ID   S40A1_DANRE             Reviewed;         562 AA.
AC   Q9I9R3; Q3B729; Q7ZZ51; Q8AW23; Q8AW28; Q8JFW0;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   03-MAY-2023, sequence version 3.
DT   27-MAR-2024, entry version 113.
DE   RecName: Full=Solute carrier family 40 member 1;
DE   AltName: Full=Ferroportin-1;
GN   Name=slc40a1; Synonyms=fpn1 {ECO:0000303|PubMed:10693807}, slc39a1;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE, FUNCTION, TRANSPORTER
RP   ACTIVITY, TISSUE SPECIFICITY, AND MUTAGENESIS OF LEU-167.
RC   TISSUE=Kidney;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen;
RX   PubMed=23594743; DOI=10.1038/nature12111;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA   Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA   Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA   White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA   Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA   Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA   Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA   Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA   Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA   Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA   Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA   Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA   Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA   McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA   Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA   Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA   Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA   Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA   Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA   Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA   Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA   Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA   Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA   Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA   Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA   Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA   de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA   Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the human
RT   genome.";
RL   Nature 496:498-503(2013).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-251.
RC   TISSUE=Heart;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
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:10693807). May be involved in transfer of Fe(2+) between
CC       maternal and fetal circulation (PubMed:10693807).
CC       {ECO:0000269|PubMed:10693807}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Fe(2+)(in) = Fe(2+)(out); Xref=Rhea:RHEA:28486,
CC         ChEBI:CHEBI:29033; Evidence={ECO:0000269|PubMed:10693807};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28487;
CC         Evidence={ECO:0000305|PubMed:10693807};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9NP59};
CC       Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9NP59}. Basolateral
CC       cell membrane {ECO:0000250|UniProtKB:Q9NP59}; Multi-pass membrane
CC       protein {ECO:0000250|UniProtKB:Q9NP59}.
CC   -!- TISSUE SPECIFICITY: Expressed in the yolk sac and placenta.
CC       {ECO:0000269|PubMed:10693807}.
CC   -!- SIMILARITY: Belongs to the ferroportin (FP) (TC 2.A.100) family. SLC40A
CC       subfamily. {ECO:0000305}.
CC   -!- CAUTION: Manganese (Mn(2+)) transport by SLC40A1 remains controversial.
CC       Some in vitro studies have suggested that SLC40A1 transports minimal
CC       amounts of Mn(2+). {ECO:0000250|UniProtKB:Q9JHI9,
CC       ECO:0000250|UniProtKB:Q9NP59}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAI07846.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR   EMBL; AF226612; AAF36695.1; -; mRNA.
DR   EMBL; AL591593; CAD43474.1; -; Genomic_DNA.
DR   EMBL; AL672145; CAD58776.1; -; Genomic_DNA.
DR   EMBL; AL672118; CAD52128.1; -; Genomic_DNA.
DR   EMBL; AL731861; CAD61076.1; -; Genomic_DNA.
DR   EMBL; BC107845; AAI07846.1; ALT_SEQ; mRNA.
DR   RefSeq; NP_571704.1; NM_131629.1.
DR   AlphaFoldDB; Q9I9R3; -.
DR   SMR; Q9I9R3; -.
DR   STRING; 7955.ENSDARP00000000250; -.
DR   TCDB; 2.A.100.1.7; the ferroportin (fpn) family.
DR   PaxDb; 7955-ENSDARP00000000250; -.
DR   GeneID; 58153; -.
DR   KEGG; dre:58153; -.
DR   AGR; ZFIN:ZDB-GENE-000511-8; -.
DR   CTD; 30061; -.
DR   ZFIN; ZDB-GENE-000511-8; slc40a1.
DR   eggNOG; KOG2601; Eukaryota.
DR   InParanoid; Q9I9R3; -.
DR   OMA; NIGNWVD; -.
DR   OrthoDB; 38357at2759; -.
DR   PhylomeDB; Q9I9R3; -.
DR   Reactome; R-DRE-425410; Metal ion SLC transporters.
DR   Reactome; R-DRE-917937; Iron uptake and transport.
DR   PRO; PR:Q9I9R3; -.
DR   Proteomes; UP000000437; Chromosome 9.
DR   GO; GO:0016323; C:basolateral plasma membrane; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; ISS:ZFIN.
