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Database: UniProt
Entry: A0A0G3VI81_CHISP
LinkDB: A0A0G3VI81_CHISP
Original site: A0A0G3VI81_CHISP 
ID   A0A0G3VI81_CHISP        Unreviewed;       560 AA.
AC   A0A0G3VI81;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Tyrosine hydroxylase long isoform {ECO:0000313|EMBL:AKL78848.1};
DE            EC=1.14.16.2 {ECO:0000313|EMBL:AKL78848.1};
DE   SubName: Full=Tyrosine hydroxylase protein 1 {ECO:0000313|EMBL:WNV48193.1};
GN   Name=TH-L {ECO:0000313|EMBL:AKL78848.1};
OS   Chilo suppressalis (Asiatic rice borer moth).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Pyraloidea;
OC   Crambidae; Crambinae; Chilo.
OX   NCBI_TaxID=168631 {ECO:0000313|EMBL:AKL78848.1};
RN   [1] {ECO:0000313|EMBL:AKL78848.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Xu G., Wu S., Huang J., Ye G.;
RT   "De novo assembly and characterization of central nervous system
RT   transcriptome reveals neurotransmitter signaling systems in Chilo
RT   suppressalis.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:WNV48193.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Xu Q.-Y.;
RT   "Tyrosine hydroxylase plays crucial roles in larval cuticle formation and
RT   larval-pupal tanning in the rice stem borer, Chilo suppressalis.";
RL   Submitted (AUG-2023) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000256|ARBA:ARBA00001954,
CC         ECO:0000256|PIRSR:PIRSR601273-2};
CC   -!- SUBCELLULAR LOCATION: Cell projection, axon
CC       {ECO:0000256|ARBA:ARBA00004489}.
CC   -!- SIMILARITY: Belongs to the biopterin-dependent aromatic amino acid
CC       hydroxylase family. {ECO:0000256|ARBA:ARBA00009712}.
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DR   EMBL; KP657623; AKL78848.1; -; mRNA.
DR   EMBL; OR472489; WNV48193.1; -; mRNA.
DR   STRING; 168631.A0A0G3VI81; -.
DR   OrthoDB; 275463at2759; -.
DR   GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0004511; F:tyrosine 3-monooxygenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009072; P:aromatic amino acid metabolic process; IEA:InterPro.
DR   GO; GO:0042423; P:catecholamine biosynthetic process; IEA:InterPro.
DR   Gene3D; 1.10.800.10; Aromatic amino acid hydroxylase; 1.
DR   InterPro; IPR045865; ACT-like_dom_sf.
DR   InterPro; IPR001273; ArAA_hydroxylase.
DR   InterPro; IPR018301; ArAA_hydroxylase_Fe/CU_BS.
DR   InterPro; IPR036951; ArAA_hydroxylase_sf.
DR   InterPro; IPR036329; Aro-AA_hydroxylase_C_sf.
DR   InterPro; IPR019774; Aromatic-AA_hydroxylase_C.
DR   InterPro; IPR005962; Tyr_3_mOase.
DR   InterPro; IPR019773; Tyrosine_3-monooxygenase-like.
DR   NCBIfam; TIGR01269; Tyr_3_monoox; 1.
DR   PANTHER; PTHR11473; AROMATIC AMINO ACID HYDROXYLASE; 1.
DR   PANTHER; PTHR11473:SF15; TYROSINE 3-MONOOXYGENASE; 1.
DR   Pfam; PF00351; Biopterin_H; 1.
DR   PIRSF; PIRSF000336; TH; 1.
DR   PRINTS; PR00372; FYWHYDRXLASE.
DR   SUPFAM; SSF55021; ACT-like; 1.
DR   SUPFAM; SSF56534; Aromatic aminoacid monoxygenases, catalytic and oligomerization domains; 1.
DR   PROSITE; PS00367; BH4_AAA_HYDROXYL_1; 1.
DR   PROSITE; PS51410; BH4_AAA_HYDROXYL_2; 1.
PE   2: Evidence at transcript level;
KW   Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR000336-1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR000336-1};
KW   Monooxygenase {ECO:0000256|ARBA:ARBA00023033};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:AKL78848.1}.
FT   DOMAIN          209..555
FT                   /note="Biopterin-dependent aromatic amino acid hydroxylase
FT                   family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS51410"
FT   REGION          56..110
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        80..95
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         388
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000336-1"
FT   BINDING         393
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000336-1"
FT   BINDING         433
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000336-1"
SQ   SEQUENCE   560 AA;  63409 MW;  6518F7EA40B1BB1E CRC64;
     MAVAAAQKNR EMFAIKKSYS IENGYPSRRR SLVDDARFET LVVKQTKQSV LEEARARAND
     SGLDSEFIQD GVPIGNGDNS PTVEDGTQQD ETKNGQLADA DIGDDASKTD EDYTLTEEEI
     ILQNAASESP EAEQAIQQAA LLLRMRDGMG SLARVLKTVD NYKGCVQHLE TRPSQVTDVQ
     FDALVKVSMS RNNLLQLIRS LRQSTAFAGV NLMTENISSK TPWFPRHASD LDNCNHLMTK
     YEPELDMNHP GFADKEYRER RKQIAEIAFA YKYGDPIPSI SYKETENATW QRVFNTVLDL
     MPKHACREYK AAFTKLQEAD IFVPHRIPQL EDVSNFLRKH TGFTLRPAAG LLTARDFLAS
     LAFRVFQSTQ YVRHANSPFH TPEPDCIHEL LGHIPLLADP SFAQFSQEIG LASLGASDSE
     IEKLSTVYWF TVEFGLCKEN HQLKAYGAAL LSSIGELLHA LSDKPELRPF EPASTSVQPY
     QDQEYQPIYY VAESFEDAKD KFRRWVSAMS RPFEVRFNPH TERVEVLDTV DKLETLIWQL
     NTEMLHLTNA VKKLKGTHFE
//
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