ID   CYAC3_HUMAN             Reviewed;         242 AA.
AC   Q8NBI2; B3KPU2; B4DLN9; J3KQH4; Q6PK96;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   27-MAR-2024, entry version 163.
DE   RecName: Full=Lysosomal membrane ascorbate-dependent ferrireductase CYB561A3 {ECO:0000305};
DE            EC=7.2.1.3 {ECO:0000250|UniProtKB:Q6P1H1};
DE   AltName: Full=Cytochrome b ascorbate-dependent protein 3 {ECO:0000312|HGNC:HGNC:23014};
DE   AltName: Full=Cytochrome b561 family member A3 {ECO:0000312|HGNC:HGNC:23014};
DE   AltName: Full=Lysosomal cytochrome b {ECO:0000250|UniProtKB:Q6P1H1};
DE            Short=LCytb {ECO:0000250|UniProtKB:Q6P1H1};
GN   Name=CYB561A3 {ECO:0000312|HGNC:HGNC:23014};
GN   Synonyms=CYBASC3 {ECO:0000312|HGNC:HGNC:23014}; ORFNames=PSEC0259;
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] (ISOFORMS 1 AND 2).
RC   TISSUE=Blood, and Placenta;
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 MRNA] (ISOFORM 1).
RX   PubMed=16303743; DOI=10.1093/dnares/12.2.117;
RA   Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
RA   Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
RA   Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
RA   Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
RA   Isogai T.;
RT   "Signal sequence and keyword trap in silico for selection of full-length
RT   human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA
RT   libraries.";
RL   DNA Res. 12:117-126(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16554811; DOI=10.1038/nature04632;
RA   Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA   Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA   Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA   Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA   Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA   Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT   "Human chromosome 11 DNA sequence and analysis including novel gene
RT   identification.";
RL   Nature 440:497-500(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] (ISOFORM 1).
RC   TISSUE=Brain, Lymph, and 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   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC   TISSUE=Placenta;
RX   PubMed=17897319; DOI=10.1111/j.1600-0854.2007.00643.x;
RA   Schroeder B., Wrocklage C., Pan C., Jaeger R., Koesters B., Schaefer H.,
RA   Elsaesser H.-P., Mann M., Hasilik A.;
RT   "Integral and associated lysosomal membrane proteins.";
RL   Traffic 8:1676-1686(2007).
CC   -!- FUNCTION: Transmembrane reductase that uses ascorbate as an electron
CC       donor in the cytoplasm and transfers electrons across membranes to
CC       reduce iron cations Fe(3+) into Fe(2+) in the lumen of the late
CC       endosome and lysosome. Reduced iron can then be extruded from the late
CC       endosome and lysosome to the cytoplasm by divalent metal-specific
CC       transporters. It is therefore most probably involved in endosomal and
CC       lysosomal cellular iron homeostasis. {ECO:0000250|UniProtKB:Q6P1H1}.
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:Q6P1H1};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30404;
CC         Evidence={ECO:0000250|UniProtKB:Q6P1H1};
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   -!- INTERACTION:
CC       Q8NBI2; Q9NUQ2: AGPAT5; NbExp=3; IntAct=EBI-10269179, EBI-6916385;
CC       Q8NBI2; Q13520: AQP6; NbExp=3; IntAct=EBI-10269179, EBI-13059134;
CC       Q8NBI2; P25942: CD40; NbExp=3; IntAct=EBI-10269179, EBI-525714;
CC       Q8NBI2; P11912: CD79A; NbExp=3; IntAct=EBI-10269179, EBI-7797864;
CC       Q8NBI2; O00501: CLDN5; NbExp=3; IntAct=EBI-10269179, EBI-18400628;
