ID C27C1_HUMAN Reviewed; 542 AA.
AC Q4G0S4; A0A590UJ17; Q6ZNI7;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2021, sequence version 3.
DT 27-MAR-2024, entry version 135.
DE RecName: Full=Cytochrome P450 27C1 {ECO:0000303|PubMed:28701464};
DE EC=1.14.19.53 {ECO:0000269|PubMed:27059013, ECO:0000269|PubMed:28701464};
DE AltName: Full=All-trans retinol 3,4-desaturase {ECO:0000303|PubMed:27059013};
DE Flags: Precursor;
GN Name=CYP27C1 {ECO:0000312|HGNC:HGNC:33480};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORMS 1 AND 2).
RX PubMed=11181995; DOI=10.1126/science.1058040;
RA Venter J.C., Adams M.D., Myers E.W., Li P.W., Mural R.J., Sutton G.G.,
RA Smith H.O., Yandell M., Evans C.A., Holt R.A., Gocayne J.D., Amanatides P.,
RA Ballew R.M., Huson D.H., Wortman J.R., Zhang Q., Kodira C.D., Zheng X.H.,
RA Chen L., Skupski M., Subramanian G., Thomas P.D., Zhang J.,
RA Gabor Miklos G.L., Nelson C., Broder S., Clark A.G., Nadeau J.,
RA McKusick V.A., Zinder N., Levine A.J., Roberts R.J., Simon M., Slayman C.,
RA Hunkapiller M., Bolanos R., Delcher A., Dew I., Fasulo D., Flanigan M.,
RA Florea L., Halpern A., Hannenhalli S., Kravitz S., Levy S., Mobarry C.,
RA Reinert K., Remington K., Abu-Threideh J., Beasley E., Biddick K.,
RA Bonazzi V., Brandon R., Cargill M., Chandramouliswaran I., Charlab R.,
RA Chaturvedi K., Deng Z., Di Francesco V., Dunn P., Eilbeck K.,
RA Evangelista C., Gabrielian A.E., Gan W., Ge W., Gong F., Gu Z., Guan P.,
RA Heiman T.J., Higgins M.E., Ji R.R., Ke Z., Ketchum K.A., Lai Z., Lei Y.,
RA Li Z., Li J., Liang Y., Lin X., Lu F., Merkulov G.V., Milshina N.,
RA Moore H.M., Naik A.K., Narayan V.A., Neelam B., Nusskern D., Rusch D.B.,
RA Salzberg S., Shao W., Shue B., Sun J., Wang Z., Wang A., Wang X., Wang J.,
RA Wei M., Wides R., Xiao C., Yan C., Yao A., Ye J., Zhan M., Zhang W.,
RA Zhang H., Zhao Q., Zheng L., Zhong F., Zhong W., Zhu S., Zhao S.,
RA Gilbert D., Baumhueter S., Spier G., Carter C., Cravchik A., Woodage T.,
RA Ali F., An H., Awe A., Baldwin D., Baden H., Barnstead M., Barrow I.,
RA Beeson K., Busam D., Carver A., Center A., Cheng M.L., Curry L.,
RA Danaher S., Davenport L., Desilets R., Dietz S., Dodson K., Doup L.,
RA Ferriera S., Garg N., Gluecksmann A., Hart B., Haynes J., Haynes C.,
RA Heiner C., Hladun S., Hostin D., Houck J., Howland T., Ibegwam C.,
RA Johnson J., Kalush F., Kline L., Koduru S., Love A., Mann F., May D.,
RA McCawley S., McIntosh T., McMullen I., Moy M., Moy L., Murphy B.,
RA Nelson K., Pfannkoch C., Pratts E., Puri V., Qureshi H., Reardon M.,
RA Rodriguez R., Rogers Y.H., Romblad D., Ruhfel B., Scott R., Sitter C.,
RA Smallwood M., Stewart E., Strong R., Suh E., Thomas R., Tint N.N., Tse S.,
RA Vech C., Wang G., Wetter J., Williams S., Williams M., Windsor S.,
RA Winn-Deen E., Wolfe K., Zaveri J., Zaveri K., Abril J.F., Guigo R.,
RA Campbell M.J., Sjolander K.V., Karlak B., Kejariwal A., Mi H., Lazareva B.,
