ID H9U0G5_TETUR Unreviewed; 1522 AA.
AC H9U0G5;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 29-MAY-2024, entry version 30.
DE RecName: Full=chitin synthase {ECO:0000256|ARBA:ARBA00012543};
DE EC=2.4.1.16 {ECO:0000256|ARBA:ARBA00012543};
DE Flags: Fragment;
GN Name=chs1 {ECO:0000313|EMBL:AFG28415.1};
OS Tetranychus urticae (Two-spotted spider mite).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Acariformes; Trombidiformes; Prostigmata; Eleutherengona; Raphignathae;
OC Tetranychoidea; Tetranychidae; Tetranychus.
OX NCBI_TaxID=32264 {ECO:0000313|EMBL:AFG28415.1};
RN [1] {ECO:0000313|EMBL:AFG28415.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=005 {ECO:0000313|EMBL:AFG28415.1};
RX PubMed=22393009; DOI=10.1073/pnas.1200068109;
RA Van Leeuwen T., Demaeght P., Osborne E.J., Dermauw W., Gohlke S., Nauen R.,
RA Grbic M., Tirry L., Merzendorfer H., Clark R.M.;
RT "Population bulk segregant mapping uncovers resistance mutations and the
RT mode of action of a chitin synthesis inhibitor in arthropods.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:4407-4412(2012).
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:0000256|ARBA:ARBA00000319};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; JQ613276; AFG28414.1; -; mRNA.
DR EMBL; JQ613277; AFG28415.1; -; mRNA.
DR GO; GO:0071944; C:cell periphery; IEA:TreeGrafter.
DR GO; GO:0030428; C:cell septum; IEA:TreeGrafter.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004100; F:chitin synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0006038; P:cell wall chitin biosynthetic process; IEA:TreeGrafter.
DR GO; GO:0006035; P:cuticle chitin biosynthetic process; IEA:TreeGrafter.
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:SF42; CHITIN SYNTHASE; 1.
DR Pfam; PF03142; Chitin_synth_2; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE 2: Evidence at transcript level;
KW Glycosyltransferase {ECO:0000313|EMBL:AFG28415.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Transferase {ECO:0000313|EMBL:AFG28415.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 31..55
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 95..113
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 134..157
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 163..180
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 192..212
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 218..235
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 263..288
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 341..359
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 371..396
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 431..450
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 462..479
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 886..910
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 917..936
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 942..964
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 976..992
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1004..1023
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1242..1262
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1300..1321
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 1144..1169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1468..1522
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1147..1161
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1468..1493
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AFG28415.1"
FT NON_TER 1522
FT /evidence="ECO:0000313|EMBL:AFG28415.1"
SQ SEQUENCE 1522 AA; 173835 MW; B36BF91F2B664C89 CRC64;
KWDVFVESPP PDDDETSSSE WIDVILKILK LCAYVITFIV VLACSVLSKG LVLFMTSIIK
PNRTGLIICS HGIPSLDRDK KYEVVLNLSD PERVAWIWAL IGVLIVPELM TLFRAARICT
FKSIRRPSKA VFSLIFIVET LHTIGIVMLV FLILPSLDVT KGVILTNCFC FIPGCLSLFS
RHSGEAGRGY KTLLDLLSVG AQLSGLILWS VAESTDNPVA IYIPITSLLI SIGWWENYID
KKSPFRAIQR LAQIKEGLQK SRYFIYIFIS AWKIILIFIA TIILRLLVDG SALYLFTQFK
SAFTSHKILI IRDRSDLSKS LSDSNVGIES EWLEMPASTS APIWMLILQI SASWFCYVFG
KFACKICIQR ISFASPLILS VPVTAMTLAQ FCVLNFENSC SLNRFLPRYL FWSCPSADTF
FTDGVFYNLH GIIWVIMYIS QFWITFHIFN PKCERLATTE KLFVNPMYCG LLIDASMILN
RRRDDKEVIK AGDIDKSVRD PDNVQDPSLH YETISEHPDD KKSTVQSTDF ITKILVCATM
WHETSEEMIQ MLKSVFRMDF DQSARHKAQK YLRVVDPDYY EFEVHILFDD AFELSDDNDD
YQVVNRFVKQ FIEVIDTAAS NIHQCEIRLK SPAKYPTPYG GKLEYILPGG NKLHVHLKDK
MKIRHRKRWS QVMYMYYLLG HRLMELPIDV NRKATMAENT YILTLDGDIN FRPEAVQLLV
DLMKKNKNLG AACGRIHPVG SGLMAWYQKF EYAVGHWLQK ATEHMIGCVL CSPGCFSLFR
AKALMDDNVM RKYTTRSDEA LHYVQYDQGE DRWLCTLLLQ RGYRVEYSAA ADAYTHCPEG
FGEFYTQRRR WAPSTMANIL DLLGDYKRTV AVNDHISLLY IVYQGMLMVG TILGPGTIFL
MLVGAMVAVF RISNWDSFLF NLIPILIFIV ICFTCKNDIQ ILVAQIMSAC YALLMMAVFV
GTAIQMAEDG VTSPSAVFFI ALSGSFVVAA LLHPQEFHCL YPCLLYFLSI PCMYLLLMIY
SLVNLNVVTW GTREVQTKKT KAELEEEKKA VEEIKKGNLL SFLNLNPNAK EEEGSIEFSL
ANLFRCSFCT YPKPNDEKIH LLKIEQHLSE MTDKLGSLEK YLDPLGGPRR KGSSIGRNAR
FSDNLSTVTE NEEHEDMDSI GSESQTDDMS IKDNEEVAPR FDEDHPYWIE DKDLRDGEIK
QLAENEIAFW KELISKYLYP IDQNKDHQAR VAVELKELRN RVVFSFFMLN ALFVLVVLIL
QLNKDILHVD WPYGIRENIT FIPETNEIRI DKEYLEMEPI GLVFVGFFGL ILLIQLIGML
FHRFGTLSHM LASVNLFQSK RDDISGEDDL KRNAIDIARQ LQKLQGFNDG ESSEDNTYGI
AARKTIQKLE MRGRQTIKTG TLDVAFREKF MAILEAQEEG TTTPVLGGKR NRETITALIK
RRKNILGYDD HVGMQTLGIK NEFVRNPARS TLDSKQRRPP NPYGTNGMVN QAFDGLSSDE
ELEPPEVPMS TYRGINRQNL NG
//