CC       Q8NBI2; O95471: CLDN7; NbExp=3; IntAct=EBI-10269179, EBI-740744;
CC       Q8NBI2; Q68CJ9: CREB3L3; NbExp=3; IntAct=EBI-10269179, EBI-852194;
CC       Q8NBI2; Q08426: EHHADH; NbExp=3; IntAct=EBI-10269179, EBI-2339219;
CC       Q8NBI2; O15552: FFAR2; NbExp=3; IntAct=EBI-10269179, EBI-2833872;
CC       Q8NBI2; Q96P66: GPR101; NbExp=3; IntAct=EBI-10269179, EBI-17935713;
CC       Q8NBI2; Q8TDT2: GPR152; NbExp=3; IntAct=EBI-10269179, EBI-13345167;
CC       Q8NBI2; O60883: GPR37L1; NbExp=3; IntAct=EBI-10269179, EBI-2927498;
CC       Q8NBI2; Q8TED1: GPX8; NbExp=3; IntAct=EBI-10269179, EBI-11721746;
CC       Q8NBI2; Q9BSE4: HERPUD2; NbExp=3; IntAct=EBI-10269179, EBI-2868124;
CC       Q8NBI2; P26715: KLRC1; NbExp=3; IntAct=EBI-10269179, EBI-9018187;
CC       Q8NBI2; Q86VI4: LAPTM4B; NbExp=3; IntAct=EBI-10269179, EBI-3267258;
CC       Q8NBI2; P15151: PVR; NbExp=3; IntAct=EBI-10269179, EBI-3919694;
CC       Q8NBI2; Q96GF1: RNF185; NbExp=3; IntAct=EBI-10269179, EBI-2340249;
CC       Q8NBI2; Q99942: RNF5; NbExp=6; IntAct=EBI-10269179, EBI-348482;
CC       Q8NBI2; Q3SXP7: SHISAL1; NbExp=3; IntAct=EBI-10269179, EBI-18037857;
CC       Q8NBI2; Q96CE8: TM4SF18; NbExp=3; IntAct=EBI-10269179, EBI-13351685;
CC   -!- SUBCELLULAR LOCATION: Late endosome membrane
CC       {ECO:0000250|UniProtKB:Q6P1H1}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:Q53TN4}. Lysosome membrane
CC       {ECO:0000269|PubMed:17897319}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:Q53TN4}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8NBI2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8NBI2-2; Sequence=VSP_047358;
CC   -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q6P1H1}.
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DR   EMBL; AK056751; BAG51804.1; -; mRNA.
DR   EMBL; AK075559; BAC11698.1; -; mRNA.
DR   EMBL; AK297084; BAG59601.1; -; mRNA.
DR   EMBL; AP003108; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471076; EAW73941.1; -; Genomic_DNA.
DR   EMBL; CH471076; EAW73942.1; -; Genomic_DNA.
DR   EMBL; BC004391; AAH04391.1; -; mRNA.
DR   EMBL; BC014045; AAH14045.2; -; mRNA.
DR   EMBL; BC047710; AAH47710.1; -; mRNA.
DR   CCDS; CCDS53639.1; -. [Q8NBI2-2]
DR   CCDS; CCDS8004.1; -. [Q8NBI2-1]
DR   RefSeq; NP_001154924.1; NM_001161452.1. [Q8NBI2-1]
DR   RefSeq; NP_001154926.1; NM_001161454.1. [Q8NBI2-2]
DR   RefSeq; NP_001287692.1; NM_001300763.1.
DR   RefSeq; NP_705839.3; NM_153611.4. [Q8NBI2-1]
DR   AlphaFoldDB; Q8NBI2; -.
DR   SMR; Q8NBI2; -.
DR   BioGRID; 128617; 24.
DR   IntAct; Q8NBI2; 21.
DR   STRING; 9606.ENSP00000389745; -.
DR   GlyCosmos; Q8NBI2; 1 site, No reported glycans.
DR   GlyGen; Q8NBI2; 1 site.
DR   BioMuta; CYB561A3; -.
DR   DMDM; 74730147; -.
DR   jPOST; Q8NBI2; -.
DR   MassIVE; Q8NBI2; -.
DR   MaxQB; Q8NBI2; -.
DR   PaxDb; 9606-ENSP00000389745; -.
DR   PeptideAtlas; Q8NBI2; -.
DR   ProteomicsDB; 72770; -. [Q8NBI2-1]
DR   Antibodypedia; 52925; 9 antibodies from 7 providers.
DR   DNASU; 220002; -.
DR   Ensembl; ENST00000294072.9; ENSP00000294072.4; ENSG00000162144.10. [Q8NBI2-1]
DR   Ensembl; ENST00000426130.6; ENSP00000398979.2; ENSG00000162144.10. [Q8NBI2-2]
DR   Ensembl; ENST00000536915.5; ENSP00000437390.1; ENSG00000162144.10. [Q8NBI2-1]
DR   GeneID; 220002; -.
DR   KEGG; hsa:220002; -.
DR   MANE-Select; ENST00000294072.9; ENSP00000294072.4; NM_153611.6; NP_705839.3.
DR   UCSC; uc001nrg.4; human. [Q8NBI2-1]
DR   AGR; HGNC:23014; -.
DR   CTD; 220002; -.
DR   GeneCards; CYB561A3; -.
DR   HGNC; HGNC:23014; CYB561A3.
DR   HPA; ENSG00000162144; Tissue enhanced (adrenal).
DR   MIM; 618757; gene.
DR   neXtProt; NX_Q8NBI2; -.
DR   OpenTargets; ENSG00000162144; -.
DR   PharmGKB; PA134880796; -.
