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Entry version 133 (16 Jan 2019)
Sequence version 1 (01 May 2000)
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Protein

Acetyl-CoA carboxylase 1

Gene

ACACA

Organism
Bos taurus (Bovine)
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 transcript leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

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

Catalyzes the rate-limiting reaction in the biogenesis of long-chain fatty acids. Carries out three functions: biotin carboxyl carrier protein, biotin carboxylase and carboxyltransferase.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 ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Protein has several cofactor binding sites:

<p>This subsection of the ‘Function’ 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

By phosphorylation (By similarity). Activity is increased by oligomerization. Citrate and MID1IP1 promote oligomerization (By similarity).By similarity

<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: malonyl-CoA biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes malonyl-CoA from acetyl-CoA.
Proteins known to be involved in this subpathway in this organism are:
  1. Acetyl-CoA carboxylase 1 (ACACA)
This subpathway is part of the pathway malonyl-CoA biosynthesis, which is itself part of Lipid metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes malonyl-CoA from acetyl-CoA, the pathway malonyl-CoA biosynthesis and in Lipid metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi424Manganese 1By similarity1
Metal bindingi437Manganese 1By similarity1
Metal bindingi437Manganese 2By similarity1
Metal bindingi439Manganese 2By similarity1
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei441By similarity1
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei1823Coenzyme ABy similarity1
Binding sitei2127Coenzyme ABy similarity1
Binding sitei2129Coenzyme ABy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi315 – 320ATPPROSITE-ProRule annotation6

<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 functionAllosteric enzyme, Ligase, Multifunctional enzyme
Biological processFatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism
LigandATP-binding, Biotin, Manganese, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

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

More...
UniPathwayi
UPA00655;UER00711

<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:
Acetyl-CoA carboxylase 1 (EC:6.4.1.2)
Short name:
ACC1
Alternative name(s):
ACC-alpha
Including the following 1 domains:
Biotin carboxylase (EC:6.3.4.14)
<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:ACACA
Synonyms:ACAC, ACCA
<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>OrganismiBos taurus (Bovine)
<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 identifieri9913 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
<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
  • UP000009136 <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: 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

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm

<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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001467631 – 2346Acetyl-CoA carboxylase 1Add BLAST2346

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 residuei5PhosphoserineBy similarity1
Modified residuei23PhosphoserineBy similarity1
Modified residuei25PhosphoserineBy similarity1
Modified residuei29PhosphoserineBy similarity1
Modified residuei34PhosphoserineBy similarity1
Modified residuei48PhosphoserineBy similarity1
Modified residuei50PhosphoserineBy similarity1
Modified residuei53PhosphoserineBy similarity1
Modified residuei58PhosphothreonineBy similarity1
Modified residuei78PhosphoserineBy similarity1
Modified residuei80Phosphoserine; by AMPKBy similarity1
Modified residuei610PhosphothreonineBy similarity1
Modified residuei786N6-biotinyllysinePROSITE-ProRule annotationBy similarity1
Modified residuei835PhosphoserineBy similarity1
Modified residuei1201PhosphoserineBy similarity1
Modified residuei1216PhosphoserineBy similarity1
Modified residuei1218PhosphoserineBy similarity1
Modified residuei1227PhosphothreonineBy similarity1
Modified residuei1259PhosphoserineBy similarity1
Modified residuei1263PhosphoserineBy similarity1
Modified residuei1273PhosphoserineBy similarity1
Modified residuei1334N6-acetyllysineBy similarity1
Modified residuei2153PhosphothreonineBy similarity1

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

Phosphorylation on Ser-1263 is required for interaction with BRCA1.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

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

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PaxDbi
Q9TTS3

PeptideAtlas

More...
PeptideAtlasi
Q9TTS3

PRoteomics IDEntifications database

More...
PRIDEi
Q9TTS3

<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

Monomer, homodimer, and homotetramer. Can form filamentous polymers. Interacts in its inactive phosphorylated form with the BRCT domains of BRCA1 which prevents ACACA dephosphorylation and inhibits lipid synthesis. Interacts with MID1IP1; interaction with MID1IP1 promotes oligomerization and increases its activity (By similarity).By similarity

