ID   S40A1_MOUSE             Reviewed;         570 AA.
AC   Q9JHI9; Q3UHZ9; Q8BME5; Q8BUM5; Q9JIM9; Q9JKP4;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   27-MAR-2024, entry version 162.
DE   RecName: Full=Solute carrier family 40 member 1;
DE   AltName: Full=Ferroportin-1;
DE   AltName: Full=Iron-regulated transporter 1;
DE   AltName: Full=Metal transporter protein 1;
DE            Short=MTP1;
GN   Name=Slc40a1; Synonyms=Fpn1, Ireg1, Slc11a3, Slc39a1;
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 [GENOMIC DNA / MRNA].
RX   PubMed=10747949; DOI=10.1074/jbc.m000713200;
RA   Abboud S., Haile D.J.;
RT   "A novel mammalian iron-regulated protein involved in intracellular iron
RT   metabolism.";
RL   J. Biol. Chem. 275:19906-19912(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RC   TISSUE=Liver;
RX   PubMed=10693807; DOI=10.1038/35001596;
RA   Donovan A., Brownlie A., Zhou Y., Shepard J., Pratt S.J., Moynihan J.,
RA   Paw B.H., Drejer A., Barut B., Zapata A., Law T.C., Brugnara C.,
RA   Lux S.E. IV, Pinkus G.S., Pinkus J.L., Kingsley P.D., Palis J.,
RA   Fleming M.D., Andrews N.C., Zon L.I.;
RT   "Positional cloning of zebrafish ferroportin1 identifies a conserved
RT   vertebrate iron exporter.";
RL   Nature 403:776-781(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=10882071; DOI=10.1016/s1097-2765(00)80425-6;
RA   McKie A.T., Marciani P., Rolfs A., Brennan K., Wehr K., Barrow D.,
RA   Miret S., Bomford A., Peters T.J., Farzaneh F., Hediger M.A., Hentze M.W.,
RA   Simpson R.J.;
RT   "A novel duodenal iron-regulated transporter, IREG1, implicated in the
RT   basolateral transfer of iron to the circulation.";
RL   Mol. Cell 5:299-309(2000).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo, Liver, Lung, 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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   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   [6]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND TRANSPORTER ACTIVITY.
RX   PubMed=16054062; DOI=10.1016/j.cmet.2005.01.003;
RA   Donovan A., Lima C.A., Pinkus J.L., Pinkus G.S., Zon L.I., Robine S.,
RA   Andrews N.C.;
RT   "The iron exporter ferroportin/Slc40a1 is essential for iron homeostasis.";
RL   Cell Metab. 1:191-200(2005).
RN   [7]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND TRANSPORTER ACTIVITY.
RX   PubMed=30213870; DOI=10.1182/blood-2018-04-842997;
RA   Zhang D.L., Ghosh M.C., Ollivierre H., Li Y., Rouault T.A.;
RT   "Ferroportin deficiency in erythroid cells causes serum iron deficiency and
RT   promotes hemolysis due to oxidative stress.";
RL   Blood 132:2078-2087(2018).
RN   [8]
RP   FUNCTION, AND TRANSPORTER ACTIVITY.
RX   PubMed=29599243; DOI=10.1126/science.aal2022;
RA   Zhang D.L., Wu J., Shah B.N., Greutelaers K.C., Ghosh M.C., Ollivierre H.,
RA   Su X.Z., Thuma P.E., Bedu-Addo G., Mockenhaupt F.P., Gordeuk V.R.,
RA   Rouault T.A.;
RT   "Erythrocytic ferroportin reduces intracellular iron accumulation,
RT   hemolysis, and malaria risk.";
RL   Science 359:1520-1523(2018).
RN   [9]
RP   FUNCTION, AND CAUTION.
RX   PubMed=30888356; DOI=10.1039/c8mt00370j;
RA   Jin L., Frazer D.M., Lu Y., Wilkins S.J., Ayton S., Bush A., Anderson G.J.;
RT   "Mice overexpressing hepcidin suggest ferroportin does not play a major
RT   role in Mn homeostasis.";
RL   Metallomics 11:959-967(2019).
RN   [10]
RP   UBIQUITINATION BY RNF217.
RX   PubMed=33895792; DOI=10.1182/blood.2020008986;
RA   Jiang L., Wang J., Wang K., Wang H., Wu Q., Yang C., Yu Y., Ni P.,
RA   Zhong Y., Song Z., Xie E., Hu R., Min J., Wang F.;
RT   "RNF217 regulates iron homeostasis through its E3 ubiquitin ligase activity
RT   by modulating ferroportin degradation.";
RL   Blood 138:689-705(2021).
