ID   STEA3_MOUSE             Reviewed;         488 AA.
AC   Q8CI59; Q3TKE4; Q80ZF3; Q8C5F0; Q924Z1;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   02-SEP-2026, entry version 155.
DE   RecName: Full=Metalloreductase STEAP3 {ECO:0000305|PubMed:16227996};
DE            EC=1.16.1.- {ECO:0000269|PubMed:16227996, ECO:0000269|PubMed:16609065, ECO:0000269|PubMed:18955558};
DE   AltName: Full=Dudulin-2;
DE   AltName: Full=Protein nm1054;
DE   AltName: Full=Six-transmembrane epithelial antigen of prostate 3;
DE   AltName: Full=Tumor suppressor-activated pathway protein 6;
GN   Name=Steap3 {ECO:0000312|MGI:MGI:1915678}; Synonyms=Tsap6;
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 2), AND TISSUE SPECIFICITY.
RX   PubMed=12606722; DOI=10.1073/pnas.0530298100;
RA   Passer B.J., Nancy-Portebois V., Amzallag N., Prieur S., Cans C.,
RA   Roborel de Climens A., Fiucci G., Bouvard V., Tuynder M., Susini L.,
RA   Morchoisne S., Crible V., Lespagnol A., Dausset J., Oren M., Amson R.,
RA   Telerman A.;
RT   "The p53-inducible TSAP6 gene product regulates apoptosis and the cell
RT   cycle and interacts with Nix and the Myt1 kinase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:2284-2289(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA   Serru V., Lamblin D., Lenoir C., Manivet P., Vaubourdolle M.,
RA   Kellermann O., Loric S.;
RL   Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Testis;
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=Czech II; TISSUE=Mammary tumor;
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   [5]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE,
RP   HEME-BINDING, COFACTOR, TISSUE SPECIFICITY, AND MUTAGENESIS OF HIS-316 AND
RP   HIS-409.
RX   PubMed=16227996; DOI=10.1038/ng1658;
RA   Ohgami R.S., Campagna D.R., Greer E.L., Antiochos B., McDonald A., Chen J.,
RA   Sharp J.J., Fujiwara Y., Barker J.E., Fleming M.D.;
RT   "Identification of a ferrireductase required for efficient transferrin-
RT   dependent iron uptake in erythroid cells.";
RL   Nat. Genet. 37:1264-1269(2005).
RN   [6]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=16609065; DOI=10.1182/blood-2006-02-003681;
RA   Ohgami R.S., Campagna D.R., McDonald A., Fleming M.D.;
RT   "The Steap proteins are metalloreductases.";
RL   Blood 108:1388-1394(2006).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [8]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND VARIANT FRAGILE-RED
RP   HIS-288.
RX   PubMed=18955558; DOI=10.1182/blood-2007-11-120402;
RA   Lambe T., Simpson R.J., Dawson S., Bouriez-Jones T., Crockford T.L.,
RA   Lepherd M., Latunde-Dada G.O., Robinson H., Raja K.B., Campagna D.R.,
RA   Villarreal G. Jr., Ellory J.C., Goodnow C.C., Fleming M.D., McKie A.T.,
RA   Cornall R.J.;
RT   "Identification of a Steap3 endosomal targeting motif essential for normal
RT   iron metabolism.";
RL   Blood 113:1805-1808(2009).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17 AND SER-20, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17 AND SER-20, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC   Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Integral membrane protein that functions as a NADPH-dependent
CC       ferric-chelate reductase, using NADPH from one side of the membrane to
CC       reduce a Fe(3+) chelate that is bound on the other side of the membrane
CC       (PubMed:16227996, PubMed:16609065, PubMed:18955558). Mediates
CC       sequential transmembrane electron transfer from NADPH to FAD and onto
CC       heme, and finally to the Fe(3+) chelate (By similarity). Can also
CC       reduce Cu(2+) to Cu(1+) (PubMed:16609065). Mediates efficient
CC       transferrin-dependent iron uptake in erythroid cells (PubMed:16227996).
