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Entry version 158 (13 Nov 2019)
Sequence version 2 (18 Mar 2008)
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Protein

Trifunctional enzyme subunit alpha, mitochondrial

Gene

Hadha

Organism
Rattus norvegicus (Rat)
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

Mitochondrial trifunctional enzyme catalyzes the last three of the four reactions of the mitochondrial beta-oxidation pathway. The mitochondrial beta-oxidation pathway is the major energy-producing process in tissues and is performed through four consecutive reactions breaking down fatty acids into acetyl-CoA. Among the enzymes involved in this pathway, the trifunctional enzyme exhibits specificity for long-chain fatty acids. Mitochondrial trifunctional enzyme is a heterotetrameric complex composed of two proteins, the trifunctional enzyme subunit alpha/HADHA described here carries the 2,3-enoyl-CoA hydratase and the 3-hydroxyacyl-CoA dehydrogenase activities while the trifunctional enzyme subunit beta/HADHB bears the 3-ketoacyl-CoA thiolase activity. Independently of the subunit beta, the trifunctional enzyme subunit alpha/HADHA also has a monolysocardiolipin acyltransferase activity. It acylates monolysocardiolipin into cardiolipin, a major mitochondrial membrane phospholipid which plays a key role in apoptosis and supports mitochondrial respiratory chain complexes in the generation of ATP. Allows the acylation of monolysocardiolipin with different acyl-CoA substrates including oleoyl-CoA for which it displays the highest activity.By similarity

<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

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: fatty acid beta-oxidation

This protein is involved in the pathway fatty acid beta-oxidation, which is part of Lipid metabolism.By similarity
View all proteins of this organism that are known to be involved in the pathway fatty acid beta-oxidation and in Lipid metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei151Important for long-chain enoyl-CoA hydratase activityBy similarity1
Sitei173Important for long-chain enoyl-CoA hydratase activityBy similarity1
Sitei498Important for hydroxyacyl-coenzyme A dehydrogenase activityBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> 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 sitei510For hydroxyacyl-coenzyme A dehydrogenase activityBy similarity1

<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

GO - Biological processi

<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 functionLyase, Multifunctional enzyme, Oxidoreductase, Transferase
Biological processFatty acid metabolism, Lipid metabolism
LigandNAD

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
1.1.1.211 5301
2.3.1.16 5301

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-RNO-1482798 Acyl chain remodeling of CL
R-RNO-77285 Beta oxidation of myristoyl-CoA to lauroyl-CoA
R-RNO-77305 Beta oxidation of palmitoyl-CoA to myristoyl-CoA
R-RNO-77310 Beta oxidation of lauroyl-CoA to decanoyl-CoA-CoA
R-RNO-77346 Beta oxidation of decanoyl-CoA to octanoyl-CoA-CoA
R-RNO-77348 Beta oxidation of octanoyl-CoA to hexanoyl-CoA
R-RNO-77350 Beta oxidation of hexanoyl-CoA to butanoyl-CoA

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00659

<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:
Trifunctional enzyme subunit alpha, mitochondrial
Alternative name(s):
Monolysocardiolipin acyltransferaseBy similarity (EC:2.3.1.-By similarity)
TP-alpha
Including the following 2 domains:
Long-chain enoyl-CoA hydratase (EC:4.2.1.17By similarity)
Long chain 3-hydroxyacyl-CoA dehydrogenase (EC:1.1.1.211By similarity)
<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:Hadha
<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>OrganismiRattus norvegicus (Rat)
<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 identifieri10116 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
<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
  • UP000002494 <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 6

Organism-specific databases

Rat genome database

More...
RGDi
620512 Hadha

<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 Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner 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 transit peptide.<p><a href='/help/transit' target='_top'>More...</a></p>Transit peptidei1 – 36MitochondrionSequence analysisAdd BLAST36
<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_000000740537 – 763Trifunctional enzyme subunit alpha, mitochondrialAdd BLAST727