DR   VEuPathDB; HostDB:ENSG00000162144; -.
DR   eggNOG; KOG1619; Eukaryota.
DR   GeneTree; ENSGT00950000183197; -.
DR   InParanoid; Q8NBI2; -.
DR   OMA; FKFHDMV; -.
DR   OrthoDB; 2877457at2759; -.
DR   PhylomeDB; Q8NBI2; -.
DR   TreeFam; TF314222; -.
DR   PathwayCommons; Q8NBI2; -.
DR   SignaLink; Q8NBI2; -.
DR   BioGRID-ORCS; 220002; 23 hits in 1157 CRISPR screens.
DR   ChiTaRS; CYB561A3; human.
DR   GenomeRNAi; 220002; -.
DR   Pharos; Q8NBI2; Tdark.
DR   PRO; PR:Q8NBI2; -.
DR   Proteomes; UP000005640; Chromosome 11.
DR   RNAct; Q8NBI2; Protein.
DR   Bgee; ENSG00000162144; Expressed in right adrenal gland and 176 other cell types or tissues.
DR   ExpressionAtlas; Q8NBI2; baseline and differential.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR   GO; GO:0031902; C:late endosome membrane; ISS:UniProtKB.
DR   GO; GO:0005765; C:lysosomal membrane; HDA:UniProtKB.
DR   GO; GO:0005730; C:nucleolus; IDA:HPA.
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:0006879; P:intracellular iron ion homeostasis; ISS:UniProtKB.
DR   CDD; cd08762; Cyt_b561_CYBASC3; 1.
DR   Gene3D; 1.20.120.1770; -; 1.
DR   InterPro; IPR043205; CYB561/CYBRD1-like.
DR   InterPro; IPR006593; Cyt_b561/ferric_Rdtase_TM.
DR   PANTHER; PTHR10106; CYTOCHROME B561-RELATED; 1.
DR   PANTHER; PTHR10106:SF0; LYSOSOMAL MEMBRANE ASCORBATE-DEPENDENT FERRIREDUCTASE CYB561A3; 1.
DR   Pfam; PF03188; Cytochrom_B561; 1.
DR   SMART; SM00665; B561; 1.
DR   PROSITE; PS50939; CYTOCHROME_B561; 1.
DR   Genevisible; Q8NBI2; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Electron transport; Endosome; Glycoprotein; Heme;
KW   Iron; Lysosome; Membrane; Metal-binding; Oxidoreductase;
KW   Reference proteome; Translocase; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..242
FT                   /note="Lysosomal membrane ascorbate-dependent
FT                   ferrireductase CYB561A3"
FT                   /id="PRO_0000314838"
FT   TOPO_DOM        1..7
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT   TRANSMEM        8..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        29..45
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT   TRANSMEM        46..66
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        67..83
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT   TRANSMEM        84..104
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        105..119
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT   TRANSMEM        120..140
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        141..154
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT   TRANSMEM        155..175
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        176..202
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT   TRANSMEM        203..223
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        224..242
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT   DOMAIN          12..219
FT                   /note="Cytochrome b561"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00242"
FT   BINDING         47
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         67
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT   BINDING         76
FT                   /ligand="L-ascorbate"
FT                   /ligand_id="ChEBI:CHEBI:38290"
FT                   /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT   BINDING         80
FT                   /ligand="L-ascorbate"
FT                   /ligand_id="ChEBI:CHEBI:38290"
FT                   /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT   BINDING         83
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         112..115
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT   BINDING         117
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         149
FT                   /ligand="L-ascorbate"
FT                   /ligand_id="ChEBI:CHEBI:38290"
FT                   /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT   BINDING         156
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         177
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT   BINDING         224
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q53TN4"
FT   CARBOHYD        38
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         1
FT                   /note="M -> MGKNFSDSFLSRECVIRM (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_047358"
FT   CONFLICT        122
FT                   /note="I -> T (in Ref. 5; AAH04391)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        168
FT                   /note="I -> N (in Ref. 1; BAG59601)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   242 AA;  27214 MW;  1D0C4904CEAED747 CRC64;
     MVSGRFYLSC LLLGSLGSMC ILFTIYWMQY WRGGFAWNGS IYMFNWHPVL MVAGMVVFYG
     GASLVYRLPQ SWVGPKLPWK LLHAALHLMA FVLTVVGLVA VFTFHNHGRT ANLYSLHSWL
     GITTVFLFAC QWFLGFAVFL LPWASMWLRS LLKPIHVFFG AAILSLSIAS VISGINEKLF
     FSLKNTTRPY HSLPSEAVFA NSTGMLVVAF GLLVLYILLA SSWKRPEPGI LTDRQPLLHD
     GE
//