ID A0A498M057_LABRO Unreviewed; 1133 AA.
AC A0A498M057;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=chitin synthase {ECO:0000256|ARBA:ARBA00012543};
DE EC=2.4.1.16 {ECO:0000256|ARBA:ARBA00012543};
GN ORFNames=ROHU_037331 {ECO:0000313|EMBL:RXN11035.1};
OS Labeo rohita (Indian major carp) (Cyprinus rohita).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Cyprinidae; Labeoninae; Labeonini; Labeo.
OX NCBI_TaxID=84645 {ECO:0000313|EMBL:RXN11035.1, ECO:0000313|Proteomes:UP000290572};
RN [1] {ECO:0000313|EMBL:RXN11035.1, ECO:0000313|Proteomes:UP000290572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DASCIFA01 {ECO:0000313|EMBL:RXN11035.1};
RC TISSUE=Testis {ECO:0000313|EMBL:RXN11035.1};
RA Das P., Kushwaha B., Joshi C.G., Kumar D., Nagpure N.S., Sahoo L.,
RA Das S.P., Bit A., Patnaik S., Meher P.K., Jayasankar P., Koringa P.G.,
RA Patel N.V., Hinsu A.T., Kumar R., Pandey M., Agarwal S., Srivastava S.,
RA Singh M., Iquebal M.A., Jaiswal S., Angadi U.B., Kumar N., Raza M.,
RA Shah T.M., Rai A., Jena J.K.;
RT "Draft genome sequence of Rohu Carp (Labeo rohita).";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RXN11035.1}.
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DR EMBL; QBIY01013157; RXN11035.1; -; Genomic_DNA.
DR STRING; 84645.A0A498M057; -.
DR Proteomes; UP000290572; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0004100; F:chitin synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd04190; Chitin_synth_C; 1.
DR CDD; cd06962; NR_DBD_FXR; 1.
DR Gene3D; 3.30.50.10; Erythroid Transcription Factor GATA-1, subunit A; 1.
DR Gene3D; 1.10.565.10; Retinoid X Receptor; 1.
DR InterPro; IPR004835; Chitin_synth.
DR InterPro; IPR035500; NHR-like_dom_sf.
DR InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
DR InterPro; IPR001723; Nuclear_hrmn_rcpt.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR001628; Znf_hrmn_rcpt.
DR InterPro; IPR013088; Znf_NHR/GATA.
DR PANTHER; PTHR22914; CHITIN SYNTHASE; 1.
DR PANTHER; PTHR22914:SF42; CHITIN SYNTHASE; 1.
DR Pfam; PF03142; Chitin_synth_2; 1.
DR Pfam; PF00104; Hormone_recep; 1.
DR Pfam; PF00105; zf-C4; 1.
DR PRINTS; PR00398; STRDHORMONER.
DR PRINTS; PR00047; STROIDFINGER.
DR SMART; SM00430; HOLI; 1.
DR SMART; SM00399; ZnF_C4; 1.
DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1.
DR SUPFAM; SSF48508; Nuclear receptor ligand-binding domain; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR PROSITE; PS51843; NR_LBD; 1.
DR PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
DR PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
PE 4: Predicted;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000290572};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT TRANSMEM 438..457
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 464..481
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 487..508
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 515..539
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 545..564
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 589..610
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 622..646
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 658..676
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 724..750
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 86..161
FT /note="Nuclear receptor"
FT /evidence="ECO:0000259|PROSITE:PS51030"
FT DOMAIN 211..444
FT /note="NR LBD"
FT /evidence="ECO:0000259|PROSITE:PS51843"
FT REGION 175..204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..191
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1133 AA; 129322 MW; 650184B614216B2C CRC64;
MPFTNYPSMQ YTSVEPSMSS PSYYSNQHCY PQYSGEEWFS PTTMFEMRKG PLEGGFDNEL
EESCPVVPTV CKRPRHAAHS GRSKGEELCV VCGDKASGYH YNALTCEGCK GFFRRSITKN
AVYKCKSGGN CEMDMYMRRK CQECRLRKCK EMGMLAECLL TEIQCKSKRL RKNTKASSDE
STGDDVVDSR DGKQVVSTTK PSKENLELSQ DQQALINYIV DAHNKHRIPQ EMAKKLLQEQ
FNAKENFLLL TEMATTHVQV LVEFTKNIPG FSTLDHEDQI ALLKGSAVEA MFLRSAQVFS
KKQPNGHTEV LEDRIRRSGM SEEFITPMFN FYRSIGELQM MQEEHALLTA ITILSPGCGP
SYNICLVSAE ICLPFSVPSS KNHSGPQPRN GGRSAVKPRI TSRSTLKPIL KPTQSWDVCK
QVPIIQDEQM PKKRVQCFKW FSCAIVGMLV FVLALLSKVL FVEFLVALGA AVLTIVAMPH
FDIVTNVMIL NSVSILSAVF QVVAECIAEE RKRFIMLPVF SIFLIVAGYV LFAISYLVFE
SSLEIKISVG LAIVATICVS VNWWENYSTL FKVPFLEDIS RDIAQSRNVV CIISSLIRIL
VTSAVLGAYV PLSGQDWKSV KLVFETVVVS LVAIQIVSSA LCRWFVVVAC KMHALRRSFV
MPMYLASITV LAAFLVPAGV RIPVSNQTCF ENHQPKSSDE WLLLLLTDTI KTLNTRDIVV
HMKIGGLVCL GCSALSWWLG LMLSTVYIWY LKIHRIERTQ DLFVRRMYEG AFLEQSMLLN
TRFEIRKRIK EKKSTKETIR VFLCATMWHE TYDEMMKIII SMFRLDKYRP KTDKHSDVEF
EFHIYFDDAF KDVDNGRHAN EYAEILVDVI KEVYTEEDPC IFKKTATLPH QTIINTPYGG
RLEYTLPKGN LMMVHLKDKT LIRHKKRWSQ IMYLYYILGW RLNRQYFTEF EAGKDLDSLK
EKLKKDRGNT YILALDGDTD FQPSAVMLLI DRLKLYPEVG AACGRIHPTG TGPMVWYQKF
EYAVGHWLQK TAEHVFGCVL CSPGCFSLFR GAALMDDNVM KRYTTKASEA SHYVQYDQGE
DRWLCTLLLQ QGWRVEYNAA SDAYTNAPQD FKEFYNQRRR WGPSTMSNTX SEV
//
