CYBR1_MOUSE
ID CYBR1_MOUSE Reviewed; 290 AA.
AC Q925G2; A2AUU8; Q9D7U1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Plasma membrane ascorbate-dependent reductase CYBRD1 {ECO:0000250|UniProtKB:Q53TN4};
DE EC=7.2.1.3 {ECO:0000250|UniProtKB:Q53TN4};
DE AltName: Full=Cytochrome b reductase 1;
DE AltName: Full=Duodenal cytochrome b {ECO:0000303|PubMed:12547225};
GN Name=Cybrd1 {ECO:0000312|MGI:MGI:2654575};
GN Synonyms=Dcytb {ECO:0000303|PubMed:12547225};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=11230685; DOI=10.1126/science.1057206;
RA McKie A.T., Barrow D., Latunde-Dada G.O., Rolfs A., Sager G., Mudaly E.,
RA Mudaly M., Richardson C., Barlow D., Bomford A., Peters T.J., Raja K.B.,
RA Shirali S., Hediger M.A., Farzaneh F., Simpson R.J.;
RT "An iron-regulated ferric reductase associated with the absorption of
RT dietary iron.";
RL Science 291:1755-1759(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Skin, and Stomach;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=12547225; DOI=10.1006/bcmd.2002.0574;
RA Latunde-Dada G.O., Van der Westhuizen J., Vulpe C.D., Anderson G.J.,
RA Simpson R.J., McKie A.T.;
RT "Molecular and functional roles of duodenal cytochrome B (Dcytb) in iron
RT metabolism.";
RL Blood Cells Mol. Dis. 29:356-360(2002).
RN [5]
RP INDUCTION.
RX PubMed=12377801; DOI=10.1136/gut.51.5.648;
RA Dupic F., Fruchon S., Bensaid M., Loreal O., Brissot P., Borot N.,
RA Roth M.P., Coppin H.;
RT "Duodenal mRNA expression of iron related genes in response to iron loading
RT and iron deficiency in four strains of mice.";
RL Gut 51:648-653(2002).
RN [6]
RP INDUCTION.
RX PubMed=12704390; DOI=10.1038/ng1152;
RA Muckenthaler M., Roy C.N., Custodio A.O., Minana B., deGraaf J.,
RA Montross L.K., Andrews N.C., Hentze M.W.;
RT "Regulatory defects in liver and intestine implicate abnormal hepcidin and
RT Cybrd1 expression in mouse hemochromatosis.";
RL Nat. Genet. 34:102-107(2003).
RN [7]
RP DISRUPTION PHENOTYPE.
RX PubMed=15961514; DOI=10.1182/blood-2005-02-0716;
RA Gunshin H., Starr C.N., Direnzo C., Fleming M.D., Jin J., Greer E.L.,
RA Sellers V.M., Galica S.M., Andrews N.C.;
RT "Cybrd1 (duodenal cytochrome b) is not necessary for dietary iron
RT absorption in mice.";
RL Blood 106:2879-2883(2005).
RN [8]
RP COMMENT ON PUBMED:15961514.
RX PubMed=16326980; DOI=10.1182/blood-2005-07-2923;
RA Frazer D.M., Wilkins S.J., Vulpe C.D., Anderson G.J.;
RT "The role of duodenal cytochrome b in intestinal iron absorption remains
RT unclear.";
RL Blood 106:4413-4413(2005).
RN [9]
RP FUNCTION.
RX PubMed=17068337; DOI=10.1074/jbc.m606543200;
RA Su D., May J.M., Koury M.J., Asard H.;
RT "Human erythrocyte membranes contain a cytochrome b561 that may be involved
RT in extracellular ascorbate recycling.";
RL J. Biol. Chem. 281:39852-39859(2006).
RN [10]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=18498772; DOI=10.1016/j.febslet.2008.05.010;
RA Wyman S., Simpson R.J., McKie A.T., Sharp P.A.;
RT "Dcytb (Cybrd1) functions as both a ferric and a cupric reductase in
RT vitro.";
RL FEBS Lett. 582:1901-1906(2008).
CC -!- FUNCTION: Plasma membrane reductase that uses cytoplasmic ascorbate as
CC an electron donor to reduce extracellular Fe(3+) into Fe(2+)
CC (PubMed:17068337). Probably functions in dietary iron absorption at the
CC brush border of duodenal enterocytes by producing Fe(2+), the divalent
CC form of iron that can be transported into enterocytes (PubMed:11230685,
CC PubMed:12547225). It is also able to reduce extracellular monodehydro-
CC L-ascorbate and may be involved in extracellular ascorbate regeneration
CC by erythrocytes in blood (PubMed:17068337). May also act as a
CC ferrireductase in airway epithelial cells (By similarity). May also
CC function as a cupric transmembrane reductase (PubMed:18498772).
