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UniProtKB - P12276 (FAS_CHICK)

Entry version 182 (23 Feb 2022)
Sequence version 5 (23 Jan 2007)
Previous versions | rss
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Protein

Fatty acid synthase

Gene

FASN

Organism
Gallus gallus (Chicken)
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.

4 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.1 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.4 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 sitei580For acyl/malonyl transferase 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 sitei670Acyl-CoABy similarity1
Binding sitei772Acyl-CoABy similarity1
Active sitei878For beta-hydroxyacyl dehydratase activityPROSITE-ProRule annotation1
Active sitei2309For thioesterase activityPROSITE-ProRule annotation1
Active sitei2482For 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 bindingi1675 – 1692NADP; for enoyl reductase activityAdd BLAST18
Nucleotide bindingi1889 – 1904NADP; 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

SABIO-RK: Biochemical Reaction Kinetics Database

More...SABIO-RKi		P12276

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		chick-fas, Thioesterase

<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:2.3.1.854 Publications)
Including the following 7 domains:
[Acyl-carrier-protein] S-acetyltransferase (EC:2.3.1.382 Publications)
[Acyl-carrier-protein] S-malonyltransferase (EC:2.3.1.392 Publications)
3-oxoacyl-[acyl-carrier-protein] synthase (EC:2.3.1.411 Publication)
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:1.3.1.391 Publication)
Acyl-[acyl-carrier-protein] hydrolase (EC:3.1.2.143 Publications)
<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
Synonyms:FAS
<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>OrganismiGallus gallus (Chicken)
<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 identifieri9031 [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 › Archelosauria › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galloanserae › Galliformes › Phasianidae › Phasianinae › Gallus
<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
  • UP000000539 <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: Unplaced

<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

<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		CHEMBL1795136

<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 <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved1 Publication
<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_00001802732 – 2512Fatty acid synthaseAdd BLAST2511

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 residuei2N-acetylglutamate1 Publication1
Modified residuei1475S-nitrosocysteineBy similarity1
Modified residuei1708N6-(pyridoxal phosphate)lysineBy similarity1
Modified residuei2093S-nitrosocysteineBy similarity1
Modified residuei2158O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation1

<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-1475 or Cys-2093 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, Phosphopantetheine, Phosphoprotein, S-nitrosylation

Proteomic databases

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

More...PaxDbi		P12276

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P12276

<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

Protein-protein interaction databases

STRING: functional protein association networks

More...STRINGi		9031.ENSGALP00000004327

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P12276

<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		P12276

Database of comparative protein structure models

More...ModBasei		Search...

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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini2120 – 2200CarrierPROSITE-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>Regioni2 – ?412Beta-ketoacyl synthaseAdd BLAST411
Regioni427 – 815Acyl and malonyl transferasesAdd BLAST389
Regioni646 – 647Acyl-CoA bindingBy similarity2
Regioni1638 – 1866Enoyl reductaseAdd BLAST229
Regioni1867 – 2119Beta-ketoacyl reductaseAdd BLAST253
Regioni2209 – 2511ThioesteraseAdd BLAST303

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG1202, Eukaryota
KOG2335, Eukaryota

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P12276

Database of Orthologous Groups

More...OrthoDBi		993446at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P12276

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
3.40.50.1820, 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_C
IPR011032, GroES-like_sf
IPR018201, Ketoacyl_synth_AS
IPR014031, Ketoacyl_synth_C
IPR014030, Ketoacyl_synth_N
IPR016036, Malonyl_transacylase_ACP-bd
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
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>Sequences (2)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.

<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 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.