DR   GO; GO:0005381; F:iron ion transmembrane transporter activity; IDA:ZFIN.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0017046; F:peptide hormone binding; IBA:GO_Central.
DR   GO; GO:0030282; P:bone mineralization; IMP:ZFIN.
DR   GO; GO:0035162; P:embryonic hemopoiesis; IMP:ZFIN.
DR   GO; GO:0042541; P:hemoglobin biosynthetic process; IMP:ZFIN.
DR   GO; GO:0006879; P:intracellular iron ion homeostasis; IMP:ZFIN.
DR   GO; GO:0034755; P:iron ion transmembrane transport; IBA:GO_Central.
DR   GO; GO:0006826; P:iron ion transport; IMP:ZFIN.
DR   GO; GO:0043362; P:nucleate erythrocyte maturation; IMP:ZFIN.
DR   GO; GO:0046688; P:response to copper ion; IDA:ZFIN.
DR   GO; GO:0010039; P:response to iron ion; IDA:ZFIN.
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.
PE   1: Evidence at protein level;
KW   Cell membrane; Ion transport; Iron; Iron transport; Membrane;
KW   Metal-binding; Reference proteome; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..562
FT                   /note="Solute carrier family 40 member 1"
FT                   /id="PRO_0000191313"
FT   TOPO_DOM        1..20
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        21..50
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NP59"
FT   TOPO_DOM        51..54
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        55..81
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NP59"
FT   TOPO_DOM        82..84
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        85..115
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NP59"
FT   TOPO_DOM        116..123
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        124..159
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NP59"
FT   TOPO_DOM        160..161
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        162..192
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NP59"
FT   TOPO_DOM        193..199
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        200..226
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NP59"
FT   TOPO_DOM        227..300
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        301..327
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NP59"
FT   TOPO_DOM        328..332
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        333..360
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NP59"
FT   TOPO_DOM        361..362
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        363..385
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NP59"
FT   TOPO_DOM        386..444
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        445..474
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NP59"
FT   TOPO_DOM        475..479
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        480..504
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NP59"
FT   TOPO_DOM        505..507
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        508..533
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NP59"
FT   TOPO_DOM        534..562
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   BINDING         36
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NP59"
FT   BINDING         320
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NP59"
FT   BINDING         498
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NP59"
FT   MUTAGEN         167
FT                   /note="L->F: In weissherbst tp85c mutant; homozygotes
FT                   develop severe anemia within 48 h after fertilization and
FT                   dies between 10 and 14 days of age."
FT                   /evidence="ECO:0000269|PubMed:10693807"
FT   CONFLICT        134
FT                   /note="I -> V (in Ref. 3; AAI07846)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        272
FT                   /note="T -> P (in Ref. 1; AAF36695)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        400
FT                   /note="E -> K (in Ref. 1; AAF36695)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   562 AA;  61765 MW;  7C2EF1201222B266 CRC64;
     MDSPASKKPR CERFREFFKS AKFLIYVGHA LSTWGDRMWN FAVAVFLVEL YGNSLLLTAV
     YGLVVAGSVL LLGAIIGDWV DKNPRLKVAQ TSLVVQNSAV ILCGALLMAV FQFKQQLSSM
     YDGWLLTTCY IMVISIANIA NLASTAMSIT IQRDWVVVVA GDDRSKLADM NATVRIIDQL
     TNILAPMLVG QIMAFGSHFI GCGFISGWNL FSMCLEYFLL WKVYQKTPAL AFKAGQKDSD
     DQELKHLNIQ KEIGNTESPV EASQLMTESS ETKKDTGCCY QMAEPIRTFK DGWVAYYNQS
     IFFAGMSLAF LYMTVLGFDC ITTGYAYTQG LNGSVLSLLM GASAVSGICG TVAFTWIRKK
     CGLIRTGFIA GVTQLSCLTL CVASVFAPGS PFDLSVSPFE EVLRHLFGDS GSLRESPTFI
     PTTEPPIQAN VTVFEEAPPV ESYMSVGLLF AGVIAARVGL WSFDLTVTQL IQENVIESER
     GVINGVQNSM NYLLDLLHFI MVILAPNPEA FGLLVIISVS FVAMGHMMYF RFAYKSLGSR
     LFLFCSPEQK PDPNIPSLPN SV
//