ID A0A1I8Q2C1_STOCA Unreviewed; 1592 AA.
AC A0A1I8Q2C1;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 28-JUN-2023, entry version 23.
DE RecName: Full=chitin synthase {ECO:0000256|ARBA:ARBA00012543};
DE EC=2.4.1.16 {ECO:0000256|ARBA:ARBA00012543};
GN Name=106085815 {ECO:0000313|EnsemblMetazoa:SCAU013201-PB};
OS Stomoxys calcitrans (Stable fly) (Conops calcitrans).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Muscoidea;
OC Muscidae; Stomoxys.
OX NCBI_TaxID=35570 {ECO:0000313|EnsemblMetazoa:SCAU013201-PB, ECO:0000313|Proteomes:UP000095300};
RN [1] {ECO:0000313|EnsemblMetazoa:SCAU013201-PB}
RP IDENTIFICATION.
RC STRAIN=USDA {ECO:0000313|EnsemblMetazoa:SCAU013201-PB};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
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 RefSeq; XP_013105691.1; XM_013250237.1.
DR STRING; 35570.A0A1I8Q2C1; -.
DR EnsemblMetazoa; SCAU013201-RB; SCAU013201-PB; SCAU013201.
DR GeneID; 106085815; -.
DR VEuPathDB; VectorBase:SCAU013201; -.
DR OrthoDB; 1331060at2759; -.
DR Proteomes; UP000095300; Unassembled WGS sequence.
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 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 77..101
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 134..153
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 174..194
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 200..220
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 298..324
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 375..397
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 409..434
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 467..485
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 953..970
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 977..1000
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1006..1027
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1039..1058
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1276..1295
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1333..1354
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1157..1215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1069..1096
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1592 AA; 180142 MW; 911AB0D38FA43F5B CRC64;
MSNIKHRPLA PPGTGDSDDN FTDDESTPLT HDIYGGSQRT IQETKGWDVF RDPPIKIETG
STANQECLEL TVKILKIVAY IITFIVVLGG GVMAKGTVLF MTSQLNKDKR VEFCNKDLGR
DKTFVVKLPE EERIAWLWAL IIAFAVPEVG ALIRSTRICF FKTFKVPQKS HFMFMFIMES
LNTFGTALLM FVVLPQLDAI QGAMLTNCLC VVPGILGLMS RTSKEGKRFA KMLIDLVALA
AQVTGFVVWP LLENRKELWV IPVACLMISC GWWENYVDSQ SSFGIIRAMG RIKDDLKYTR
YFSHMFLSIW KIALFMCSVL FIYWTQGDEP GNIFTMFGDA FGPHKISVDE LATTLSGSLP
DTIDAANIDS IDIDAAHYTV IYVLLIQIFG AYLCYIFGKF ACKILIQGFS YAFPVSLTIP
ISVSLLIAAC GIRIDDPCFF HDTIPDYLFF TSPSNFRFND FVTQQMAWAW ILWLLSQTWI
SLHIWTPKCE RLATTEKLFV KPMYCALLID QSMAMNRRRD DQADVKTEDL SEIDKEKGDE
YYETISVHTD GSAIQSKPTV KSSDHITRIY ACATMWHETK DEMMEFLKSV MRLDEDQCAR
RVAQKYLRIV DPDYYEFETH TFFDDAFEIS DHSDDDIQVN RFVKLLVATM DDAASEIHQT
TIRLRPPKKY PTPYGGRLVW TLPGKTKFIA HLKDKDRIRH RKRWSQVMYM YYLLGHRLME
LPISADRKDT IALNTYLLTL DGDIDFKPNA VTLLVDLMKK NKNLGAACGR IHPVGSGPMV
WYQLFEYAIG HWLQKATEHM IGCVLCSPGC FSLFRGKALM DDNVMKKYTT QSDEARHYVQ
YDQGEDRWLC TLLLQRGYRV EYSAASDAYT HCPEGFNEFY NQRRRWVPST IANIMDLLGD
AKRTIKINDN ISLLYIFYQM MLMGGTILGP GTIFLMLVGA FVAAFRIDNW TSFHYNIVPI
LAFMVVCFTC KSNIQLFVAQ VLSTAYALIM MAVIVGTALQ LGEDGIGSPS AIFLIAMTGS
FFIAACLHPQ EFWCISCGLI YLLSIPSMYL LLILYSIINL NVVSWGTREV VAKKTKKELE
AEKKAAEEAA KKVKQKSMLG FLQGGMGSNA DDEGSVEFSL AGLFRCVFCT HGKTSDEKQQ
LTAIAESLDT IKTRIDSIEQ TVNPHETSHR HGRRRTTSGS SKDHHLLSSV AEKSGDESDE
TESDSSGEPK QERDFLTNPY WIEDPDLRKG EVDFLSSSEI QFWKDLIDKY LFPIDNDPVE
QARIASDLIE LRNKSVFAFF MANALFVLIV FLLQLNKDKL HIVWPLGVKT NITYIEETSE
VHISKEYLQL EPIGLVFVFF FALILVIQFT AMLFHRFGTL AHILSSTELN FCKKKTEDMS
QDALIDKHAV EIVKNLQRLQ GIDGDYDNDS GSGPDRIARR KTIQNLEKAR QPRRQIGTLD
VAFKKRFMKL TADAENNPST PILTRRLTMR AETIRALEVR KNSVMAERRK SAMQTLGAKN
EYGITTATAL NNNGGIPNAR SGRISNAGIS IKDVFNVNGG PGEQIYGSNG GGTINQGYEH
VTEEDEVNSL RLTTRNPPQV TWGTNSNSSG RL
//
