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UniProtKB - P38071 (ETR1_YEAST)

Entry version 165 (13 Feb 2019)
Sequence version 3 (17 Oct 2006)
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Protein

Enoyl-[acyl-carrier-protein] reductase, mitochondrial

Gene

ETR1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's 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

Catalyzes the NADPH-dependent reduction of trans-2-enoyl thioesters in mitochondrial fatty acid synthesis (fatty acid synthesis type II). Fatty acid chain elongation in mitochondria uses acyl carrier protein (ACP) as an acyl group carrier, but the enzyme accepts both ACP and CoA thioesters as substrates in vitro. Required for respiration and the maintenance of the mitochondrial compartment.2 Publications

Miscellaneous

Present with 1560 molecules/cell in log phase SD medium.1 Publication

Caution

Was originally (PubMed:8195160) thought to be a nuclear protein involved in transcriptional regulation of genes required for the functional assembly of mitochondrial respiratory proteins. This was later proven not to be the case (PubMed:11509667).2 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei73Proton donorBy similarity1
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei157NADPBy similarity1
Binding sitei373NADPBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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 bindingi185 – 188NADPBy similarity4
Nucleotide bindingi208 – 210NADPBy similarity3
Nucleotide bindingi283 – 286NADPBy similarity4
Nucleotide bindingi308 – 310NADPBy similarity3

<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

  • DNA binding Source: UniProtKB-KW
  • enoyl-[acyl-carrier-protein] reductase activity Source: SGD
  • trans-2-enoyl-CoA reductase (NADPH) activity Source: GO_Central
View the complete GO annotation on QuickGO ...

GO - Biological processi

  • aerobic respiration Source: SGD
  • fatty acid biosynthetic process Source: SGD
  • fatty acid metabolic process Source: GO_Central
View the 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 functionDNA-binding, Oxidoreductase
Biological processFatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism
LigandNADP

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		MetaCyc:G3O-29006-MONOMER
YEAST:G3O-29006-MONOMER

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		1.3.1.10 984

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-SCE-6798695 Neutrophil degranulation
R-SCE-6803205 TP53 regulates transcription of several additional cell death genes whose specific roles in p53-dependent apoptosis remain uncertain
R-SCE-77346 Beta oxidation of decanoyl-CoA to octanoyl-CoA-CoA

Chemistry databases

SwissLipids knowledge resource for lipid biology

More...SwissLipidsi		SLP:000001784

<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_and_taxonomy_section">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:
Enoyl-[acyl-carrier-protein] reductase, mitochondrialCurated (EC:1.3.1.1042 Publications)
Alternative name(s):
2-enoyl thioester reductase1 Publication
Mitochondrial respiratory function protein 11 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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:ETR1
Synonyms:MRF1, MRF1'
Ordered Locus Names:YBR026C
ORF Names:YBR0310
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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>OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 identifieri559292 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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
  • UP000002311 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">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

Eukaryotic Pathogen Database Resources

More...EuPathDBi		FungiDB:YBR026C

Saccharomyces Genome Database

More...SGDi		S000000230 ETR1

<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

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Mitochondrion

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi73Y → N: 0.1% of catalytic activity. No specific ARS1 binding. 1 Publication1

<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 transit peptide.<p><a href='/help/transit' target='_top'>More...</a></p>Transit peptidei1 – 9Mitochondrion1 Publication9
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000016092410 – 380Enoyl-[acyl-carrier-protein] reductase, mitochondrialAdd BLAST371

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 residuei339PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQB - The MaxQuant DataBase

More...MaxQBi		P38071

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

More...PaxDbi		P38071

PRoteomics IDEntifications database

More...PRIDEi		P38071

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P38071

<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

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer or in a complex with other proteins (PubMed:11509667). Interacts with ARS1 (PubMed:8195160).2 Publications

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		32729, 394 interactors

Protein interaction database and analysis system

More...IntActi		P38071, 2 interactors

Molecular INTeraction database

More...MINTi		P38071

STRING: functional protein association networks

More...STRINGi		4932.YBR026C

<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

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...ProteinModelPortali		P38071

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

More...SMRi		P38071

Database of comparative protein structure models

More...ModBasei		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		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

<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 zinc-containing alcohol dehydrogenase family. Quinone oxidoreductase subfamily.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

Ensembl GeneTree

More...GeneTreei		ENSGT00940000156592

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000294683

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P38071

KEGG Orthology (KO)

More...KOi		K07512

Identification of Orthologs from Complete Genome Data

More...OMAi		KPKFPAV

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR013149 ADH_C
IPR011032 GroES-like_sf
IPR036291 NAD(P)-bd_dom_sf

