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UniProtKB - P12785 (FAS_RAT)

Entry version 202 (25 May 2022)
Sequence version 3 (01 Nov 1997)
Previous versions | rss
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Protein

Fatty acid synthase

Gene

Fasn

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

Fatty acid synthetase is a multifunctional enzyme that catalyzes the de novo biosynthesis of long-chain saturated fatty acids starting from acetyl-CoA and malonyl-CoA in the presence of NADPH. This multifunctional protein contains 7 catalytic activities and a site for the binding of the prosthetic group 4'-phosphopantetheine of the acyl carrier protein ([ACP]) domain.

1 Publication4 Publications

<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 <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Cerulenin, a potent non-competitive pharmacological inhibitor of FAS, binds covalently to the active site of the condensing enzyme region, inactivating a key enzyme step in fatty acid synthesis (PubMed:16969344). Another inhibitor, though less efficient, is C75, a member of the alpha-methylene-gamma-butyrolactone chemical class, also proposed as an antitumour and anti-obesity agent (PubMed:15715522).2 Publications

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. Vmax=300 nmol/min/mg enzyme for the overall fatty acid synthase reaction1 Publication
  2. Vmax=900 nmol/min/mg enzyme for the beta-ketoacyl reductase reaction of acetoacetyl-CoA1 Publication
  3. Vmax=25 nmol/min/mg enzyme for the enoyl reductase reaction1 Publication
  4. Vmax=25 nmol/min/mg enzyme for the thioesterase reaction1 Publication
  5. Vmax=3 nmol/min/mg enzyme for the beta-ketoacyl synthase reaction2 Publications
  6. Vmax=16 nmol/min/µg enzyme for the transferase reaction using malonyl-CoA as donor1 Publication
  7. Vmax=1.6 nmol/min/µg enzyme for the beta-ketoacyl reductase reaction of acetoacetyl-CoA1 Publication
  8. Vmax=2.5 nmol/min/µg enzyme for the fatty acid synthase reaction1 Publication
  9. Vmax=0.72 nmol/min/µg enzyme for the thioesterase reaction1 Publication
  10. Vmax=1.9 nmol/min/µg enzyme for the enoyl reductase reaction1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'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 biosynthesis

This protein is involved in the pathway fatty acid biosynthesis, which is part of Lipid metabolism.3 Publications
View all proteins of this organism that are known to be involved in the pathway fatty acid biosynthesis and in Lipid metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 sitei161For beta-ketoacyl synthase activityPROSITE-ProRule annotation1
Active sitei581For malonyltransferase activityPROSITE-ProRule annotation1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 sitei671Acyl-CoABy similarity1
Binding sitei773Acyl-CoABy similarity1
Active sitei878For beta-hydroxyacyl dehydratase activityPROSITE-ProRule annotation1
Active sitei2302For thioesterase activityPROSITE-ProRule annotation1
Active sitei2475For thioesterase activityPROSITE-ProRule annotation1

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 bindingi1665 – 1682NADP; for enoyl reductase activityAdd BLAST18
Nucleotide bindingi1765 – 1780NADP; for ketoreductase activityAdd BLAST16

<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 functionHydrolase, Lyase, Multifunctional enzyme, Oxidoreductase, Transferase
Biological processFatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism
LigandNAD, NADP, Pyridoxal phosphate

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-RNO-163765, ChREBP activates metabolic gene expression
R-RNO-199220, Vitamin B5 (pantothenate) metabolism
R-RNO-75105, Fatty acyl-CoA biosynthesis

SABIO-RK: Biochemical Reaction Kinetics Database

More...SABIO-RKi		P12785

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

More...UniPathwayi		UPA00094

Protein family/group databases

ESTHER database of the Alpha/Beta-hydrolase fold superfamily of proteins

More...ESTHERi		ratno-fas, Thioesterase

Chemistry databases

SwissLipids knowledge resource for lipid biology

More...SwissLipidsi		SLP:000001864

<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:
Fatty acid synthase (EC:2.3.1.853 Publications)
Alternative name(s):
Type I FAS1 Publication
Including the following 7 domains:
[Acyl-carrier-protein] S-acetyltransferase (EC:2.3.1.383 Publications)
[Acyl-carrier-protein] S-malonyltransferase (EC:2.3.1.391 Publication)
3-oxoacyl-[acyl-carrier-protein] synthase (EC:2.3.1.413 Publications)
3-oxoacyl-[acyl-carrier-protein] reductase (EC:1.1.1.1003 Publications)
3-hydroxyacyl-[acyl-carrier-protein] dehydratase (EC:4.2.1.592 Publications)
Enoyl-[acyl-carrier-protein] reductase (EC:1.3.1.393 Publications)
Acyl-[acyl-carrier-protein] hydrolase (EC:3.1.2.14)
<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:Fasn
<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>OrganismiRattus norvegicus (Rat)
<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 identifieri10116 [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 › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus
<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
  • UP000002494 <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 10