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 residuei46N6-acetyllysine; alternateBy similarity1
Modified residuei46N6-succinyllysine; alternateBy similarity1
Modified residuei60N6-acetyllysine; alternateBy similarity1
Modified residuei60N6-succinyllysine; alternateBy similarity1
Modified residuei129N6-acetyllysineBy similarity1
Modified residuei166N6-acetyllysine; alternateBy similarity1
Modified residuei166N6-succinyllysine; alternateBy similarity1
Modified residuei213N6-succinyllysineBy similarity1
Modified residuei214N6-acetyllysine; alternateBy similarity1
Modified residuei214N6-succinyllysine; alternateBy similarity1
Modified residuei230N6-succinyllysineBy similarity1
Modified residuei231PhosphoserineBy similarity1
Modified residuei249N6-acetyllysine; alternateBy similarity1
Modified residuei249N6-succinyllysine; alternateBy similarity1
Modified residuei289N6-acetyllysineBy similarity1
Modified residuei295N6-acetyllysineBy similarity1
Modified residuei303N6-acetyllysine; alternateBy similarity1
Modified residuei303N6-succinyllysine; alternateBy similarity1
Modified residuei326N6-acetyllysine; alternateBy similarity1
Modified residuei326N6-succinyllysine; alternateBy similarity1
Modified residuei334N6-acetyllysine; alternateBy similarity1
Modified residuei334N6-succinyllysine; alternateBy similarity1
Modified residuei350N6-acetyllysine; alternateBy similarity1
Modified residuei350N6-succinyllysine; alternateBy similarity1
Modified residuei353N6-acetyllysineBy similarity1
Modified residuei395PhosphothreonineBy similarity1
Modified residuei399Omega-N-methylarginineBy similarity1
Modified residuei406N6-acetyllysine; alternateBy similarity1
Modified residuei406N6-succinyllysine; alternateBy similarity1
Modified residuei411N6-acetyllysine; alternateBy similarity1
Modified residuei411N6-succinyllysine; alternateBy similarity1
Modified residuei415N6-succinyllysineBy similarity1
Modified residuei419PhosphoserineCombined sources1
Modified residuei436N6-acetyllysine; alternateBy similarity1
Modified residuei436N6-succinyllysine; alternateBy similarity1
Modified residuei440N6-succinyllysineBy similarity1
Modified residuei460N6-acetyllysine; alternateBy similarity1
Modified residuei460N6-succinyllysine; alternateBy similarity1
Modified residuei505N6-acetyllysine; alternateBy similarity1
Modified residuei505N6-succinyllysine; alternateBy similarity1
Modified residuei519N6-acetyllysine; alternateBy similarity1
Modified residuei519N6-succinyllysine; alternateBy similarity1
Modified residuei540N6-acetyllysineBy similarity1
Modified residuei569N6-acetyllysine; alternateBy similarity1
Modified residuei569N6-succinyllysine; alternateBy similarity1
Modified residuei620N6-succinyllysineBy similarity1
Modified residuei634N6-succinyllysineBy similarity1
Modified residuei644N6-acetyllysine; alternateBy similarity1
Modified residuei644N6-succinyllysine; alternateBy similarity1
Modified residuei646N6-succinyllysineBy similarity1
Modified residuei650PhosphoserineCombined sources1
Modified residuei664N6-acetyllysine; alternateBy similarity1
Modified residuei664N6-succinyllysine; alternateBy similarity1
Modified residuei728N6-acetyllysine; alternateBy similarity1
Modified residuei728N6-succinyllysine; alternateBy similarity1
Modified residuei735N6-acetyllysineBy similarity1
Modified residuei759N6-acetyllysine; alternateBy similarity1
Modified residuei759N6-succinyllysine; alternateBy similarity1

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
Q64428

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

More...
PaxDbi
Q64428

PRoteomics IDEntifications database

More...
PRIDEi
Q64428

PTM databases

CarbonylDB database of protein carbonylation sites

More...
CarbonylDBi
Q64428

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q64428

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
Q64428

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
Q64428

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSRNOG00000024629 Expressed in 10 organ(s), highest expression level in heart

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q64428 RN

<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

Heterotetramer of 2 alpha/HADHA and 2 beta/HADHB subunits; forms the mitochondrial trifunctional enzyme (By similarity). Also purified as higher order heterooligomers including a 4 alpha/HADHA and 4 beta/HADHB heterooligomer which physiological significance remains unclear (PubMed:1730633).

