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Protein

Acetyl-CoA carboxylase 1

Gene

ACACA

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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.1 Publication

Catalytic activityi

ATP + acetyl-CoA + HCO3- = ADP + phosphate + malonyl-CoA.1 Publication
ATP + biotin-[carboxyl-carrier-protein] + HCO3- = ADP + phosphate + carboxy-biotin-[carboxyl-carrier-protein].1 Publication

Cofactori

Protein has several cofactor binding sites:
  • biotin
  • Mn2+Note: Binds 2 manganese ions per subunit.

Enzyme regulationi

By phosphorylation (By similarity). Activity is increased by oligomerization. Citrate and MID1IP1 promote oligomerization.By similarity1 Publication

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), Acetyl-CoA carboxylase 2 (ACACB)
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
Metal bindingi424Manganese 1By similarity1
Metal bindingi437Manganese 1By similarity1
Metal bindingi437Manganese 2By similarity1
Metal bindingi439Manganese 2By similarity1
Active sitei441By similarity1
Binding sitei1823Coenzyme ABy similarity1
Binding sitei2127Coenzyme ABy similarity1
Binding sitei2129Coenzyme ABy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi315 – 320ATPPROSITE-ProRule annotation6

GO - Molecular functioni

  • acetyl-CoA carboxylase activity Source: UniProtKB
  • ATP binding Source: UniProtKB-KW
  • biotin carboxylase activity Source: UniProtKB-EC
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

Keywords - Ligandi

ATP-binding, Biotin, Manganese, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciZFISH:BCCP-MONOMER.
BRENDAi6.4.1.2. 2681.
ReactomeiR-HSA-163765. ChREBP activates metabolic gene expression.
R-HSA-196780. Biotin transport and metabolism.
R-HSA-200425. Import of palmitoyl-CoA into the mitochondrial matrix.
R-HSA-2426168. Activation of gene expression by SREBF (SREBP).
R-HSA-3371599. Defective HLCS causes multiple carboxylase deficiency.
R-HSA-75105. Fatty Acyl-CoA Biosynthesis.
SABIO-RKQ13085.
SIGNORiQ13085.
UniPathwayiUPA00655; UER00711.

Chemistry databases

SwissLipidsiSLP:000000729.

Names & Taxonomyi

Protein namesi
Recommended name:
Acetyl-CoA carboxylase 1 (EC:6.4.1.21 Publication)
Short name:
ACC1
Alternative name(s):
ACC-alpha
Including the following 1 domains:
Biotin carboxylase (EC:6.3.4.141 Publication)
Gene namesi
Name:ACACA
Synonyms:ACAC, ACC1, ACCA
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:84. ACACA.

Subcellular locationi

GO - Cellular componenti

  • actin cytoskeleton Source: HPA
  • cytoplasm Source: HPA
  • cytosol Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • mitochondrion Source: Ensembl
  • nucleolus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Involvement in diseasei

Acetyl-CoA carboxylase 1 deficiency (ACACAD)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn inborn error of de novo fatty acid synthesis associated with severe brain damage, persistent myopathy and poor growth.
See also OMIM:613933

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi78S → A: No effect on interaction with BRCA1. 1 Publication1
Mutagenesisi344S → A: No effect on interaction with BRCA1. 1 Publication1
Mutagenesisi432S → A: No effect on interaction with BRCA1. 1 Publication1
Mutagenesisi1201S → A: No effect on interaction with BRCA1. 1 Publication1
Mutagenesisi1263S → A: Abolishes interaction with BRCA1. 1 Publication1
Mutagenesisi1585S → A: No effect on interaction with BRCA1. 1 Publication1
Mutagenesisi1952S → A: No effect on interaction with BRCA1. 1 Publication1
Mutagenesisi2211S → A: No effect on interaction with BRCA1. 1 Publication1

Organism-specific databases

DisGeNETi31.
MalaCardsiACACA.
MIMi613933. phenotype.
OpenTargetsiENSG00000275176.
ENSG00000278540.
PharmGKBiPA24421.

Chemistry databases

ChEMBLiCHEMBL3351.
DrugBankiDB00121. Biotin.
GuidetoPHARMACOLOGYi1263.