CC   -!- FUNCTION: Transports Fe(2+) from the inside of a cell to the outside of
CC       the cell, playing a key role for maintaining systemic iron homeostasis
CC       (PubMed:16054062, PubMed:30213870). Transports iron from intestinal,
CC       splenic, hepatic cells, macrophages and erythrocytes into the blood to
CC       provide iron to other tissues. Controls therefore dietary iron uptake,
CC       iron recycling by macrophages and erythrocytes, and release of iron
CC       stores in hepatocytes (PubMed:16054062, PubMed:30213870). When iron is
CC       in excess in serum, circulating HAMP/hepcidin levels increase resulting
CC       in a degradation of SLC40A1, thus limiting the iron efflux to plasma
CC       (By similarity). {ECO:0000250|UniProtKB:Q9NP59,
CC       ECO:0000269|PubMed:16054062, ECO:0000269|PubMed:30213870}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Fe(2+)(in) = Fe(2+)(out); Xref=Rhea:RHEA:28486,
CC         ChEBI:CHEBI:29033; Evidence={ECO:0000269|PubMed:16054062,
CC         ECO:0000269|PubMed:30213870};
CC   -!- ACTIVITY REGULATION: During elevated serum iron levels, liver-derived
CC       hepcidin/HAMP negatively regulates cell surface ferroportin/SLC40A1 by
CC       inducing its ubiquitination, internalization, and degradation. Indeed,
CC       hepcidin/HAMP affinity towards ferroportin/SLC40A1 increases by 80-fold
CC       in the presence of iron. {ECO:0000250|UniProtKB:Q9NP59}.
CC   -!- SUBUNIT: Identified in a complex with STOM. Interacts with HAMP; this
CC       interaction promotes SLC40A1 rapid ubiquitination.
CC       {ECO:0000250|UniProtKB:Q9NP59}.
CC   -!- INTERACTION:
CC       Q9JHI9; P12023: App; NbExp=2; IntAct=EBI-2931424, EBI-78814;
CC       Q9JHI9; Q9JHI9: Slc40a1; NbExp=2; IntAct=EBI-2931424, EBI-2931424;
CC       Q9JHI9; O60674: JAK2; Xeno; NbExp=3; IntAct=EBI-2931424, EBI-518647;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9NP59};
CC       Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9NP59}. Basolateral
CC       cell membrane {ECO:0000269|PubMed:10693807}; Multi-pass membrane
CC       protein {ECO:0000250|UniProtKB:Q9NP59}. Note=Localized to the
CC       basolateral membrane of polarized epithelial cells.
CC       {ECO:0000269|PubMed:10693807}.
CC   -!- TISSUE SPECIFICITY: High expression in spleen, liver, kidney, heart and
CC       duodenum. {ECO:0000269|PubMed:10693807}.
CC   -!- PTM: Polyubiquitinated by RNF217; leading to proteasomal degradation
CC       (PubMed:33895792). Ubiquitination is necessary for its internalization
CC       by hepcidin/HAMP (By similarity). {ECO:0000250|UniProtKB:Q9NP59,
CC       ECO:0000269|PubMed:33895792}.
CC   -!- DISRUPTION PHENOTYPE: Deficient mice exhibit embryonic lethality. These
CC       mice cannot transfer iron from the extraembryonic visceral endoderm
CC       into the embryo proper, leading to a defect in embryonic growth and
CC       consequent death (PubMed:16054062). Erythroid-specific deletion reduces
CC       serum iron but increased tissue iron contents (PubMed:30213870).
CC       {ECO:0000269|PubMed:16054062, ECO:0000269|PubMed:30213870}.
CC   -!- SIMILARITY: Belongs to the ferroportin (FP) (TC 2.A.100) family. SLC40A
CC       subfamily. {ECO:0000305}.
CC   -!- CAUTION: Manganese (Mn) transport by SLC40A1 remains controversial.
CC       Some in vitro studies have suggested that SLC40A1 transports minimal
CC       amounts of Mn(2+) (By similarity). Other groups have suggested that it
CC       does not (By similarity). The predicted apparent affinity of SLC40A1
CC       for manganese is extremely low compared with iron, implying that any
CC       SLC40A1-mediated Mn transport in vivo would likely be trivial (By
CC       similarity). A recent study examined the role of SLC40A1 in Mn
CC       homeostasis by using Tmprss6-O mice, which express high levels of
CC       hepcidin/HAMP and therefore have very low SLC40A1 levels in their
CC       tissues. These mice show frank iron deficiency and reduced iron levels
CC       in most tissues, but manganese levels are largely unaffected
CC       (PubMed:30888356). These studies suggest that manganese is propably not
CC       the physiological substrate of SLC40A1. {ECO:0000250|UniProtKB:Q9NP59,
CC       ECO:0000269|PubMed:30888356, ECO:0000305}.
