ID H9U0G5_TETUR Unreviewed; 1522 AA. AC H9U0G5; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 22-FEB-2023, entry version 29. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; JQ613276; AFG28414.1; -; mRNA. DR EMBL; JQ613277; AFG28415.1; -; mRNA. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell. DR GO; GO:0004100; F:chitin synthase activity; IEA:UniProtKB-EC. 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 //