Polymorphism and mutation databases

BioMutaiACACA.
DMDMi118601083.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001467641 – 2346Acetyl-CoA carboxylase 1Add BLAST2346

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineCombined sources1 Publication1
Modified residuei5PhosphoserineCombined sources1
Modified residuei23PhosphoserineCombined sources1
Modified residuei25PhosphoserineCombined sources1
Modified residuei29PhosphoserineCombined sources1
Modified residuei34PhosphoserineBy similarity1
Modified residuei48PhosphoserineCombined sources1
Modified residuei50PhosphoserineBy similarity1
Modified residuei53PhosphoserineCombined sources1
Modified residuei58PhosphothreonineBy similarity1
Modified residuei78PhosphoserineBy similarity1
Modified residuei80PhosphoserineCombined sources1 Publication1
Modified residuei488PhosphoserineCombined sources1
Modified residuei610PhosphothreonineCombined sources1
Modified residuei786N6-biotinyllysinePROSITE-ProRule annotationBy similarity1
Modified residuei835PhosphoserineCombined sources1
Modified residuei1201PhosphoserineBy similarity1
Modified residuei1216PhosphoserineBy similarity1
Modified residuei1218PhosphoserineBy similarity1
Modified residuei1227PhosphothreonineBy similarity1
Modified residuei1259PhosphoserineBy similarity1
Modified residuei1263Phosphoserine1 Publication1
Modified residuei1273PhosphoserineCombined sources1
Modified residuei1334N6-acetyllysineCombined sources1
Modified residuei2153PhosphothreonineCombined sources1

Post-translational modificationi

Phosphorylation on Ser-1263 is required for interaction with BRCA1.2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ13085.
MaxQBiQ13085.
PaxDbiQ13085.
PeptideAtlasiQ13085.
PRIDEiQ13085.

PTM databases

iPTMnetiQ13085.
PhosphoSitePlusiQ13085.
SwissPalmiQ13085.

Expressioni

Tissue specificityi

Expressed in brain, placental, skeletal muscle, renal, pancreatic and adipose tissues; expressed at low level in pulmonary tissue; not detected in the liver.

Gene expression databases

BgeeiENSG00000132142.
ExpressionAtlasiQ13085. baseline and differential.
GenevisibleiQ13085. HS.

Organism-specific databases

HPAiCAB013715.
HPA036650.
HPA063018.

Interactioni

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.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
AKR1B10O602184EBI-717681,EBI-1572139
BRCA1P383982EBI-717681,EBI-349905
SIRT1Q96EB63EBI-717681,EBI-1802965

Protein-protein interaction databases

BioGridi106549. 75 interactors.
DIPiDIP-36122N.
IntActiQ13085. 31 interactors.
MINTiMINT-1415014.
STRINGi9606.ENSP00000344789.

Chemistry databases

BindingDBiQ13085.

Structurei

Secondary structure

12346
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi105 – 111Combined sources7
Beta strandi120 – 123Combined sources4
Helixi127 – 145Combined sources19
Beta strandi150 – 157Combined sources8
Helixi159 – 163Combined sources5
Helixi168 – 171Combined sources4
Beta strandi172 – 177Combined sources6
Helixi183 – 185Combined sources3
Turni186 – 188Combined sources3
Helixi190 – 199Combined sources10
Beta strandi203 – 206Combined sources4
Turni211 – 214Combined sources4
Helixi217 – 224Combined sources8
Beta strandi228 – 231Combined sources4
Helixi234 – 241Combined sources8
Helixi243 – 252Combined sources10
Turni261 – 264Combined sources4
Helixi283 – 289Combined sources7
Helixi294 – 304Combined sources11
Beta strandi306 – 312Combined sources7
Beta strandi320 – 324Combined sources5
Turni327 – 329Combined sources3
Helixi330 – 340Combined sources11
Beta strandi346 – 350Combined sources5
Beta strandi356 – 364Combined sources9
Beta strandi370 – 382Combined sources13
Beta strandi385 – 392Combined sources8
Helixi398 – 415Combined sources18
Beta strandi419 – 427Combined sources9
Beta strandi433 – 439Combined sources7
Turni444 – 446Combined sources3
Helixi447 – 453Combined sources7
Helixi457 – 465Combined sources9
Helixi470 – 472Combined sources3
Helixi474 – 479Combined sources6
Turni492 – 495Combined sources4
Beta strandi496 – 498Combined sources3
Beta strandi503 – 510Combined sources8
Beta strandi526 – 530Combined sources5
Beta strandi537 – 542Combined sources6
Beta strandi557 – 566Combined sources10
Helixi567 – 582Combined sources16
Helixi589 – 599Combined sources11
Helixi601 – 604Combined sources4
Helixi612 – 616Combined sources5
Helixi1582 – 1592Combined sources11
Helixi1598 – 1600Combined sources3
Helixi1601 – 1619Combined sources19
Helixi1628 – 1631Combined sources4
Beta strandi1632 – 1639Combined sources8
Beta strandi1645 – 1648Combined sources4
Beta strandi1656 – 1666Combined sources11
Beta strandi1675 – 1682Combined sources8
Helixi1687 – 1689Combined sources3
Helixi1693 – 1709Combined sources17
Beta strandi1713 – 1717Combined sources5
Helixi1728 – 1731Combined sources4
Beta strandi1735 – 1739Combined sources5
Helixi1744 – 1746Combined sources3
Beta strandi1748 – 1753Combined sources6
Helixi1755 – 1761Combined sources7
Helixi1762 – 1764Combined sources3
Beta strandi1767 – 1774Combined sources8
Beta strandi1777 – 1785Combined sources9
Helixi1795 – 1813Combined sources19
Beta strandi1816 – 1820Combined sources5
Beta strandi1822 – 1825Combined sources4
Helixi1827 – 1834Combined sources8
Beta strandi1837 – 1841Combined sources5
Beta strandi1845 – 1849Combined sources5
Helixi1851 – 1858Combined sources8
Helixi1866 – 1870Combined sources5
Helixi1872 – 1875Combined sources4
Turni1876 – 1879Combined sources4
Beta strandi1882 – 1887Combined sources6
Helixi1888 – 1899Combined sources12
Beta strandi1914 – 1917Combined sources4
Helixi1934 – 1939Combined sources6
Beta strandi1944 – 1946Combined sources3
Beta strandi1961 – 1964Combined sources4
Beta strandi1971 – 1978Combined sources8
Beta strandi1981 – 1988Combined sources8
Beta strandi1993 – 1996Combined sources4
Beta strandi2010 – 2013Combined sources4
Helixi2020 – 2036Combined sources17
Beta strandi2040 – 2043Combined sources4
Helixi2053 – 2057Combined sources5
Helixi2060 – 2072Combined sources13
Beta strandi2078 – 2082Combined sources5
Beta strandi2087 – 2089Combined sources3
Helixi2090 – 2094Combined sources5
Helixi2098 – 2100Combined sources3
Turni2102 – 2104Combined sources3
Beta strandi2105 – 2110Combined sources6
Beta strandi2114 – 2118Combined sources5
Helixi2120 – 2127Combined sources8
Helixi2130 – 2140Combined sources11
Helixi2142 – 2150Combined sources9
Helixi2158 – 2188Combined sources31
Helixi2193 – 2198Combined sources6
Beta strandi2201 – 2206Combined sources6
Helixi2208 – 2210Combined sources3
Helixi2211 – 2235Combined sources25
Helixi2241 – 2256Combined sources16
Helixi2258 – 2265Combined sources8
Helixi2267 – 2278Combined sources12
Helixi2289 – 2310Combined sources22
Helixi2312 – 2314Combined sources3
Helixi2315 – 2322Combined sources8
Helixi2323 – 2325Combined sources3
Helixi2328 – 2337Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2YL2X-ray2.30A/B78-617[»]
3COJX-ray3.21H/I/J/K/L/M/N/O1258-1270[»]
4ASIX-ray2.80A/B/C/D/E/F1571-2338[»]
ProteinModelPortaliQ13085.
SMRiQ13085.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ13085.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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
Regioni1576 – 2234CarboxyltransferasePROSITE-ProRule annotationAdd BLAST659