By similarity1 Publication

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
250974, 3 interactors

Protein interaction database and analysis system

More...
IntActi
Q64428, 3 interactors

Molecular INTeraction database

More...
MINTi
Q64428

STRING: functional protein association networks

More...
STRINGi
10116.ENSRNOP00000038073

<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
Q64428

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

<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

In the N-terminal section; belongs to the enoyl-CoA hydratase/isomerase family.Curated
In the central section; belongs to the 3-hydroxyacyl-CoA dehydrogenase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG1683 Eukaryota
COG1024 LUCA
COG1250 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000154677

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000027939

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q64428

KEGG Orthology (KO)

More...
KOi
K07515

Identification of Orthologs from Complete Genome Data

More...
OMAi
PFRYMDT

Database of Orthologous Groups

More...
OrthoDBi
219667at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q64428

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR006180 3-OHacyl-CoA_DH_CS
IPR006176 3-OHacyl-CoA_DH_NAD-bd
IPR006108 3HC_DH_C
IPR008927 6-PGluconate_DH-like_C_sf
IPR029045 ClpP/crotonase-like_dom_sf
IPR018376 Enoyl-CoA_hyd/isom_CS
IPR001753 Enoyl-CoA_hydra/iso
IPR012803 Fa_ox_alpha_mit
IPR036291 NAD(P)-bd_dom_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00725 3HCDH, 2 hits
PF02737 3HCDH_N, 1 hit
PF00378 ECH_1, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF48179 SSF48179, 2 hits
SSF51735 SSF51735, 1 hit
SSF52096 SSF52096, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR02441 fa_ox_alpha_mit, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00067 3HCDH, 1 hit
PS00166 ENOYL_COA_HYDRATASE, 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>. 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_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.

Q64428-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MVASRAIGSL SRFSAFRILR SRGCICHSFT TSSALLSRTH INYGVKGDVA
60 70 80 90 100
VIRINSPNSK VNTLNKEVQS EFVEVMNEIW ANDQIRSAVL ISSKPGCFVA
110 120 130 140 150
GADINMLASC TTPQEAARIS QEGQKMFEKL EKSPKPVVAA ISGSCLGGGL
160 170 180 190 200
ELAIACQYRI ATKDRKTVLG VPEVLLGILP GAGGTQRLPK MVGVPAAFDM
210 220 230 240 250
MLTGRNIRAD RAKKMGLVDQ LVDPLGPGIK SPEERTIEYL EEVAVNFAKG
260 270 280 290 300
LADRKVSAKQ SKGLMEKLTS YAMTIPFVRQ QVYKTVEEKV KKQTKGLYPA
310 320 330 340 350
PLKIIDAVKT GLEQGNDAGY LAESEKFGEL ALTKESKALM GLYNGQVLCK
360 370 380 390 400
KNKFGAPQKT VQQLAILGAG LMGAGIAQVS VDKGLKTLLK DTTVTGLGRG
410 420 430 440 450
QQQVFKGLND KVKKKALTSF ERDSIFSNLI GQLDYKGFEK ADMVIEAVFE
460 470 480 490 500
DLAVKHKVLK EVESVTPEHC IFASNTSALP INQIAAVSQR PEKVIGMHYF
510 520 530 540 550
SPVDKMQLLE IITTDKTSKD TTASAVAVGL KQGKVIIVVK DGPGFYTTRC
560 570 580 590 600
LAPMMSEVIR ILQEGVDPKK LDALTTGFGF PVGAATLADE VGIDVAQHVA
610 620 630 640 650
EDLGKAFGER FGGGSVELLK LMVSKGFLGR KSGKGFYIYQ SGSKNKNLNS
660 670 680 690 700
EIDNILVNLR LPAKPEVSSD EDIQYRVITR FVNEAVLCLQ EGILATPEEG
710 720 730 740 750
DIGAVFGLGF PPCLGGPFRF VDLYGAQKVV DRLRKYESAY GTQFTPCQLL
760
RDLANNSSKK FYQ
Length:763
Mass (Da):82,665
Last modified:March 18, 2008 - v2
<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:iA16648B82AE7D62E
GO

