FRP1_SCHPO
ID FRP1_SCHPO Reviewed; 564 AA.
AC Q04800;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Ferric reductase transmembrane component 1 {ECO:0000305};
DE EC=1.16.1.9 {ECO:0000250|UniProtKB:P32791};
DE AltName: Full=Ferric-chelate reductase 1 {ECO:0000305};
GN Name=frp1; ORFNames=SPBC1683.09c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8321236; DOI=10.1128/mcb.13.7.4342-4350.1993;
RA Roman D.G., Dancis A., Anderson G.J., Klausner R.D.;
RT "The fission yeast ferric reductase gene frp1+ is required for ferric iron
RT uptake and encodes a protein that is homologous to the gp91-phox subunit of
RT the human NADPH phagocyte oxidoreductase.";
RL Mol. Cell. Biol. 13:4342-4350(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-362; SER-381 AND SER-383, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: Metalloreductase responsible for reducing extracellular iron
CC and copper prior to import (By similarity). Catalyzes the reductive
CC uptake of Fe(3+)-salts and Fe(3+) bound to catecholate or hydroxamate
CC siderophores (By similarity). Fe(3+) is reduced to Fe(2+), which then
CC dissociates from the siderophore and can be imported by the high-
CC affinity Fe(2+) transport complex in the plasma membrane (By
CC similarity). Also participates in Cu(2+) reduction and Cu(+) uptake (By
CC similarity). {ECO:0000250|UniProtKB:P32791}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 a Fe(II)-siderophore + H(+) + NADP(+) = 2 a Fe(III)-
CC siderophore + NADPH; Xref=Rhea:RHEA:28795, Rhea:RHEA-COMP:11342,
CC Rhea:RHEA-COMP:11344, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033,
CC ChEBI:CHEBI:29034, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.16.1.9;
CC Evidence={ECO:0000250|UniProtKB:P32791};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:P32791};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P32791};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P32791};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the ferric reductase (FRE) family.
CC {ECO:0000305}.
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DR EMBL; L07749; AAA68045.1; -; Genomic_DNA.
DR EMBL; CU329671; CAB91171.1; -; Genomic_DNA.
DR PIR; A48141; A48141.
DR RefSeq; NP_595065.1; NM_001020971.2.
DR AlphaFoldDB; Q04800; -.
DR SMR; Q04800; -.
DR BioGRID; 276264; 23.
DR STRING; 4896.SPBC1683.09c.1; -.
DR TCDB; 5.B.1.5.5; the phagocyte (gp91(phox)) nadph oxidase family.
DR iPTMnet; Q04800; -.
DR MaxQB; Q04800; -.
DR PaxDb; Q04800; -.
DR PRIDE; Q04800; -.
DR EnsemblFungi; SPBC1683.09c.1; SPBC1683.09c.1:pep; SPBC1683.09c.
DR GeneID; 2539711; -.
DR KEGG; spo:SPBC1683.09c; -.
DR PomBase; SPBC1683.09c; frp1.
DR VEuPathDB; FungiDB:SPBC1683.09c; -.
DR eggNOG; KOG0039; Eukaryota.
DR HOGENOM; CLU_035348_0_0_1; -.
DR InParanoid; Q04800; -.
DR OMA; WMMGIAY; -.
DR PhylomeDB; Q04800; -.
DR PRO; PR:Q04800; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR GO; GO:0016021; C:integral component of membrane; ISS:PomBase.
DR GO; GO:0005886; C:plasma membrane; ISO:PomBase.
DR GO; GO:0052851; F:ferric-chelate reductase (NADPH) activity; IEA:UniProtKB-EC.
DR GO; GO:0000293; F:ferric-chelate reductase activity; IMP:PomBase.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; ISM:PomBase.
DR GO; GO:0005506; F:iron ion binding; ISM:PomBase.
DR GO; GO:0016175; F:superoxide-generating NAD(P)H oxidase activity; IBA:GO_Central.
DR GO; GO:0010106; P:cellular response to iron ion starvation; IMP:PomBase.
DR GO; GO:0035434; P:copper ion transmembrane transport; ISO:PomBase.
DR GO; GO:0033215; P:reductive iron assimilation; IMP:PomBase.
DR Gene3D; 3.40.50.80; -; 1.
DR InterPro; IPR013112; FAD-bd_8.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR013130; Fe3_Rdtase_TM_dom.
DR InterPro; IPR013121; Fe_red_NAD-bd_6.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR Pfam; PF08022; FAD_binding_8; 1.
DR Pfam; PF01794; Ferric_reduct; 1.
DR Pfam; PF08030; NAD_binding_6; 1.
DR SUPFAM; SSF52343; SSF52343; 1.
DR SUPFAM; SSF63380; SSF63380; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Electron transport; FAD; Flavoprotein; Glycoprotein; Heme;
KW Ion transport; Iron; Iron transport; Membrane; Metal-binding; NADP;
KW Oxidoreductase; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..564
FT /note="Ferric reductase transmembrane component 1"
FT /id="PRO_0000210152"
FT TRANSMEM 10..30
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 73..93
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 117..137
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 160..180
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 193..213
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 417..437
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 121..254
FT /note="Ferric oxidoreductase"
FT /evidence="ECO:0000255"
FT DOMAIN 255..410
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT BINDING 157
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
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:P32791"
FT BINDING 171
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
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:P32791"
FT BINDING 225
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
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:P32791"
FT BINDING 239
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
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:P32791"
FT BINDING 317..323
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
FT BINDING 419..427
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255"
FT MOD_RES 362
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 381
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 383
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT CARBOHYD 4
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 111
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 268
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 360
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 501
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 564 AA; 64092 MW; 336CC2AF934A736B CRC64;
MAINSSDKWT VIAICLILGI LLAFILMFWL ERFRVIIKSN AHKHDPSDKR QIWLEKYYLF
VRQIYTYLVT HKVILTLIAV PVVFAISIPF IGMQTPASSH GKQTTQVSTG NWSKNAVAAR
LGFLACGLYV TSYFFSIKNN PFALLLISSH EKMNYVHRRL SQYAIMIGAI HGFAYIGLAA
QGKRALLTAR VTIIGYVILG LMVIMIVSSL PFFRRRFYEW FFVLHHMCSI GFLITIWLHH
RRCVVYMKVC VAVYVFDRGC RMLRSFLNRS KFDVVLVEDD LIYMKGPRPK KSFFGLPWGA
GNHMYINIPS LSYWQIHPFT IASVPSDDFI ELFVAVRAGF TKRLAKKVSS KSLSDVSDIN
ISDEKIEKNG DVGIEVMERH SLSQEDLVFE SSAAKVSVLM DGPYGPVSNP YKDYSYLFLF
AGGVGVSYIL PIILDTIKKQ SRTVHITFVW SARSSALLNI VHKSLCEAVR YTEMNINIFC
HLTNSYPVEE VSSLNSQSAR NYSLQYLNGR PDVNDYFKDF LHATGTQTAA LASCGSDKLL
RHLKSCVNTH SPSTVDLYQH YEEI