Sequence similaritiesi

Contains 1 ATP-grasp domain.PROSITE-ProRule annotation
Contains 1 biotin carboxylation domain.Curated
Contains 1 biotinyl-binding domain.PROSITE-ProRule annotationCurated
Contains 1 CoA carboxyltransferase C-terminal domain.PROSITE-ProRule annotation
Contains 1 CoA carboxyltransferase N-terminal domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0368. Eukaryota.
COG0439. LUCA.
COG0511. LUCA.
COG4799. LUCA.
GeneTreeiENSGT00550000074703.
HOVERGENiHBG005371.
InParanoidiQ13085.
KOiK11262.
OMAiDWHENDF.
OrthoDBiEOG091G02ND.
PhylomeDBiQ13085.
TreeFamiTF300061.

Family and domain databases

Gene3Di3.30.1490.20. 1 hit.
3.30.470.20. 1 hit.
3.40.50.20. 1 hit.
3.90.226.10. 3 hits.
InterProiIPR013537. AcCoA_COase_cen.
IPR011761. ATP-grasp.
IPR013815. ATP_grasp_subdomain_1.
IPR013816. ATP_grasp_subdomain_2.
IPR005481. BC-like_N.
IPR001882. Biotin_BS.
IPR011764. Biotin_carboxylation_dom.
IPR005482. Biotin_COase_C.
IPR000089. Biotin_lipoyl.
IPR000022. Carboxyl_trans.
IPR005479. CbamoylP_synth_lsu-like_ATP-bd.
IPR029045. ClpP/crotonase-like_dom.
IPR011763. COA_CT_C.
IPR011762. COA_CT_N.
IPR016185. PreATP-grasp_dom.
IPR011054. Rudment_hybrid_motif.
IPR011053. Single_hybrid_motif.
[Graphical view]
PfamiPF08326. 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.
[Graphical view]
SMARTiSM00878. Biotin_carb_C. 1 hit.
[Graphical view]
SUPFAMiSSF51230. SSF51230. 1 hit.
SSF51246. SSF51246. 1 hit.
SSF52096. SSF52096. 2 hits.
SSF52440. SSF52440. 1 hit.
PROSITEiPS50975. 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]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative promoter usage. AlignAdd to basket