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DR   EMBL; AF215637; AAF80987.1; -; mRNA.
DR   EMBL; AF216834; AAF82036.1; -; Genomic_DNA.
DR   EMBL; AF226613; AAF36696.1; -; mRNA.
DR   EMBL; AF231120; AAF44329.1; -; mRNA.
DR   EMBL; AK008700; BAB25840.1; -; mRNA.
DR   EMBL; AK032732; BAC28001.1; -; mRNA.
DR   EMBL; AK083288; BAC38844.1; -; mRNA.
DR   EMBL; AK144780; BAE26063.1; -; mRNA.
DR   EMBL; AK147137; BAE27707.1; -; mRNA.
DR   EMBL; AK159294; BAE34969.1; -; mRNA.
DR   EMBL; AK159855; BAE35431.1; -; mRNA.
DR   EMBL; BC003438; AAH03438.1; -; mRNA.
DR   CCDS; CCDS14933.1; -.
DR   RefSeq; NP_058613.2; NM_016917.2.
DR   RefSeq; XP_006496200.1; XM_006496137.2.
DR   RefSeq; XP_017177198.1; XM_017321709.1.
DR   AlphaFoldDB; Q9JHI9; -.
DR   SMR; Q9JHI9; -.
DR   DIP; DIP-58649N; -.
DR   IntAct; Q9JHI9; 4.
DR   STRING; 10090.ENSMUSP00000027137; -.
DR   ChEMBL; CHEMBL4523462; -.
DR   GuidetoPHARMACOLOGY; 1194; -.
DR   TCDB; 2.A.100.1.1; the ferroportin (fpn) family.
DR   GlyCosmos; Q9JHI9; 1 site, No reported glycans.
DR   GlyGen; Q9JHI9; 1 site.
DR   iPTMnet; Q9JHI9; -.
DR   PhosphoSitePlus; Q9JHI9; -.
DR   SwissPalm; Q9JHI9; -.
DR   MaxQB; Q9JHI9; -.
DR   PaxDb; 10090-ENSMUSP00000027137; -.
DR   ProteomicsDB; 256902; -.
DR   Antibodypedia; 34022; 443 antibodies from 33 providers.
DR   DNASU; 53945; -.
DR   Ensembl; ENSMUST00000027137.11; ENSMUSP00000027137.5; ENSMUSG00000025993.11.
DR   GeneID; 53945; -.
DR   KEGG; mmu:53945; -.
DR   UCSC; uc007awu.1; mouse.
DR   AGR; MGI:1315204; -.
DR   CTD; 30061; -.
DR   MGI; MGI:1315204; Slc40a1.
DR   VEuPathDB; HostDB:ENSMUSG00000025993; -.
DR   eggNOG; KOG2601; Eukaryota.
DR   GeneTree; ENSGT00390000015143; -.
DR   HOGENOM; CLU_020370_1_1_1; -.
DR   InParanoid; Q9JHI9; -.
DR   OMA; NIGNWVD; -.
DR   OrthoDB; 38357at2759; -.
DR   PhylomeDB; Q9JHI9; -.
DR   TreeFam; TF313463; -.
DR   Reactome; R-MMU-425410; Metal ion SLC transporters.
DR   Reactome; R-MMU-917937; Iron uptake and transport.
DR   BioGRID-ORCS; 53945; 3 hits in 79 CRISPR screens.
DR   ChiTaRS; Slc40a1; mouse.
DR   PRO; PR:Q9JHI9; -.
DR   Proteomes; UP000000589; Chromosome 1.
DR   RNAct; Q9JHI9; Protein.
DR   Bgee; ENSMUSG00000025993; Expressed in epithelium of small intestine and 240 other cell types or tissues.
DR   ExpressionAtlas; Q9JHI9; baseline and differential.
DR   GO; GO:0016323; C:basolateral plasma membrane; IGI:BHF-UCL.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0008021; C:synaptic vesicle; IDA:MGI.
DR   GO; GO:0015093; F:ferrous iron transmembrane transporter activity; IDA:BHF-UCL.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0005381; F:iron ion transmembrane transporter activity; IDA:BHF-UCL.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0017046; F:peptide hormone binding; IPI:BHF-UCL.
DR   GO; GO:0006915; P:apoptotic process; IMP:MGI.
DR   GO; GO:0003158; P:endothelium development; IMP:MGI.
DR   GO; GO:0051649; P:establishment of localization in cell; IGI:MGI.
DR   GO; GO:0006879; P:intracellular iron ion homeostasis; ISO:MGI.
DR   GO; GO:1903988; P:iron ion export across plasma membrane; IDA:ARUK-UCL.
DR   GO; GO:0034755; P:iron ion transmembrane transport; IGI:MGI.
