FPN_BDEBA
ID FPN_BDEBA Reviewed; 440 AA.
AC Q6MLJ0;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Ferreportin {ECO:0000303|PubMed:26608034};
DE Short=Fpn;
GN Name=slc39; OrderedLocusNames=Bd2019;
OS Bdellovibrio bacteriovorus (strain ATCC 15356 / DSM 50701 / NCIMB 9529 /
OS HD100).
OC Bacteria; Proteobacteria; Oligoflexia; Bdellovibrionales;
OC Bdellovibrionaceae; Bdellovibrio.
OX NCBI_TaxID=264462;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15356 / DSM 50701 / NCIMB 9529 / HD100;
RX PubMed=14752164; DOI=10.1126/science.1093027;
RA Rendulic S., Jagtap P., Rosinus A., Eppinger M., Baar C., Lanz C.,
RA Keller H., Lambert C., Evans K.J., Goesmann A., Meyer F., Sockett R.E.,
RA Schuster S.C.;
RT "A predator unmasked: life cycle of Bdellovibrio bacteriovorus from a
RT genomic perspective.";
RL Science 303:689-692(2004).
RN [2]
RP FUNCTION, AND MUTAGENESIS OF ASP-24; ASP-28; ASP-162; GLU-166; HIS-261 AND
RP ARG-348.
RX PubMed=26608034; DOI=10.1016/j.febslet.2015.11.025;
RA Bonaccorsi di Patti M.C., Polticelli F., Tortosa V., Furbetta P.A.,
RA Musci G.;
RT "A bacterial homologue of the human iron exporter ferroportin.";
RL FEBS Lett. 589:3829-3835(2015).
RN [3] {ECO:0007744|PDB:5AYM, ECO:0007744|PDB:5AYN}
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 1-433 IN COMPLEX WITH IRON,
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF ASP-24 AND ASN-196.
RX PubMed=26461048; DOI=10.1038/ncomms9545;
RA Taniguchi R., Kato H.E., Font J., Deshpande C.N., Wada M., Ito K.,
RA Ishitani R., Jormakka M., Nureki O.;
RT "Outward- and inward-facing structures of a putative bacterial transition-
RT metal transporter with homology to ferroportin.";
RL Nat. Commun. 6:8545-8545(2015).
RN [4] {ECO:0007744|PDB:6BTX}
RP X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) OF 1-433, COFACTOR, AND MUTAGENESIS
RP OF ASP-24; GLN-84; ASN-196 AND GLU-203.
RX PubMed=30082682; DOI=10.1038/s41467-018-05446-4;
RA Deshpande C.N., Ruwe T.A., Shawki A., Xin V., Vieth K.R., Valore E.V.,
RA Qiao B., Ganz T., Nemeth E., Mackenzie B., Jormakka M.;
RT "Calcium is an essential cofactor for metal efflux by the ferroportin
RT transporter family.";
RL Nat. Commun. 9:3075-3075(2018).
CC -!- FUNCTION: Iron transpoter that exports Fe(2+) from the cell. Also binds
CC to Co(2+) and Ni(2+). May act as a multivalent divalent metal
CC transporter (PubMed:26608034). The transporter is composed of 12
CC transmembrane (TM) helices organized into N-terminal (TM1-6) and C-
CC terminal (TM7-12) domains. The substrate-binding site is formed at the
CC interface of the two domains and is alternately accessible from either
CC side of the membrane. The transport cycle is viewed as a series of
CC ligand-induced conformational changes that include open outward and
CC open inward states (PubMed:26461048, PubMed:30082682).
CC {ECO:0000269|PubMed:26461048, ECO:0000269|PubMed:26608034,
CC ECO:0000269|PubMed:30082682}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:30082682};
CC Note=The cofactor facilitates a conformational change critical to the
CC transport cycle. The binding of Ca2+ from extracellular fluid activates
CC the transporter by triggering a conformational change that enables the
CC transition from the open outward to open inward states.
CC {ECO:0000269|PubMed:30082682};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:26461048};
CC Multi-pass membrane protein {ECO:0000269|PubMed:26461048}.
CC -!- SIMILARITY: Belongs to the ferroportin (FP) (TC 2.A.100) family.
CC {ECO:0000305}.
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DR EMBL; BX842651; CAE79867.1; -; Genomic_DNA.
DR RefSeq; WP_011164469.1; NC_005363.1.
DR PDB; 5AYM; X-ray; 3.00 A; A=1-433.
DR PDB; 5AYN; X-ray; 2.20 A; A=1-433.
DR PDB; 5AYO; X-ray; 3.30 A; A=1-433.