Isoform 1 (identifier: Q13085-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' 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
MDEPSPLAQP LELNQHSRFI IGSVSEDNSE DEISNLVKLD LLEEKEGSLS
60 70 80 90 100
PASVGSDTLS DLGISSLQDG LALHIRSSMS 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 SGSGLRVDWQ ENDFSKRILN VPQELYEKGY VKDVDDGLQA
310 320 330 340 350
AEEVGYPVMI KASEGGGGKG IRKVNNADDF PNLFRQVQAE VPGSPIFVMR
360 370 380 390 400
LAKQSRHLEV QILADQYGNA ISLFGRDCSV QRRHQKIIEE APATIATPAV
410 420 430 440 450
FEHMEQCAVK LAKMVGYVSA GTVEYLYSQD GSFYFLELNP RLQVEHPCTE
460 470 480 490 500
MVADVNLPAA QLQIAMGIPL YRIKDIRMMY GVSPWGDSPI DFEDSAHVPC
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
ESFQMNRIDT GWLDRLIAEK VQAERPDTML GVVCGALHVA DVSLRNSVSN
660 670 680 690 700
FLHSLERGQV LPAHTLLNTV DVELIYEGVK YVLKVTRQSP NSYVVIMNGS
710 720 730 740 750
CVEVDVHRLS DGGLLLSYDG SSYTTYMKEE VDRYRITIGN KTCVFEKEND
760 770 780 790 800
PSVMRSPSAG KLIQYIVEDG GHVFAGQCYA EIEVMKMVMT LTAVESGCIH
810 820 830 840 850
YVKRPGAALD PGCVLAKMQL DNPSKVQQAE LHTGSLPRIQ STALRGEKLH
860 870 880 890 900
RVFHYVLDNL VNVMNGYCLP DPFFSSKVKD 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 HAQVTKKNLL VTMLIDQLCG
1060 1070 1080 1090 1100
RDPTLTDELL NILTELTQLS KTTNAKVALR ARQVLIASHL PSYELRHNQV
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 LLDNSFTPPC QRMGGMVSFR TFEDFVRIFD
1260 1270 1280 1290 1300
EVMGCFSDSP PQSPTFPEAG HTSLYDEDKV PRDEPIHILN VAIKTDCDIE
1310 1320 1330 1340 1350
DDRLAAMFRE FTQQNKATLV DHGIRRLTFL VAQKDFRKQV NYEVDRRFHR
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 DLLQSKRFQA QSLGTTYIYD
1610 1620 1630 1640 1650
IPEMFRQSLI KLWESMSTQA FLPSPPLPSD MLTYTELVLD DQGQLVHMNR
1660 1670 1680 1690 1700
LPGGNEIGMV AWKMTFKSPE YPEGRDIIVI GNDITYRIGS FGPQEDLLFL
1710 1720 1730 1740 1750
RASELARAEG IPRIYVSANS GARIGLAEEI RHMFHVAWVD PEDPYKGYRY
1760 1770 1780 1790 1800
LYLTPQDYKR VSALNSVHCE HVEDEGESRY KITDIIGKEE GIGPENLRGS
1810 1820 1830 1840 1850
GMIAGESSLA YNEIITISLV TCRAIGIGAY LVRLGQRTIQ VENSHLILTG
1860 1870 1880 1890 1900
AGALNKVLGR EVYTSNNQLG GIQIMHNNGV THCTVCDDFE GVFTVLHWLS
1910 1920 1930 1940 1950
YMPKSVHSSV PLLNSKDPID RIIEFVPTKT 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 LRECCQPVLV YIPPQAELRG GSWVVIDSSI
2110 2120 2130 2140 2150
NPRHMEMYAD RESRGSVLEP EGTVEIKFRR KDLVKTMRRV DPVYIHLAER
2160 2170 2180 2190 2200
LGTPELSTAE RKELENKLKE REEFLIPIYH QVAVQFADLH DTPGRMQEKG
2210 2220 2230 2240 2250
VISDILDWKT SRTFFYWRLR RLLLEDLVKK KIHNANPELT DGQIQAMLRR
2260 2270 2280 2290 2300
WFVEVEGTVK AYVWDNNKDL AEWLEKQLTE EDGVHSVIEE NIKCISRDYV
2310 2320 2330 2340
LKQIRSLVQA NPEVAMDSII HMTQHISPTQ RAEVIRILST MDSPST
Length:2,346
Mass (Da):265,554
Last modified:October 31, 2006 - v2
Checksum:iF1F0A518F8824FFC
GO
Isoform 2 (identifier: Q13085-2) [UniParc]FASTAAdd to basket
Also known as: E5A

The sequence of this isoform differs from the canonical sequence as follows:
     1-75: MDEPSPLAQP...SLQDGLALHI → MEGSPEENKEMRYYMLQ

Show »
Length:2,288
Mass (Da):259,686
Checksum:i4E2C75958216CC8B
GO
Isoform 3 (identifier: Q13085-3) [UniParc]FASTAAdd to basket
Also known as: E5B

The sequence of this isoform differs from the canonical sequence as follows:
     1-78: Missing.

Show »
Length:2,268
Mass (Da):257,239
Checksum:iC78033F62C492D3E
GO
Isoform 4 (identifier: Q13085-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MWWSTLMSILRARSFWKWISTQTVRIIRAVRAHFGGIM

