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Protein

Acetyl-CoA carboxylase 2

Gene

Acacb

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the ATP-dependent carboxylation of acetyl-CoA to malonyl-CoA (By similarity). Carries out three functions: biotin carboxyl carrier protein, biotin carboxylase and carboxyltransferase (By similarity). Involved in inhibition of fatty acid and glucose oxidation and enhancement of fat storage (PubMed:11283375, PubMed:12920182, PubMed:15677334, PubMed:18487439, PubMed:22362781). May play a role in regulation of mitochondrial fatty acid oxidation through malonyl-CoA-dependent inhibition of carnitine palmitoyltransferase 1 (PubMed:10677481).1 PublicationBy similarity5 Publications

Catalytic activityi

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

Cofactori

Protein has several cofactor binding sites:
  • biotinBy similarity
  • Mn2+PROSITE-ProRule annotationNote: Binds 2 manganese ions per subunit.PROSITE-ProRule annotation

Enzyme regulationi

Activity is increased by oligomerization. Activated by citrate. Citrate and MID1IP1 promote oligomerization. Inhibited by malonyl-CoA.By similarity

Pathway:imalonyl-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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi557 – 5571Manganese 1PROSITE-ProRule annotation
Metal bindingi570 – 5701Manganese 1PROSITE-ProRule annotation
Metal bindingi570 – 5701Manganese 2PROSITE-ProRule annotation
Metal bindingi572 – 5721Manganese 2PROSITE-ProRule annotation
Active sitei574 – 5741By similarity
Binding sitei1924 – 19241Coenzyme ABy similarity
Binding sitei2228 – 22281Coenzyme ABy similarity
Binding sitei2230 – 22301Coenzyme ABy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi434 – 49158ATPPROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

  • acetyl-CoA metabolic process Source: MGI
  • fatty acid biosynthetic process Source: MGI
  • malonyl-CoA biosynthetic process Source: UniProtKB
  • negative regulation of fatty acid oxidation Source: UniProtKB
  • positive regulation of heart growth Source: UniProtKB
  • positive regulation of lipid storage Source: UniProtKB
  • protein homotetramerization Source: MGI
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

BRENDAi6.4.1.2. 3474.
ReactomeiREACT_293784. Import of palmitoyl-CoA into the mitochondrial matrix.
REACT_303828. Activation of gene expression by SREBF (SREBP).
REACT_333418. Biotin transport and metabolism.
REACT_333964. ChREBP activates metabolic gene expression.
UniPathwayiUPA00655; UER00711.

Names & Taxonomyi

Protein namesi
Recommended name:
Acetyl-CoA carboxylase 2By similarity (EC:6.4.1.2By similarity)
Alternative name(s):
ACC-betaBy similarity
Including the following 1 domains:
Biotin carboxylaseBy similarity (EC:6.3.4.14)
Gene namesi
Name:AcacbImported
Synonyms:Acc21 Publication, AccbImported
OrganismiMus musculus (Mouse)Imported
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:2140940. Acacb.

Subcellular locationi

GO - Cellular componenti

  • endomembrane system Source: UniProtKB-SubCell
  • membrane Source: UniProtKB-KW
  • mitochondrion Source: UniProtKB
  • nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Nucleus

Pathology & Biotechi

Disruption phenotypei

Normal morphology, fertility, growth rate and lifespan but higher than normal food consumption and fatty acid oxidation rate and decreased fat content in adipose tissue and liver (PubMed:11283375). A high-fat/high-carbohydrate diet results in maintenance of normal insulin and glucose levels with less weight gain and less fat accumulation than wild-type mice (PubMed:12920182). Elevated levels of Ucp2 in adipose tissue and heart but not in skeletal muscle or liver, and elevated levels of Ucp3 in skeletal muscle but not in heart or brown adipose tissue (PubMed:12920182). Significant decrease in body weight, weight of epidydimal fat pads and levels of hepatic triglycerides under a range of dietary conditions including normal chow diet, fasting and refeeding a fat-free high-carbohydrate diet, and a high-fat/high-carbohydrate diet (PubMed:22362781). Up-regulation of lipogenic enzymes under de novo lipogenic conditions but reduced fat accumulation in liver (PubMed:22362781). Primary cultured adipocytes show increased fatty acid and glucose oxidation rates and increased lipolysis (PubMed:15677334). Reduced heart size, reduced Mlycd and malonyl-CoA levels in mutant hearts, reduced myocardial triglyceride levels, higher myocardial oleate and glucose oxidation rates, reduced levels of Ppara and reduced activation of Mtor (PubMed:18487439, PubMed:22730442). However, it has also been reported that mutants show no differences in body weight, food intake, body composition or glucose homeostasis as compared with controls fed on chow or a high-fat diet (PubMed:20368432).7 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi212 – 2121S → A: No phosphorylation by AMPK, reduced fatty acid oxidation in skeletal muscle, increased lipid deposition in skeletal muscle, and development of insulin resistance. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 2448Acetyl-CoA carboxylase 21 PublicationPRO_0000430774
Transit peptidei1 – ?Mitochondrion1 Publication

