C27C1_LITCT
ID C27C1_LITCT Reviewed; 537 AA.
AC P0DOX0;
DT 15-FEB-2017, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2017, sequence version 1.
DT 03-AUG-2022, entry version 17.
DE RecName: Full=Cytochrome P450 27C1;
DE EC=1.14.19.53 {ECO:0000250|UniProtKB:A8WGA0};
DE AltName: Full=All-trans retinol 3,4-desaturase {ECO:0000250|UniProtKB:Q4G0S4};
GN Name=cyp27c1;
OS Lithobates catesbeianus (American bullfrog) (Rana catesbeiana).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Lithobates.
OX NCBI_TaxID=8400;
RN [1]
RP PRELIMINARY NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
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:0000250|UniProtKB:A8WGA0}.
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:0000250|UniProtKB:A8WGA0};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in the dorsal third of retinal pigment
CC epithelium, but not in the ventral counterpart (at protein level).
CC {ECO:0000269|PubMed:26549260}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {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 AlphaFoldDB; P0DOX0; -.
DR SMR; P0DOX0; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0061896; F:all-trans retinol 3,4-desaturase activity; IEA:RHEA.
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: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.
FT CHAIN 1..537
FT /note="Cytochrome P450 27C1"
FT /id="PRO_0000438913"
FT BINDING 483
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 537 AA; 61621 MW; D8712BA2CD2CCF12 CRC64;
MLWQCWLQQA QRMRMMMKAL LRFRATRLDS EMMGGWRRGA QRLAAGVVEG QRTLPQEGAA
AGPRNLKEMP GPSTFRNLLE FFWRDGFSRI HEIQQNHIRE YGRIFKSHFG PQFVVSIADR
DMVAQILRAE RDAPQRANME SWQEYRDLRG RSTGLISAEG KKWLAMRSVL RQKILRPRDV
FIYAGGVNEV VSDLIKRIKT LRSREDDGET VTNVNDLYFK YSMEAVATIL YECRLGCLQN
EVPKQTLEYI EALELMFSMF KTTMYAGAIP KWLRPFIPKP WEEFCRSWDG LFRFSQIHVD
GRLREIQACL DRGEEVKGGL LTSILISKEL TLEELYANMT EMLLAGVDTT SFTLSWATYL
LAKNPQAQQM VYDQIVQNLG KDTVPTAEDV PKLPLIRAVL KETLRLFPVL PGNGRVTQDD
LVLGGYLIPK GTQLALCHYS TSYDQEYFTA AEDFQPGRWL RHGHLDRVEN FGSIPFGYGI
RSCIGKRVAE LEIHLALIQL LQNFEIRTSP KTQTVLPKTH GLLCPAGAIN VRFVNRE
