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UniProtKB/Swiss-Prot entry Q04800


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name FRP1_SCHPO
Primary accession number Q04800
Secondary accession numbers None
Integrated into Swiss-Prot on February 1, 1994
Sequence was last modified on February 1, 1994 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 68)
Name and origin of the protein
Protein name Ferric reductase transmembrane component 1
Synonyms EC 1.16.1.7
Ferric-chelate reductase 1
Gene name
Name: frp1
ORFNames: SPBC1683.09c
From
Schizosaccharomyces pombe (Fission yeast) [TaxID: 4896] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae; Schizosaccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8321236 [NCBI, ExPASy, EBI, Israel, Japan]
Roman D.G., Dancis A., Anderson G.J., Klausner R.D.;
"The fission yeast ferric reductase gene frp1+ is required for ferric iron uptake and encodes a protein that is homologous to the gp91-phox subunit of the human NADPH phagocyte oxidoreductase.";
Mol. Cell. Biol. 13:4342-4350(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 38366 / 972;
DOI=10.1038/nature724; PubMed=11859360 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[3]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-362; SER-381 AND SER-383, AND MASS SPECTROMETRY.
DOI=10.1021/pr7006335; PubMed=18257517 [NCBI, ExPASy, EBI, Israel, Japan]
Wilson-Grady J.T., Villen J., Gygi S.P.;
"Phosphoproteome analysis of fission yeast.";
J. Proteome Res. 7:1088-1097(2008).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
L07749; AAA68045.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CU329671; CAB91171.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A48141; A48141.
RefSeq NP_595065.1; -.
3D structure databases
ModBase Q04800.
Enzyme and pathway databases
BioCyc SPOM-XXX-01:SPOM-XXX-01-003170-MON; -.
Organism-specific databases
GeneDB_Spombe SPBC1683.09c; -.
Gene expression databases
ArrayExpress Q04800; -.
Ontologies
GO
GO:0005783; Cellular component: endoplasmic reticulum (inferred from direct assay from GeneDB_SPombe).
GO:0000293; Molecular function: ferric-chelate reductase activity (traceable author statement from GeneDB_SPombe).
GO:0033215; Biological process: iron assimilation by reduction and transport (inferred from mutant phenotype from GeneDB_SPombe).
QuickGo view.
Family and domain databases
InterPro IPR013112; FAD_bd_8.
IPR013130; Fe3_reduct_TM_N.
IPR013121; Fe_red_NAD_bd_6.
IPR000778; GP91PhoX.
Graphical view of domain structure.
Pfam PF08022; FAD_binding_8; 1.
PF01794; Ferric_reduct; 1.
PF08030; NAD_binding_6; 1.
Pfam graphical view of domain structure.
PRINTS PR00466; GP91PHOX.
PROSITE PS51384; FAD_FR; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS Q04800.
ProtoNet Q04800.
Genome annotation databases
GeneID 2539711; -.
KEGG spo:SPBC1683.09c; -.
NMPDR fig|4896.1.peg.931; -.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Electron transport; FAD; Glycoprotein; Ion transport; Iron; Iron transport; Membrane; NAD; Oxidoreductase; Phosphoprotein; Transmembrane; Transport.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   564  564     Ferric reductase transmembrane component 1. PRO_0000210152
TRANSMEM   10    30  21     Potential. 
TRANSMEM   73    93  21     Potential. 
TRANSMEM   117   137  21     Potential. 
TRANSMEM   160   180  21     Potential. 
TRANSMEM   193   213  21     Potential. 
TRANSMEM   417   437  21     Potential. 
DOMAIN   121   254  134     Ferric oxidoreductase. 
DOMAIN   255   410  156     FAD-binding FR-type. 
NP_BIND   317   323  7     FAD (Potential). 
NP_BIND   419   427  9     NAD (Potential). 
MOD_RES   362   362        Phosphoserine. 
MOD_RES   381   381        Phosphoserine. 
MOD_RES   383   383        Phosphoserine. 
CARBOHYD   4     4        N-linked (GlcNAc...) (Potential). 
CARBOHYD   111   111        N-linked (GlcNAc...) (Potential). 
CARBOHYD   268   268        N-linked (GlcNAc...) (Potential). 
CARBOHYD   360   360        N-linked (GlcNAc...) (Potential). 
CARBOHYD   501   501        N-linked (GlcNAc...) (Potential). 
Sequence information
Length: 564 AA [This is the length of the unprocessed precursor] Molecular weight: 64092 Da [This is the MW of the unprocessed precursor] CRC64: 336CC2AF934A736B [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAINSSDKWT VIAICLILGI LLAFILMFWL ERFRVIIKSN AHKHDPSDKR QIWLEKYYLF 

        70         80         90        100        110        120 
VRQIYTYLVT HKVILTLIAV PVVFAISIPF IGMQTPASSH GKQTTQVSTG NWSKNAVAAR 

       130        140        150        160        170        180 
LGFLACGLYV TSYFFSIKNN PFALLLISSH EKMNYVHRRL SQYAIMIGAI HGFAYIGLAA 

       190        200        210        220        230        240 
QGKRALLTAR VTIIGYVILG LMVIMIVSSL PFFRRRFYEW FFVLHHMCSI GFLITIWLHH 

       250        260        270        280        290        300 
RRCVVYMKVC VAVYVFDRGC RMLRSFLNRS KFDVVLVEDD LIYMKGPRPK KSFFGLPWGA 

       310        320        330        340        350        360 
GNHMYINIPS LSYWQIHPFT IASVPSDDFI ELFVAVRAGF TKRLAKKVSS KSLSDVSDIN 

       370        380        390        400        410        420 
ISDEKIEKNG DVGIEVMERH SLSQEDLVFE SSAAKVSVLM DGPYGPVSNP YKDYSYLFLF 

       430        440        450        460        470        480 
AGGVGVSYIL PIILDTIKKQ SRTVHITFVW SARSSALLNI VHKSLCEAVR YTEMNINIFC 

       490        500        510        520        530        540 
HLTNSYPVEE VSSLNSQSAR NYSLQYLNGR PDVNDYFKDF LHATGTQTAA LASCGSDKLL 

       550        560 
RHLKSCVNTH SPSTVDLYQH YEEI 

Q04800 in FASTA format

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