CC {ECO:0000250|UniProtKB:Q53TN4, ECO:0000269|PubMed:11230685,
CC ECO:0000269|PubMed:12547225, ECO:0000269|PubMed:17068337,
CC ECO:0000269|PubMed:18498772}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Fe(3+)(out) + L-ascorbate(in) = Fe(2+)(out) + H(+) +
CC monodehydro-L-ascorbate radical(in); Xref=Rhea:RHEA:30403,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034,
CC ChEBI:CHEBI:38290, ChEBI:CHEBI:59513; EC=7.2.1.3;
CC Evidence={ECO:0000250|UniProtKB:Q53TN4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30404;
CC Evidence={ECO:0000250|UniProtKB:Q53TN4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cu(2+)(out) + L-ascorbate(in) = Cu(+)(out) + H(+) +
CC monodehydro-L-ascorbate radical(in); Xref=Rhea:RHEA:66656,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29036, ChEBI:CHEBI:38290,
CC ChEBI:CHEBI:49552, ChEBI:CHEBI:59513;
CC Evidence={ECO:0000269|PubMed:18498772};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66657;
CC Evidence={ECO:0000269|PubMed:18498772};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-ascorbate(in) + monodehydro-L-ascorbate radical(out) = L-
CC ascorbate(out) + monodehydro-L-ascorbate radical(in);
CC Xref=Rhea:RHEA:66524, ChEBI:CHEBI:38290, ChEBI:CHEBI:59513;
CC Evidence={ECO:0000250|UniProtKB:Q53TN4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66525;
CC Evidence={ECO:0000250|UniProtKB:Q53TN4};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000250|UniProtKB:Q53TN4};
CC Note=Binds 2 heme b groups non-covalently.
CC {ECO:0000250|UniProtKB:Q53TN4};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q53TN4}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q53TN4};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:Q53TN4}. Apical cell
CC membrane {ECO:0000305|PubMed:11230685, ECO:0000305|PubMed:12547225};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:Q53TN4}.
CC Note=Localized at the brush border of duodenal cells.
CC {ECO:0000269|PubMed:11230685, ECO:0000269|PubMed:12547225}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q925G2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q925G2-2; Sequence=VSP_030396, VSP_030397;
CC -!- TISSUE SPECIFICITY: Highly expressed in the brush-border membrane of
CC duodenal enterocytes (at protein level). Also expressed in liver and
CC spleen. {ECO:0000269|PubMed:11230685, ECO:0000269|PubMed:12547225}.
CC -!- INDUCTION: By iron deficiency. Up-regulated in duodenal mucosa of mice
CC lacking transferrin or Hfe (at protein level).
CC {ECO:0000269|PubMed:11230685, ECO:0000269|PubMed:12377801,
CC ECO:0000269|PubMed:12547225, ECO:0000269|PubMed:12704390}.
CC -!- DISRUPTION PHENOTYPE: Mice are normal and do not display iron stores
CC defects, even in the setting of iron deficiency. These results,
CC reported by PubMed:15961514, suggest that Cybrd1 is not an essential
CC component of intestinal iron apparatus. However, according to
CC PubMed:16326980, no direct measurements of iron absorption were made by
CC PubMed:15961514, suggesting that final conclusions can be drawn only
CC when direct iron absorption studies are carried out or mice are
CC maintained on a diet containing ferric iron only.
CC {ECO:0000269|PubMed:15961514}.
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DR EMBL; AF354666; AAK50909.1; -; mRNA.
DR EMBL; AK008849; BAB25928.1; -; mRNA.
DR EMBL; AK029112; BAC26304.1; -; mRNA.
DR EMBL; AL929228; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS50603.1; -. [Q925G2-1]
DR RefSeq; NP_082869.2; NM_028593.2. [Q925G2-1]
DR AlphaFoldDB; Q925G2; -.
DR SMR; Q925G2; -.
DR STRING; 10090.ENSMUSP00000028403; -.
DR iPTMnet; Q925G2; -.
DR PhosphoSitePlus; Q925G2; -.
DR MaxQB; Q925G2; -.
DR PaxDb; Q925G2; -.
DR PRIDE; Q925G2; -.
DR ProteomicsDB; 283995; -. [Q925G2-1]
DR ProteomicsDB; 283996; -. [Q925G2-2]
DR Antibodypedia; 19375; 109 antibodies from 29 providers.
DR Ensembl; ENSMUST00000028403; ENSMUSP00000028403; ENSMUSG00000027015. [Q925G2-1]
DR GeneID; 73649; -.
DR KEGG; mmu:73649; -.
DR UCSC; uc008kaf.2; mouse. [Q925G2-1]
DR CTD; 79901; -.
