ID D5MRK5_PAPMA Unreviewed; 561 AA.
AC D5MRK5;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Tyrosine 3-monooxygenase {ECO:0000313|EMBL:KPJ09226.1};
DE SubName: Full=Tyrosine hydroxylase {ECO:0000313|EMBL:BAJ07587.1};
GN Name=TH {ECO:0000313|EMBL:BAJ07587.1};
GN ORFNames=RR48_15367 {ECO:0000313|EMBL:KPJ09226.1};
OS Papilio machaon (Old World swallowtail butterfly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC Papilionidae; Papilioninae; Papilio.
OX NCBI_TaxID=76193 {ECO:0000313|EMBL:BAJ07587.1};
RN [1] {ECO:0000313|EMBL:BAJ07587.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Epidermis {ECO:0000313|EMBL:BAJ07587.1};
RA Shirataki H., Futahashi R., Fujiwara H.;
RT "Species-specific coordinated gene expression and trans-regulation of
RT larval color pattern in three swallowtail butterflies.";
RL Evol. Dev. 12:305-314(2010).
RN [2] {ECO:0000313|EMBL:KPJ09226.1, ECO:0000313|Proteomes:UP000053240}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ya'a_city_454_Pm {ECO:0000313|EMBL:KPJ09226.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KPJ09226.1};
RX PubMed=26354079; DOI=10.1038/ncomms9212;
RA Li X., Fan D., Zhang W., Liu G., Zhang L., Zhao L., Fang X., Chen L.,
RA Dong Y., Chen Y., Ding Y., Zhao R., Feng M., Zhu Y., Feng Y., Jiang X.,
RA Zhu D., Xiang H., Feng X., Li S., Wang J., Zhang G., Kronforst M.R.,
RA Wang W.;
RT "Outbred genome sequencing and CRISPR/Cas9 gene editing in butterflies.";
RL Nat. Commun. 6:8212-8212(2015).
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; AB525737; BAJ07587.1; -; mRNA.
DR EMBL; KQ461108; KPJ09226.1; -; Genomic_DNA.
DR RefSeq; NP_001303944.1; NM_001317015.1.
DR STRING; 76193.D5MRK5; -.
DR GeneID; 106717258; -.
DR OMA; VRYNPHT; -.
DR OrthoDB; 275463at2759; -.
DR Proteomes; UP000053240; Unassembled WGS sequence.
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:InterPro.
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, ECO:0000313|EMBL:KPJ09226.1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000053240}.
FT DOMAIN 210..556
FT /note="Biopterin-dependent aromatic amino acid hydroxylase
FT family profile"
FT /evidence="ECO:0000259|PROSITE:PS51410"
FT REGION 53..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..88
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 89..108
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 389
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|PIRSR:PIRSR000336-1"
FT BINDING 394
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|PIRSR:PIRSR000336-1"
FT BINDING 434
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|PIRSR:PIRSR000336-1"
SQ SEQUENCE 561 AA; 63349 MW; 6648140DDC17D8C2 CRC64;
MAVAAAQKNR EMFAIKKSYS IENGYPSRRR SLVDDARFET LVVKQTKQSV LEEARARAND
SGLDSEFQDA ATHNGNDANT PTVEDGTQQD ETKNGHLADA DIGDDAGKAD EDYTLTEEEV
ILQNAASESP EAEQAIQQAA LLLRMRDGMG TLARILKTID NYKGCVEHLE TRPSQAAGVQ
FDALVKVSMS RINLLQLIRS LRQSTSFAGV DLMSDNNIST KTPWFPRHAS DLDNCNHLMT
KYEPELDMNH PGFADKEYRE RRKQIAEIAF AYKYGDQIPS ITYTESENAT WQRVFNTVLD
LMPKHACREY KAAFGKLQAA DIFVPHRIPQ LEDVSNFLRK HTGFTLRPAA GLLTARDFLA
SLAFRVFQST QYVRHANSPF HTPEPDCIHE LLGHIPLLAD PSFAQFSQEI GLASLGASDP
EIEKLSTVYW FTVEFGLCKE NQQLKAYGAA LLSSIGELLH ALSDKPELRA FEPASTSVQP
YQDQEYQPIY YVAESFEDAK EKFRRWVSTM SRPFEVRFNP HTERVEVLDS VDKLETLIWQ
LNTEMLHLTN AVKKLKGLHF E
//