DR PDB; 6BTX; X-ray; 3.20 A; A=1-433.
DR PDBsum; 5AYM; -.
DR PDBsum; 5AYN; -.
DR PDBsum; 5AYO; -.
DR PDBsum; 6BTX; -.
DR SMR; Q6MLJ0; -.
DR STRING; 264462.Bd2019; -.
DR TCDB; 2.A.100.2.1; the ferroportin (fpn) family.
DR EnsemblBacteria; CAE79867; CAE79867; Bd2019.
DR KEGG; bba:Bd2019; -.
DR HOGENOM; CLU_622092_0_0_7; -.
DR OrthoDB; 1115612at2; -.
DR Proteomes; UP000008080; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005381; F:iron ion transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd17480; MFS_SLC40A1_like; 1.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR009716; Ferroportin-1.
DR InterPro; IPR036259; MFS_trans_sf.
DR PANTHER; PTHR11660; PTHR11660; 1.
DR Pfam; PF06963; FPN1; 2.
DR SUPFAM; SSF103473; SSF103473; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Membrane; Metal-binding; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport; Zinc.
FT CHAIN 1..440
FT /note="Ferreportin"
FT /id="PRO_0000453803"
FT TOPO_DOM 1..8
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:26461048"
FT TRANSMEM 9..38
FT /note="Helical; Name=1"
FT /evidence="ECO:0000269|PubMed:26461048,
FT ECO:0007744|PDB:5AYN"
FT TOPO_DOM 39..42
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:26461048"
FT TRANSMEM 43..69
FT /note="Helical; Name=2"
FT /evidence="ECO:0000269|PubMed:26461048,
FT ECO:0007744|PDB:5AYN"
FT TOPO_DOM 70..72
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:26461048"
FT TRANSMEM 73..103
FT /note="Helical; Name=3"
FT /evidence="ECO:0000269|PubMed:26461048,
FT ECO:0007744|PDB:5AYN"
FT TOPO_DOM 104..109
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:26461048"
FT TRANSMEM 110..145
FT /note="Helical; Name=4"
FT /evidence="ECO:0000269|PubMed:26461048,
FT ECO:0007744|PDB:5AYN"
FT TOPO_DOM 146..147
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:26461048"
FT TRANSMEM 148..176
FT /note="Helical; Name=5"
FT /evidence="ECO:0000269|PubMed:26461048,
FT ECO:0007744|PDB:5AYN"
FT TOPO_DOM 177..186
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:26461048"
FT TRANSMEM 187..213
FT /note="Helical; Name=6"
FT /evidence="ECO:0000269|PubMed:26461048,
FT ECO:0007744|PDB:5AYN"
FT TOPO_DOM 214..242
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:26461048"
FT TRANSMEM 243..271
FT /note="Helical; Name=7"
FT /evidence="ECO:0000269|PubMed:26461048,
FT ECO:0007744|PDB:5AYN"
FT TOPO_DOM 272..276
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:26461048"
FT TRANSMEM 277..304
FT /note="Helical; Name=8"
FT /evidence="ECO:0000269|PubMed:26461048,
FT ECO:0007744|PDB:5AYN"
FT TOPO_DOM 305..306
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:26461048"
FT TRANSMEM 307..329
FT /note="Helical; Name=9"
FT /evidence="ECO:0000269|PubMed:26461048,
FT ECO:0007744|PDB:5AYN"
FT TOPO_DOM 330..335
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:26461048"
FT TRANSMEM 336..365
FT /note="Helical; Name=10"
FT /evidence="ECO:0000269|PubMed:26461048,
FT ECO:0007744|PDB:5AYN"
FT TOPO_DOM 366..370
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:26461048"
FT TRANSMEM 371..395
FT /note="Helical; Name=11"
FT /evidence="ECO:0000269|PubMed:26461048,
FT ECO:0007744|PDB:5AYN"
FT TOPO_DOM 396..398
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:26461048"
FT TRANSMEM 399..424
FT /note="Helical; Name=12"
FT /evidence="ECO:0000269|PubMed:26461048,
FT ECO:0007744|PDB:5AYN"
FT TOPO_DOM 425..440
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:26461048"
FT BINDING 24
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:30082682,
FT ECO:0007744|PDB:6BTX"
FT BINDING 84
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:30082682,
FT ECO:0007744|PDB:6BTX"
FT BINDING 196
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:30082682,
FT ECO:0007744|PDB:6BTX"
FT BINDING 203
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:30082682,
FT ECO:0007744|PDB:6BTX"
FT MUTAGEN 24
FT /note="D->A: Slows down the kinetics of iron transport,
FT while not affecting the iron binding ability. Complete loss
FT of calcium binding."
FT /evidence="ECO:0000269|PubMed:26461048,
FT ECO:0000269|PubMed:26608034, ECO:0000269|PubMed:30082682"
FT MUTAGEN 28
FT /note="D->A: No effect."
FT /evidence="ECO:0000269|PubMed:26608034"
FT MUTAGEN 84
FT /note="Q->E: Complete loss of calcium binding."
FT /evidence="ECO:0000269|PubMed:30082682"
FT MUTAGEN 162
FT /note="D->A: No effect."
FT /evidence="ECO:0000269|PubMed:26608034"
FT MUTAGEN 166
FT /note="E->A: Slows down the kinetics of iron transport,
FT while not affecting the iron binding ability."
FT /evidence="ECO:0000269|PubMed:26608034"
FT MUTAGEN 196
FT /note="N->A: Reduces transport activity. Complete loss of
FT calcium binding."
FT /evidence="ECO:0000269|PubMed:26461048,
FT ECO:0000269|PubMed:30082682"
FT MUTAGEN 203
FT /note="E->A: Complete loss of calcium binding."
FT /evidence="ECO:0000269|PubMed:30082682"
FT MUTAGEN 261
FT /note="H->D: Complete loss of iron binding. Completely
FT abolishes the transport ability."
FT /evidence="ECO:0000269|PubMed:26608034"
FT MUTAGEN 348
FT /note="R->M: Complete loss of iron binding. Completely
FT abolishes the transport ability."
FT /evidence="ECO:0000269|PubMed:26608034"
FT HELIX 9..38
FT /evidence="ECO:0007829|PDB:5AYN"
FT HELIX 43..68
FT /evidence="ECO:0007829|PDB:5AYN"
FT HELIX 73..103
FT /evidence="ECO:0007829|PDB:5AYN"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:5AYO"
FT HELIX 110..139
FT /evidence="ECO:0007829|PDB:5AYN"
FT HELIX 141..145
FT /evidence="ECO:0007829|PDB:5AYN"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:5AYN"
FT HELIX 151..176
FT /evidence="ECO:0007829|PDB:5AYN"
FT HELIX 187..212
FT /evidence="ECO:0007829|PDB:5AYN"
FT HELIX 215..217
FT /evidence="ECO:0007829|PDB:5AYN"
FT HELIX 236..239
FT /evidence="ECO:0007829|PDB:5AYN"
FT HELIX 243..251
FT /evidence="ECO:0007829|PDB:5AYN"
FT HELIX 252..255
FT /evidence="ECO:0007829|PDB:5AYN"
FT HELIX 263..271
FT /evidence="ECO:0007829|PDB:5AYN"
FT HELIX 277..305
FT /evidence="ECO:0007829|PDB:5AYN"
FT HELIX 307..330
FT /evidence="ECO:0007829|PDB:5AYN"
FT HELIX 334..336
FT /evidence="ECO:0007829|PDB:5AYN"
FT HELIX 337..365
FT /evidence="ECO:0007829|PDB:5AYN"
FT HELIX 368..370
FT /evidence="ECO:0007829|PDB:5AYN"
FT HELIX 371..395
FT /evidence="ECO:0007829|PDB:5AYN"
FT HELIX 399..401
FT /evidence="ECO:0007829|PDB:5AYN"
FT HELIX 402..424
FT /evidence="ECO:0007829|PDB:5AYN"
SQ SEQUENCE 440 AA; 48363 MW; 0556E226F80B874E CRC64;
MKVQSLLRIE TQLLLGRLLT RSGDQAWDFV VPFALLVIFP GKLQVAAFYY LIVKIGTFLL
TPSSGKWIDT HPRIQVVKWG VWLQFFAILA GMVFFGMLDG LVRAGGRESW LLSVLFIALA
LSGVMASLGS QITDISVGND LAPSLVAPEK LTHFNSWLRR IDLATEVGAP ILAGALFAFH
PEQLPLAGLF LIGLWNLVSF VPEYFLLRNV IQRSGLKIKV LTEAQSWKDT FHINLRGSFS
DPIFWLILSY ALLWLSVLSP HGVLLAAYLK DEMRLPETEI GLFRGLGAVF GLISTVSFPY
LVRRLGLISS SRWHLGFQGV TLGIAVTAFA MGSTASVYVF LGCILLSRVG LYGFSNGEFE
LRQRLIPEGR RGELNSLSSL TTTSATLILF SAGSLLPQTE DFKYLVYVSL AAVLLANVVF
IKWSSRQGVV TSGAAEPVES
