ID   C56D2_HUMAN             Reviewed;         222 AA.
AC   O14569; A8K552;
DT   10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   27-MAR-2024, entry version 152.
DE   RecName: Full=Transmembrane reductase CYB561D2 {ECO:0000305|PubMed:23235316, ECO:0000305|PubMed:23641721};
DE            EC=7.2.1.3 {ECO:0000269|PubMed:23235316, ECO:0000269|PubMed:23641721};
DE   AltName: Full=Cytochrome b561 domain-containing protein 2 {ECO:0000312|HGNC:HGNC:30253};
DE   AltName: Full=Putative tumor suppressor protein 101F6 {ECO:0000303|PubMed:19734123};
GN   Name=CYB561D2 {ECO:0000312|HGNC:HGNC:30253};
GN   Synonyms=101F6 {ECO:0000303|PubMed:19734123}; ORFNames=LUCA12.2;
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].
RA   Bader S., Lee C.-C., Latif F., Sekido Y., Duh F.-M., Wei M.-H., Cundiff S.,
RA   Lerman M.I., Minna J.D.;
RT   "A new candidate tumor suppressor gene located in the 3p21.3 small cell
RT   lung cancer homozygous deletion region.";
RL   Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16641997; DOI=10.1038/nature04728;
RA   Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA   Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA   Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA   Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA   Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA   Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA   Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA   Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA   Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA   Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA   Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA   Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA   Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA   Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA   Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA   Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA   Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA   Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA   Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT   "The DNA sequence, annotation and analysis of human chromosome 3.";
RL   Nature 440:1194-1198(2006).
RN   [4]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Pancreas;
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   [6]
RP   PROTEIN SEQUENCE [LARGE SCALE ANALYSIS] OF 2-14.
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19892738; DOI=10.1073/pnas.0908958106;
RA   Xu G., Shin S.B., Jaffrey S.R.;
RT   "Global profiling of protease cleavage sites by chemoselective labeling of
RT   protein N-termini.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:19310-19315(2009).
RN   [7]
RP   DISCUSSION OF SEQUENCE.
RX   PubMed=11085536;
RG   The international lung cancer chromosome 3p21.3 tumor suppressor gene consortium;
RA   Lerman M.I., Minna J.D.;
RT   "The 630-kb lung cancer homozygous deletion region on human chromosome
RT   3p21.3: identification and evaluation of the resident candidate tumor
RT   suppressor genes.";
RL   Cancer Res. 60:6116-6133(2000).
RN   [8]
RP   COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=19734123; DOI=10.3233/bio-2009-1075;
RA   Recuenco M.C., Fujito M., Rahman M.M., Sakamoto Y., Takeuchi F.,
RA   Tsubaki M.;
RT   "Functional expression and characterization of human 101F6 protein, a
RT   homologue of cytochrome b561 and a candidate tumor suppressor gene
RT   product.";
RL   BioFactors 34:219-230(2009).
RN   [9]
RP   FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=23641721; DOI=10.1021/bi301607s;
RA   Recuenco M.C., Rahman M.M., Takeuchi F., Kobayashi K., Tsubaki M.;
RT   "Electron transfer reactions of candidate tumor suppressor 101F6 protein, a
RT   cytochrome b561 homologue, with ascorbate and monodehydroascorbate
RT   radical.";
RL   Biochemistry 52:3660-3668(2013).
RN   [10]
RP   FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=23235316; DOI=10.1093/jb/mvs139;
RA   Recuenco M.C., Rahman M.M., Sakamoto Y., Takeuchi F., Hori H., Tsubaki M.;
RT   "Functional characterization of the recombinant human tumour suppressor
RT   101F6 protein, a cytochrome b(561) homologue.";
RL   J. Biochem. 153:233-242(2013).
CC   -!- FUNCTION: Transmembrane reductase that may use ascorbate as an electron
CC       donor in the cytoplasm and transfer electrons across endoplasmic
CC       reticulum membranes to reduce monodehydro-L-ascorbate radical and iron
CC       cations Fe(3+) in the lumen of that compartment.
CC       {ECO:0000269|PubMed:23235316, ECO:0000269|PubMed:23641721}.
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:0000269|PubMed:23235316, ECO:0000269|PubMed:23641721};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66525;
CC         Evidence={ECO:0000305|PubMed:23641721};
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:Q9WUE3};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30404;
CC         Evidence={ECO:0000250|UniProtKB:Q9WUE3};
CC   -!- COFACTOR:
CC       Name=heme b; Xref=ChEBI:CHEBI:60344;
CC         Evidence={ECO:0000269|PubMed:19734123, ECO:0000269|PubMed:23235316,
CC         ECO:0000269|PubMed:23641721};
CC       Note=Binds 2 heme b groups non-covalently.
