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Protein

Ferric/cupric reductase transmembrane component 2

Gene

frp2

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

Functioni

Metalloreductase responsible for reducing extracellular iron and copper prior to import (By similarity). Catalyzes the reductive uptake of Fe3+-salts and Fe3+ bound to catecholate or hydroxamate siderophores (By similarity). Fe3+ is reduced to Fe2+, which then dissociates from the siderophore and can be imported by the high-affinity Fe2+ transport complex in the plasma membrane (By similarity). Also participates in Cu2+ reduction and Cu+ uptake (By similarity).By similarity

Catalytic activityi

2 Fe(II)-siderophore + NADP+ + H+ = 2 Fe(III)-siderophore + NADPH.By similarity

Cofactori

Protein has several cofactor binding sites:
  • FADBy similarity
  • hemeBy similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi150 – 1501Iron (heme 1 axial ligand)By similarity
Metal bindingi164 – 1641Iron (heme 2 axial ligand)By similarity
Metal bindingi218 – 2181Iron (heme 1 axial ligand)By similarity
Metal bindingi232 – 2321Iron (heme 2 axial ligand)By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi310 – 3167FADSequence analysis
Nucleotide bindingi419 – 4279NADSequence analysis

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Electron transport, Ion transport, Iron transport, Transport

Keywords - Ligandi

FAD, Flavoprotein, Heme, Iron, Metal-binding, NADP

Names & Taxonomyi

Protein namesi
Recommended name:
Ferric/cupric reductase transmembrane component 2Curated (EC:1.16.1.9By similarity)
Alternative name(s):
Ferric-chelate reductase 2Curated
Gene namesi
Name:frp2
ORF Names:SPBC947.05c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:SPBC947.05c.
PomBaseiSPBC947.05c. frp2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei10 – 3021HelicalSequence analysisAdd
BLAST
Transmembranei66 – 8621HelicalSequence analysisAdd
BLAST
Transmembranei110 – 13021HelicalSequence analysisAdd
BLAST
Transmembranei152 – 17221HelicalSequence analysisAdd
BLAST
Transmembranei184 – 20421HelicalSequence analysisAdd
BLAST
Transmembranei210 – 23021HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 564564Ferric/cupric reductase transmembrane component 2PRO_0000337260Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi106 – 1061N-linked (GlcNAc...)Sequence analysis
Glycosylationi261 – 2611N-linked (GlcNAc...)Sequence analysis
Glycosylationi350 – 3501N-linked (GlcNAc...)Sequence analysis
Glycosylationi442 – 4421N-linked (GlcNAc...)Sequence analysis
Glycosylationi496 – 4961N-linked (GlcNAc...)Sequence analysis
Glycosylationi548 – 5481N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiO94727.

PTM databases

SwissPalmiO94727.

Interactioni

Protein-protein interaction databases

BioGridi277741. 14 interactions.
MINTiMINT-4686541.

Structurei

3D structure databases

ProteinModelPortaliO94727.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini114 – 229116Ferric oxidoreductaseSequence analysisAdd
BLAST
Domaini254 – 410157FAD-binding FR-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the ferric reductase (FRE) family.Curated
Contains 1 FAD-binding FR-type domain.PROSITE-ProRule annotation
Contains 1 ferric oxidoreductase domain.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

HOGENOMiHOG000112645.
InParanoidiO94727.
OMAiNITIHIT.
OrthoDBiEOG75TMMM.
PhylomeDBiO94727.