Organism-specific databases

Rat genome database

More...RGDi		620665, Fasn

<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

Keywords - Cellular componenti

Cytoplasm

<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

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL3783

<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_00001802791 – 2505Fatty acid synthaseAdd BLAST2505

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 residuei1N-acetylmethionineBy similarity1
Modified residuei59N6-acetyllysineBy similarity1
Modified residuei63PhosphoserineBy similarity1
Modified residuei70N6-acetyllysineBy similarity1
Modified residuei207PhosphoserineBy similarity1
Modified residuei298N6-acetyllysineBy similarity1
Modified residuei528N6-acetyllysineBy similarity1
Modified residuei673N6-acetyllysineBy similarity1
Modified residuei725PhosphoserineCombined sources1
Modified residuei790N6-acetyllysineBy similarity1
Modified residuei993N6-acetyllysineBy similarity1
Modified residuei1276N6-acetyllysineBy similarity1
Modified residuei1464S-nitrosocysteineBy similarity1
Modified residuei1578PhosphoserineCombined sources1
Modified residuei1588PhosphoserineBy similarity1
Modified residuei1698N6-(pyridoxal phosphate)lysine; alternateBy similarity1
Modified residuei1698N6-acetyllysine; alternateBy similarity1
Modified residuei1765N6-acetyllysineBy similarity1
Modified residuei1841N6-acetyllysineBy similarity1
Modified residuei1989N6-acetyllysineBy similarity1
Modified residuei2085S-nitrosocysteineBy similarity1
Modified residuei2151O-(pantetheine 4'-phosphoryl)serine; alternatePROSITE-ProRule annotation1
Modified residuei2151Phosphoserine; alternateCombined sources1
Modified residuei2191PhosphoserineCombined sources1
Modified residuei2230PhosphoserineBy similarity1
Modified residuei2385N6-acetyllysineBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki2443Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

S-nitrosylation of Fatty acid synthase at cysteine residues Cys-1464 or Cys-2085 is important for the enzyme dimerization. In adipocytes, S-nitrosylation of Fatty acid synthase occurs under physiological conditions and gradually increases during adipogenesis.By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphopantetheine, Phosphoprotein, S-nitrosylation, Ubl conjugation

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P12785

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

More...PaxDbi		P12785

PRoteomics IDEntifications database

More...PRIDEi		P12785

PTM databases

CarbonylDB database of protein carbonylation sites

More...CarbonylDBi		P12785

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P12785

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

More...PhosphoSitePlusi		P12785

<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

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Up-regulated in livers of rats fed on a high carbohydrate diet.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSRNOG00000045636, Expressed in liver and 21 other tissues

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P12785, 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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer which is arranged in a head to tail fashion (By similarity).

Interacts with CEACAM1; this interaction is insulin and phosphorylation-dependent; reduces fatty-acid synthase activity (PubMed:16054098).

By similarity1 Publication

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

P12785
With#Exp.IntAct
itself9EBI-493558,EBI-493558

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		248415, 5 interactors

Database of interacting proteins

More...DIPi		DIP-33893N

Protein interaction database and analysis system

More...IntActi		P12785, 2 interactors

Molecular INTeraction database

More...MINTi		P12785

STRING: functional protein association networks

More...STRINGi		10116.ENSRNOP00000064445

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P12785

<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

Secondary structure

12505
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

AlphaFold Protein Structure Database

More...AlphaFoldDBi		P12785

Biological Magnetic Resonance Data Bank

More...BMRBi		P12785

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

More...SMRi		P12785

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P12785

<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>Domaini2113 – 2193CarrierPROSITE-ProRule annotationAdd BLAST81

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1 – 413Beta-ketoacyl synthaseAdd BLAST413
Regioni429 – 817Acyl and malonyl transferasesAdd BLAST389
Regioni647 – 648Acyl-CoA bindingBy similarity2
Regioni1629 – 1857Enoyl reductaseAdd BLAST229
Regioni1858 – 2113Beta-ketoacyl reductaseAdd BLAST256
Regioni2202 – 2505ThioesteraseAdd BLAST304

