ID   CP2CI_HUMAN             Reviewed;         490 AA.
AC   P33260; B2R8K2; Q16703; Q16751; Q4VAT5; Q6GRG1;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 3.
DT   27-MAR-2024, entry version 199.
DE   RecName: Full=Cytochrome P450 2C18;
DE            EC=1.14.14.1 {ECO:0000269|PubMed:11093772};
DE   AltName: Full=CYPIIC18;
DE   AltName: Full=Cytochrome P450-6b/29c;
DE   Flags: Precursor;
GN   Name=CYP2C18 {ECO:0000303|PubMed:11093772,
GN   ECO:0000312|HGNC:HGNC:2620};
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 [MRNA] (ISOFORM 1), AND VARIANT MET-385.
RC   TISSUE=Liver;
RX   PubMed=2009263; DOI=10.1021/bi00227a012;
RA   Romkes M., Faletto M.B., Blaisdell J.A., Raucy J.L., Goldstein J.A.;
RT   "Cloning and expression of complementary DNAs for multiple members of the
RT   human cytochrome P450IIC subfamily.";
RL   Biochemistry 30:3247-3255(1991).
RN   [2]
RP   ERRATUM OF PUBMED:2009263, AND SEQUENCE REVISION.
RX   PubMed=8095407; DOI=10.1021/bi00056a025;
RA   Romkes M., Faletto M.B., Blaisdell J.A., Raucy J.L., Goldstein J.A.;
RL   Biochemistry 32:1390-1390(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT MET-385.
RC   TISSUE=Liver;
RX   PubMed=8333835; DOI=10.1006/bbrc.1993.1803;
RA   de Morais S.M., Schweikl H., Blaisdell J., Goldstein J.A.;
RT   "Gene structure and upstream regulatory regions of human CYP2C9 and
RT   CYP2C18.";
RL   Biochem. Biophys. Res. Commun. 194:194-201(1993).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Stomach;
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15164054; DOI=10.1038/nature02462;
RA   Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA   Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA   Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA   Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA   Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA   Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA   Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA   Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA   Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA   Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA   Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA   Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA   Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA   McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA   Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA   Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA   Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA   Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA   Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA   Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA   Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA   Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT   "The DNA sequence and comparative analysis of human chromosome 10.";
RL   Nature 429:375-381(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [8]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP   LOCATION, AND PATHWAY.
RX   PubMed=11093772; DOI=10.1124/mol.58.6.1341;
RA   Marill J., Cresteil T., Lanotte M., Chabot G.G.;
RT   "Identification of human cytochrome P450s involved in the formation of all-
RT   trans-retinoic acid principal metabolites.";
RL   Mol. Pharmacol. 58:1341-1348(2000).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 72-80.
RX   PubMed=16963442; DOI=10.1074/jbc.m606755200;
RA   Archbold J.K., Macdonald W.A., Miles J.J., Brennan R.M., Kjer-Nielsen L.,
RA   McCluskey J., Burrows S.R., Rossjohn J.;
RT   "Alloreactivity between disparate cognate and allogeneic pMHC-I complexes
RT   is the result of highly focused, peptide-dependent structural mimicry.";
RL   J. Biol. Chem. 281:34324-34332(2006).
CC   -!- FUNCTION: A cytochrome P450 monooxygenase involved in retinoid
CC       metabolism. Hydroxylates all trans-retinoic acid (atRA) to 4-
CC       hydroxyretinoate and may modulate atRA signaling and clearance.
CC       Mechanistically, uses molecular oxygen inserting one oxygen atom into a
CC       substrate, and reducing the second into a water molecule, with two
CC       electrons provided by NADPH via cytochrome P450 reductase (CPR; NADPH-
CC       ferrihemoprotein reductase). {ECO:0000269|PubMed:11093772}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an organic molecule + O2 + reduced [NADPH--hemoprotein
CC         reductase] = an alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein
CC         reductase]; Xref=Rhea:RHEA:17149, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC         COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:30879, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC         ChEBI:CHEBI:142491; EC=1.14.14.1;
CC         Evidence={ECO:0000269|PubMed:11093772};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17150;
CC         Evidence={ECO:0000305|PubMed:11093772};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=all-trans-retinoate + O2 + reduced [NADPH--hemoprotein
CC         reductase] = all-trans-4-hydroxyretinoate + H(+) + H2O + oxidized
CC         [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:51984, 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:134178;
CC         Evidence={ECO:0000269|PubMed:11093772};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51985;
CC         Evidence={ECO:0000305|PubMed:11093772};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=16 uM for all-trans-retinoate {ECO:0000269|PubMed:11093772};
CC         Vmax=251 pmol/min/nmol enzyme toward all-trans-retinoate
CC         {ECO:0000269|PubMed:11093772};
CC   -!- PATHWAY: Cofactor metabolism; retinol metabolism.
CC       {ECO:0000269|PubMed:11093772}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:11093772}; Peripheral membrane protein. Microsome
CC       membrane {ECO:0000269|PubMed:11093772}; Peripheral membrane protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P33260-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P33260-2; Sequence=VSP_042520;
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; M61853; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; M61856; AAB59356.1; -; mRNA.