DR MGI; MGI:2654575; Cybrd1.
DR VEuPathDB; HostDB:ENSMUSG00000027015; -.
DR eggNOG; KOG1619; Eukaryota.
DR GeneTree; ENSGT00950000183197; -.
DR HOGENOM; CLU_069712_1_2_1; -.
DR InParanoid; Q925G2; -.
DR OMA; SAEFNWH; -.
DR OrthoDB; 1503869at2759; -.
DR PhylomeDB; Q925G2; -.
DR TreeFam; TF314222; -.
DR Reactome; R-MMU-917937; Iron uptake and transport.
DR BioGRID-ORCS; 73649; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Cybrd1; mouse.
DR PRO; PR:Q925G2; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q925G2; protein.
DR Bgee; ENSMUSG00000027015; Expressed in epithelium of cochlear duct and 149 other tissues.
DR Genevisible; Q925G2; MM.
DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR GO; GO:0031526; C:brush border membrane; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR GO; GO:0005765; C:lysosomal membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0016722; F:oxidoreductase activity, acting on metal ions; ISO:MGI.
DR GO; GO:0140571; F:transmembrane ascorbate ferrireductase activity; IDA:UniProtKB.
DR GO; GO:0140575; F:transmembrane monodehydroascorbate reductase activity; ISS:UniProtKB.
DR GO; GO:0140576; P:ascorbate homeostasis; ISS:UniProtKB.
DR GO; GO:0006879; P:cellular iron ion homeostasis; ISO:MGI.
DR GO; GO:0055072; P:iron ion homeostasis; ISS:UniProtKB.
DR GO; GO:0010039; P:response to iron ion; IDA:MGI.
DR InterPro; IPR043205; CYB561/CYBRD1-like.
DR InterPro; IPR028838; CYBRD1.
DR InterPro; IPR006593; Cyt_b561/ferric_Rdtase_TM.
DR PANTHER; PTHR10106; PTHR10106; 1.
DR PANTHER; PTHR10106:SF12; PTHR10106:SF12; 1.
DR Pfam; PF03188; Cytochrom_B561; 1.
DR SMART; SM00665; B561; 1.
DR PROSITE; PS50939; CYTOCHROME_B561; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Electron transport; Heme; Iron;
KW Membrane; Metal-binding; Oxidoreductase; Phosphoprotein;
KW Reference proteome; Translocase; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..290
FT /note="Plasma membrane ascorbate-dependent reductase
FT CYBRD1"
FT /id="PRO_0000314831"
FT TOPO_DOM 1..7
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT TRANSMEM 8..32
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT TOPO_DOM 33..47
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT TRANSMEM 48..69
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT TOPO_DOM 70..78
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT TRANSMEM 79..105
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT TOPO_DOM 106..118
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT TRANSMEM 119..144
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT TOPO_DOM 145..151
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT TRANSMEM 152..179
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT TOPO_DOM 180..197
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT TRANSMEM 198..222
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT TOPO_DOM 223..290
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT DOMAIN 15..220
FT /note="Cytochrome b561"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00242"
FT REGION 257..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 50
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT BINDING 70
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT BINDING 79
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT BINDING 79
FT /ligand="L-ascorbate"
FT /ligand_id="ChEBI:CHEBI:38290"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT BINDING 83
FT /ligand="L-ascorbate"
FT /ligand_id="ChEBI:CHEBI:38290"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT BINDING 86
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT BINDING 108
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_note="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT BINDING 115..118
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT BINDING 120
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT BINDING 152
FT /ligand="L-ascorbate"
FT /ligand_id="ChEBI:CHEBI:38290"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT BINDING 159
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT BINDING 180
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT BINDING 225
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT MOD_RES 232
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT MOD_RES 289
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT VAR_SEQ 243..244
FT /note="EC -> D (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_030396"
FT VAR_SEQ 261..263
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_030397"
FT CONFLICT 188
FT /note="H -> R (in Ref. 1; AAK50909)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 290 AA; 31844 MW; F5098086F0EA937E CRC64;
MAMEGYRGFL GLLVSALLVG FLSVIFVLIW VLHFREGLGW NGSGLEFNWH PVLAVTGFVF
IQGIAIIVYR LPWTWKCSKL LMKSIHAGLN AVAAILAIIS VVAVFEYHNV QKVPHMYSLH
SWVGLTALIL YIQQLVVGFF VFLLPWAPPS LRAIVMPIHV YSGLLLFGTV IATVLMGVTE
KLFFVLKHPS YHSFPPEGVF TNTLGLLILV FGALIFWIVT RPQWKRPREP GSVPLQLNGG
NAECRMEGAI AISSAHSMDA ADPADAESSS EGAARKRTLG LADSGQRSTM