DR   GO; GO:0006826; P:iron ion transport; IDA:MGI.
DR   GO; GO:0002260; P:lymphocyte homeostasis; IMP:MGI.
DR   GO; GO:0060586; P:multicellular organismal-level iron ion homeostasis; IMP:BHF-UCL.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IMP:MGI.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IGI:MGI.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:MGI.
DR   GO; GO:0048536; P:spleen development; IMP:MGI.
DR   GO; GO:0060345; P:spleen trabecula formation; IMP:MGI.
DR   GO; GO:0006366; P:transcription by RNA polymerase II; IGI:MGI.
DR   CDD; cd17480; MFS_SLC40A1_like; 1.
DR   Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 1.
DR   InterPro; IPR009716; Ferroportin-1.
DR   InterPro; IPR036259; MFS_trans_sf.
DR   PANTHER; PTHR11660; SOLUTE CARRIER FAMILY 40 MEMBER; 1.
DR   PANTHER; PTHR11660:SF47; SOLUTE CARRIER FAMILY 40 MEMBER 1; 1.
DR   Pfam; PF06963; FPN1; 1.
DR   SUPFAM; SSF103473; MFS general substrate transporter; 1.
DR   Genevisible; Q9JHI9; MM.
PE   1: Evidence at protein level;
KW   Cell membrane; Glycoprotein; Ion transport; Iron; Iron transport; Membrane;
KW   Metal-binding; Reference proteome; Transmembrane; Transmembrane helix;
KW   Transport; Ubl conjugation.
FT   CHAIN           1..570
FT                   /note="Solute carrier family 40 member 1"
FT                   /id="PRO_0000191311"
FT   TOPO_DOM        1..23
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NP59"
FT   TRANSMEM        24..53
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NP59"
FT   TOPO_DOM        54..57
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NP59"
FT   TRANSMEM        58..84
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NP59"
FT   TOPO_DOM        85..87
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NP59"
FT   TRANSMEM        88..118
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NP59"
FT   TOPO_DOM        119..126
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NP59"
FT   TRANSMEM        127..162
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NP59"
FT   TOPO_DOM        163..164
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NP59"
FT   TRANSMEM        165..195
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NP59"
FT   TOPO_DOM        196..202
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NP59"
FT   TRANSMEM        203..229
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NP59"
FT   TOPO_DOM        230..306
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NP59"
FT   TRANSMEM        307..333
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NP59"
FT   TOPO_DOM        334..338
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NP59"
FT   TRANSMEM        339..366
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NP59"
FT   TOPO_DOM        367..368
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NP59"
FT   TRANSMEM        369..391
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NP59"
FT   TOPO_DOM        392..452
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NP59"
FT   TRANSMEM        453..482
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NP59"
FT   TOPO_DOM        483..487
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NP59"
FT   TRANSMEM        488..512
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NP59"
FT   TOPO_DOM        513..515
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NP59"
FT   TRANSMEM        516..541
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NP59"
FT   TOPO_DOM        542..570
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NP59"
FT   BINDING         39
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NP59"
FT   BINDING         43
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NP59"
FT   BINDING         326
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NP59"
FT   BINDING         506
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NP59"
FT   CARBOHYD        437
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   570 AA;  62702 MW;  7125CC6171394A0A CRC64;
     MTKARDQTHQ EGCCGSLANY LTSAKFLLYL GHSLSTWGDR MWHFAVSVFL VELYGNSLLL
     TAVYGLVVAG SVLVLGAIIG DWVDKNARLK VAQTSLVVQN VSVILCGIIL MMVFLHKNEL
     LTMYHGWVLT VCYILIITIA NIANLASTAT AITIQRDWIV VVAGENRSRL ADMNATIRRI
     DQLTNILAPM AVGQIMTFGS PVIGCGFISG WNLVSMCVEY FLLWKVYQKT PALAVKAALK
     VEESELKQLT SPKDTEPKPL EGTHLMGEKD SNIRELECEQ EPTCASQMAE PFRTFRDGWV
     SYYNQPVFLA GMGLAFLYMT VLGFDCITTG YAYTQGLSGS ILSILMGASA ITGIMGTVAF
     TWLRRKCGLV RTGLFSGLAQ LSCLILCVIS VFMPGSPLDL SVSPFEDIRS RFVNVEPVSP
     TTKIPETVFT TEMHMSNMSN VHEMSTKPIP IVSVSLLFAG VIAARIGLWS FDLTVTQLLQ
     ENVIESERGI INGVQNSMNY LLDLLHFIMV ILAPNPEAFG LLVLISVSFV AMGHLMYFRF
     AQKTLGNQIF VCGPDEKEVT DENQPNTSVV
//