRKIERKL QSLERRTNGQ GNNAEEEGKE EEETGKSEQE
     RKEGREEGKE EEGKMSKRKK EEMDLKGWME LEPFRRFEPI VLDTEEESFW REMIEKYLRP
     ILPNSNEQAR IQRGLNELRN TCCSAFFMVN IVFIIVVLVL QLQKDCLHIE WPLGPLVNQT
     RVQCGGGGGR DFEGEEWIMS RLQLEPMGFV FIVFFLIILF IQFLAMLFHR FGTFTHIIAS
     TELCCAQRPL DKLSEEELVA QNAVEIVREL QAIRGIDSSL SRSEQFQQQP LQRQTRQHFP
     RTLSLGKRQQ NAQIPPRCEK GGNERGEESP TSLPAPPVIN WSEVHRNHQR VQPMEGGQQF
     DPRKDTLDAA FRQRFFALSS SSIAADHHQN NGGHLVDTTG TGHIGAAALP LTLNRRTLRA
     LEQRRNILYQ RGDRKRIPAL NQQFHSIFPS SSESEGEEGE GGGRGRGREQ ERDKCLEGKK
     EKFRQRVEEG PARCHRLEEL FGKSRKGGPQ KRGKVNGENM KFLGTTNKRA K