Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q04800 (FRP1_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ferric reductase transmembrane component 1
EC=1.16.1.7
Alternative name(s):
Ferric-chelate reductase 1
Gene names
Name:frp1
ORF Names:SPBC1683.09c
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length564 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Is required for the uptake of Fe3+ ions. May participate in the transport of electrons from cytoplasm to an extracellular substrate (Fe3+ ion) via FAD and heme intermediates.

Catalytic activity

2 Fe2+ + NAD+ + H+ = 2 Fe3+ + NADH.

Cofactor

FAD Probable.

Subcellular location

Membrane; Multi-pass membrane protein.

Sequence similarities

Belongs to the ferric reductase (FRE) family.

Contains 1 FAD-binding FR-type domain.

Contains 1 ferric oxidoreductase domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 564564Ferric reductase transmembrane component 1
PRO_0000210152

Regions

Transmembrane10 – 3021Helical; Potential
Transmembrane73 – 9321Helical; Potential
Transmembrane117 – 13721Helical; Potential
Transmembrane160 – 18021Helical; Potential
Transmembrane193 – 21321Helical; Potential
Transmembrane417 – 43721Helical; Potential
Domain121 – 254134Ferric oxidoreductase
Domain255 – 410156FAD-binding FR-type
Nucleotide binding317 – 3237FAD Potential
Nucleotide binding419 – 4279NAD Potential

Amino acid modifications

Modified residue3621Phosphoserine Ref.3
Modified residue3811Phosphoserine Ref.3
Modified residue3831Phosphoserine Ref.3
Glycosylation41N-linked (GlcNAc...) Potential
Glycosylation1111N-linked (GlcNAc...) Potential
Glycosylation2681N-linked (GlcNAc...) Potential
Glycosylation3601N-linked (GlcNAc...) Potential
Glycosylation5011N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q04800 [UniParc].

Last modified February 1, 1994. Version 1.
Checksum: 336CC2AF934A736B

FASTA56464,092
        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

« Hide

References

« Hide 'large scale' references
[1]"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."
Roman D.G., Dancis A., Anderson G.J., Klausner R.D.
Mol. Cell. Biol. 13:4342-4350(1993) [PubMed: 8321236] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The genome sequence of Schizosaccharomyces pombe."
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. expand/collapse author list , 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.
Nature 415:871-880(2002) [PubMed: 11859360] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 972 / ATCC 24843.
[3]"Phosphoproteome analysis of fission yeast."
Wilson-Grady J.T., Villen J., Gygi S.P.
J. Proteome Res. 7:1088-1097(2008) [PubMed: 18257517] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-362; SER-381 AND SER-383, MASS SPECTROMETRY.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		L07749 Genomic DNA. Translation: AAA68045.1.
CU329671 Genomic DNA. Translation: CAB91171.1.
PIRA48141.
RefSeqNP_595065.1. NM_001020971.1.

3D structure databases

ProteinModelPortalQ04800.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPBC1683.09c.1; SPBC1683.09c.1:pep; SPBC1683.09c.
GeneID2539711.
GenomeReviewsGene locus frp1 in contig CU329671_GR.
KEGGspo:SPBC1683.09c.
NMPDRfig|4896.1.peg.931.

Organism-specific databases

GeneDB_SpombeSPBC1683.09c.

Phylogenomic databases

eggNOGfuNOG09525.
GeneTreeEFGT00050000003069.
HOGENOMHBG208126.
OMAGISHALI.
OrthoDBEOG4N6056.

Enzyme and pathway databases

BioCycSPOM-XXX-01:SPOM-XXX-01-003170-MONOMER.

Gene expression databases

ArrayExpressQ04800.

Family and domain databases

InterProIPR013112. FAD-bd_8.
IPR017927. Fd_Rdtase_FAD-bd.
IPR013121. Fe_red_NAD-bd_6.
IPR013130. Flavoprotein_TM.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
KOK00521.
PfamPF08022. FAD_binding_8. 1 hit.
PF01794. Ferric_reduct. 1 hit.
PF08030. NAD_binding_6. 1 hit.
[Graphical view]
SUPFAMSSF63380. Riboflavin_synthase_like_b-brl. 1 hit.
PROSITEPS51384. FAD_FR. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFRP1_SCHPO
AccessionPrimary (citable) accession number: Q04800
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: December 14, 2011
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents