C27C1_DANRE
ID C27C1_DANRE Reviewed; 540 AA.
AC A8WGA0; F1QMI2;
DT 15-FEB-2017, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2017, sequence version 2.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Cytochrome P450 27C1;
DE EC=1.14.19.53 {ECO:0000269|PubMed:26549260};
DE AltName: Full=All-trans retinol 3,4-desaturase {ECO:0000250|UniProtKB:Q4G0S4};
GN Name=cyp27c1;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (NOV-2008) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION BY
RP L-THYROXINE, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=26549260; DOI=10.1016/j.cub.2015.10.018;
RA Enright J.M., Toomey M.B., Sato S.Y., Temple S.E., Allen J.R., Fujiwara R.,
RA Kramlinger V.M., Nagy L.D., Johnson K.M., Xiao Y., How M.J., Johnson S.L.,
RA Roberts N.W., Kefalov V.J., Guengerich F.P., Corbo J.C.;
RT "Cyp27c1 Red-Shifts the Spectral Sensitivity of Photoreceptors by
RT Converting Vitamin A1 into A2.";
RL Curr. Biol. 25:3048-3057(2015).
CC -!- FUNCTION: Efficiently catalyzes the conversion of all-trans retinol
CC (also called vitamin A1, the precursor of 11-cis retinal) to 3,4-
CC didehydroretinol (also called vitamin A2, the precursor of 11-cis 3,4-
CC didehydroretinal). Also acts on all-trans retinal and all-trans
CC retinoic acid. The replacement of 11-cis retinal chromophore in
CC photopigments with 11-cis 3,4-didehydroretinal enhances sensitivity to
CC long-wavelength light. This may improve vision in fresh water which is
CC often turbid. {ECO:0000269|PubMed:26549260}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=all-trans-retinol + 2 H(+) + O2 + 2 reduced [adrenodoxin] =
CC all-trans-3,4-didehydroretinol + 2 H2O + 2 oxidized [adrenodoxin];
CC Xref=Rhea:RHEA:50292, Rhea:RHEA-COMP:9998, Rhea:RHEA-COMP:9999,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:17336, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738,
CC ChEBI:CHEBI:132246; EC=1.14.19.53;
CC Evidence={ECO:0000269|PubMed:26549260};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.0 uM for all-trans retinol {ECO:0000269|PubMed:26549260};
CC KM=0.48 uM for retinal {ECO:0000269|PubMed:26549260};
CC KM=0.34 uM for retinoic acid {ECO:0000269|PubMed:26549260};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Following L-thyroxine, expressed in the retinal
CC pigment epithelium (at protein level). {ECO:0000269|PubMed:26549260}.
CC -!- INDUCTION: In the retinal pigment epithelium, up-regulated by L-
CC thyroxine (at protein level). {ECO:0000269|PubMed:26549260}.
CC -!- DISRUPTION PHENOTYPE: Mutant fish survive to adulthood without overt
CC developmental abnormalities. Upon treatment with L-thyroxine, the
CC mutant fish eyes fail to produce any vitamin A2 and their
CC photoreceptors fail to undergo a red-shift in sensitivity.
CC {ECO:0000269|PubMed:26549260}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI54633.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAI71576.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAI71578.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Seeing through the murk
CC - Issue 192 of June 2017;
CC URL="https://web.expasy.org/spotlight/back_issues/192/";
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DR EMBL; BX927387; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC154632; AAI54633.1; ALT_INIT; mRNA.
DR EMBL; BC171576; AAI71576.1; ALT_INIT; mRNA.
DR EMBL; BC171578; AAI71578.1; ALT_INIT; mRNA.
DR RefSeq; NP_001106808.2; NM_001113337.2.
DR AlphaFoldDB; A8WGA0; -.
DR SMR; A8WGA0; -.
DR STRING; 7955.ENSDARP00000118349; -.
DR PeptideAtlas; A8WGA0; -.
DR Ensembl; ENSDART00000144335; ENSDARP00000118349; ENSDARG00000092660.
DR GeneID; 558396; -.
DR KEGG; dre:558396; -.
DR CTD; 339761; -.
DR ZFIN; ZDB-GENE-080204-68; cyp27c1.
DR eggNOG; KOG0159; Eukaryota.
DR GeneTree; ENSGT00950000182905; -.
DR OMA; QRANMGS; -.
DR OrthoDB; 481145at2759; -.
DR PhylomeDB; A8WGA0; -.
DR TreeFam; TF105094; -.
DR BRENDA; 1.14.19.53; 928.
DR PRO; PR:A8WGA0; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 6.
DR Bgee; ENSDARG00000092660; Expressed in gastrula and 20 other tissues.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0061897; F:all-trans retinal 3,4-desaturase activity; IBA:GO_Central.
DR GO; GO:0061898; F:all-trans retinoic acid 3,4-desaturase activity; IBA:GO_Central.
DR GO; GO:0061896; F:all-trans retinol 3,4-desaturase activity; IBA:GO_Central.
DR GO; GO:1904768; F:all-trans-retinol binding; IBA:GO_Central.
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:0001972; F:retinoic acid binding; IBA:GO_Central.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR002401; Cyt_P450_E_grp-I.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; SSF48264; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 1: Evidence at protein level;
KW Heme; Iron; Lipid metabolism; Membrane; Metal-binding; Monooxygenase;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..540
FT /note="Cytochrome P450 27C1"
FT /id="PRO_0000438858"
FT BINDING 486
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:0000250|UniProtKB:P04798"
SQ SEQUENCE 540 AA; 61492 MW; A73A0790A0BE7BDC CRC64;
MALQSTILHM ARKNLLQESC RQLLIQTHGL HKSVASGSLE IAAHSQADLK EESAVSPAEE
VQKAARVKSL KEMPGPSTVA NLLEFFYRDG FSRIHEIQME HAKKYGKIFK SRFGPQFVVS
IADRDMVAQV LRSESATPQR GNMESWKEYR DLRGRSTGLI SAEGDEWLKM RSVLRQLIMR
PRDVAVFSSD VNDVVADLVK RVKTLRSQQD DSQTVLNIND LFFKYAMEGV ATILYETRLG
CLENEIPKMS QEYITALHLM FSSFKTTMYA GAIPKWLRPI IPKPWEEFCS SWDGLFKFSQ
IHVDKRLSEI KKQMEKSEEI KGGLLTHMLV TREMNLEEIY ANMTEMLLAG VDTTSFTLSW
STYLLARHPT IQQQIFEEVD RVLGGRVPTG EDVPYLPLIR GLVKETLRLF PVLPGNGRVT
HDDLIVGGYL IPKGTQLALC HYSTSMDEEN FPRPEEFRPD RWIRKDASDR VDNFGSIPFG
YGIRSCIGRR IAELEMHLAL TQLLQNFHIE VSPQTTEVHA KTHGLLCPGA SINLRFTDRK