This entry describes 2 <p>This subsection of the 'Sequence' section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket
Isoform 2 (identifier: P12276-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <p><strong>What is the canonical sequence?</strong><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MEDVVIAGIA GKLPESENLQ EFWENLLNGV DMVTEDDRRW KPGIYGLPKR 
        60         70         80         90        100
NGKLKDIKKF DASFFGVHPK QAHTMDPQLR LLLEVSYEAI LDGGINPTAL 
       110        120        130        140        150
RGTDTGVWVG ASGSEALEAL SQDPEELLGY SMTGCQRAML ANRISYFYDF 
       160        170        180        190        200
TGPSLTIDTA CSSSLMALEN AYKAIRHGQC SAALVGGVNI LLKPNTSVQF 
       210        220        230        240        250
MKLGMLSPDG ACKAFDVSGN GYCRSEAVVV VLLTKKSMAK RVYATIVNAG 
       260        270        280        290        300
SNTDGFKEQG VTFPSGEMQQ QLVGSLYREC GIKPGDVEYV EAHGTGTKVG 
       310        320        330        340        350
DPQEVNGIVN VFCQCEREPL LIGSTKSNMG HPEPASGLAA LAKVILSLEH 
       360        370        380        390        400
GLWAPNLHFN DPNPDIPALH DGSLKVVCKP TPVKGGLVSI NSFGFGGSNA 
       410        420        430        440        450
HVILRPNEKK CQPQETCNLP RLVQVCGRTQ EAVEILIEES RKHGGCSPFL 
       460        470        480        490        500
SLLSDISAVP VSSMPYRGYT LVGTESDITE IQQVQASGRP LWYICSGMGT 
       510        520        530        540        550
QWKGMGLSLM KLDLFRQSIL RSDEALKSTG LKVSDLLLNA DENTFDDTVH 
       560        570        580        590        600
AFVGLAAIQI AQIDVLKAAG LQPDGILGHS VGELACGYAD NSLSHEEAVL 
       610        620        630        640        650
AAYWRGRCVK EAKLPPGGMA AVGLTWEECK QRCPPNVVPA CHNSEDTVTV 
       660        670        680        690        700
SGPLDSVSEF VTKLKKDGVF AKEVRRAGVA FHSYYMASIA PALLSALKKV 
       710        720        730        740        750
IPHPKPRSAR WISTSIPESQ WQSDLARNSS AEYHVNNLVN PVLFHEGLKH 
       760        770        780        790        800
IPENAVVVEI APHALLQAIL RRTLKPTCTI LPLMKKDHKN NLEFFLTQTG 
       810        820        830        840        850
KIHLTGINVL GNNLFPPVEY PVPVGTPLIS PYIKWDHSQD WDVPKAEDFP 
       860        870        880        890        900
SGSKGSASAS VYNIDVSPDS PDHYLVGHCI DGRVLYPATG YLVLAWRTLA 
       910        920        930        940        950
RSLGMVMEQT AVMFEEVTIH QATILPKKGS TQLEVRIMPA SHSFEVSGNG 
       960        970        980        990       1000
NLAVSGKISL LENDALKNFH NQLADFQSQA NVTAKSGLLM EDVYQELHLR 
      1010       1020       1030       1040       1050
GYNYGPTFQG VLECNSEGSA GKILWNGNWV TFLDTLLHLI VLAETGRSLR 
      1060       1070       1080       1090       1100
LPTRIRSVYI DPVLHQEQVY QYQDNVEAFD VVVDRCLDSL KAGGVQINGL 
      1110       1120       1130       1140       1150
HASVAPRRQQ ERISPTLEKF SFVPYIESDC LSSSTQLHAY LEHCKGLIQK 
      1160       1170       1180       1190       1200
LQAKMALHGV KLVIHGLETK GAAAGSPPAQ KGLQHILTEI CRLELNGNPH 
      1210       1220       1230       1240       1250
SELEQIVTQE KMHLQDDPLL NGLLDSSELK TCLDVAKENT TSHRMKIVEA 
      1260       1270       1280       1290       1300
LAGSGRLFSR VQSILNTQPL LQLDYIATDC TPETLSDNET ELHDAGISFS 
      1310       1320       1330       1340       1350
QWDPSSLPSG NLTNADLAVC NCSTSVLGNT AEIISNLAAA VKEGGFVLLH 
      1360       1370       1380       1390       1400
TLLKEETLGE IVSFLTSPDL QQKHSFLSQA QWEELFSKAS LNLVAMKRSF 
      1410       1420       1430       1440       1450
FGSVIFLCRR QSPAKAPILL PVDDTHYKWV DSLKEILADS SEQPLWLTAT 
      1460       1470       1480       1490       1500
NCGNSGILGM VNCLRLEAEG HRIRCVFVSN LSPSSTVPAT SLSSLEMQKI 
      1510       1520       1530       1540       1550
IERDLVMNVY RDGKWGSFRH LPLQQAQPQE LTECAYVNVL TRGDLSSLRW 
      1560       1570       1580       1590       1600
IVSPLRHFQT TNPNVQLCKV YYASLNFWDI MLATGKLSPD AIPGNWTLQQ 
      1610       1620       1630       1640       1650
CMLGMEFSGR DLAGRRVMGL LPAKGLATVV DCDKRFLWEV PENWTLEEAA 
      1660       1670       1680       1690       1700
SVPVVYATAY YALVVRGGMK KGESVLIHSG SGGVGQAAIA IALSMGCRVF 
      1710       1720       1730       1740       1750
ATVGSAEKRE YLQARFPQLD ANSFASSRNT TFQQHILRVT NGKGVSLVLN 
      1760       1770       1780       1790       1800
SLAEEKLQAS LRCLAQHGRF LEIGKFDLSN NSQLGMALFL KNVAFHGILL 
      1810       1820       1830       1840       1850
DSIFEEGNQE WEVVSELLTK GIKDGVVKPL RTTVFGKEEV EAAFRFMAQG 
      1860       1870       1880       1890       1900
KHIGKVMIKI QEEEKQYPLR SEPVKLSAIS RTSCPPTKSY IITGGLGGFG 
      1910       1920       1930       1940       1950
LELAQWLIER GAQKLVLTSR SGIRTGYQAK CVREWKALGI QVLVSTSDVG 
      1960       1970       1980       1990       2000
TLEGTQLLIE EALKLGPVGG IFNLAVVLKD AMIENQTPEL FWEVNKPKYS 
      2010       2020       2030       2040       2050
GTLHLDWVTR KKCPDLDYFV VFSSVSCGRG NAGQSNYGFA NSAMERICEQ 
      2060       2070       2080       2090       2100
RHHDGLPGLA VQWGAIGDVG ILKAMGNREV VIGGTVLQQI SSCLEVLDMF 
      2110       2120       2130       2140       2150
LNQPHPVMSS FVLAEKVSVK SEGGSQRDLV EAVAHILGVR DVSSLNAESS 
      2160       2170       2180       2190       2200
LADLGLDSLM GVEVRQTLER DYDIVMTMRE IRLLTINKLR ELSSKTGTAE 
      2210       2220       2230       2240       2250
ELKPSQVLKT GPGEPPKLDL NNLLVNPEGP TITRLNEVQS TERPLFLVHP 
      2260       2270       2280       2290       2300
IEGSIAVFYT LASKLHMPCY GLQCTKAAPL DSIQSLASYY IDCMKQIQPE 
      2310       2320       2330       2340       2350
GPYRIAGYSF GACVAFEMCS QLQAQQNASH ALNSLFLFDG SHSFVAAYTQ 
      2360       2370       2380       2390       2400
SYRAKLTQGN EAALETEALC AFVQQFTGIE YNKLLEILLP LEDLEARVNA 
      2410       2420       2430       2440       2450
AADLITQIHK NINREALSFA AASFYHKLKA ADKYIPESKY HGNVTLMRAK 
      2460       2470       2480       2490       2500
THNEYEEGLG GDYRLSEVCD GKVSVHIIEG DHRTLLEGDG VESIIGIIHG 
      2510 
SLAEPRVSVR EG
Length:2,512
Mass (Da):274,782
Last modified:January 23, 2007 - v5
<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:i66FDE22F5CCF603C
GO
Isoform 1 (identifier: P12276-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     2349-2349: T → TQCFSFSLF

