Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q9TTS3 (ACACA_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Acetyl-CoA carboxylase 1
Short name=ACC1
EC=6.4.1.2
Alternative name(s):
ACC-alpha

Including the following 1 domains:

  1. Biotin carboxylase
    EC=6.3.4.14
Gene names
Name:ACACA
Synonyms:ACAC, ACCA
OrganismBos taurus (Bovine)
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length2346 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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.

Catalytic activity

ATP + acetyl-CoA + HCO3- = ADP + phosphate + malonyl-CoA.

ATP + biotin-[carboxyl-carrier-protein] + CO2 = ADP + phosphate + carboxy-biotin-[carboxyl-carrier-protein].

Cofactor

Biotin By similarity.

Binds 2 manganese ions per subunit By similarity.

Enzyme regulation

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

Pathway

Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1.

Subunit structure

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.

Subcellular location

Cytoplasm.

Post-translational modification

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

Sequence similarities

Contains 1 ATP-grasp domain.

Contains 1 biotin carboxylation domain.

Contains 1 biotinyl-binding domain.

Contains 1 carboxyltransferase domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 23462346Acetyl-CoA carboxylase 1
PRO_0000146763

Regions

Domain117 – 618502Biotin carboxylation
Domain275 – 466192ATP-grasp
Domain752 – 81867Biotinyl-binding
Domain1698 – 2194497Carboxyltransferase
Nucleotide binding315 – 3206ATP Potential

Sites

Active site4411 By similarity
Metal binding4241Manganese 1 By similarity
Metal binding4371Manganese 1 By similarity
Metal binding4371Manganese 2 By similarity
Metal binding4391Manganese 2 By similarity
Binding site18231Coenzyme A By similarity
Binding site21271Coenzyme A By similarity
Binding site21291Coenzyme A By similarity

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue51Phosphoserine By similarity
Modified residue231Phosphoserine By similarity
Modified residue251Phosphoserine By similarity
Modified residue291Phosphoserine By similarity
Modified residue481Phosphoserine By similarity
Modified residue501Phosphoserine By similarity
Modified residue531Phosphoserine By similarity
Modified residue561Phosphoserine By similarity
Modified residue581Phosphothreonine By similarity
Modified residue601Phosphoserine By similarity
Modified residue781Phosphoserine By similarity
Modified residue801Phosphoserine; by AMPK By similarity
Modified residue7861N6-biotinyllysine By similarity
Modified residue10421Phosphothreonine By similarity
Modified residue12011Phosphoserine By similarity
Modified residue12631Phosphoserine By similarity
Modified residue13341N6-acetyllysine By similarity
Modified residue15801N6-acetyllysine By similarity
Modified residue18441Phosphoserine By similarity
Modified residue21081Phosphotyrosine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9TTS3 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 32886C5D03EEAE0E

FASTA2,346265,303
        10         20         30         40         50         60 
MDEPSSLAKP LELNQHSRFI IGSVSEDNSE DEISNLVKLD LLEEKEGSLS PASVSSDTLS 

        70         80         90        100        110        120 
DLGISSLQDG LALHMRSSMS GLHLVKQGRD RKKIDSQRDF TVASPAEFVT RFGGNKVIEK 

       130        140        150        160        170        180 
VLIANNGIAA VKCMRSIRRW SYEMFRNERA IRFVVMVTPE DLKANAEYIK MADHYVPVPG 

       190        200        210        220        230        240 
GPNNNNYANV ELILDIAKRI PVQAVWAGWG HASENPKLPE LLLKNGIAFM GPPSQAMWAL 

       250        260        270        280        290        300 
GDKIASSIVA QTAGIPTLPW SGSGLCVDWH ENDFSKRILN VPQELYEKGY VKDVDDGLKA 

       310        320        330        340        350        360 
AEEVGYPVMI KASEGGGGKG IRKVNNADDF PNLFRQVQAE VPGSPIFVMR LAKQSRHLEV 

       370        380        390        400        410        420 
QILADQYGNA ISLFGRDCSV QRRHQKIIEE APAAIATPAV FEHMEQCAVK LARMVGYVSA 

       430        440        450        460        470        480 
GTVEYLYSQD GSFYFLELNP RLQVEHPCTE MVADVNLPAA QLQIAMGIPL YRIKDIRMMY 

       490        500        510        520        530        540 
GVSPWGDAPI DFENSAHVPC PRGHVIAARI TSENPDEGFK PSSGTVQELN FRSNKNVWGY 

       550        560        570        580        590        600 
FSVAAAGGLH EFADSQFGHC FSWGENREEA ISNMVVALKE LSIRGDFRTT VEYLIKLLET 

       610        620        630        640        650        660 
ESFQLNRIGT GWLDRLIAEK VQAERPDTML GVVCGALHVA DVSLRNSISN FLHSLERGQV 

       670        680        690        700        710        720 
LTAHTLLNTV DVELIYEGVK YVLKVTRQSP NSYVVIMNGS CVEVDVHRLS DGGLLLSYDV 

       730        740        750        760        770        780 
SSYTTYMKEE VDRYRITIGN KTCVFEKEND PSVLRSPSAG KLIQYIVEDG GHVFAGQCYA 

       790        800        810        820        830        840 
EIEVMKMVMT LTAAESGCIH YVKRPGAALD PGCVIAKMQL DNPSKVQQAE LHTGSLPRIQ 

       850        860        870        880        890        900 
STALRGEKLH RVFHYVLDNL VNVMNGYCLP DPFFSSRVKD WVERLMKTLR DPSLPLLELQ 

       910        920        930        940        950        960 
DIMTSVSGRI PPNVEKSIKK EMAQYASNIT SVLCQFPSQQ IANILDSHAA TLNRKSEREV 

       970        980        990       1000       1010       1020 
FFMNTQSIVQ LVQRYRSGIR GHMKAVVMDL LRQYLRVETQ FQNGHYDKCV FALREENKSD 

      1030       1040       1050       1060       1070       1080 
MNTVLNYIFS HAQVTRKNLL VTMLIDQLCG RGPTLTDELL NILTELTQLS KTTNAKVALR 

      1090       1100       1110       1120       1130       1140 
ARQVLIASHL PSYELRLNQV ESIFLSAIDM YGHQFCIENL QKLILSETSI FDVLPNFFYH 

      1150       1160       1170       1180       1190       1200 
SNQVVRMAAL EVYVRRAYIA YELNSVQHRQ LKDNTCVVEF QFMLPTSHPN RGNIPTLNRM 

      1210       1220       1230       1240       1250       1260 
SFSSNLNHYG MTHVASVSDV LLDNAFTPPC QRMGGMVSFR TFEDFVRIFD EVMGCFCDSP 

      1270       1280       1290       1300       1310       1320 
PQSPTFPEAG HTSLYDEDKV PRDEPIHILN VAIKTDCDIE DDSLAAMFRE FTQQNKATLV 

      1330       1340       1350       1360       1370       1380 
EHGIRRLTFL VAQKDFRKQV NYEVDQRFHR EFPKFFTFRA RDKFEEDRIY RHLEPALAFQ 

      1390       1400       1410       1420       1430       1440 
LELNRMRNFD LTAIPCANHK MHLYLGAAKV EVGTEVTDYR FFVRAIIRHS DLVTKEASFE 

      1450       1460       1470       1480       1490       1500 
YLQNEGERLL LEAMDELEVA FNNTNVRTDC NHIFLNFVPT VIMDPSKIEE SVRSMVMRYG 

      1510       1520       1530       1540       1550       1560 
SRLWKLRVLQ AELKINIRLT PTGKAIPIRL FLTNESGYYL DISLYKEVTD SRTAQIMFQA 

      1570       1580       1590       1600       1610       1620 
YGDKQGPLHG MLINTPYVTK DQLQSKRFQA QSLGTTYIYD IPEMFRQSLI KLWESMSSQA 

      1630       1640       1650       1660       1670       1680 
FLPPPPLPSD ILTYTELVLD DQGQLVHMNR LPGGNEIGMV AWKMTLKSPE YPDGRDIIVI 

      1690       1700       1710       1720       1730       1740 
GNDITYRIGS FGPQEDLLFL RASELARAEG IPRIYVAANS GARIGLAEEI RHMFHVAWVD 

      1750       1760       1770       1780       1790       1800 
PEDPYKGYKY LYLTPQDYKR VSALNSVHCE HVEDEGESRY KITDIIGKEE GLGAENLRGS 

      1810       1820       1830       1840       1850       1860 
GMIAGESSLA YDEIITISLV TCRAIGIGAY LVRLGQRTIQ VENSHLILTG AGALNKVLGR 

      1870       1880       1890       1900       1910       1920 
EVYTSNNQLG GIQIMHNNGV THSTVCDDFE GVFTVLHWLS YMPKSVYSSV PLLNSKDPID 

      1930       1940       1950       1960       1970       1980 
RVIEFVPTKA PYDPRWMLAG RPHPTQKGQW LSGFFDYGSF SEIMQPWAQT VVVGRARLGG 

      1990       2000       2010       2020       2030       2040 
IPVGVVAVET RTVELSIPAD PANLDSEAKI IQQAGQVWFP DSAFKTYQAI KDFNREGLPL 

      2050       2060       2070       2080       2090       2100 
MVFANWRGFS GGMKDMYDQV LKFGAYIVDG LRECSQPVMV YIPPQAELRG GSWVVIDPTI 

      2110       2120       2130       2140       2150       2160 
NPRHMEMYAD RESRGSVLEP EGTVEIKFRR KDLVKTMRRV DPVYIHLAER LGTPELSVAE 

      2170       2180       2190       2200       2210       2220 
RKELESKLKE REEFLLPIYH QVAVQFADLH DTPGRMQEKG VINDILDWKT SRTFFYWRLR 

      2230       2240       2250       2260       2270       2280 
RLLLEDLVKK KIHNANPELT DGQIQAMLRR WFVEVEGTVK AYVWDNNKDL VEWLEKQLTE 

      2290       2300       2310       2320       2330       2340 
EDGVRSVIEE NIKYISRDYV LKQIRSLVQA NPEVAMDSIV HMTQHISPTQ RAEVVRILST 


MDSPST

« Hide

References

[1]"Genomic distribution of three promoters of the bovine gene encoding acetyl-CoA carboxylase alpha and evidence that the nutritionally regulated promoter I contains a repressive element different from that in rat."
Mao J., Marcos S., Davis S.K., Burzlaff J., Seyfert H.-M.
Biochem. J. 358:127-135(2001) [PubMed: 11485560] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AJ132890 mRNA. Translation: CAB56826.1.
IPIIPI00924054.
RefSeqNP_776649.1. NM_174224.2.
UniGeneBt.88312.

3D structure databases

ProteinModelPortalQ9TTS3.
SMRQ9TTS3. Positions 97-616, 742-834, 1574-2308.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ9TTS3.

Proteomic databases

PRIDEQ9TTS3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID281590.
KEGGbta:281590.

Organism-specific databases

CTD31.

Phylogenomic databases

GeneTreeENSGT00550000074703.
HOVERGENHBG005371.
InParanoidQ9TTS3.
PhylomeDBQ9TTS3.

Family and domain databases

InterProIPR013537. AcCoA_COase_cen.
IPR011761. ATP-grasp.
IPR013815. ATP_grasp_subdomain_1.
IPR013816. ATP_grasp_subdomain_2.
IPR001882. Biotin_BS.
IPR011764. Biotin_carboxylation_dom.
IPR005482. Biotin_COase_C.
IPR000089. Biotin_lipoyl.
IPR005479. CarbamoylP_synth_lsu_ATP-bd.
IPR005481. CarbamoylP_synth_lsu_N.
IPR000022. Carboxyl_trans.
IPR011763. COA_CT_C.
IPR011762. COA_CT_N.
IPR013817. Pre-ATP_grasp.
IPR016185. PreATP-grasp-like.
IPR011054. Rudment_hybrid_motif.
IPR011053. Single_hybrid_motif.
[Graphical view]
Gene3DG3DSA:3.30.1490.20. ATP_grasp_subdomain_1. 1 hit.
G3DSA:3.30.470.20. ATP_grasp_subdomain_2. 1 hit.
G3DSA:3.40.50.20. Pre-ATP_grasp. 1 hit.
KOK11262.
PfamPF08326. ACC_central. 1 hit.
PF02785. Biotin_carb_C. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
PF01039. Carboxyl_trans. 1 hit.
PF00289. CPSase_L_chain. 1 hit.
PF02786. CPSase_L_D2. 1 hit.
[Graphical view]
SMARTSM00878. Biotin_carb_C. 1 hit.
[Graphical view]
SUPFAMSSF51230. Hybrid_motif. 1 hit.
SSF52440. PreATP-grasp-like. 1 hit.
SSF51246. Rudmnt_hyb_motif. 1 hit.
PROSITEPS50975. 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.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameACACA_BOVIN
AccessionPrimary (citable) accession number: Q9TTS3
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: May 1, 2000
Last modified: November 16, 2011
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents