ACACB

Protein identityUniProt · HPA

UniProt accession

O00763

Gene

ACACB

Ensembl

ENSG00000076555

Chromosome

12

Canonical length

2458 aa

Protein class

Enzymes, Metabolic proteins, Plasma proteins, Predicted intracellular proteins

Secretome location

Intracellular and membrane

Quaternary structure

Homotetramer

OverviewNCBI Gene

Acetyl-CoA carboxylase (ACC) is a complex multifunctional enzyme system. ACC is a biotin-containing enzyme which catalyzes the carboxylation of acetyl-CoA to malonyl-CoA, the rate-limiting step in fatty acid synthesis. ACC-beta is thought to control fatty acid oxidation by means of the ability of malonyl-CoA to inhibit carnitine-palmitoyl-CoA transferase I, the rate-limiting step in fatty acid uptake and oxidation by mitochondria. ACC-beta may be involved in the regulation of fatty acid oxidation, rather than fatty acid biosynthesis. [provided by RefSeq, Oct 2022]

Canonical amino-acid sequenceUniProt

2458 residues, UniProt reviewed canonical sequence.

>O00763|ACACB
     1  MVLLLCLSCL IFSCLTFSWL KIWGKMTDSK PITKSKSEAN LIPSQEPFPA SDNSGETPQR
    61  NGEGHTLPKT PSQAEPASHK GPKDAGRRRN SLPPSHQKPP RNPLSSSDAA PSPELQANGT
   121  GTQGLEATDT NGLSSSARPQ GQQAGSPSKE DKKQANIKRQ LMTNFILGSF DDYSSDEDSV
   181  AGSSRESTRK GSRASLGALS LEAYLTTGEA ETRVPTMRPS MSGLHLVKRG REHKKLDLHR
   241  DFTVASPAEF VTRFGGDRVI EKVLIANNGI AAVKCMRSIR RWAYEMFRNE RAIRFVVMVT
   301  PEDLKANAEY IKMADHYVPV PGGPNNNNYA NVELIVDIAK RIPVQAVWAG WGHASENPKL
   361  PELLCKNGVA FLGPPSEAMW ALGDKIASTV VAQTLQVPTL PWSGSGLTVE WTEDDLQQGK
   421  RISVPEDVYD KGCVKDVDEG LEAAERIGFP LMIKASEGGG GKGIRKAESA EDFPILFRQV
   481  QSEIPGSPIF LMKLAQHARH LEVQILADQY GNAVSLFGRD CSIQRRHQKI VEEAPATIAP
   541  LAIFEFMEQC AIRLAKTVGY VSAGTVEYLY SQDGSFHFLE LNPRLQVEHP CTEMIADVNL
   601  PAAQLQIAMG VPLHRLKDIR LLYGESPWGV TPISFETPSN PPLARGHVIA ARITSENPDE
   661  GFKPSSGTVQ ELNFRSSKNV WGYFSVAATG GLHEFADSQF GHCFSWGENR EEAISNMVVA
   721  LKELSIRGDF RTTVEYLINL LETESFQNND IDTGWLDYLI AEKVQAEKPD IMLGVVCGAL
   781  NVADAMFRTC MTDFLHSLER GQVLPADSLL NLVDVELIYG GVKYILKVAR QSLTMFVLIM
   841  NGCHIEIDAH RLNDGGLLLS YNGNSYTTYM KEEVDSYRIT IGNKTCVFEK ENDPTVLRSP
   901  SAGKLTQYTV EDGGHVEAGS SYAEMEVMKM IMTLNVQERG RVKYIKRPGA VLEAGCVVAR
   961  LELDDPSKVH PAEPFTGELP AQQTLPILGE KLHQVFHSVL ENLTNVMSGF CLPEPVFSIK
  1021  LKEWVQKLMM TLRHPSLPLL ELQEIMTSVA GRIPAPVEKS VRRVMAQYAS NITSVLCQFP
  1081  SQQIATILDC HAATLQRKAD REVFFINTQS IVQLVQRYRS GIRGYMKTVV LDLLRRYLRV
  1141  EHHFQQAHYD KCVINLREQF KPDMSQVLDC IFSHAQVAKK NQLVIMLIDE LCGPDPSLSD
  1201  ELISILNELT QLSKSEHCKV ALRARQILIA SHLPSYELRH NQVESIFLSA IDMYGHQFCP
  1261  ENLKKLILSE TTIFDVLPTF FYHANKVVCM ASLEVYVRRG YIAYELNSLQ HRQLPDGTCV
  1321  VEFQFMLPSS HPNRMTVPIS ITNPDLLRHS TELFMDSGFS PLCQRMGAMV AFRRFEDFTR
  1381  NFDEVISCFA NVPKDTPLFS EARTSLYSED DCKSLREEPI HILNVSIQCA DHLEDEALVP
  1441  ILRTFVQSKK NILVDYGLRR ITFLIAQEKE FPKFFTFRAR DEFAEDRIYR HLEPALAFQL
  1501  ELNRMRNFDL TAVPCANHKM HLYLGAAKVK EGVEVTDHRF FIRAIIRHSD LITKEASFEY
  1561  LQNEGERLLL EAMDELEVAF NNTSVRTDCN HIFLNFVPTV IMDPFKIEES VRYMVMRYGS
  1621  RLWKLRVLQA EVKINIRQTT TGSAVPIRLF ITNESGYYLD ISLYKEVTDS RSGNIMFHSF
  1681  GNKQGPQHGM LINTPYVTKD LLQAKRFQAQ TLGTTYIYDF PEMFRQALFK LWGSPDKYPK
  1741  DILTYTELVL DSQGQLVEMN RLPGGNEVGM VAFKMRFKTQ EYPEGRDVIV IGNDITFRIG
  1801  SFGPGEDLLY LRASEMARAE GIPKIYVAAN SGARIGMAEE IKHMFHVAWV DPEDPHKGFK
  1861  YLYLTPQDYT RISSLNSVHC KHIEEGGESR YMITDIIGKD DGLGVENLRG SGMIAGESSL
  1921  AYEEIVTISL VTCRAIGIGA YLVRLGQRVI QVENSHIILT GASALNKVLG REVYTSNNQL
  1981  GGVQIMHYNG VSHITVPDDF EGVYTILEWL SYMPKDNHSP VPIITPTDPI DREIEFLPSR
  2041  APYDPRWMLA GRPHPTLKGT WQSGFFDHGS FKEIMAPWAQ TVVTGRARLG GIPVGVIAVE
  2101  TRTVEVAVPA DPANLDSEAK IIQQAGQVWF PDSAYKTAQA VKDFNREKLP LMIFANWRGF
  2161  SGGMKDMYDQ VLKFGAYIVD GLRQYKQPIL IYIPPYAELR GGSWVVIDAT INPLCIEMYA
  2221  DKESRGGVLE PEGTVEIKFR KKDLIKSMRR IDPAYKKLME QLGEPDLSDK DRKDLEGRLK
  2281  AREDLLLPIY HQVAVQFADF HDTPGRMLEK GVISDILEWK TARTFLYWRL RRLLLEDQVK
  2341  QEILQASGEL SHVHIQSMLR RWFVETEGAV KAYLWDNNQV VVQWLEQHWQ AGDGPRSTIR
  2401  ENITYLKHDS VLKTIRGLVE ENPEVAVDCV IYLSQHISPA ERAQVVHLLS TMDSPAST

