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Protein

Ferric reductase transmembrane component 1

Gene

frp1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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 bindingi157 – 1571Iron (heme 1 axial ligand)By similarity
Metal bindingi171 – 1711Iron (heme 2 axial ligand)By similarity
Metal bindingi225 – 2251Iron (heme 1 axial ligand)By similarity
Metal bindingi239 – 2391Iron (heme 2 axial ligand)By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi317 – 3237FADSequence analysis
Nucleotide bindingi419 – 4279NADSequence analysis

GO - Molecular functioni

GO - Biological processi

  • cellular response to iron ion starvation Source: PomBase
  • copper ion transmembrane transport Source: PomBase
  • iron assimilation by reduction and transport Source: PomBase
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 reductase transmembrane component 1Curated (EC:1.16.1.9By similarity)
Alternative name(s):
Ferric-chelate reductase 1Curated
Gene namesi
Name:frp1
ORF Names:SPBC1683.09c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:SPBC1683.09c.
PomBaseiSPBC1683.09c. frp1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei10 – 3021HelicalSequence analysisAdd
BLAST
Transmembranei73 – 9321HelicalSequence analysisAdd
BLAST
Transmembranei117 – 13721HelicalSequence analysisAdd
BLAST
Transmembranei160 – 18021HelicalSequence analysisAdd
BLAST
Transmembranei193 – 21321HelicalSequence analysisAdd
BLAST
Transmembranei417 – 43721HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

  • endoplasmic reticulum Source: PomBase
  • integral component of membrane Source: PomBase
  • plasma membrane Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 564564Ferric reductase transmembrane component 1PRO_0000210152Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi4 – 41N-linked (GlcNAc...)Sequence analysis
Glycosylationi111 – 1111N-linked (GlcNAc...)Sequence analysis
Glycosylationi268 – 2681N-linked (GlcNAc...)Sequence analysis
Glycosylationi360 – 3601N-linked (GlcNAc...)Sequence analysis
Modified residuei362 – 3621Phosphoserine1 Publication
Modified residuei381 – 3811Phosphoserine1 Publication
Modified residuei383 – 3831Phosphoserine1 Publication
Glycosylationi501 – 5011N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ04800.

PTM databases

iPTMnetiQ04800.

Interactioni

Protein-protein interaction databases

BioGridi276264. 22 interactions.
MINTiMINT-4693503.

Structurei

3D structure databases

ProteinModelPortaliQ04800.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini121 – 254134Ferric oxidoreductaseSequence analysisAdd
BLAST
Domaini255 – 410156FAD-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.
InParanoidiQ04800.
OrthoDBiEOG092C1B1K.
PhylomeDBiQ04800.

Family and domain databases

InterProiIPR013112. 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]
SUPFAMiSSF63380. SSF63380. 1 hit.
PROSITEiPS51384. FAD_FR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q04800-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAINSSDKWT VIAICLILGI LLAFILMFWL ERFRVIIKSN AHKHDPSDKR
60 70 80 90 100
QIWLEKYYLF VRQIYTYLVT HKVILTLIAV PVVFAISIPF IGMQTPASSH
110 120 130 140 150
GKQTTQVSTG NWSKNAVAAR LGFLACGLYV TSYFFSIKNN PFALLLISSH
160 170 180 190 200
EKMNYVHRRL SQYAIMIGAI HGFAYIGLAA QGKRALLTAR VTIIGYVILG
210 220 230 240 250
LMVIMIVSSL PFFRRRFYEW FFVLHHMCSI GFLITIWLHH RRCVVYMKVC
260 270 280 290 300
VAVYVFDRGC RMLRSFLNRS KFDVVLVEDD LIYMKGPRPK KSFFGLPWGA
310 320 330 340 350
GNHMYINIPS LSYWQIHPFT IASVPSDDFI ELFVAVRAGF TKRLAKKVSS
360 370 380 390 400
KSLSDVSDIN ISDEKIEKNG DVGIEVMERH SLSQEDLVFE SSAAKVSVLM
410 420 430 440 450
DGPYGPVSNP YKDYSYLFLF AGGVGVSYIL PIILDTIKKQ SRTVHITFVW
460 470 480 490 500
SARSSALLNI VHKSLCEAVR YTEMNINIFC HLTNSYPVEE VSSLNSQSAR
510 520 530 540 550
NYSLQYLNGR PDVNDYFKDF LHATGTQTAA LASCGSDKLL RHLKSCVNTH
560
SPSTVDLYQH YEEI
Length:564
Mass (Da):64,092
Last modified:February 1, 1994 - v1
Checksum:i336CC2AF934A736B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L07749 Genomic DNA. Translation: AAA68045.1.
CU329671 Genomic DNA. Translation: CAB91171.1.
PIRiA48141.
RefSeqiNP_595065.1. NM_001020971.2.

Genome annotation databases

EnsemblFungiiSPBC1683.09c.1; SPBC1683.09c.1:pep; SPBC1683.09c.
GeneIDi2539711.
KEGGispo:SPBC1683.09c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L07749 Genomic DNA. Translation: AAA68045.1.
CU329671 Genomic DNA. Translation: CAB91171.1.
PIRiA48141.
RefSeqiNP_595065.1. NM_001020971.2.

3D structure databases

ProteinModelPortaliQ04800.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi276264. 22 interactions.
MINTiMINT-4693503.

PTM databases

iPTMnetiQ04800.

Proteomic databases

MaxQBiQ04800.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBC1683.09c.1; SPBC1683.09c.1:pep; SPBC1683.09c.
GeneIDi2539711.
KEGGispo:SPBC1683.09c.

Organism-specific databases

EuPathDBiFungiDB:SPBC1683.09c.
PomBaseiSPBC1683.09c. frp1.

Phylogenomic databases

HOGENOMiHOG000112645.
InParanoidiQ04800.
OrthoDBiEOG092C1B1K.
PhylomeDBiQ04800.

Miscellaneous databases

PROiQ04800.

Family and domain databases

InterProiIPR013112. 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]
SUPFAMiSSF63380. SSF63380. 1 hit.
PROSITEiPS51384. FAD_FR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiFRP1_SCHPO
AccessioniPrimary (citable) accession number: Q04800
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: September 7, 2016
This is version 129 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.