CC       {ECO:0000269|PubMed:23235316, ECO:0000269|PubMed:23641721};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 6-7 for the electron donation reaction to
CC         monodehydroascorbate reaction (PubMed:23641721). Optimum pH is around
CC         6.5 for re-reduction reaction process of the oxidized heme with
CC         ascorbate (PubMed:23641721). {ECO:0000269|PubMed:23641721};
CC       Redox potential:
CC         E(0) is +89.5 mV for the high potential heme and +13.1 mV for the low
CC         potential heme (PubMed:19734123). E(0) is +109 mV for the high
CC         potential heme and +26 mV for the low potential heme
CC         (PubMed:23235316). {ECO:0000269|PubMed:19734123,
CC         ECO:0000269|PubMed:23235316};
CC   -!- INTERACTION:
CC       O14569; Q3SXY8: ARL13B; NbExp=3; IntAct=EBI-717654, EBI-11343438;
CC       O14569; P11912: CD79A; NbExp=3; IntAct=EBI-717654, EBI-7797864;
CC       O14569; O95471: CLDN7; NbExp=3; IntAct=EBI-717654, EBI-740744;
CC       O14569; Q86T13: CLEC14A; NbExp=3; IntAct=EBI-717654, EBI-17710733;
CC       O14569; O75208: COQ9; NbExp=3; IntAct=EBI-717654, EBI-724524;
CC       O14569; Q96BA8: CREB3L1; NbExp=3; IntAct=EBI-717654, EBI-6942903;
CC       O14569; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-717654, EBI-781551;
CC       O14569; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-717654, EBI-18304435;
CC       O14569; Q8TED1: GPX8; NbExp=3; IntAct=EBI-717654, EBI-11721746;
CC       O14569; P27815-4: PDE4A; NbExp=3; IntAct=EBI-717654, EBI-12080840;
CC       O14569; O15173: PGRMC2; NbExp=3; IntAct=EBI-717654, EBI-1050125;
CC       O14569; P54829: PTPN5; NbExp=3; IntAct=EBI-717654, EBI-1220572;
CC       O14569; Q96TC7: RMDN3; NbExp=3; IntAct=EBI-717654, EBI-1056589;
CC       O14569; P54219-3: SLC18A1; NbExp=3; IntAct=EBI-717654, EBI-17595455;
CC       O14569; Q9BRI3: SLC30A2; NbExp=3; IntAct=EBI-717654, EBI-8644112;
CC       O14569; Q6P9G4: TMEM154; NbExp=3; IntAct=EBI-717654, EBI-13329239;
CC       O14569; Q96B21: TMEM45B; NbExp=3; IntAct=EBI-717654, EBI-3923061;
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:Q9WUE3}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:Q53TN4}. Cytoplasmic vesicle membrane
CC       {ECO:0000250|UniProtKB:Q9WUE3}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:Q53TN4}.
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DR   EMBL; AF040704; AAC70911.1; -; mRNA.
DR   EMBL; AK291167; BAF83856.1; -; mRNA.
DR   EMBL; AC002481; AAB67309.1; -; Genomic_DNA.
DR   EMBL; CH471055; EAW65113.1; -; Genomic_DNA.
DR   EMBL; BC047691; AAH47691.1; -; mRNA.
DR   CCDS; CCDS2827.1; -.
DR   RefSeq; NP_001278213.1; NM_001291284.1.
DR   RefSeq; NP_008953.1; NM_007022.4.
DR   AlphaFoldDB; O14569; -.
DR   SMR; O14569; -.
DR   BioGRID; 116252; 27.
DR   IntAct; O14569; 19.
DR   STRING; 9606.ENSP00000391209; -.
DR   iPTMnet; O14569; -.
DR   PhosphoSitePlus; O14569; -.
DR   BioMuta; CYB561D2; -.
DR   EPD; O14569; -.
DR   jPOST; O14569; -.
DR   MassIVE; O14569; -.
DR   MaxQB; O14569; -.
DR   PaxDb; 9606-ENSP00000391209; -.
DR   PeptideAtlas; O14569; -.
DR   ProteomicsDB; 48090; -.
DR   Pumba; O14569; -.
DR   Antibodypedia; 30954; 167 antibodies from 28 providers.
DR   DNASU; 11068; -.
DR   Ensembl; ENST00000232508.9; ENSP00000232508.5; ENSG00000114395.11.
DR   Ensembl; ENST00000418577.1; ENSP00000391209.1; ENSG00000114395.11.
DR   Ensembl; ENST00000424512.5; ENSP00000410663.1; ENSG00000114395.11.
DR   Ensembl; ENST00000425346.6; ENSP00000400454.1; ENSG00000114395.11.