CC       May play a role downstream of p53/TP53 to interface apoptosis and cell
CC       cycle progression (By similarity). Indirectly involved in exosome
CC       secretion by facilitating the secretion of proteins such as TCTP (By
CC       similarity). {ECO:0000250|UniProtKB:Q5RKL5,
CC       ECO:0000250|UniProtKB:Q658P3, ECO:0000250|UniProtKB:Q687X5,
CC       ECO:0000269|PubMed:16227996, ECO:0000269|PubMed:16609065,
CC       ECO:0000269|PubMed:18955558}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 Fe(2+) + NADP(+) + H(+) = 2 Fe(3+) + NADPH;
CC         Xref=Rhea:RHEA:71767, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033,
CC         ChEBI:CHEBI:29034, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC         Evidence={ECO:0000269|PubMed:16227996, ECO:0000269|PubMed:16609065,
CC         ECO:0000269|PubMed:18955558};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:71769;
CC         Evidence={ECO:0000305|PubMed:16609065};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 Cu(+) + NADP(+) + H(+) = 2 Cu(2+) + NADPH;
CC         Xref=Rhea:RHEA:71771, ChEBI:CHEBI:15378, ChEBI:CHEBI:29036,
CC         ChEBI:CHEBI:49552, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC         Evidence={ECO:0000269|PubMed:16609065};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:71773;
CC         Evidence={ECO:0000305|PubMed:16609065};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000250|UniProtKB:Q658P3};
CC   -!- COFACTOR:
CC       Name=heme b; Xref=ChEBI:CHEBI:60344;
CC         Evidence={ECO:0000250|UniProtKB:Q658P3};
CC   -!- SUBUNIT: Homodimer. Interacts with BNIP3L, MYT1, RHBDL4/RHBDD1 and TCTP
CC       (By similarity). {ECO:0000250|UniProtKB:Q658P3}.
CC   -!- SUBCELLULAR LOCATION: Endosome membrane {ECO:0000269|PubMed:16227996,
CC       ECO:0000269|PubMed:18955558}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8CI59-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8CI59-2; Sequence=VSP_024832;
CC   -!- TISSUE SPECIFICITY: Highly expressed in fetal liver (the site of
CC       midgestational hematopoiesis). {ECO:0000269|PubMed:12606722,
CC       ECO:0000269|PubMed:16227996}.
CC   -!- PTM: Proteolytically cleaved by RHBDL4/RHBDD1. RHBDL4/RHBDD1-induced
CC       cleavage occurs at multiple sites in a glycosylation-independent manner
CC       (By similarity). {ECO:0000250|UniProtKB:Q658P3}.
CC   -!- PTM: Glycosylated. {ECO:0000250|UniProtKB:Q658P3}.
CC   -!- DISEASE: Note=Defects in Steap3 are the cause of fragile-red phenotype
CC       characterized by hypochromic microcytic anemia.
CC       {ECO:0000269|PubMed:18955558}.
CC   -!- DISRUPTION PHENOTYPE: Mice display iron deficiency anemia, due to a
CC       defect in iron release through the transferrin cycle.
CC       {ECO:0000269|PubMed:16227996}.
CC   -!- SIMILARITY: Belongs to the STEAP family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK50539.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AY214462; AAO38239.1; -; mRNA.
DR   EMBL; AY029586; AAK50539.1; ALT_FRAME; mRNA.
DR   EMBL; AK078769; BAC37383.1; -; mRNA.
DR   EMBL; AK167028; BAE39201.1; -; mRNA.
DR   EMBL; AK171237; BAE42333.1; -; mRNA.
DR   EMBL; BC037435; AAH37435.1; -; mRNA.
DR   CCDS; CCDS48343.1; -. [Q8CI59-1]
DR   RefSeq; NP_001078878.1; NM_001085409.2.
DR   RefSeq; NP_573449.2; NM_133186.4.
DR   AlphaFoldDB; Q8CI59; -.
DR   SMR; Q8CI59; -.
DR   BioGRID; 212849; 4.
DR   FunCoup; Q8CI59; 386.
DR   IntAct; Q8CI59; 4.
DR   STRING; 10090.ENSMUSP00000108260; -.
DR   GlyCosmos; Q8CI59; 1 site, No reported glycans.
DR   GlyGen; Q8CI59; 1 site.
DR   iPTMnet; Q8CI59; -.