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence BAA03939 differs from that shown. Reason: Frameshift.Curated

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
D16478 mRNA Translation: BAA03939.1 Frameshift.
BC091697 mRNA Translation: AAH91697.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A49681

NCBI Reference Sequences

More...
RefSeqi
NP_570839.2, NM_130826.2

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSRNOT00000038649; ENSRNOP00000038073; ENSRNOG00000024629

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
170670

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
rno:170670

UCSC genome browser

More...
UCSCi
RGD:620512 rat

<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
D16478 mRNA Translation: BAA03939.1 Frameshift.
BC091697 mRNA Translation: AAH91697.1
PIRiA49681
RefSeqiNP_570839.2, NM_130826.2

3D structure databases

SMRiQ64428
ModBaseiSearch...

Protein-protein interaction databases

BioGridi250974, 3 interactors
IntActiQ64428, 3 interactors
MINTiQ64428
STRINGi10116.ENSRNOP00000038073

PTM databases

CarbonylDBiQ64428
iPTMnetiQ64428
PhosphoSitePlusiQ64428
SwissPalmiQ64428

Proteomic databases

jPOSTiQ64428
PaxDbiQ64428
PRIDEiQ64428

Genome annotation databases

EnsembliENSRNOT00000038649; ENSRNOP00000038073; ENSRNOG00000024629
GeneIDi170670
KEGGirno:170670
UCSCiRGD:620512 rat

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
3030
RGDi620512 Hadha

Phylogenomic databases

eggNOGiKOG1683 Eukaryota
COG1024 LUCA
COG1250 LUCA
GeneTreeiENSGT00940000154677
HOGENOMiHOG000027939
InParanoidiQ64428
KOiK07515
OMAiPFRYMDT
OrthoDBi219667at2759
PhylomeDBiQ64428

Enzyme and pathway databases

UniPathwayiUPA00659
BRENDAi1.1.1.211 5301
2.3.1.16 5301
ReactomeiR-RNO-1482798 Acyl chain remodeling of CL
R-RNO-77285 Beta oxidation of myristoyl-CoA to lauroyl-CoA
R-RNO-77305 Beta oxidation of palmitoyl-CoA to myristoyl-CoA
R-RNO-77310 Beta oxidation of lauroyl-CoA to decanoyl-CoA-CoA
R-RNO-77346 Beta oxidation of decanoyl-CoA to octanoyl-CoA-CoA
R-RNO-77348 Beta oxidation of octanoyl-CoA to hexanoyl-CoA
R-RNO-77350 Beta oxidation of hexanoyl-CoA to butanoyl-CoA

Miscellaneous databases

Protein Ontology

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PROi
PR:Q64428

Gene expression databases

BgeeiENSRNOG00000024629 Expressed in 10 organ(s), highest expression level in heart
GenevisibleiQ64428 RN

Family and domain databases

InterProiView protein in InterPro
IPR006180 3-OHacyl-CoA_DH_CS
IPR006176 3-OHacyl-CoA_DH_NAD-bd
IPR006108 3HC_DH_C
IPR008927 6-PGluconate_DH-like_C_sf
IPR029045 ClpP/crotonase-like_dom_sf
IPR018376 Enoyl-CoA_hyd/isom_CS
IPR001753 Enoyl-CoA_hydra/iso
IPR012803 Fa_ox_alpha_mit
IPR036291 NAD(P)-bd_dom_sf
PfamiView protein in Pfam
PF00725 3HCDH, 2 hits
PF02737 3HCDH_N, 1 hit
PF00378 ECH_1, 1 hit
SUPFAMiSSF48179 SSF48179, 2 hits
SSF51735 SSF51735, 1 hit
SSF52096 SSF52096, 1 hit
TIGRFAMsiTIGR02441 fa_ox_alpha_mit, 1 hit
PROSITEiView protein in PROSITE
PS00067 3HCDH, 1 hit
PS00166 ENOYL_COA_HYDRATASE, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<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 nameiECHA_RAT
<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: Q64428
Secondary accession number(s): Q5BIZ5
<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: November 1, 1997
Last sequence update: March 18, 2008
Last modified: November 13, 2019
This is version 158 of the entry and version 2 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 programChordata 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, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
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