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Ferric/cupric reductase transmembrane component 2 (EC 1.16.1.9) (Ferric-chelate reductase 2)

 FRP2_SCHPO              Reviewed;         564 AA.
O94727;
20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
01-MAY-1999, sequence version 1.
20-JUN-2018, entry version 108.
RecName: Full=Ferric/cupric reductase transmembrane component 2 {ECO:0000305};
EC=1.16.1.9 {ECO:0000250|UniProtKB:P32791};
AltName: Full=Ferric-chelate reductase 2 {ECO:0000305};
Name=frp2; ORFNames=SPBC947.05c;
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
Schizosaccharomycetes; Schizosaccharomycetales;
Schizosaccharomycetaceae; Schizosaccharomyces.
NCBI_TaxID=284812;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=972 / ATCC 24843;
PubMed=11859360; DOI=10.1038/nature724;
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M.,
Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A.,
Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G.,
Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K.,
James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J.,
Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C.,
Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E.,
Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S.,
Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K.,
Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S.,
Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B.,
Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S.,
Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D.,
Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R.,
Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B.,
Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S.,
Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M.,
Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G.,
Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J.,
Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L.,
Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J.,
Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.;
"The genome sequence of Schizosaccharomyces pombe.";
Nature 415:871-880(2002).
[2]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=16823372; DOI=10.1038/nbt1222;
Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
Yoshida M.;
"ORFeome cloning and global analysis of protein localization in the
fission yeast Schizosaccharomyces pombe.";
Nat. Biotechnol. 24:841-847(2006).
-!- FUNCTION: Metalloreductase responsible for reducing extracellular
iron and copper prior to import (By similarity). Catalyzes the
reductive uptake of Fe(3+)-salts and Fe(3+) bound to catecholate
or hydroxamate siderophores (By similarity). Fe(3+) is reduced to
Fe(2+), which then dissociates from the siderophore and can be
imported by the high-affinity Fe(2+) transport complex in the
plasma membrane (By similarity). Also participates in Cu(2+)
reduction and Cu(+) uptake (By similarity).
{ECO:0000250|UniProtKB:P32791}.
-!- CATALYTIC ACTIVITY: 2 Fe(II)-siderophore + NADP(+) + H(+) = 2
Fe(III)-siderophore + NADPH. {ECO:0000250|UniProtKB:P32791}.
-!- COFACTOR:
Name=FAD; Xref=ChEBI:CHEBI:57692;
Evidence={ECO:0000250|UniProtKB:P32791};
-!- COFACTOR:
Name=heme; Xref=ChEBI:CHEBI:30413;
Evidence={ECO:0000250|UniProtKB:P32791};
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:P32791}; Multi-pass membrane protein
{ECO:0000255}. Endoplasmic reticulum membrane
{ECO:0000269|PubMed:16823372}; Multi-pass membrane protein
{ECO:0000255}.
-!- SIMILARITY: Belongs to the ferric reductase (FRE) family.
{ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; CU329671; CAA17033.1; -; Genomic_DNA.
PIR; T40777; T40777.
RefSeq; NP_595271.1; NM_001021178.1.
ProteinModelPortal; O94727; -.
BioGrid; 277741; 14.
STRING; 4896.SPBC947.05c.1; -.
SwissPalm; O94727; -.
MaxQB; O94727; -.
PaxDb; O94727; -.
PRIDE; O94727; -.
EnsemblFungi; SPBC947.05c.1; SPBC947.05c.1:pep; SPBC947.05c.
GeneID; 2541227; -.
KEGG; spo:SPBC947.05c; -.
EuPathDB; FungiDB:SPBC947.05c; -.
PomBase; SPBC947.05c; frp2.
HOGENOM; HOG000112645; -.
InParanoid; O94727; -.
OMA; LDSYGHA; -.
OrthoDB; EOG092C2JFA; -.
PhylomeDB; O94727; -.
PRO; PR:O94727; -.
Proteomes; UP000002485; Chromosome II.
GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; ISM:PomBase.
GO; GO:0005886; C:plasma membrane; ISO:PomBase.
GO; GO:0052851; F:ferric-chelate reductase (NADPH) activity; IEA:UniProtKB-EC.
GO; GO:0000293; F:ferric-chelate reductase activity; ISO:PomBase.
GO; GO:0050660; F:flavin adenine dinucleotide binding; ISM:PomBase.
GO; GO:0005506; F:iron ion binding; ISM:PomBase.
GO; GO:0006879; P:cellular iron ion homeostasis; IC:PomBase.
GO; GO:0015677; P:copper ion import; ISO:PomBase.
GO; GO:0034755; P:iron ion transmembrane transport; ISO:PomBase.
GO; GO:0015891; P:siderophore transport; ISS:PomBase.
InterPro; IPR000778; Cyt_b245_heavy_chain.
InterPro; IPR013112; FAD-bd_8.
InterPro; IPR017927; Fd_Rdtase_FAD-bd.
InterPro; IPR013130; Fe3_Rdtase_TM_dom.
InterPro; IPR013121; Fe_red_NAD-bd_6.
InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
Pfam; PF08022; FAD_binding_8; 1.
Pfam; PF01794; Ferric_reduct; 1.
Pfam; PF08030; NAD_binding_6; 1.
PRINTS; PR00466; GP91PHOX.
SUPFAM; SSF63380; SSF63380; 1.
PROSITE; PS51384; FAD_FR; 1.
3: Inferred from homology;
Cell membrane; Complete proteome; Electron transport;
Endoplasmic reticulum; FAD; Flavoprotein; Glycoprotein; Heme;
Ion transport; Iron; Iron transport; Membrane; Metal-binding; NADP;
Oxidoreductase; Reference proteome; Transmembrane;
Transmembrane helix; Transport.
CHAIN 1 564 Ferric/cupric reductase transmembrane
component 2.
/FTId=PRO_0000337260.
TRANSMEM 10 30 Helical. {ECO:0000255}.
TRANSMEM 66 86 Helical. {ECO:0000255}.
TRANSMEM 110 130 Helical. {ECO:0000255}.
TRANSMEM 152 172 Helical. {ECO:0000255}.
TRANSMEM 184 204 Helical. {ECO:0000255}.
TRANSMEM 210 230 Helical. {ECO:0000255}.
DOMAIN 114 229 Ferric oxidoreductase. {ECO:0000255}.
DOMAIN 254 410 FAD-binding FR-type.
{ECO:0000255|PROSITE-ProRule:PRU00716}.
NP_BIND 310 316 FAD. {ECO:0000255}.
NP_BIND 419 427 NAD. {ECO:0000255}.
METAL 150 150 Iron (heme 1 axial ligand).
{ECO:0000250|UniProtKB:P32791}.
METAL 164 164 Iron (heme 2 axial ligand).
{ECO:0000250|UniProtKB:P32791}.
METAL 218 218 Iron (heme 1 axial ligand).
{ECO:0000250|UniProtKB:P32791}.
METAL 232 232 Iron (heme 2 axial ligand).
{ECO:0000250|UniProtKB:P32791}.
CARBOHYD 106 106 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 261 261 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 350 350 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 442 442 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 496 496 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 548 548 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
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


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