DR   EMBL; L16876; AAA02630.1; -; Genomic_DNA.
DR   EMBL; L16871; AAA02630.1; JOINED; Genomic_DNA.
DR   EMBL; L16872; AAA02630.1; JOINED; Genomic_DNA.
DR   EMBL; L16869; AAA02630.1; JOINED; Genomic_DNA.
DR   EMBL; L16870; AAA02630.1; JOINED; Genomic_DNA.
DR   EMBL; L16875; AAA02630.1; JOINED; Genomic_DNA.
DR   EMBL; L16873; AAA02630.1; JOINED; Genomic_DNA.
DR   EMBL; L16874; AAA02630.1; JOINED; Genomic_DNA.
DR   EMBL; AK313403; BAG36199.1; -; mRNA.
DR   EMBL; AL583836; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471066; EAW50024.1; -; Genomic_DNA.
DR   EMBL; BC069666; AAH69666.1; -; mRNA.
DR   EMBL; BC096257; AAH96257.1; -; mRNA.
DR   EMBL; BC096258; AAH96258.1; -; mRNA.
DR   EMBL; BC096260; AAH96260.1; -; mRNA.
DR   CCDS; CCDS44460.1; -. [P33260-2]
DR   CCDS; CCDS7435.1; -. [P33260-1]
DR   PIR; A61269; A61269.
DR   RefSeq; NP_000763.1; NM_000772.2. [P33260-1]
DR   RefSeq; NP_001122397.1; NM_001128925.1. [P33260-2]
DR   PDB; 2CIK; X-ray; 1.75 A; C=72-80.
DR   PDB; 2H6P; X-ray; 1.90 A; C=72-80.
DR   PDBsum; 2CIK; -.
DR   PDBsum; 2H6P; -.
DR   AlphaFoldDB; P33260; -.
DR   SMR; P33260; -.
DR   BioGRID; 107938; 30.
DR   IntAct; P33260; 6.
DR   STRING; 9606.ENSP00000285979; -.
DR   BindingDB; P33260; -.
DR   ChEMBL; CHEMBL2408; -.
DR   DrugBank; DB08496; (R)-warfarin.
DR   DrugBank; DB14055; (S)-Warfarin.
DR   DrugBank; DB01424; Aminophenazone.
DR   DrugBank; DB01435; Antipyrine.
DR   DrugBank; DB00921; Buprenorphine.
DR   DrugBank; DB00349; Clobazam.
DR   DrugBank; DB01559; Clotiazepam.
DR   DrugBank; DB00531; Cyclophosphamide.
DR   DrugBank; DB00250; Dapsone.
DR   DrugBank; DB00829; Diazepam.
DR   DrugBank; DB00586; Diclofenac.
DR   DrugBank; DB09166; Etizolam.
DR   DrugBank; DB00986; Glycopyrronium.
DR   DrugBank; DB01181; Ifosfamide.
DR   DrugBank; DB00458; Imipramine.
DR   DrugBank; DB11757; Istradefylline.
DR   DrugBank; DB00448; Lansoprazole.
DR   DrugBank; DB00333; Methadone.
DR   DrugBank; DB07670; N,4-Dimethyl-N-(1-phenyl-1H-pyrazol-5-yl)benzenesulfonamide.
DR   DrugBank; DB01183; Naloxone.
DR   DrugBank; DB00338; Omeprazole.
DR   DrugBank; DB00850; Perphenazine.
DR   DrugBank; DB01174; Phenobarbital.
DR   DrugBank; DB00252; Phenytoin.
DR   DrugBank; DB00818; Propofol.
DR   DrugBank; DB01124; Tolbutamide.
DR   DrugBank; DB00755; Tretinoin.
DR   DrugBank; DB00661; Verapamil.
DR   DrugBank; DB00682; Warfarin.
DR   GuidetoPHARMACOLOGY; 1327; -.
DR   SwissLipids; SLP:000001875; -.
DR   iPTMnet; P33260; -.
DR   PhosphoSitePlus; P33260; -.
DR   BioMuta; CYP2C18; -.
DR   DMDM; 67476954; -.
DR   MassIVE; P33260; -.
DR   PaxDb; 9606-ENSP00000285979; -.
DR   PeptideAtlas; P33260; -.
DR   ProteomicsDB; 54905; -. [P33260-1]
DR   ProteomicsDB; 54906; -. [P33260-2]
DR   Antibodypedia; 30592; 130 antibodies from 23 providers.
DR   DNASU; 1562; -.
DR   Ensembl; ENST00000285979.11; ENSP00000285979.6; ENSG00000108242.13. [P33260-1]
DR   Ensembl; ENST00000339022.6; ENSP00000341293.5; ENSG00000108242.13. [P33260-2]
DR   GeneID; 1562; -.
DR   KEGG; hsa:1562; -.
DR   MANE-Select; ENST00000285979.11; ENSP00000285979.6; NM_000772.3; NP_000763.1.
DR   UCSC; uc001kjv.6; human. [P33260-1]
DR   AGR; HGNC:2620; -.