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
9913.ENSBTAP00000023364

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

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
Q9TTS3

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

More...
SMRi
Q9TTS3

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">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>Domaini117 – 618Biotin carboxylationAdd BLAST502
Domaini275 – 466ATP-graspPROSITE-ProRule annotationAdd BLAST192
Domaini745 – 819Biotinyl-bindingPROSITE-ProRule annotationAdd BLAST75
Domaini1576 – 1914CoA carboxyltransferase N-terminalPROSITE-ProRule annotationAdd BLAST339
Domaini1918 – 2234CoA carboxyltransferase C-terminalPROSITE-ProRule annotationAdd BLAST317

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>Regioni1576 – 2234CarboxyltransferasePROSITE-ProRule annotationAdd BLAST659

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0368 Eukaryota
COG0439 LUCA
COG0511 LUCA
COG4799 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000214115

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG005371

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q9TTS3

KEGG Orthology (KO)

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KOi
K11262

Database of Orthologous Groups

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OrthoDBi
156081at2759

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.30.1490.20, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR034733 AcCoA_carboxyl
IPR013537 AcCoA_COase_cen
IPR011761 ATP-grasp
IPR013815 ATP_grasp_subdomain_1
IPR005481 BC-like_N
IPR001882 Biotin_BS
IPR011764 Biotin_carboxylation_dom
IPR005482 Biotin_COase_C
IPR000089 Biotin_lipoyl
IPR005479 CbamoylP_synth_lsu-like_ATP-bd
IPR029045 ClpP/crotonase-like_dom_sf
IPR011763 COA_CT_C
IPR011762 COA_CT_N
IPR016185 PreATP-grasp_dom_sf
IPR011054 Rudment_hybrid_motif
IPR011053 Single_hybrid_motif

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF08326 ACC_central, 1 hit
PF02785 Biotin_carb_C, 1 hit
PF00289 Biotin_carb_N, 1 hit
PF00364 Biotin_lipoyl, 1 hit
PF01039 Carboxyl_trans, 1 hit
PF02786 CPSase_L_D2, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00878 Biotin_carb_C, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF51230 SSF51230, 1 hit
SSF51246 SSF51246, 1 hit
SSF52096 SSF52096, 2 hits
SSF52440 SSF52440, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50975 ATP_GRASP, 1 hit
PS50979 BC, 1 hit
PS00188 BIOTIN, 1 hit
PS50968 BIOTINYL_LIPOYL, 1 hit
PS50989 COA_CT_CTER, 1 hit
PS50980 COA_CT_NTER, 1 hit
PS00866 CPSASE_1, 1 hit
PS00867 CPSASE_2, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