DR   GeneID; 11068; -.
DR   KEGG; hsa:11068; -.
DR   MANE-Select; ENST00000425346.6; ENSP00000400454.1; NM_001291284.2; NP_001278213.1.
DR   UCSC; uc003dal.4; human.
DR   AGR; HGNC:30253; -.
DR   CTD; 11068; -.
DR   DisGeNET; 11068; -.
DR   GeneCards; CYB561D2; -.
DR   HGNC; HGNC:30253; CYB561D2.
DR   HPA; ENSG00000114395; Low tissue specificity.
DR   MalaCards; CYB561D2; -.
DR   MIM; 607068; gene.
DR   neXtProt; NX_O14569; -.
DR   OpenTargets; ENSG00000114395; -.
DR   PharmGKB; PA134977950; -.
DR   VEuPathDB; HostDB:ENSG00000114395; -.
DR   eggNOG; ENOG502QRPJ; Eukaryota.
DR   GeneTree; ENSGT00440000038072; -.
DR   HOGENOM; CLU_072399_3_0_1; -.
DR   InParanoid; O14569; -.
DR   OMA; TSWFSWH; -.
DR   OrthoDB; 51140at2759; -.
DR   PhylomeDB; O14569; -.
DR   TreeFam; TF323584; -.
DR   PathwayCommons; O14569; -.
DR   SignaLink; O14569; -.
DR   BioGRID-ORCS; 11068; 18 hits in 1152 CRISPR screens.
DR   ChiTaRS; CYB561D2; human.
DR   GenomeRNAi; 11068; -.
DR   Pharos; O14569; Tbio.
DR   PRO; PR:O14569; -.
DR   Proteomes; UP000005640; Chromosome 3.
DR   RNAct; O14569; Protein.
DR   Bgee; ENSG00000114395; Expressed in granulocyte and 150 other cell types or tissues.
DR   ExpressionAtlas; O14569; baseline and differential.
DR   GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0031982; C:vesicle; ISS:UniProtKB.
DR   GO; GO:0020037; F:heme binding; IDA: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:0140571; F:transmembrane ascorbate ferrireductase activity; ISS:UniProtKB.
DR   GO; GO:0140575; F:transmembrane monodehydroascorbate reductase activity; IDA:UniProtKB.
DR   GO; GO:0140576; P:ascorbate homeostasis; IDA:UniProtKB.
DR   CDD; cd08761; Cyt_b561_CYB561D2_like; 1.
DR   Gene3D; 1.20.120.1770; -; 1.
DR   InterPro; IPR045150; CYB561D1/2.
DR   InterPro; IPR006593; Cyt_b561/ferric_Rdtase_TM.
DR   PANTHER; PTHR15422; OS05G0565100 PROTEIN; 1.
DR   PANTHER; PTHR15422:SF21; TRANSMEMBRANE REDUCTASE CYB561D2; 1.
DR   Pfam; PF03188; Cytochrom_B561; 1.
DR   SMART; SM00665; B561; 1.
DR   PROSITE; PS50939; CYTOCHROME_B561; 1.
DR   Genevisible; O14569; HS.
PE   1: Evidence at protein level;
KW   Cytoplasmic vesicle; Direct protein sequencing; Electron transport;
KW   Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding;
KW   Reference proteome; Translocase; Transmembrane; Transmembrane helix;
KW   Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:19892738"
FT   CHAIN           2..222
FT                   /note="Transmembrane reductase CYB561D2"
FT                   /id="PRO_0000151036"
FT   TOPO_DOM        2..17
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT   TRANSMEM        18..38
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        39..46
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT   TRANSMEM        47..67
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        68..85
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT   TRANSMEM        86..106
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        107..122
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT   TRANSMEM        123..143
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        144..162
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT   TRANSMEM        163..183
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        184..186
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT   TRANSMEM        187..207
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        208..222
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT   DOMAIN          14..217
FT                   /note="Cytochrome b561"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00242"
FT   BINDING         48
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         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         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         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"
SQ   SEQUENCE   222 AA;  23974 MW;  3AEEE64D8CB91A32 CRC64;
     MALSAETESH IYRALRTASG AAAHLVALGF TIFVAVLARP GSSLFSWHPV LMSLAFSFLM
     TEALLVFSPE SSLLHSLSRK GRARCHWVLQ LLALLCALLG LGLVILHKEQ LGKAHLVTRH
     GQAGLLAVLW AGLQCSGGVG LLYPKLLPRW PLAKLKLYHA TSGLVGYLLG SASLLLGMCS
     LWFTASVTGA AWYLAVLCPV LTSLVIMNQV SNAYLYRKRI QP
//