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UniProtKB - Q04800 (FRP1_SCHPO)

Entry version 160 (23 Feb 2022)
Sequence version 1 (01 Feb 1994)
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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

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Protein has several cofactor binding sites:

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi157Iron (heme 1 axial ligand)By similarity1
Metal bindingi171Iron (heme 2 axial ligand)By similarity1
Metal bindingi225Iron (heme 1 axial ligand)By similarity1
Metal bindingi239Iron (heme 2 axial ligand)By similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi317 – 323FADSequence analysis7
Nucleotide bindingi419 – 427NADSequence analysis9

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionOxidoreductase
Biological processElectron transport, Ion transport, Iron transport, Transport
LigandFAD, Flavoprotein, Heme, Iron, Metal-binding, NADP

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Ferric reductase transmembrane component 1Curated (EC:1.16.1.9By similarity)
Alternative name(s):
Ferric-chelate reductase 1Curated
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:frp1
ORF Names:SPBC1683.09c
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri284812 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces ›
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002485 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome II

Organism-specific databases

Schizosaccharomyces pombe database

More...PomBasei		SPBC1683.09c, frp1

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		FungiDB:SPBC1683.09c

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei10 – 30HelicalSequence analysisAdd BLAST21
Transmembranei73 – 93HelicalSequence analysisAdd BLAST21
Transmembranei117 – 137HelicalSequence analysisAdd BLAST21
Transmembranei160 – 180HelicalSequence analysisAdd BLAST21
Transmembranei193 – 213HelicalSequence analysisAdd BLAST21
Transmembranei417 – 437HelicalSequence analysisAdd BLAST21

Keywords - Cellular componenti

Cell membrane, Membrane

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002101521 – 564Ferric reductase transmembrane component 1Add BLAST564

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi4N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi111N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi268N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi360N-linked (GlcNAc...) asparagineSequence analysis1
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei362Phosphoserine1 Publication1
Modified residuei381Phosphoserine1 Publication1
Modified residuei383Phosphoserine1 Publication1
Glycosylationi501N-linked (GlcNAc...) asparagineSequence analysis1

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

MaxQB - The MaxQuant DataBase

More...MaxQBi		Q04800

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		Q04800

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		Q04800

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		276264, 23 interactors

STRING: functional protein association networks

More...STRINGi		4896.SPBC1683.09c.1

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		Q04800

Database of comparative protein structure models

More...ModBasei		Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini121 – 254Ferric oxidoreductaseSequence analysisAdd BLAST134
Domaini255 – 410FAD-binding FR-typePROSITE-ProRule annotationAdd BLAST156

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the ferric reductase (FRE) family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG0039, Eukaryota

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_035348_0_0_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q04800

Identification of Orthologs from Complete Genome Data

More...OMAi		YMYATFA

Database for complete collections of gene phylogenies

More...PhylomeDBi		Q04800

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.40.50.80, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR013112, FAD-bd_8
IPR017927, FAD-bd_FR_type
IPR013130, Fe3_Rdtase_TM_dom
IPR013121, Fe_red_NAD-bd_6
IPR039261, FNR_nucleotide-bd
IPR017938, Riboflavin_synthase-like_b-brl

Pfam protein domain database

More...Pfami		View protein in Pfam
PF08022, FAD_binding_8, 1 hit
PF01794, Ferric_reduct, 1 hit
PF08030, NAD_binding_6, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF52343, SSF52343, 1 hit
SSF63380, SSF63380, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS51384, FAD_FR, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i336CC2AF934A736B
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
L07749 Genomic DNA Translation: AAA68045.1
CU329671 Genomic DNA Translation: CAB91171.1

Protein sequence database of the Protein Information Resource

More...PIRi		A48141

NCBI Reference Sequences

More...RefSeqi		NP_595065.1, NM_001020971.2

Genome annotation databases

Ensembl fungal genome annotation project

More...EnsemblFungii		SPBC1683.09c.1; SPBC1683.09c.1:pep; SPBC1683.09c

Database of genes from NCBI RefSeq genomes

More...GeneIDi		2539711

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		spo:SPBC1683.09c

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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

SMRiQ04800
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi276264, 23 interactors
STRINGi4896.SPBC1683.09c.1

PTM databases

iPTMnetiQ04800

Proteomic databases

MaxQBiQ04800
PaxDbiQ04800

Genome annotation databases

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

Organism-specific databases

PomBaseiSPBC1683.09c, frp1
VEuPathDBiFungiDB:SPBC1683.09c

Phylogenomic databases

eggNOGiKOG0039, Eukaryota
HOGENOMiCLU_035348_0_0_1
InParanoidiQ04800
OMAiYMYATFA
PhylomeDBiQ04800

Miscellaneous databases

Protein Ontology

More...PROi		PR:Q04800

Family and domain databases

Gene3Di3.40.50.80, 1 hit
InterProiView protein in InterPro
IPR013112, FAD-bd_8
IPR017927, FAD-bd_FR_type
IPR013130, Fe3_Rdtase_TM_dom
IPR013121, Fe_red_NAD-bd_6
IPR039261, FNR_nucleotide-bd
IPR017938, Riboflavin_synthase-like_b-brl
PfamiView protein in Pfam
PF08022, FAD_binding_8, 1 hit
PF01794, Ferric_reduct, 1 hit
PF08030, NAD_binding_6, 1 hit
SUPFAMiSSF52343, SSF52343, 1 hit
SSF63380, SSF63380, 1 hit
PROSITEiView protein in PROSITE
PS51384, FAD_FR, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiFRP1_SCHPO
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q04800
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: February 23, 2022
This is version 160 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Reference proteome

Documents

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