Q9TTS3-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MDEPSSLAKP LELNQHSRFI IGSVSEDNSE DEISNLVKLD LLEEKEGSLS
60 70 80 90 100
PASVSSDTLS DLGISSLQDG LALHMRSSMS GLHLVKQGRD RKKIDSQRDF
110 120 130 140 150
TVASPAEFVT RFGGNKVIEK VLIANNGIAA VKCMRSIRRW SYEMFRNERA
160 170 180 190 200
IRFVVMVTPE DLKANAEYIK MADHYVPVPG GPNNNNYANV ELILDIAKRI
210 220 230 240 250
PVQAVWAGWG HASENPKLPE LLLKNGIAFM GPPSQAMWAL GDKIASSIVA
260 270 280 290 300
QTAGIPTLPW SGSGLCVDWH ENDFSKRILN VPQELYEKGY VKDVDDGLKA
310 320 330 340 350
AEEVGYPVMI KASEGGGGKG IRKVNNADDF PNLFRQVQAE VPGSPIFVMR
360 370 380 390 400
LAKQSRHLEV QILADQYGNA ISLFGRDCSV QRRHQKIIEE APAAIATPAV
410 420 430 440 450
FEHMEQCAVK LARMVGYVSA GTVEYLYSQD GSFYFLELNP RLQVEHPCTE
460 470 480 490 500
MVADVNLPAA QLQIAMGIPL YRIKDIRMMY GVSPWGDAPI DFENSAHVPC
510 520 530 540 550
PRGHVIAARI TSENPDEGFK PSSGTVQELN FRSNKNVWGY FSVAAAGGLH
560 570 580 590 600
EFADSQFGHC FSWGENREEA ISNMVVALKE LSIRGDFRTT VEYLIKLLET
610 620 630 640 650
ESFQLNRIGT GWLDRLIAEK VQAERPDTML GVVCGALHVA DVSLRNSISN
660 670 680 690 700
FLHSLERGQV LTAHTLLNTV DVELIYEGVK YVLKVTRQSP NSYVVIMNGS
710 720 730 740 750
CVEVDVHRLS DGGLLLSYDV SSYTTYMKEE VDRYRITIGN KTCVFEKEND
760 770 780 790 800
PSVLRSPSAG KLIQYIVEDG GHVFAGQCYA EIEVMKMVMT LTAAESGCIH
810 820 830 840 850
YVKRPGAALD PGCVIAKMQL DNPSKVQQAE LHTGSLPRIQ STALRGEKLH
860 870 880 890 900
RVFHYVLDNL VNVMNGYCLP DPFFSSRVKD WVERLMKTLR DPSLPLLELQ
910 920 930 940 950
DIMTSVSGRI PPNVEKSIKK EMAQYASNIT SVLCQFPSQQ IANILDSHAA
960 970 980 990 1000
TLNRKSEREV FFMNTQSIVQ LVQRYRSGIR GHMKAVVMDL LRQYLRVETQ
1010 1020 1030 1040 1050
FQNGHYDKCV FALREENKSD MNTVLNYIFS HAQVTRKNLL VTMLIDQLCG
1060 1070 1080 1090 1100
RGPTLTDELL NILTELTQLS KTTNAKVALR ARQVLIASHL PSYELRLNQV
1110 1120 1130 1140 1150
ESIFLSAIDM YGHQFCIENL QKLILSETSI FDVLPNFFYH SNQVVRMAAL
1160 1170 1180 1190 1200
EVYVRRAYIA YELNSVQHRQ LKDNTCVVEF QFMLPTSHPN RGNIPTLNRM
1210 1220 1230 1240 1250
SFSSNLNHYG MTHVASVSDV LLDNAFTPPC QRMGGMVSFR TFEDFVRIFD
1260 1270 1280 1290 1300
EVMGCFCDSP PQSPTFPEAG HTSLYDEDKV PRDEPIHILN VAIKTDCDIE
1310 1320 1330 1340 1350
DDSLAAMFRE FTQQNKATLV EHGIRRLTFL VAQKDFRKQV NYEVDQRFHR
1360 1370 1380 1390 1400
EFPKFFTFRA RDKFEEDRIY RHLEPALAFQ LELNRMRNFD LTAIPCANHK
1410 1420 1430 1440 1450
MHLYLGAAKV EVGTEVTDYR FFVRAIIRHS DLVTKEASFE YLQNEGERLL
1460 1470 1480 1490 1500
LEAMDELEVA FNNTNVRTDC NHIFLNFVPT VIMDPSKIEE SVRSMVMRYG
1510 1520 1530 1540 1550
SRLWKLRVLQ AELKINIRLT PTGKAIPIRL FLTNESGYYL DISLYKEVTD
1560 1570 1580 1590 1600
SRTAQIMFQA YGDKQGPLHG MLINTPYVTK DQLQSKRFQA QSLGTTYIYD
1610 1620 1630 1640 1650
IPEMFRQSLI KLWESMSSQA FLPPPPLPSD ILTYTELVLD DQGQLVHMNR
1660 1670 1680 1690 1700
LPGGNEIGMV AWKMTLKSPE YPDGRDIIVI GNDITYRIGS FGPQEDLLFL
1710 1720 1730 1740 1750
RASELARAEG IPRIYVAANS GARIGLAEEI RHMFHVAWVD PEDPYKGYKY
1760 1770 1780 1790 1800
LYLTPQDYKR VSALNSVHCE HVEDEGESRY KITDIIGKEE GLGAENLRGS
1810 1820 1830 1840 1850
GMIAGESSLA YDEIITISLV TCRAIGIGAY LVRLGQRTIQ VENSHLILTG
1860 1870 1880 1890 1900
AGALNKVLGR EVYTSNNQLG GIQIMHNNGV THSTVCDDFE GVFTVLHWLS
1910 1920 1930 1940 1950
YMPKSVYSSV PLLNSKDPID RVIEFVPTKA PYDPRWMLAG RPHPTQKGQW
1960 1970 1980 1990 2000
LSGFFDYGSF SEIMQPWAQT VVVGRARLGG IPVGVVAVET RTVELSIPAD
2010 2020 2030 2040 2050
PANLDSEAKI IQQAGQVWFP DSAFKTYQAI KDFNREGLPL MVFANWRGFS
2060 2070 2080 2090 2100
GGMKDMYDQV LKFGAYIVDG LRECSQPVMV YIPPQAELRG GSWVVIDPTI
2110 2120 2130 2140 2150
NPRHMEMYAD RESRGSVLEP EGTVEIKFRR KDLVKTMRRV DPVYIHLAER
2160 2170 2180 2190 2200
LGTPELSVAE RKELESKLKE REEFLLPIYH QVAVQFADLH DTPGRMQEKG
2210 2220 2230 2240 2250
VINDILDWKT SRTFFYWRLR RLLLEDLVKK KIHNANPELT DGQIQAMLRR
2260 2270 2280 2290 2300
WFVEVEGTVK AYVWDNNKDL VEWLEKQLTE EDGVRSVIEE NIKYISRDYV
2310 2320 2330 2340
LKQIRSLVQA NPEVAMDSIV HMTQHISPTQ RAEVVRILST MDSPST
Length:2,346
Mass (Da):265,303
Last modified:May 1, 2000 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i32886C5D03EEAE0E
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AJ132890 mRNA Translation: CAB56826.1