DR   PhosphoSitePlus; Q8CI59; -.
DR   SwissPalm; Q8CI59; -.
DR   jPOST; Q8CI59; -.
DR   PaxDb; 10090-ENSMUSP00000108260; -.
DR   PeptideAtlas; Q8CI59; -.
DR   ProteomicsDB; 257489; -. [Q8CI59-1]
DR   ProteomicsDB; 257490; -. [Q8CI59-2]
DR   Pumba; Q8CI59; -.
DR   GeneID; 68428; -.
DR   KEGG; mmu:68428; -.
DR   AGR; MGI:1915678; -.
DR   CTD; 55240; -.
DR   MGI; MGI:1915678; Steap3.
DR   eggNOG; ENOG502QRP3; Eukaryota.
DR   InParanoid; Q8CI59; -.
DR   OrthoDB; 550646at2759; -.
DR   PhylomeDB; Q8CI59; -.
DR   Reactome; R-MMU-6803204; TP53 Regulates Transcription of Genes Involved in Cytochrome C Release.
DR   Reactome; R-MMU-9013406; RHOQ GTPase cycle.
DR   Reactome; R-MMU-9035034; RHOF GTPase cycle.
DR   Reactome; R-MMU-917977; Transferrin endocytosis and recycling.
DR   BioGRID-ORCS; 68428; 1 hit in 77 CRISPR screens.
DR   PRO; PR:Q8CI59; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; Q8CI59; protein.
DR   GO; GO:0005737; C:cytoplasm; ISO:GO_Central.
DR   GO; GO:0005768; C:endosome; IDA:MGI.
DR   GO; GO:0010008; C:endosome membrane; IMP:UniProtKB.
DR   GO; GO:0005771; C:multivesicular body; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0008823; F:cupric reductase (NADH) activity; IDA:MGI.
DR   GO; GO:0071949; F:FAD binding; ISS:UniProtKB.
DR   GO; GO:0052851; F:ferric-chelate reductase (NADPH) activity; IDA:MGI.
DR   GO; GO:0000293; F:ferric-chelate reductase activity; IDA:MGI.
DR   GO; GO:0020037; F:heme binding; ISS:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; ISO:GO_Central.
DR   GO; GO:0015677; P:copper ion import; IDA:MGI.
DR   GO; GO:1990182; P:exosomal secretion; IMP:MGI.
DR   GO; GO:0033212; P:iron import into cell; IDA:MGI.
DR   GO; GO:0098711; P:iron ion import across plasma membrane; IDA:MGI.
DR   GO; GO:0006826; P:iron ion transport; IMP:MGI.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; ISO:GO_Central.
DR   GO; GO:1902167; P:positive regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; IMP:MGI.
DR   GO; GO:0009306; P:protein secretion; ISS:UniProtKB.
DR   FunFam; 3.40.50.720:FF:000051; STEAP2 metalloreductase; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR013130; Fe3_Rdtase_TM_dom.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR028939; P5C_Rdtase_cat_N.
DR   InterPro; IPR051267; STEAP_metalloreductase.
DR   PANTHER; PTHR14239; DUDULIN-RELATED; 1.
DR   PANTHER; PTHR14239:SF8; METALLOREDUCTASE STEAP3; 1.
DR   Pfam; PF03807; F420_oxidored; 1.