DR   CTD; 1562; -.
DR   DisGeNET; 1562; -.
DR   GeneCards; CYP2C18; -.
DR   HGNC; HGNC:2620; CYP2C18.
DR   HPA; ENSG00000108242; Tissue enhanced (intestine, liver, stomach).
DR   MIM; 601131; gene.
DR   neXtProt; NX_P33260; -.
DR   OpenTargets; ENSG00000108242; -.
DR   PharmGKB; PA127; -.
DR   VEuPathDB; HostDB:ENSG00000108242; -.
DR   eggNOG; KOG0156; Eukaryota.
DR   GeneTree; ENSGT00940000162913; -.
DR   HOGENOM; CLU_001570_22_0_1; -.
DR   InParanoid; P33260; -.
DR   OMA; CWFNRVV; -.
DR   OrthoDB; 2900138at2759; -.
DR   PhylomeDB; P33260; -.
DR   TreeFam; TF352043; -.
DR   PathwayCommons; P33260; -.
DR   Reactome; R-HSA-211981; Xenobiotics.
DR   SABIO-RK; P33260; -.
DR   SignaLink; P33260; -.
DR   UniPathway; UPA00912; -.
DR   BioGRID-ORCS; 1562; 17 hits in 1145 CRISPR screens.
DR   ChiTaRS; CYP2C18; human.
DR   EvolutionaryTrace; P33260; -.
DR   GeneWiki; CYP2C18; -.
DR   GenomeRNAi; 1562; -.
DR   Pharos; P33260; Tchem.
DR   PRO; PR:P33260; -.
DR   Proteomes; UP000005640; Chromosome 10.
DR   RNAct; P33260; Protein.
DR   Bgee; ENSG00000108242; Expressed in jejunal mucosa and 81 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR   GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR   GO; GO:0008392; F:arachidonic acid epoxygenase activity; IBA:GO_Central.
DR   GO; GO:0070330; F:aromatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0020037; F:heme binding; IBA:GO_Central.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0071614; F:linoleic acid epoxygenase activity; IEA:Ensembl.
DR   GO; GO:0004497; F:monooxygenase activity; TAS:Reactome.
DR   GO; GO:0016712; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen; IBA:GO_Central.
DR   GO; GO:0019825; F:oxygen binding; TAS:ProtInc.
DR   GO; GO:0008401; F:retinoic acid 4-hydroxylase activity; IDA:UniProtKB.
DR   GO; GO:0019373; P:epoxygenase P450 pathway; IBA:GO_Central.
DR   GO; GO:0043651; P:linoleic acid metabolic process; IEA:Ensembl.
DR   GO; GO:0042573; P:retinoic acid metabolic process; IDA:UniProtKB.
DR   GO; GO:0042572; P:retinol metabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006805; P:xenobiotic metabolic process; IBA:GO_Central.
DR   CDD; cd20665; CYP2C-like; 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; PTHR24300:SF374; CYTOCHROME P450 2C18; 1.
DR   PANTHER; PTHR24300; CYTOCHROME P450 508A4-RELATED; 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.
DR   Genevisible; P33260; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Endoplasmic reticulum; Heme; Iron;
KW   Lipid metabolism; Membrane; Metal-binding; Microsome; Monooxygenase;
KW   Oxidoreductase; Reference proteome; Signal.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..490
FT                   /note="Cytochrome P450 2C18"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000051707"
FT   BINDING         435
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"
FT   VAR_SEQ         214..272
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_042520"
FT   VARIANT         385
FT                   /note="T -> M (in dbSNP:rs1126545)"
FT                   /evidence="ECO:0000269|PubMed:2009263,
FT                   ECO:0000269|PubMed:8333835"
FT                   /id="VAR_001254"
SQ   SEQUENCE   490 AA;  55711 MW;  C933CF31F078FD1E CRC64;
     MDPAVALVLC LSCLFLLSLW RQSSGRGRLP SGPTPLPIIG NILQLDVKDM SKSLTNFSKV
     YGPVFTVYFG LKPIVVLHGY EAVKEALIDH GEEFSGRGSF PVAEKVNKGL GILFSNGKRW
     KEIRRFCLMT LRNFGMGKRS IEDRVQEEAR CLVEELRKTN ASPCDPTFIL GCAPCNVICS
     VIFHDRFDYK DQRFLNLMEK FNENLRILSS PWIQVCNNFP ALIDYLPGSH NKIAENFAYI
     KSYVLERIKE HQESLDMNSA RDFIDCFLIK MEQEKHNQQS EFTVESLIAT VTDMFGAGTE
     TTSTTLRYGL LLLLKYPEVT AKVQEEIECV VGRNRSPCMQ DRSHMPYTDA VVHEIQRYID
     LLPTNLPHAV TCDVKFKNYL IPKGTTIITS LTSVLHNDKE FPNPEMFDPG HFLDKSGNFK
     KSDYFMPFSA GKRMCMGEGL ARMELFLFLT TILQNFNLKS QVDPKDIDIT PIANAFGRVP
     PLYQLCFIPV
//