NCBI Reference Sequences

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RefSeqi
NP_776649.1, NM_174224.2

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Bt.88312

Genome annotation databases

Database of genes from NCBI RefSeq genomes

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GeneIDi
281590

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
bta:281590

<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
AJ132890 mRNA Translation: CAB56826.1
RefSeqiNP_776649.1, NM_174224.2
UniGeneiBt.88312

3D structure databases

ProteinModelPortaliQ9TTS3
SMRiQ9TTS3
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000023364

Proteomic databases

PaxDbiQ9TTS3
PeptideAtlasiQ9TTS3
PRIDEiQ9TTS3

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi281590
KEGGibta:281590

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
31

Phylogenomic databases

eggNOGiKOG0368 Eukaryota
COG0439 LUCA
COG0511 LUCA
COG4799 LUCA
HOGENOMiHOG000214115
HOVERGENiHBG005371
InParanoidiQ9TTS3
KOiK11262
OrthoDBi156081at2759

Enzyme and pathway databases

UniPathwayi
UPA00655;UER00711

Family and domain databases

Gene3Di3.30.1490.20, 1 hit
InterProiView protein in InterPro
IPR034733 AcCoA_carboxyl
IPR013537 AcCoA_COase_cen
IPR011761 ATP-grasp
IPR013815 ATP_grasp_subdomain_1
IPR005481 BC-like_N
IPR001882 Biotin_BS
IPR011764 Biotin_carboxylation_dom
IPR005482 Biotin_COase_C
IPR000089 Biotin_lipoyl
IPR005479 CbamoylP_synth_lsu-like_ATP-bd
IPR029045 ClpP/crotonase-like_dom_sf
IPR011763 COA_CT_C
IPR011762 COA_CT_N
IPR016185 PreATP-grasp_dom_sf
IPR011054 Rudment_hybrid_motif
IPR011053 Single_hybrid_motif
PfamiView protein in Pfam
PF08326 ACC_central, 1 hit
PF02785 Biotin_carb_C, 1 hit
PF00289 Biotin_carb_N, 1 hit
PF00364 Biotin_lipoyl, 1 hit
PF01039 Carboxyl_trans, 1 hit
PF02786 CPSase_L_D2, 1 hit
SMARTiView protein in SMART
SM00878 Biotin_carb_C, 1 hit
SUPFAMiSSF51230 SSF51230, 1 hit
SSF51246 SSF51246, 1 hit
SSF52096 SSF52096, 2 hits
SSF52440 SSF52440, 1 hit
PROSITEiView protein in PROSITE
PS50975 ATP_GRASP, 1 hit
PS50979 BC, 1 hit
PS00188 BIOTIN, 1 hit
PS50968 BIOTINYL_LIPOYL, 1 hit
PS50989 COA_CT_CTER, 1 hit
PS50980 COA_CT_NTER, 1 hit
PS00866 CPSASE_1, 1 hit
PS00867 CPSASE_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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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 nameiACACA_BOVIN
<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: Q9TTS3
<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: April 27, 2001
Last sequence update: May 1, 2000
Last modified: January 16, 2019
This is version 133 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
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