LocalizationUniProt · AlphaFold · HPA

Whether an antibody against ACACB can act on the native protein depends on physical access: surface and secreted proteins are reachable by circulating antibodies, intracellular proteins usually are not.

Antibody reachability

Intracellular

Secreted

No

Transmembrane segments

0

Mean surface accessibility (rSASA)

0.29

Highest tissue expression

172 nTPM

Expression across tissuesHPA

DiseaseUniProt · ClinVar · IEDB · PubMed

Four sources answering four different questions about ACACB.

Disease | ImmuneIEDB

Conditions an epitope on ACACB was assayed in.

• skin melanoma T cell

Genetic constraint and essentialitygnomAD · DepMap

Does the body need this protein intact? Low LOEUF or a strong DepMap dependency means loss or blockade of the protein is likely to be felt.

gnomAD LOEUF (loss-of-function intolerance)

0.86

gnomAD pLI

0

gnomAD missense Z

1.57

DepMap mean gene effect

-0.11

DepMap dependency class

selective

Cancer expressionTCGA

Across TCGA tumor cohorts, this protein is over-expressed in roughly 4% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).

OntologyGO

Biological processes

• acetyl-CoA metabolic process
• D-glucose import
• energy homeostasis
• fatty acid biosynthetic process
• fatty acid homeostasis
• fatty acid oxidation
• intracellular glutamate homeostasis
• malonyl-CoA biosynthetic process
• negative regulation of fatty acid beta-oxidation
• pentose-phosphate shunt
• positive regulation of heart growth
• positive regulation of lipid storage
• protein homotetramerization
• regulation of cardiac muscle hypertrophy in response to stress
• regulation of glucose metabolic process
• response to caloric restriction
• response to nutrient
• response to xenobiotic stimulus
• tricarboxylic acid metabolic process
• intracellular aspartate homeostasis
• lactic acid secretion

Molecular functions

• acetyl-CoA carboxylase activity
• ATP binding
• biotin binding
• identical protein binding
• metal ion binding

Cellular components

• cytosol
• mitochondrial fatty acid beta-oxidation multienzyme complex
• mitochondrial outer membrane
• mitochondrion
• nucleus

Protein domainsUniProt · Pfam · InterPro

• Biotin/lipoyl attachment
• Carbamoyl phosphate synthase, ATP-binding domain
• Biotin carboxylase-like, N-terminal domain
• Biotin carboxylase, C-terminal
• Single hybrid motif
• Rudiment single hybrid motif
• ATP-grasp fold
• Acetyl-coenzyme A carboxyltransferase, N-terminal
• Acetyl-coenzyme A carboxyltransferase, C-terminal
• Biotin carboxylation domain
• Acetyl-CoA carboxylase, central domain
• ATP-grasp fold, subdomain 1
• Pre-ATP-grasp domain superfamily
• ClpP/crotonase-like domain superfamily
• Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta
• Acetyl-CoA carboxylase, BT domain
• Acetyl-CoA carboxylase
• Biotin carboxylase, N-terminal domain
• Biotin-requiring enzyme
• Carboxyl transferase domain
• Biotin carboxylase C-terminal domain
• Carbamoyl-phosphate synthase L chain, ATP binding domain
• Acetyl-CoA carboxylase, central region
• Acetyl-CoA carboxylase, BT domain

KeywordsUniProt

• Allosteric enzyme
• ATP-binding
• Biotin
• Fatty acid biosynthesis
• Fatty acid metabolism
• Ligase
• Lipid biosynthesis
• Lipid metabolism
• Magnesium
• Manganese
• Metal-binding
• Mitochondrion
• Multifunctional enzyme
• Nucleotide-binding
• Phosphoprotein
• Transit peptide

InteractionsUniProt · HPA

Protein binding partners of ACACB in the human serome: UniProt-annotated complex subunits plus reported interactors. Each links to its own Seroatlas record.

• MID1IP1
• HLCS