FRP2_SCHPO
ID FRP2_SCHPO Reviewed; 564 AA.
AC O94727;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Ferric/cupric reductase transmembrane component 2 {ECO:0000305};
DE EC=1.16.1.9 {ECO:0000250|UniProtKB:P32791};
DE AltName: Full=Ferric-chelate reductase 2 {ECO:0000305};
GN Name=frp2; ORFNames=SPBC947.05c;
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 [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 [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
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}. Endoplasmic reticulum
CC membrane {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the ferric reductase (FRE) family.
CC {ECO:0000305}.
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DR EMBL; CU329671; CAA17033.1; -; Genomic_DNA.
DR PIR; T40777; T40777.
DR RefSeq; NP_595271.1; NM_001021178.1.
DR AlphaFoldDB; O94727; -.
DR SMR; O94727; -.
DR BioGRID; 277741; 14.
DR STRING; 4896.SPBC947.05c.1; -.
DR TCDB; 5.B.1.5.6; the phagocyte (gp91(phox)) nadph oxidase family.
DR SwissPalm; O94727; -.
DR MaxQB; O94727; -.
DR PaxDb; O94727; -.
DR EnsemblFungi; SPBC947.05c.1; SPBC947.05c.1:pep; SPBC947.05c.
DR GeneID; 2541227; -.
DR KEGG; spo:SPBC947.05c; -.
DR PomBase; SPBC947.05c; frp2.
DR VEuPathDB; FungiDB:SPBC947.05c; -.
DR eggNOG; KOG0039; Eukaryota.
DR HOGENOM; CLU_035348_0_0_1; -.
DR InParanoid; O94727; -.
DR OMA; WQVHPFT; -.
DR PhylomeDB; O94727; -.
DR PRO; PR:O94727; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; ISM: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; IBA:GO_Central.
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:0015677; P:copper ion import; ISO:PomBase.
DR GO; GO:0034755; P:iron ion transmembrane transport; ISO:PomBase.
DR GO; GO:0033215; P:reductive iron assimilation; IBA:GO_Central.
DR GO; GO:0015891; P:siderophore transport; ISS:PomBase.
DR Gene3D; 3.40.50.80; -; 1.
DR InterPro; IPR000778; Cyt_b245_heavy_chain.
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 PRINTS; PR00466; GP91PHOX.
DR SUPFAM; SSF52343; SSF52343; 1.
DR SUPFAM; SSF63380; SSF63380; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 3: Inferred from homology;
KW Cell membrane; Electron transport; Endoplasmic reticulum; FAD;
KW Flavoprotein; Glycoprotein; Heme; Ion transport; Iron; Iron transport;
KW Membrane; Metal-binding; NADP; Oxidoreductase; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..564
FT /note="Ferric/cupric reductase transmembrane component 2"
FT /id="PRO_0000337260"
FT TRANSMEM 10..30
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 66..86
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 110..130
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 152..172
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 184..204
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 210..230
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 114..229
FT /note="Ferric oxidoreductase"
FT /evidence="ECO:0000255"
FT DOMAIN 254..410
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT BINDING 150
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 164
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 218
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 232
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 310..316
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 CARBOHYD 106
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 261
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 350
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 442
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 496
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 548
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 564 AA; 65262 MW; 8890551FB5AAFD40 CRC64;
MILARDDKWT LGSIALIFVL LIGFALLFLL ERFRVKEKSR TFKDCVNVYQ CPSKGERVYL
ALRHWFIFLA THKAQMTLIL SPLVMLVTIP FTGKETKNSI ASYDWNLTGV AARLGYLSCG
LFFVSYFFSL KNNPFCLMLF SSHEKMNYLH RWLSVYAVLI SVLHGILFMI FSAQSYKPLL
YDKISIYGYF ITVVLFLMTV ASLPSVRRKF FEWFFVLHHT CSVLIIFLIW LHHPRTIVYM
KACIIIYAFD RGCRLFRSIW NRSNFRIYLL NEDMIYMVGR KPKRSFFALP WAAGSHVYIN
IPSLSYWQVH PFTLASAPFD DFIELFVAVH SGFTERLANR LYSMPHEYPN FSLAPGTPES
LSNTYRELNS FKSYAVEIEN TAQGHTYEPE DLYLETTVFM DGPYGTTSNV FKEYSYVLLI
AGGVGFSYTL PILRDLILKE CNVTSITFIW SCRSLSLLKV ASKSLNSLLH QSNVRLKIIN
HFTGSISCKE SSEFSNQTTE NSEMEFFDDR PDLDMYIQKF FDYVGYQTAA LAACGSQSFL
KRIKNSVNKS ISSTTDIYQH YEEL