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG1202, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00940000157276

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_000022_31_7_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P12785

Identification of Orthologs from Complete Genome Data

More...OMAi		KMRGGEF

Database of Orthologous Groups

More...OrthoDBi		19161at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P12785

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.10.1200.10, 1 hit
3.10.129.110, 1 hit
3.40.366.10, 1 hit
3.40.47.10, 1 hit
3.40.50.150, 1 hit
3.40.50.1820, 2 hits

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR029058, AB_hydrolase
IPR001227, Ac_transferase_dom_sf
IPR036736, ACP-like_sf
IPR014043, Acyl_transferase
IPR016035, Acyl_Trfase/lysoPLipase
IPR013149, ADH-like_C
IPR011032, GroES-like_sf
IPR018201, Ketoacyl_synth_AS
IPR014031, Ketoacyl_synth_C
IPR014030, Ketoacyl_synth_N
IPR016036, Malonyl_transacylase_ACP-bd
IPR013217, Methyltransf_12
IPR036291, NAD(P)-bd_dom_sf
IPR032821, PKS_assoc
IPR020841, PKS_Beta-ketoAc_synthase_dom
IPR020807, PKS_dehydratase
IPR042104, PKS_dehydratase_sf
IPR020843, PKS_ER
IPR013968, PKS_KR
IPR020806, PKS_PP-bd
IPR009081, PP-bd_ACP
IPR006162, Ppantetheine_attach_site
IPR029063, SAM-dependent_MTases
IPR001031, Thioesterase
IPR016039, Thiolase-like

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00698, Acyl_transf_1, 1 hit
PF00107, ADH_zinc_N, 1 hit
PF16197, KAsynt_C_assoc, 1 hit
PF00109, ketoacyl-synt, 1 hit
PF02801, Ketoacyl-synt_C, 1 hit
PF08659, KR, 1 hit
PF08242, Methyltransf_12, 1 hit
PF00550, PP-binding, 1 hit
PF14765, PS-DH, 1 hit
PF00975, Thioesterase, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00827, PKS_AT, 1 hit
SM00826, PKS_DH, 1 hit
SM00829, PKS_ER, 1 hit
SM00825, PKS_KS, 1 hit
SM00823, PKS_PP, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF47336, SSF47336, 1 hit
SSF50129, SSF50129, 1 hit
SSF51735, SSF51735, 2 hits
SSF52151, SSF52151, 1 hit
SSF53335, SSF53335, 1 hit
SSF53474, SSF53474, 1 hit
SSF53901, SSF53901, 1 hit
SSF55048, SSF55048, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00606, B_KETOACYL_SYNTHASE, 1 hit
PS50075, CARRIER, 1 hit
PS00012, PHOSPHOPANTETHEINE, 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>Sequence (1+)i

<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.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