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00107 ADH_zinc_N, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF50129 SSF50129, 1 hit
SSF51735 SSF51735, 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_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P38071-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MLPTFKRYMS SSAHQIPKHF KSLIYSTHEV EDCTKVLSVK NYTPKQDLSQ 
        60         70         80         90        100
SIVLKTLAFP INPSDINQLQ GVYPSRPEKT YDYSTDEPAA IAGNEGVFEV 
       110        120        130        140        150
VSLPSGSSKG DLKLGDRVIP LQANQGTWSN YRVFSSSSDL IKVNDLDLFS 
       160        170        180        190        200
AATVSVNGCT GFQLVSDYID WNSNGNEWII QNAGTSSVSK IVTQVAKAKG 
       210        220        230        240        250
IKTLSVIRDR DNFDEVAKVL EDKYGATKVI SESQNNDKTF AKEVLSKILG 
       260        270        280        290        300
ENARVRLALN SVGGKSSASI ARKLENNALM LTYGGMSKQP VTLPTSLHIF 
       310        320        330        340        350
KGLTSKGYWV TEKNKKNPQS KIDTISDFIK MYNYGHIISP RDEIETLTWN 
       360        370        380
TNTTTDEQLL ELVKKGITGK GKKKMVVLEW
Length:380
Mass (Da):42,067
Last modified:October 17, 2006 - v3
<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:i9795013283C3E9F8
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti24I → T in AAS56198 (PubMed:17322287).Curated1

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
D26606 Genomic DNA Translation: BAA05651.1
Z35895 Genomic DNA Translation: CAA84968.1
X76078 Genomic DNA Translation: CAA53683.1
AY557872 Genomic DNA Translation: AAS56198.1
BK006936 Genomic DNA Translation: DAA07148.1

NCBI Reference Sequences

More...RefSeqi		NP_009582.1, NM_001178374.1

Genome annotation databases

Ensembl fungal genome annotation project

More...EnsemblFungii		YBR026C_mRNA; YBR026C_mRNA; YBR026C

Database of genes from NCBI RefSeq genomes

More...GeneIDi		852314

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		sce:YBR026C

<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
D26606 Genomic DNA Translation: BAA05651.1
Z35895 Genomic DNA Translation: CAA84968.1
X76078 Genomic DNA Translation: CAA53683.1
AY557872 Genomic DNA Translation: AAS56198.1
BK006936 Genomic DNA Translation: DAA07148.1
RefSeqiNP_009582.1, NM_001178374.1

3D structure databases

ProteinModelPortaliP38071
SMRiP38071
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32729, 394 interactors
IntActiP38071, 2 interactors
MINTiP38071
STRINGi4932.YBR026C

Chemistry databases

SwissLipidsiSLP:000001784

PTM databases

iPTMnetiP38071

Proteomic databases

MaxQBiP38071
PaxDbiP38071
PRIDEiP38071

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYBR026C_mRNA; YBR026C_mRNA; YBR026C
GeneIDi852314
KEGGisce:YBR026C

Organism-specific databases

EuPathDBiFungiDB:YBR026C
SGDiS000000230 ETR1

Phylogenomic databases

GeneTreeiENSGT00940000156592
HOGENOMiHOG000294683
InParanoidiP38071
KOiK07512
OMAiKPKFPAV

Enzyme and pathway databases

BioCyciMetaCyc:G3O-29006-MONOMER
YEAST:G3O-29006-MONOMER
BRENDAi1.3.1.10 984
ReactomeiR-SCE-6798695 Neutrophil degranulation
R-SCE-6803205 TP53 regulates transcription of several additional cell death genes whose specific roles in p53-dependent apoptosis remain uncertain
R-SCE-77346 Beta oxidation of decanoyl-CoA to octanoyl-CoA-CoA

Miscellaneous databases

Protein Ontology

More...PROi		PR:P38071

Family and domain databases

InterProiView protein in InterPro
IPR013149 ADH_C
IPR011032 GroES-like_sf
IPR036291 NAD(P)-bd_dom_sf
PfamiView protein in Pfam
PF00107 ADH_zinc_N, 1 hit
SUPFAMiSSF50129 SSF50129, 1 hit
SSF51735 SSF51735, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		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 nameiETR1_YEAST
<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: P38071
Secondary accession number(s): D6VQ28, Q6Q5P2
<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_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 17, 2006
Last modified: February 13, 2019
This is version 165 of the entry and version 3 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  2. Yeast chromosome II
    Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names
  3. SIMILARITY comments
    Index of protein domains and families
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