ID A0A3L8SLL5_CHLGU Unreviewed; 493 AA.
AC A0A3L8SLL5;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Cytochrome P450 26A1 {ECO:0000256|ARBA:ARBA00040248};
GN ORFNames=DV515_00005946 {ECO:0000313|EMBL:RLW04007.1};
OS Chloebia gouldiae (Gouldian finch) (Erythrura gouldiae).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Passeridae;
OC Chloebia.
OX NCBI_TaxID=44316 {ECO:0000313|EMBL:RLW04007.1, ECO:0000313|Proteomes:UP000276834};
RN [1] {ECO:0000313|EMBL:RLW04007.1, ECO:0000313|Proteomes:UP000276834}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Red01 {ECO:0000313|EMBL:RLW04007.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:RLW04007.1};
RX PubMed=30282656;
RA Toomey M.B., Marques C.I., Andrade P., Araujo P.M., Sabatino S.,
RA Gazda M.A., Afonso S., Lopes R.J., Corbo J.C., Carneiro M.;
RT "A non-coding region near Follistatin controls head colour polymorphism in
RT the Gouldian finch.";
RL Proc. R. Soc. B 285:0-0(2018).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=all-trans-retinoate + O2 + reduced [NADPH--hemoprotein
CC reductase] = all-trans-(4S)-hydroxyretinoate + H(+) + H2O + oxidized
CC [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:51492, Rhea:RHEA-
CC COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:35291,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:134185;
CC Evidence={ECO:0000256|ARBA:ARBA00036912};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51493;
CC Evidence={ECO:0000256|ARBA:ARBA00036912};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|PIRSR:PIRSR602403-1};
CC -!- SUBCELLULAR LOCATION: Microsome membrane
CC {ECO:0000256|ARBA:ARBA00004174}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004174}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC {ECO:0000256|ARBA:ARBA00010617, ECO:0000256|RuleBase:RU000461}.
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:RLW04007.1}.
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DR EMBL; QUSF01000014; RLW04007.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3L8SLL5; -.
DR STRING; 44316.ENSEGOP00005011120; -.
DR Ensembl; ENSEGOT00005012658; ENSEGOP00005011120; ENSEGOG00005008680.
DR OMA; KLWEVYM; -.
DR Proteomes; UP000276834; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR CDD; cd20638; CYP26A1; 1.
DR Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR002403; Cyt_P450_E_grp-IV.
DR InterPro; IPR036396; Cyt_P450_sf.
DR PANTHER; PTHR24286; CYTOCHROME P450 26; 1.
DR PANTHER; PTHR24286:SF194; CYTOCHROME P450 26A1; 1.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00465; EP450IV.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; Cytochrome P450; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 3: Inferred from homology;
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR602403-1};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR602403-1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR602403-1};
KW Monooxygenase {ECO:0000256|RuleBase:RU000461};
KW Oxidoreductase {ECO:0000256|RuleBase:RU000461};
KW Reference proteome {ECO:0000313|Proteomes:UP000276834}.
FT BINDING 438
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR602403-1"
SQ SEQUENCE 493 AA; 55383 MW; 46D3233A51C4FDC2 CRC64;
MGFSALVASA LCTFLLPLLL FLAAVKLWDL YCVSSRDPSC PLPLPPGTMG LPFFGETLQL
VLQRRKFLQM KRRKYGFIYK THLFGRPTVR VMGAENVRHI LLGEHRLVSV QWPASVRTIL
GSGCLSNLHN GQHKHRKKVI MRAFSRDALQ HYVPVIQEEV SACLARWLGA AGPCLLVYPE
VKRLMFRIAM RILLGFQPRQ ASPDGEQQLV EAFEEMIRNL FSLPIDVPFS GLYRGLRARN
IIHAKIEENI RAKMACKEPE GGYKDALQLL MEHTQGNGEQ LNMQELKESA TELLFGGHET
TASAATSLIA FLGLHHEVLQ KVRKELQVKG LLCSSNQEKQ LDMEVLEQLK YTGCVIKETL
RLSPPVPGGF RIALKTLELN GYQIPKGWNV IYSICDTHDV ADLFTNKEEF NPDRFMSPSP
EDSSRFSFIP FGGGLRSCVG KEFAKVLLKI FTVELARSCD WQLLNGPPTM KTGPIVYPVD
NLPTKFIGFS GQI
//