DR   Pfam; PF01794; Ferric_reduct; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Apoptosis; Cell cycle; Copper; Endosome; FAD;
KW   Flavoprotein; Glycoprotein; Heme; Ion transport; Iron; Iron transport;
KW   Membrane; Metal-binding; NADP; Oxidoreductase; Phosphoprotein;
KW   Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..488
FT                   /note="Metalloreductase STEAP3"
FT                   /id="PRO_0000285172"
FT   TOPO_DOM        1..207
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        208..228
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        229..258
FT                   /note="Vesicular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        259..279
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        280..304
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        305..325
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        326..358
FT                   /note="Vesicular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        359..379
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        380..390
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        391..411
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        412..433
FT                   /note="Vesicular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        434..454
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        455..488
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          259..407
FT                   /note="Ferric oxidoreductase"
FT   BINDING         36..39
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q658P3"
FT   BINDING         58..59
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q658P3"
FT   BINDING         91..98
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q658P3"
FT   BINDING         116
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q658P3"
FT   BINDING         151
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q658P3"
FT   BINDING         152
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q687X5"
FT   BINDING         160
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q687X5"
FT   BINDING         229
FT                   /ligand="Fe(3+)"
FT                   /ligand_id="ChEBI:CHEBI:29034"
FT                   /evidence="ECO:0000250|UniProtKB:Q658P3"
FT   BINDING         281
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q687X5"
FT   BINDING         302
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q658P3"
FT   BINDING         303
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q658P3"
FT   BINDING         316
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250|UniProtKB:Q687X5"
FT   BINDING         319
FT                   /ligand="Fe(3+)"
FT                   /ligand_id="ChEBI:CHEBI:29034"
FT                   /evidence="ECO:0000250|UniProtKB:Q658P3"
FT   BINDING         378
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q687X5"
FT   BINDING         395
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q687X5"
FT   BINDING         409
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250|UniProtKB:Q687X5"
FT   SITE            325..326
FT                   /note="Cleavage; by RHBDL4/RHBDD1"
FT                   /evidence="ECO:0000250|UniProtKB:Q658P3"
FT   MOD_RES         11
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q658P3"
FT   MOD_RES         17
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19144319,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         20
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT   MOD_RES         486
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q658P3"
FT   CARBOHYD        256
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         1
FT                   /note="M -> MAAEAHRQQGSCPTIPSEGCGKSPEKKGSAADSRPGTAM (in
FT                   isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:12606722"
FT                   /id="VSP_024832"
FT   VARIANT         288
FT                   /note="Y -> H (in fragile-red; loss of endosomal membrane
FT                   localization; 2-fold decrease in ferric-chelate reductase
FT                   activity)"
FT                   /evidence="ECO:0000269|PubMed:18955558"
FT   MUTAGEN         316
FT                   /note="H->L: Loss of ferric-chelate reductase activity."
FT                   /evidence="ECO:0000269|PubMed:16227996"
FT   MUTAGEN         409
FT                   /note="H->L: Loss of ferric-chelate reductase activity."
FT                   /evidence="ECO:0000269|PubMed:16227996"
FT   CONFLICT        81
FT                   /note="V -> M (in Ref. 3; BAC37383)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        157
FT                   /note="G -> V (in Ref. 2; AAK50539)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        169..172
FT                   /note="SDQP -> GNQQ (in Ref. 2; AAK50539)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        176..179
FT                   /note="RTIS -> QRVM (in Ref. 2; AAK50539)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        212
FT                   /note="W -> G (in Ref. 2; AAK50539)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        350
FT                   /note="V -> A (in Ref. 3; BAC37383/BAE39201)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        455
FT                   /note="S -> N (in Ref. 3; BAC37383/BAE39201)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   488 AA;  54749 MW;  9A08D99C90CF83F4 CRC64;
     MSGEMDKPLI SRRLVDSDGS LAEVPKEAPK VGILGSGDFA RSLATRLVGS GFSVVVGSRN
     PKRTAGLFPS LAQVTFQEEA VSSPEVIFVA VFREHYSSLC SLADQLAGKI LVDVSNPTEK
     EHLQHRQSNA EYLASLFPAC TVVKAFNVIS AWALQAGPRD GNRQVLICSD QPEAKRTISE
     MARAMGFTPL DMGSLASARE VEAIPLRLLP SWKVPTLLAL GLFVCFYTYN FIRDVLQPYI
     RKDENKFYKM PLSVVNTTLP CVAYVLLSLV YLPGVLAAAL QLRRGTKYQR FPDWLDHWLQ
     HRKQIGLLSF FFAMLHALYS FCLPLRRSHR YDLVNLAVKQ VLANKSRLWV EEEVWRMEIY
     LSLGVLALGM LSLLAVTSLP SIANSLNWKE FSFVQSTLGF VALILSTMHT LTYGWTRAFE
     ENHYKFYLPP TFTLTLLLPC VIILAKGLFL LPCLSRRLTK IRRGWEKDGA VKFMLPGDHT
     QGEKTSHV
//