RA Hatton T., Narechania A., Diemer K., Muruganujan A., Guo N., Sato S.,
RA Bafna V., Istrail S., Lippert R., Schwartz R., Walenz B., Yooseph S.,
RA Allen D., Basu A., Baxendale J., Blick L., Caminha M., Carnes-Stine J.,
RA Caulk P., Chiang Y.H., Coyne M., Dahlke C., Mays A., Dombroski M.,
RA Donnelly M., Ely D., Esparham S., Fosler C., Gire H., Glanowski S.,
RA Glasser K., Glodek A., Gorokhov M., Graham K., Gropman B., Harris M.,
RA Heil J., Henderson S., Hoover J., Jennings D., Jordan C., Jordan J.,
RA Kasha J., Kagan L., Kraft C., Levitsky A., Lewis M., Liu X., Lopez J.,
RA Ma D., Majoros W., McDaniel J., Murphy S., Newman M., Nguyen T., Nguyen N.,
RA Nodell M., Pan S., Peck J., Peterson M., Rowe W., Sanders R., Scott J.,
RA Simpson M., Smith T., Sprague A., Stockwell T., Turner R., Venter E.,
RA Wang M., Wen M., Wu D., Wu M., Xia A., Zandieh A., Zhu X.;
RT "The sequence of the human genome.";
RL Science 291:1304-1351(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORMS 1 AND 2).
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=12477932; DOI=10.1073/pnas.242603899;
RG Mammalian Gene Collection Program Team;
RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G., Klausner R.D.,
RA Collins F.S., Wagner L., Shenmen C.M., Schuler G.D., Altschul S.F.,
RA Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K., Hopkins R.F., Jordan H.,
RA Moore T., Max S.I., Wang J., Hsieh F., Diatchenko L., Marusina K.,
RA Farmer A.A., Rubin G.M., Hong L., Stapleton M., Soares M.B., Bonaldo M.F.,
RA Casavant T.L., Scheetz T.E., Brownstein M.J., Usdin T.B., Toshiyuki S.,
RA Carninci P., Prange C., Raha S.S., Loquellano N.A., Peters G.J.,
RA Abramson R.D., Mullahy S.J., Bosak S.A., McEwan P.J., McKernan K.J.,
RA Malek J.A., Gunaratne P.H., Richards S., Worley K.C., Hale S., Garcia A.M.,
RA Gay L.J., Hulyk S.W., Villalon D.K., Muzny D.M., Sodergren E.J., Lu X.,
RA Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S.,
RA Sanchez A., Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G.,
RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C., Rodriguez A.C.,
RA Grimwood J., Schmutz J., Myers R.M., Butterfield Y.S., Krzywinski M.I.,
RA Skalska U., Smailus D.E., Schnerch A., Schein J.E., Jones S.J., Marra M.A.;
RT "Generation and initial analysis of more than 15,000 full-length human and
RT mouse cDNA sequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
RN [5]
RP PARTIAL PROTEIN SEQUENCE (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY
RP (ISOFORM 2), AND TISSUE SPECIFICITY.
RX PubMed=16360114; DOI=10.1016/j.abb.2005.11.002;
RA Wu Z.L., Bartleson C.J., Ham A.J., Guengerich F.P.;
RT "Heterologous expression, purification, and properties of human cytochrome
RT P450 27C1.";
RL Arch. Biochem. Biophys. 445:138-146(2006).
RN [6]
RP FUNCTION (ISOFORM 2), CATALYTIC ACTIVITY (ISOFORM 2), BIOPHYSICOCHEMICAL
RP PROPERTIES (ISOFORM 2), AND PATHWAY (ISOFORM 2).
RX PubMed=27059013; DOI=10.1002/1873-3468.12167;
RA Kramlinger V.M., Nagy L.D., Fujiwara R., Johnson K.M., Phan T.T., Xiao Y.,
RA Enright J.M., Toomey M.B., Corbo J.C., Guengerich F.P.;
RT "Human cytochrome P450 27C1 catalyzes 3,4-desaturation of retinoids.";
RL FEBS Lett. 590:1304-1312(2016).
RN [7]
RP PROTEIN SEQUENCE OF 1-33; 79-89; 112-125; 157-170; 184-201; 208-225;
RP 267-276; 292-307; 310-317; 369-378; 388-397; 411-420; 473-486 AND 524-542,
RP IDENTIFICATION BY MASS SPECTROMETRY (ISOFORM 2), FUNCTION (ISOFORM 2),
RP CATALYTIC ACTIVITY (ISOFORM 2), TISSUE SPECIFICITY (ISOFORM 2), AND PATHWAY
RP (ISOFORM 2).
RX PubMed=28701464; DOI=10.1074/jbc.m116.773937;
RA Johnson K.M., Phan T.T.N., Albertolle M.E., Guengerich F.P.;
RT "Human mitochondrial cytochrome P450 27C1 is localized in skin and
RT preferentially desaturates trans-retinol to 3,4-dehydroretinol.";
RL J. Biol. Chem. 292:13672-13687(2017).
CC -!- FUNCTION: [Isoform 2]: A cytochrome P450 monooxygenase that catalyzes
CC the 3,4 desaturation of all-trans-retinol (also called vitamin A1) to
CC all-trans-3,4-didehydroretinol (also called vitamin A2) in the skin.
CC Desaturates with lower efficiency all-trans retinal and all-trans
CC retinoic acid. Forms minor amounts of 3-hydroxy and 4-hydroxy all-
CC trans-retinol derivatives. Mechanistically, uses molecular oxygen
CC inserting one oxygen atom into a substrate and reducing the second into
CC a water molecule. Two electrons are provided by NADPH via a two-protein
CC mitochondrial transfer system comprising flavoprotein FDXR
CC (adrenodoxin/ferredoxin reductase) and nonheme iron-sulfur protein FDX1
CC or FDX2 (adrenodoxin/ferredoxin). {ECO:0000269|PubMed:27059013,
CC ECO:0000269|PubMed:28701464}.
CC -!- CATALYTIC ACTIVITY: [Isoform 2]:
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:27059013, ECO:0000269|PubMed:28701464};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50293;
CC Evidence={ECO:0000305|PubMed:27059013, ECO:0000305|PubMed:28701464};
CC -!- CATALYTIC ACTIVITY: [Isoform 2]:
CC Reaction=all-trans-retinol + 2 H(+) + O2 + 2 reduced [adrenodoxin] =
CC all-trans-4-hydroxyretinol + H2O + 2 oxidized [adrenodoxin];
CC Xref=Rhea:RHEA:50300, 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:132259; Evidence={ECO:0000269|PubMed:27059013,
CC ECO:0000269|PubMed:28701464};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50301;
CC Evidence={ECO:0000305|PubMed:27059013, ECO:0000305|PubMed:28701464};
CC -!- CATALYTIC ACTIVITY: [Isoform 2]:
CC Reaction=all-trans-retinol + 2 H(+) + O2 + 2 reduced [adrenodoxin] =
CC all-trans-3-hydroxyretinol + H2O + 2 oxidized [adrenodoxin];
CC Xref=Rhea:RHEA:65520, 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:156530; Evidence={ECO:0000269|PubMed:28701464};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65521;
CC Evidence={ECO:0000305|PubMed:28701464};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P19099};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES: [Isoform 2]:
CC Kinetic parameters:
CC KM=0.5 uM for all-trans retinol {ECO:0000269|PubMed:27059013};
CC KM=0.35 uM for all-trans retinal {ECO:0000269|PubMed:27059013};
CC KM=0.87 uM for all-trans retinoic acid {ECO:0000269|PubMed:27059013};
CC -!- PATHWAY: [Isoform 2]: Cofactor metabolism; retinol metabolism.
CC {ECO:0000269|PubMed:27059013, ECO:0000269|PubMed:28701464}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Mitochondrion membrane
CC {ECO:0000250|UniProtKB:P14137}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P14137}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage; Named isoforms=2;
CC Name=2;
CC IsoId=Q4G0S4-2; Sequence=Displayed;
CC Name=1;
CC IsoId=Q4G0S4-1; Sequence=VSP_060866;
CC -!- TISSUE SPECIFICITY: Widely expressed, with highest levels in the liver,
CC kidney and pancreas. {ECO:0000269|PubMed:16360114}.
CC -!- TISSUE SPECIFICITY: [Isoform 2]: Expressed in the skin (at protein
CC level). {ECO:0000269|PubMed:28701464}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAW95310.1; Type=Erroneous initiation; Note=Extended 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/";
CC ---------------------------------------------------------------------------
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DR EMBL; AK131190; BAD18388.1; -; mRNA.
DR EMBL; CH471103; EAW95310.1; ALT_INIT; Genomic_DNA.
DR EMBL; AC110926; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC039307; AAH39307.1; -; mRNA.
DR CCDS; CCDS33285.1; -. [Q4G0S4-1]
DR RefSeq; NP_001001665.3; NM_001001665.3. [Q4G0S4-1]
DR AlphaFoldDB; Q4G0S4; -.
DR SMR; Q4G0S4; -.
DR BioGRID; 130927; 31.
DR IntAct; Q4G0S4; 2.
DR STRING; 9606.ENSP00000334128; -.
DR SwissLipids; SLP:000001617; -.
DR iPTMnet; Q4G0S4; -.
DR PhosphoSitePlus; Q4G0S4; -.
DR BioMuta; CYP27C1; -.
DR DMDM; 296434415; -.
DR EPD; Q4G0S4; -.
DR MassIVE; Q4G0S4; -.
DR PaxDb; 9606-ENSP00000334128; -.
DR PeptideAtlas; Q4G0S4; -.
DR ProteomicsDB; 62124; -.
DR Antibodypedia; 47562; 105 antibodies from 18 providers.
DR DNASU; 339761; -.
DR Ensembl; ENST00000335247.11; ENSP00000334128.7; ENSG00000186684.14. [Q4G0S4-1]
DR Ensembl; ENST00000409327.2; ENSP00000387198.1; ENSG00000186684.14. [Q4G0S4-1]
DR GeneID; 339761; -.
DR KEGG; hsa:339761; -.
DR UCSC; uc002tod.3; human. [Q4G0S4-2]
DR AGR; HGNC:33480; -.
DR CTD; 339761; -.
DR DisGeNET; 339761; -.
DR GeneCards; CYP27C1; -.
DR HGNC; HGNC:33480; CYP27C1.
DR HPA; ENSG00000186684; Tissue enhanced (cervix, skin).
DR MIM; 620605; gene.
DR neXtProt; NX_Q4G0S4; -.
DR OpenTargets; ENSG00000186684; -.
DR PharmGKB; PA162383091; -.
DR VEuPathDB; HostDB:ENSG00000186684; -.
DR eggNOG; KOG0159; Eukaryota.
DR GeneTree; ENSGT00950000182905; -.
DR HOGENOM; CLU_001570_28_3_1; -.
DR InParanoid; Q4G0S4; -.
DR OMA; ERTYFYQ; -.
DR OrthoDB; 2658719at2759; -.
DR PhylomeDB; Q4G0S4; -.
DR TreeFam; TF105094; -.
DR BRENDA; 1.14.19.53; 2681.
DR PathwayCommons; Q4G0S4; -.
DR SignaLink; Q4G0S4; -.
DR UniPathway; UPA00912; -.
DR BioGRID-ORCS; 339761; 7 hits in 1151 CRISPR screens.
DR ChiTaRS; CYP27C1; human.