P12785-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MEEVVIAGMS GKLPESENLQ EFWANLIGGV DMVTDDDRRW KAGLYGLPKR 
        60         70         80         90        100
SGKLKDLSKF DASFFGVHPK QAHTMDPQLR LLLEVSYEAI VDGGINPASL 
       110        120        130        140        150
RGTNTGVWVG VSGSEASEAL SRDPETLLGY SMVGCQRAMM ANRLSFFFDF 
       160        170        180        190        200
KGPSIALDTA CSSSLLALQN AYQAIRSGEC PAAIVGGINL LLKPNTSVQF 
       210        220        230        240        250
MKLGMLSPDG TCRSFDDSGN GYCRAEAVVA VLLTKKSLAR RVYATILNAG 
       260        270        280        290        300
TNTDGCKEQG VTFPSGEAQE QLIRSLYQPG GVAPESLEYI EAHGTGTKVG 
       310        320        330        340        350
DPQELNGITR SLCAFRQSPL LIGSTKSNMG HPEPASGLAA LTKVLLSLEN 
       360        370        380        390        400
GVWAPNLHFH NPNPEIPALL DGRLQVVDRP LPVRGGIVGI NSFGFGGANV 
       410        420        430        440        450
HVILQPNTQQ APAPAPHAAL PHLLHASGRT MEAVQGLLEQ GRQHSQDLAF 
       460        470        480        490        500
VSMLNDIAAT PTAAMPFRGY TVLGVEGHVQ EVQQVPASQR PLWFICSGMG 
       510        520        530        540        550
TQWRGMGLSL MRLDSFRESI LRSDEALKPL GVKVSDLLLS TDEHTFDDIV 
       560        570        580        590        600
HSFVSLTAIQ IALIDLLTSM GLKPDGIIGH SLGEVACGYA DGCLSQREAV 
       610        620        630        640        650
LAAYWRGQCI KDANLPAGSM AAVGLSWEEC KQRCPPGVVP ACHNSEDTVT 
       660        670        680        690        700
ISGPQAAVNE FVEQLKQEGV FAKEVRTGGL AFHSYFMEGI APTLLQALKK 
       710        720        730        740        750
VIREPRPRSA RWLSTSIPEA QWQSSLARTS SAEYNVNNLV SPVLFQEALW 
       760        770        780        790        800
HVPEHAVVLE IAPHALLQAV LKRGVKPSCT IIPLMKRDHK DNLEFFLTNL 
       810        820        830        840        850
GKVHLTGIDI NPNALFPPVE FPVPRGTPLI SPHIKWDHSQ TWDIPVAEDF 
       860        870        880        890        900
PNGSSSSSAT VYNIDASSES SDHYLVDHCI DGRVLFPGTG YLYLVWKTLA 
       910        920        930        940        950
RSLSLSLEET PVVFENVTFH QATILPRTGT VPLEVRLLEA SHAFEVSDSG 
       960        970        980        990       1000
NLIVSGKVYQ WEDPDSKLFD HPEVPIPAES ESVSRLTQGE VYKELRLRGY 
      1010       1020       1030       1040       1050
DYGPHFQGVY EATLEGEQGK LLWKDNWVTF MDTMLQISIL GFSKQSLQLP 
      1060       1070       1080       1090       1100
TRVTAIYIDP ATHLQKVYML EGDTQVADVT TSRCLGVTVS GGVYISRLQT 
      1110       1120       1130       1140       1150
TATSRRQQEQ LVPTLEKFVF TPHVEPECLS ESAILQKELQ LCKGLAKALQ 
      1160       1170       1180       1190       1200
TKATQQGLKM TVPGLEDLPQ HGLPRLLAAA CQLQLNGNLQ LELGEVLARE 
      1210       1220       1230       1240       1250
RLLLPEDPLI SGLLNSQALK ACIDTALENL STLKMKVVEV LAGEGHLYSH 
      1260       1270       1280       1290       1300
ISALLNTQPM LQLEYTATDR HPQALKDVQT KLQQHDVAQG QWDPSGPAPT 
      1310       1320       1330       1340       1350
NLGALDLVVC NCALATLGDP ALALDNMVAA LKDGGFLLMH TVLKGHALGE 
      1360       1370       1380       1390       1400
TLACLPSEVQ PGPSFLSQEE WESLFSRKAL HLVGLKKSFY GTALFLCRRL 
      1410       1420       1430       1440       1450
SPQDKPIFLP VEDTSFQWVD SLKSILATSS SQPVWLTAMN CPTSGVVGLV 
      1460       1470       1480       1490       1500
NCLRKEPGGH RIRCILLSNL SSTSHVPKLD PGSSELQKVL ESDLVMNVYR 
      1510       1520       1530       1540       1550
DGAWGAFRHF QLEQDKPEEQ TAHAFVNVLT RGDLASIRWV SSPLKHMQPP 
      1560       1570       1580       1590       1600
SSSGAQLCTV YYASLNFRDI MLATGKLSPD AIPGKWASRD CMLGMEFSGR 
      1610       1620       1630       1640       1650
DKCGRRVMGL VPAEGLATSV LLSPDFLWDV PSSWTLEEAA SVPVVYTTAY 
      1660       1670       1680       1690       1700
YSLVVRGRIQ HGETVLIHSG SGGVGQAAIS IALSLGCRVF TTVGSAEKRA 
      1710       1720       1730       1740       1750
YLQARFPQLD DTSFANSRDT SFEQHVLLHT GGKGVDLVLN SLAEEKLQAS 
      1760       1770       1780       1790       1800
VRCLAQHGRF LEIGKFDLSN NHPLGMAIFL KNVTFHGILL DALFEGANDS 
      1810       1820       1830       1840       1850
WREVAELLKA GIRDGVVKPL KCTVFPKAQV EDAFRYMAQG KHIGKVLVQV 
      1860       1870       1880       1890       1900
REEEPEAMLP GAQPTLISAI SKTFCPEHKS YIITGGLGGF GLELARWLVL 
      1910       1920       1930       1940       1950
RGAQRLVLTS RSGIRTGYQA KHVREWRRQG IHVLVSTSNV SSLEGARALI 
      1960       1970       1980       1990       2000
AEATKLGPVG GVFNLAMVLR DAMLENQTPE LFQDVNKPKY NGTLNLDRAT 
      2010       2020       2030       2040       2050
REACPELDYF VAFSSVSCGR GNAGQSNYGF ANSTMERICE QRRHDGLPGL 
      2060       2070       2080       2090       2100
AVQWGAIGDV GIILEAMGTN DTVVGGTLPQ RISSCMEVLD LFLNQPHAVL 
      2110       2120       2130       2140       2150
SSFVLAEKKA VAHGDGEAQR DLVKAVAHIL GIRDLAGINL DSSLADLGLD 
      2160       2170       2180       2190       2200
SLMGVEVRQI LEREHDLVLP IREVRQLTLR KLQEMSSKAG SDTELAAPKS 
      2210       2220       2230       2240       2250
KNDTSLKQAQ LNLSILLVNP EGPTLTRLNS VQSSERPLFL VHPIEGSITV 
      2260       2270       2280       2290       2300
FHSLAAKLSV PTYGLQCTQA APLDSIPNLA AYYIDCIKQV QPEGPYRVAG 
      2310       2320       2330       2340       2350
YSFGACVAFE MCSQLQAQQG PAPAHNNLFL FDGSHTYVLA YTQSYRAKLT 
      2360       2370       2380       2390       2400
PGCEAEAEAE AICFFIKQFV DAEHSKVLEA LLPLKSLEDR VAAAVDLITR 
      2410       2420       2430       2440       2450
SHQSLDRRDL SFAAVSFYYK LRAADQYKPK AKYHGNVILL RAKTGGTYGE 
      2460       2470       2480       2490       2500
DLGADYNLSQ VCDGKVSVHI IEGDHRTLLE GRGLESIINI IHSSLAEPRV 

SVREG
Length:2,505
Mass (Da):272,650
Last modified:November 1, 1997 - 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:i5810EC13D37F3114
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A8I6A2Z2A0A8I6A2Z2_RAT
Fatty acid synthase
Fasn
2,521Annotation score:

Annotation score:1 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 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 conflicti184I → T in AAA41145 (PubMed:1736293).Curated1
Sequence conflicti871S → P in CAA31780 (PubMed:2915923).Curated1
Sequence conflicti2085C → P in AAA41144 (PubMed:2891707).Curated1
Sequence conflicti2106A → V in AAA57219 (PubMed:2717611).Curated1
Sequence conflicti2106A → V in AAA41145 (PubMed:1736293).Curated1
Sequence conflicti2106A → V in CAA31882 (PubMed:3109907).Curated1
Sequence conflicti2296Y → H in AAA57219 (PubMed:2717611).Curated1
Sequence conflicti2296Y → H in CAA31882 (PubMed:3109907).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
M76767 mRNA Translation: AAA57219.1
X62888 mRNA Translation: CAA44679.1
X62889 Genomic DNA Translation: CAA44680.1
M84761 Genomic DNA Translation: AAA41145.1
X13415 mRNA Translation: CAA31780.1
X13527 mRNA Translation: CAA31882.1
J03514 mRNA Translation: AAA41144.1

Protein sequence database of the Protein Information Resource

More...PIRi		A30313, XYRTFA

NCBI Reference Sequences

More...RefSeqi		NP_059028.1, NM_017332.1

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENSRNOT00000073321; ENSRNOP00000064445; ENSRNOG00000045636

Database of genes from NCBI RefSeq genomes

More...GeneIDi		50671

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		rno:50671

<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
M76767 mRNA Translation: AAA57219.1
X62888 mRNA Translation: CAA44679.1
X62889 Genomic DNA Translation: CAA44680.1
M84761 Genomic DNA Translation: AAA41145.1
X13415 mRNA Translation: CAA31780.1
X13527 mRNA Translation: CAA31882.1
J03514 mRNA Translation: AAA41144.1
PIRiA30313, XYRTFA
RefSeqiNP_059028.1, NM_017332.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2PNGNMR-A2114-2202[»]
AlphaFoldDBiP12785
BMRBiP12785
SMRiP12785
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi248415, 5 interactors
DIPiDIP-33893N
IntActiP12785, 2 interactors
MINTiP12785
STRINGi10116.ENSRNOP00000064445

Chemistry databases

BindingDBiP12785
ChEMBLiCHEMBL3783
SwissLipidsiSLP:000001864

Protein family/group databases

ESTHERiratno-fas, Thioesterase

PTM databases

CarbonylDBiP12785
iPTMnetiP12785
PhosphoSitePlusiP12785

Proteomic databases

jPOSTiP12785
PaxDbiP12785
PRIDEiP12785

Genome annotation databases

EnsembliENSRNOT00000073321; ENSRNOP00000064445; ENSRNOG00000045636
GeneIDi50671
KEGGirno:50671

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		2194
RGDi620665, Fasn

Phylogenomic databases

eggNOGiKOG1202, Eukaryota
GeneTreeiENSGT00940000157276
HOGENOMiCLU_000022_31_7_1
InParanoidiP12785
OMAiKMRGGEF
OrthoDBi19161at2759
PhylomeDBiP12785

Enzyme and pathway databases

UniPathwayiUPA00094
ReactomeiR-RNO-163765, ChREBP activates metabolic gene expression
R-RNO-199220, Vitamin B5 (pantothenate) metabolism
R-RNO-75105, Fatty acyl-CoA biosynthesis
SABIO-RKiP12785

Miscellaneous databases

EvolutionaryTraceiP12785

Protein Ontology

More...PROi		PR:P12785

Gene expression databases

BgeeiENSRNOG00000045636, Expressed in liver and 21 other tissues
GenevisibleiP12785, RN

Family and domain databases

Gene3Di1.10.1200.10, 1 hit
3.10.129.110, 1 hit
3.40.366.10, 1 hit
3.40.47.10, 1 hit
3.40.50.150, 1 hit
3.40.50.1820, 2 hits
InterProiView protein in InterPro
IPR029058, AB_hydrolase
IPR001227, Ac_transferase_dom_sf
IPR036736, ACP-like_sf
IPR014043, Acyl_transferase
IPR016035, Acyl_Trfase/lysoPLipase
IPR013149, ADH-like_C
IPR011032, GroES-like_sf
IPR018201, Ketoacyl_synth_AS
IPR014031, Ketoacyl_synth_C
IPR014030, Ketoacyl_synth_N
IPR016036, Malonyl_transacylase_ACP-bd
IPR013217, Methyltransf_12
IPR036291, NAD(P)-bd_dom_sf
IPR032821, PKS_assoc
IPR020841, PKS_Beta-ketoAc_synthase_dom
IPR020807, PKS_dehydratase
IPR042104, PKS_dehydratase_sf
IPR020843, PKS_ER
IPR013968, PKS_KR
IPR020806, PKS_PP-bd
IPR009081, PP-bd_ACP
IPR006162, Ppantetheine_attach_site
IPR029063, SAM-dependent_MTases
IPR001031, Thioesterase
IPR016039, Thiolase-like
PfamiView protein in Pfam
PF00698, Acyl_transf_1, 1 hit
PF00107, ADH_zinc_N, 1 hit
PF16197, KAsynt_C_assoc, 1 hit
PF00109, ketoacyl-synt, 1 hit
PF02801, Ketoacyl-synt_C, 1 hit
PF08659, KR, 1 hit
PF08242, Methyltransf_12, 1 hit
PF00550, PP-binding, 1 hit
PF14765, PS-DH, 1 hit
PF00975, Thioesterase, 1 hit
SMARTiView protein in SMART
SM00827, PKS_AT, 1 hit
SM00826, PKS_DH, 1 hit
SM00829, PKS_ER, 1 hit
SM00825, PKS_KS, 1 hit
SM00823, PKS_PP, 1 hit
SUPFAMiSSF47336, SSF47336, 1 hit
SSF50129, SSF50129, 1 hit
SSF51735, SSF51735, 2 hits
SSF52151, SSF52151, 1 hit
SSF53335, SSF53335, 1 hit
SSF53474, SSF53474, 1 hit
SSF53901, SSF53901, 1 hit
SSF55048, SSF55048, 1 hit
PROSITEiView protein in PROSITE
PS00606, B_KETOACYL_SYNTHASE, 1 hit
PS50075, CARRIER, 1 hit
PS00012, PHOSPHOPANTETHEINE, 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 nameiFAS_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: P12785
Secondary accession number(s): O09187
, O09190, Q63577, Q64717
<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: October 1, 1989
Last sequence update: November 1, 1997
Last modified: May 25, 2022
This is version 202 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 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

3D-structure, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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