Family and domain databases

InterProiIPR000778. Cyt_b245_heavy_chain.
IPR013112. FAD-bd_8.
IPR017927. Fd_Rdtase_FAD-bd.
IPR013130. Fe3_Rdtase_TM_dom.
IPR013121. Fe_red_NAD-bd_6.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PfamiPF08022. FAD_binding_8. 1 hit.
PF01794. Ferric_reduct. 1 hit.
PF08030. NAD_binding_6. 1 hit.
[Graphical view]
PRINTSiPR00466. GP91PHOX.
SUPFAMiSSF63380. SSF63380. 1 hit.
PROSITEiPS51384. FAD_FR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O94727-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MILARDDKWT LGSIALIFVL LIGFALLFLL ERFRVKEKSR TFKDCVNVYQ
60 70 80 90 100
CPSKGERVYL ALRHWFIFLA THKAQMTLIL SPLVMLVTIP FTGKETKNSI
110 120 130 140 150
ASYDWNLTGV AARLGYLSCG LFFVSYFFSL KNNPFCLMLF SSHEKMNYLH
160 170 180 190 200
RWLSVYAVLI SVLHGILFMI FSAQSYKPLL YDKISIYGYF ITVVLFLMTV
210 220 230 240 250
ASLPSVRRKF FEWFFVLHHT CSVLIIFLIW LHHPRTIVYM KACIIIYAFD
260 270 280 290 300
RGCRLFRSIW NRSNFRIYLL NEDMIYMVGR KPKRSFFALP WAAGSHVYIN
310 320 330 340 350
IPSLSYWQVH PFTLASAPFD DFIELFVAVH SGFTERLANR LYSMPHEYPN
360 370 380 390 400
FSLAPGTPES LSNTYRELNS FKSYAVEIEN TAQGHTYEPE DLYLETTVFM
410 420 430 440 450
DGPYGTTSNV FKEYSYVLLI AGGVGFSYTL PILRDLILKE CNVTSITFIW
460 470 480 490 500
SCRSLSLLKV ASKSLNSLLH QSNVRLKIIN HFTGSISCKE SSEFSNQTTE
510 520 530 540 550
NSEMEFFDDR PDLDMYIQKF FDYVGYQTAA LAACGSQSFL KRIKNSVNKS
560
ISSTTDIYQH YEEL
Length:564
Mass (Da):65,262
Last modified:May 1, 1999 - v1
Checksum:i8890551FB5AAFD40
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAA17033.1.
PIRiT40777.
RefSeqiNP_595271.1. NM_001021178.1.

Genome annotation databases

EnsemblFungiiSPBC947.05c.1; SPBC947.05c.1:pep; SPBC947.05c.
GeneIDi2541227.
KEGGispo:SPBC947.05c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAA17033.1.
PIRiT40777.
RefSeqiNP_595271.1. NM_001021178.1.

3D structure databases

ProteinModelPortaliO94727.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi277741. 14 interactions.
MINTiMINT-4686541.

PTM databases

SwissPalmiO94727.

Proteomic databases

MaxQBiO94727.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBC947.05c.1; SPBC947.05c.1:pep; SPBC947.05c.
GeneIDi2541227.
KEGGispo:SPBC947.05c.

Organism-specific databases

EuPathDBiFungiDB:SPBC947.05c.
PomBaseiSPBC947.05c. frp2.

Phylogenomic databases

HOGENOMiHOG000112645.
InParanoidiO94727.
OMAiNITIHIT.
OrthoDBiEOG75TMMM.
PhylomeDBiO94727.

Miscellaneous databases

PROiO94727.

Family and domain databases

InterProiIPR000778. Cyt_b245_heavy_chain.
IPR013112. FAD-bd_8.
IPR017927. Fd_Rdtase_FAD-bd.
IPR013130. Fe3_Rdtase_TM_dom.
IPR013121. Fe_red_NAD-bd_6.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PfamiPF08022. FAD_binding_8. 1 hit.
PF01794. Ferric_reduct. 1 hit.
PF08030. NAD_binding_6. 1 hit.
[Graphical view]
PRINTSiPR00466. GP91PHOX.
SUPFAMiSSF63380. SSF63380. 1 hit.
PROSITEiPS51384. FAD_FR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "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.
    , 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  2. "ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe."
    Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.
    Nat. Biotechnol. 24:841-847(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiFRP2_SCHPO
AccessioniPrimary (citable) accession number: O94727
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: May 1, 1999
Last modified: June 8, 2016
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.