Show »
Length:2,520
Mass (Da):275,742
Checksum:iCA1DA253E4BD0956
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 AAA82106 differs from that shown. Reason: Frameshift.Curated

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 conflicti78 – 79QL → PV in AAA48767 (PubMed:2734291).Curated2
Sequence conflicti117L → A in AAA48767 (PubMed:2734291).Curated1
Sequence conflicti676R → S in AAA48767 (PubMed:2734291).Curated1
Sequence conflicti1170K → N in AAA48767 (PubMed:2734291).Curated1
Sequence conflicti1179A → T in AAA48767 (PubMed:2734291).Curated1
Sequence conflicti1192R → H in AAA48767 (PubMed:2734291).Curated1
Sequence conflicti1199P → L in AAA48767 (PubMed:2734291).Curated1
Sequence conflicti1287 – 1288DN → ND in AAA48767 (PubMed:2734291).Curated2
Sequence conflicti1373K → E in AAA48767 (PubMed:2734291).Curated1
Sequence conflicti1534C → Y in AAA48767 (PubMed:2734291).Curated1
Sequence conflicti1578W → R in AAA48767 (PubMed:2734291).Curated1
Sequence conflicti1686 – 1697QAAIA…LSMGC → ASSHCHRLEHGLA in AAA48767 (PubMed:2734291).CuratedAdd BLAST12
Sequence conflicti1733Q → E in AAA48767 (PubMed:2734291).Curated1
Sequence conflicti1746S → N in AAA48767 (PubMed:2734291).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0001492349T → TQCFSFSLF in isoform 1. 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
J03860 mRNA Translation: AAA48767.1
J04485 mRNA Translation: AAB46389.1
J02839 Genomic DNA Translation: AAA82106.1 Frameshift.

Protein sequence database of the Protein Information Resource

More...PIRi		S57248, XYCHFA

Keywords - Coding sequence diversityi

Alternative splicing

<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
J03860 mRNA Translation: AAA48767.1
J04485 mRNA Translation: AAB46389.1
J02839 Genomic DNA Translation: AAA82106.1 Frameshift.
PIRiS57248, XYCHFA

3D structure databases

SMRiP12276
ModBaseiSearch...

Protein-protein interaction databases

STRINGi9031.ENSGALP00000004327

Chemistry databases

BindingDBiP12276
ChEMBLiCHEMBL1795136

Protein family/group databases

ESTHERichick-fas, Thioesterase

PTM databases

iPTMnetiP12276

Proteomic databases

PaxDbiP12276

Phylogenomic databases

eggNOGiKOG1202, Eukaryota
KOG2335, Eukaryota
InParanoidiP12276
OrthoDBi993446at2759
PhylomeDBiP12276

Enzyme and pathway databases

UniPathwayiUPA00094
SABIO-RKiP12276

Miscellaneous databases

Protein Ontology

More...PROi		PR:P12276

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
3.40.50.1820, 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_C
IPR011032, GroES-like_sf
IPR018201, Ketoacyl_synth_AS
IPR014031, Ketoacyl_synth_C
IPR014030, Ketoacyl_synth_N
IPR016036, Malonyl_transacylase_ACP-bd
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
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_CHICK
<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: P12276
<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: January 23, 2007
Last modified: February 23, 2022
This is version 182 of the entry and version 5 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

Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
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