Show »
Length:2,383
Mass (Da):269,999
Checksum:i1F2B8F96208B9983
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti66S → A in AAC50139 (PubMed:7732023).Curated1
Sequence conflicti79M → W in AAC50139 (PubMed:7732023).Curated1
Sequence conflicti89R → G in AAC50139 (PubMed:7732023).Curated1
Sequence conflicti182P → A in AAC50139 (PubMed:7732023).Curated1
Sequence conflicti234S → N in AAC50139 (PubMed:7732023).Curated1
Sequence conflicti299Q → K in AAC50139 (PubMed:7732023).Curated1
Sequence conflicti303E → K in AAC50139 (PubMed:7732023).Curated1
Sequence conflicti364A → V in AAP94122 (PubMed:12810950).Curated1
Sequence conflicti446H → Q in AAC50139 (PubMed:7732023).Curated1
Sequence conflicti494D → N in AAC50139 (PubMed:7732023).Curated1
Sequence conflicti554D → G in AAC50139 (PubMed:7732023).Curated1
Sequence conflicti622Q → R in AAC50139 (PubMed:7732023).Curated1
Sequence conflicti640A → G in AAC50139 (PubMed:7732023).Curated1
Sequence conflicti814V → I in AAP94122 (PubMed:12810950).Curated1
Sequence conflicti1061N → S in AAC50139 (PubMed:7732023).Curated1
Sequence conflicti1094 – 1095EL → DV in AAC50139 (PubMed:7732023).Curated2
Sequence conflicti1225S → A in AAC50139 (PubMed:7732023).Curated1
Sequence conflicti1257S → C in AAC50139 (PubMed:7732023).Curated1
Sequence conflicti1297C → G in AAC50139 (PubMed:7732023).Curated1
Sequence conflicti1320V → A in AAC50139 (PubMed:7732023).Curated1
Sequence conflicti1444N → S in AAC50139 (PubMed:7732023).Curated1
Sequence conflicti1474F → L in AAC50139 (PubMed:7732023).Curated1
Sequence conflicti1665 – 1666TF → SL in AAC50139 (PubMed:7732023).Curated2
Sequence conflicti1677I → V in AAC50139 (PubMed:7732023).Curated1
Sequence conflicti1741P → S in AAC50139 (PubMed:7732023).Curated1
Sequence conflicti1762S → G in AAC50139 (PubMed:7732023).Curated1
Sequence conflicti1822C → S in AAC50139 (PubMed:7732023).Curated1
Sequence conflicti1875M → T in AAC50139 (PubMed:7732023).Curated1
Sequence conflicti1888D → G in AAC50139 (PubMed:7732023).Curated1
Sequence conflicti1997I → V in AAC50139 (PubMed:7732023).Curated1
Sequence conflicti2013Q → H in AAC50139 (PubMed:7732023).Curated1
Sequence conflicti2058D → H in AAC50139 (PubMed:7732023).Curated1
Sequence conflicti2075C → S in AAC50139 (PubMed:7732023).Curated1
Sequence conflicti2098 – 2099SS → PT in AAC50139 (PubMed:7732023).Curated2
Sequence conflicti2158 – 2159TA → PT in AAC50139 (PubMed:7732023).Curated2
Sequence conflicti2166N → S in AAC50139 (PubMed:7732023).Curated1
Sequence conflicti2234N → S in AAC50139 (PubMed:7732023).Curated1
Sequence conflicti2321H → R in AAP94122 (PubMed:12810950).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_042941838R → W.Corresponds to variant rs2287351dbSNPEnsembl.1
Natural variantiVAR_0365141687R → Q in a colorectal cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_0289292271A → V Rare polymorphism; frequency <0.004; may play a role in breast cancer susceptibility. 1 PublicationCorresponds to variant rs146351326dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0260981 – 78Missing in isoform 3. 2 PublicationsAdd BLAST78
Alternative sequenceiVSP_0260991 – 75MDEPS…LALHI → MEGSPEENKEMRYYMLQ in isoform 2. 2 PublicationsAdd BLAST75
Alternative sequenceiVSP_0261001M → MWWSTLMSILRARSFWKWIS TQTVRIIRAVRAHFGGIM in isoform 4. 2 Publications1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U19822 mRNA. Translation: AAC50139.1.
AY315619 mRNA. Translation: AAP94114.1.
AY315620 mRNA. Translation: AAP94115.1.
AY315621 mRNA. Translation: AAP94116.1.
AY315623 mRNA. Translation: AAP94118.1.
AY315627 mRNA. Translation: AAP94122.1.
AY237919 mRNA. Translation: AAP69841.1.
BC137287 mRNA. Translation: AAI37288.1.
AJ534888 mRNA. Translation: CAD59556.1.
AJ534889 mRNA. Translation: CAD59557.1.
AJ564444 mRNA. Translation: CAD92089.1.
CCDSiCCDS11317.1. [Q13085-1]
CCDS11318.1. [Q13085-2]
CCDS42302.1. [Q13085-4]
CCDS42303.1. [Q13085-3]
PIRiI38928.
RefSeqiNP_942131.1. NM_198834.2. [Q13085-4]
NP_942133.1. NM_198836.2. [Q13085-1]
NP_942134.1. NM_198837.1. [Q13085-2]
NP_942135.1. NM_198838.1. [Q13085-3]
NP_942136.1. NM_198839.2. [Q13085-1]
XP_011523005.1. XM_011524703.1. [Q13085-1]
XP_016880044.1. XM_017024555.1. [Q13085-1]
UniGeneiHs.160556.

Genome annotation databases

EnsembliENST00000611803; ENSP00000479901; ENSG00000275176. [Q13085-2]
ENST00000612895; ENSP00000482269; ENSG00000278540. [Q13085-2]
ENST00000613687; ENSP00000483674; ENSG00000275176. [Q13085-1]
ENST00000614428; ENSP00000478547; ENSG00000278540. [Q13085-1]
ENST00000616317; ENSP00000483300; ENSG00000278540. [Q13085-4]
ENST00000617649; ENSP00000482368; ENSG00000278540. [Q13085-3]
ENST00000619487; ENSP00000478577; ENSG00000275176. [Q13085-4]
ENST00000621312; ENSP00000480031; ENSG00000275176. [Q13085-3]
GeneIDi31.
KEGGihsa:31.
UCSCiuc002hnk.4. human. [Q13085-1]

Keywords - Coding sequence diversityi

Alternative promoter usage, Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

Acetyl-CoA carboxylase entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U19822 mRNA. Translation: AAC50139.1.
AY315619 mRNA. Translation: AAP94114.1.
AY315620 mRNA. Translation: AAP94115.1.
AY315621 mRNA. Translation: AAP94116.1.
AY315623 mRNA. Translation: AAP94118.1.
AY315627 mRNA. Translation: AAP94122.1.
AY237919 mRNA. Translation: AAP69841.1.
BC137287 mRNA. Translation: AAI37288.1.
AJ534888 mRNA. Translation: CAD59556.1.
AJ534889 mRNA. Translation: CAD59557.1.
AJ564444 mRNA. Translation: CAD92089.1.
CCDSiCCDS11317.1. [Q13085-1]
CCDS11318.1. [Q13085-2]
CCDS42302.1. [Q13085-4]
CCDS42303.1. [Q13085-3]
PIRiI38928.
RefSeqiNP_942131.1. NM_198834.2. [Q13085-4]
NP_942133.1. NM_198836.2. [Q13085-1]
NP_942134.1. NM_198837.1. [Q13085-2]
NP_942135.1. NM_198838.1. [Q13085-3]
NP_942136.1. NM_198839.2. [Q13085-1]
XP_011523005.1. XM_011524703.1. [Q13085-1]
XP_016880044.1. XM_017024555.1. [Q13085-1]
UniGeneiHs.160556.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2YL2X-ray2.30A/B78-617[»]
3COJX-ray3.21H/I/J/K/L/M/N/O1258-1270[»]
4ASIX-ray2.80A/B/C/D/E/F1571-2338[»]
ProteinModelPortaliQ13085.
SMRiQ13085.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106549. 75 interactors.
DIPiDIP-36122N.
IntActiQ13085. 31 interactors.
MINTiMINT-1415014.
STRINGi9606.ENSP00000344789.

Chemistry databases

BindingDBiQ13085.
ChEMBLiCHEMBL3351.
DrugBankiDB00121. Biotin.
GuidetoPHARMACOLOGYi1263.
SwissLipidsiSLP:000000729.

PTM databases

iPTMnetiQ13085.
PhosphoSitePlusiQ13085.
SwissPalmiQ13085.

Polymorphism and mutation databases

BioMutaiACACA.
DMDMi118601083.

Proteomic databases

EPDiQ13085.
MaxQBiQ13085.
PaxDbiQ13085.
PeptideAtlasiQ13085.
PRIDEiQ13085.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000611803; ENSP00000479901; ENSG00000275176. [Q13085-2]
ENST00000612895; ENSP00000482269; ENSG00000278540. [Q13085-2]
ENST00000613687; ENSP00000483674; ENSG00000275176. [Q13085-1]
ENST00000614428; ENSP00000478547; ENSG00000278540. [Q13085-1]
ENST00000616317; ENSP00000483300; ENSG00000278540. [Q13085-4]
ENST00000617649; ENSP00000482368; ENSG00000278540. [Q13085-3]
ENST00000619487; ENSP00000478577; ENSG00000275176. [Q13085-4]
ENST00000621312; ENSP00000480031; ENSG00000275176. [Q13085-3]
GeneIDi31.
KEGGihsa:31.
UCSCiuc002hnk.4. human. [Q13085-1]

Organism-specific databases

CTDi31.
DisGeNETi31.
GeneCardsiACACA.
HGNCiHGNC:84. ACACA.
HPAiCAB013715.
HPA036650.
HPA063018.
MalaCardsiACACA.
MIMi200350. gene.
613933. phenotype.
neXtProtiNX_Q13085.
OpenTargetsiENSG00000275176.
ENSG00000278540.
PharmGKBiPA24421.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0368. Eukaryota.
COG0439. LUCA.
COG0511. LUCA.
COG4799. LUCA.
GeneTreeiENSGT00550000074703.
HOVERGENiHBG005371.
InParanoidiQ13085.
KOiK11262.
OMAiDWHENDF.
OrthoDBiEOG091G02ND.
PhylomeDBiQ13085.
TreeFamiTF300061.

Enzyme and pathway databases

UniPathwayiUPA00655; UER00711.
BioCyciZFISH:BCCP-MONOMER.
BRENDAi6.4.1.2. 2681.
ReactomeiR-HSA-163765. ChREBP activates metabolic gene expression.
R-HSA-196780. Biotin transport and metabolism.
R-HSA-200425. Import of palmitoyl-CoA into the mitochondrial matrix.
R-HSA-2426168. Activation of gene expression by SREBF (SREBP).
R-HSA-3371599. Defective HLCS causes multiple carboxylase deficiency.
R-HSA-75105. Fatty Acyl-CoA Biosynthesis.
SABIO-RKQ13085.
SIGNORiQ13085.

Miscellaneous databases

ChiTaRSiACACA. human.
EvolutionaryTraceiQ13085.
GeneWikiiACACA.
GenomeRNAii31.
PROiQ13085.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000132142.
ExpressionAtlasiQ13085. baseline and differential.
GenevisibleiQ13085. HS.

Family and domain databases

Gene3Di3.30.1490.20. 1 hit.
3.30.470.20. 1 hit.
3.40.50.20. 1 hit.
3.90.226.10. 3 hits.
InterProiIPR013537. AcCoA_COase_cen.
IPR011761. ATP-grasp.
IPR013815. ATP_grasp_subdomain_1.
IPR013816. ATP_grasp_subdomain_2.
IPR005481. BC-like_N.
IPR001882. Biotin_BS.
IPR011764. Biotin_carboxylation_dom.
IPR005482. Biotin_COase_C.
IPR000089. Biotin_lipoyl.
IPR000022. Carboxyl_trans.
IPR005479. CbamoylP_synth_lsu-like_ATP-bd.
IPR029045. ClpP/crotonase-like_dom.
IPR011763. COA_CT_C.
IPR011762. COA_CT_N.
IPR016185. PreATP-grasp_dom.
IPR011054. Rudment_hybrid_motif.
IPR011053. Single_hybrid_motif.
[Graphical view]
PfamiPF08326. 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.
[Graphical view]
SMARTiSM00878. Biotin_carb_C. 1 hit.
[Graphical view]
SUPFAMiSSF51230. SSF51230. 1 hit.
SSF51246. SSF51246. 1 hit.
SSF52096. SSF52096. 2 hits.
SSF52440. SSF52440. 1 hit.
PROSITEiPS50975. 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]
ProtoNetiSearch...

Entry informationi

Entry nameiACACA_HUMAN
AccessioniPrimary (citable) accession number: Q13085
Secondary accession number(s): B2RP68
, Q6KEV6, Q6XDA8, Q7Z2G8, Q7Z561, Q7Z563, Q7Z564, Q86WB2, Q86WB3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: October 31, 2006
Last modified: November 30, 2016
This is version 173 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Allosteric enzyme, Complete proteome, Direct protein sequencing, Multifunctional enzyme, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.