DR GeneWiki; CYP27C1; -.
DR GenomeRNAi; 339761; -.
DR Pharos; Q4G0S4; Tbio.
DR PRO; PR:Q4G0S4; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q4G0S4; Protein.
DR Bgee; ENSG00000186684; Expressed in tendon of biceps brachii and 98 other cell types or tissues.
DR ExpressionAtlas; Q4G0S4; baseline and differential.
DR Genevisible; Q4G0S4; HS.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005502; F:11-cis retinal binding; IDA:UniProtKB.
DR GO; GO:0061899; F:11-cis-retinal 3,4-desaturase activity; IDA:UniProtKB.
DR GO; GO:0061897; F:all-trans retinal 3,4-desaturase activity; IDA:UniProtKB.
DR GO; GO:0005503; F:all-trans retinal binding; IDA:UniProtKB.
DR GO; GO:0061898; F:all-trans retinoic acid 3,4-desaturase activity; IDA:UniProtKB.
DR GO; GO:0061896; F:all-trans retinol 3,4-desaturase activity; IDA:UniProtKB.
DR GO; GO:1904768; F:all-trans-retinol binding; IDA:UniProtKB.
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; IDA:UniProtKB.
DR GO; GO:0042574; P:retinal metabolic process; IDA:UniProtKB.
DR GO; GO:0042573; P:retinoic acid metabolic process; IDA:UniProtKB.
DR GO; GO:0042572; P:retinol metabolic process; IDA:UniProtKB.
DR CDD; cd20647; CYP27C1; 1.
DR Gene3D; 1.10.630.10; Cytochrome P450; 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 PANTHER; PTHR24279; -; 1.
DR PANTHER; PTHR24279:SF119; CYTOCHROME P450 FAMILY 27 SUBFAMILY C MEMBER 1; 1.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; Cytochrome P450; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 1: Evidence at protein level;
KW Alternative promoter usage; Direct protein sequencing; Heme; Iron;
KW Lipid metabolism; Membrane; Metal-binding; Mitochondrion; Monooxygenase;
KW Oxidoreductase; Reference proteome; Transit peptide.
FT TRANSIT 1..80
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 81..542
FT /note="Cytochrome P450 27C1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000293732"
FT REGION 20..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 488
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:P19099"
FT VAR_SEQ 1..170
FT /note="Missing (in isoform 1)"
FT /id="VSP_060866"
FT VARIANT 529
FT /note="T -> M (in dbSNP:rs35075135)"
FT /id="VAR_033120"
FT CONFLICT 365
FT /note="L -> I (in Ref. 3; AAH39307)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 542 AA; 60920 MW; 71EE32EE3593C7AA CRC64;
MQTSAMALLA RILRAGLRPA PERGGLLGGG APRRPQPAGA RLPAGARAED KGAGRPGSPP
GGGRAEGPRS LAAMPGPRTL ANLAEFFCRD GFSRIHEIQQ KHTREYGKIF KSHFGPQFVV
SIADRDMVAQ VLRAEGAAPQ RANMESWREY RDLRGRATGL ISAEGEQWLK MRSVLRQRIL
KPKDVAIYSG EVNQVIADLI KRIYLLRSQA EDGETVTNVN DLFFKYSMEG VATILYESRL
GCLENSIPQL TVEYIEALEL MFSMFKTSMY AGAIPRWLRP FIPKPWREFC RSWDGLFKFS
QIHVDNKLRD IQYQMDRGRR VSGGLLTYLF LSQALTLQEI YANVTEMLLA GVDTTSFTLS
WTVYLLARHP EVQQTVYREI VKNLGERHVP TAADVPKVPL VRALLKETLR LFPVLPGNGR
VTQEDLVIGG YLIPKGTQLA LCHYATSYQD ENFPRAKEFR PERWLRKGDL DRVDNFGSIP
FGHGVRSCIG RRIAELEIHL VVIQLLQHFE IKTSSQTNAV HAKTHGLLTP GGPIHVRFVN
RK
//
