ID   H9U0G5_TETUR            Unreviewed;      1522 AA.
AC   H9U0G5;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   31-JUL-2019, entry version 19.
DE   SubName: Full=Chitin synthase 1 {ECO:0000313|EMBL:AFG28415.1};
DE            EC=2.4.1.16 {ECO:0000313|EMBL:AFG28415.1};
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;
OC   Acari; Acariformes; Trombidiformes; Prostigmata; Eleutherengona;
OC   Raphignathae; 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.,
RA   Nauen R., Grbic M., Tirry L., Merzendorfer H., Clark R.M.;
RT   "Population bulk segregant mapping uncovers resistance mutations and
RT   the mode of action of a chitin synthesis inhibitor in arthropods.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:4407-4412(2012).
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DR   EMBL; JQ613276; AFG28414.1; -; mRNA.
DR   EMBL; JQ613277; AFG28415.1; -; mRNA.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004100; F:chitin synthase activity; IEA:UniProtKB-EC.
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   2: Evidence at transcript level;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Glycosyltransferase {ECO:0000313|EMBL:AFG28415.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Transferase {ECO:0000313|EMBL:AFG28415.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     31     55       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     95    113       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    134    157       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    163    180       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    192    212       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    218    235       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    263    288       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    341    359       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    371    396       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    431    450       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    462    479       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    886    910       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    917    936       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    942    964       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    976    992       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1004   1023       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1242   1262       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1300   1321       Helical. {ECO:0000256|SAM:Phobius}.
FT   REGION     1144   1169       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   REGION     1468   1522       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COILED     1034   1054       {ECO:0000256|SAM:Coils}.
FT   COMPBIAS   1147   1161       Polyampholyte. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS   1468   1493       Polar. {ECO:0000256|SAM:MobiDB-lite}.
FT   NON_TER       1      1       {ECO:0000313|EMBL:AFG28415.1}.
FT   NON_TER    1522   1522       {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
//