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei35 – 351PhosphoserineBy similarity
Modified residuei81 – 811PhosphoserineBy similarity
Modified residuei85 – 851PhosphoserineBy similarity
Modified residuei190 – 1901PhosphoserineBy similarity
Modified residuei212 – 2121Phosphoserine; by AMPK1 Publication
Modified residuei459 – 4591PhosphoserineBy similarity
Modified residuei919 – 9191N6-biotinyllysinePROSITE-ProRule annotationBy similarity

Post-translational modificationi

Phosphorylated by AMPK, leading to inactivation of the enzyme. Required for the maintenance of skeletal muscle lipid and glucose homeostasis.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiE9Q4Z2.
PRIDEiE9Q4Z2.

PTM databases

PhosphoSiteiQ6JIZ0.

Expressioni

Gene expression databases

ExpressionAtlasiE9Q4Z2. baseline and differential.
GenevisibleiE9Q4Z2. MM.

Interactioni

Subunit structurei

Monomer, homodimer, and homotetramer. Can form filamentous polymers. Interacts with MID1IP1; interaction with MID1IP1 promotes oligomerization and increases its activity.By similarity

Protein-protein interaction databases

BioGridi221514. 1 interaction.
MINTiMINT-1859452.
STRINGi10090.ENSMUSP00000031583.

Structurei

3D structure databases

ProteinModelPortaliE9Q4Z2.
SMRiE9Q4Z2. Positions 227-748, 881-950, 1687-2435.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini249 – 751503Biotin carboxylationSequence AnalysisAdd
BLAST
Domaini408 – 599192ATP-graspPROSITE-ProRule annotationAdd
BLAST
Domaini878 – 95275Biotinyl-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1799 – 2295497CarboxyltransferaseSequence AnalysisAdd
BLAST

Sequence similaritiesi

Contains 1 ATP-grasp domain.PROSITE-ProRule annotation
Contains 1 biotin carboxylation domain.SAAS annotation
Contains 1 biotinyl-binding domain.PROSITE-ProRule annotation
Contains 1 carboxyltransferase domain.Sequence Analysis

Keywords - Domaini

Transit peptide

Phylogenomic databases

GeneTreeiENSGT00550000074703.
HOGENOMiHOG000214115.
HOVERGENiHBG005371.
InParanoidiE9Q4Z2.
KOiK11262.
OMAiWYEENKK.
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.
IPR011764. Biotin_carboxylation_dom.
IPR005482. Biotin_COase_C.
IPR000089. Biotin_lipoyl.
IPR005481. CarbamoylP_synth_lsu_N.
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.
PF00364. Biotin_lipoyl. 1 hit.
PF01039. Carboxyl_trans. 1 hit.
PF00289. CPSase_L_chain. 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.
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]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

E9Q4Z2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVLLLFLTCL VFSCLTFSWL KIWGKMTDSK PLTNSKVEAN LLSSEESLSA
60 70 80 90 100
SELSGEQLQE HGDHSCLSYR GPRDASQQRN SLPSSCQRPP RNPLSSNDTW
110 120 130 140 150
PSPELQTNWT AAPGPEVPDA NGLSFPARPP SQRTVSPSRE DRKQAHIKRQ
160 170 180 190 200
LMTSFILGSL DDNSSDEDPS AGSFQNSSRK SSRASLGTLS QEAALNTSDP
210 220 230 240 250
ESHAPTMRPS MSGLHLVKRG REHKKLDLHR DFTVASPAEF VTRFGGNRVI
260 270 280 290 300
EKVLIANNGI AAVKCMRSIR RWAYEMFRNE RAIRFVVMVT PEDLKANAEY
310 320 330 340 350
IKMADQYVPV PGGPNNNNYA NVELIIDIAK RIPVQAVWAG WGHASENPKL
360 370 380 390 400
PELLCKHEIA FLGPPSEAMW ALGDKIASTI VAQTLQIPTL PWSGSGLTVE
410 420 430 440 450
WTEDSRHQGK CISVPEDVYE QGCVKDVDEG LQAAEKIGFP LMIKASEGGG
460 470 480 490 500
GKGIRKAESA EDFPMLFRQV QSEIPGSPIF LMKLAQNARH LEVQVLADQY
510 520 530 540 550
GNAVSLFGRD CSIQRRHQKI IEEAPATIAA PAVFEFMEQC AVLLAKMVGY
560 570 580 590 600
VSAGTVEYLY SQDGSFHFLE LNPRLQVEHP CTEMIADVNL PAAQLQIAMG
610 620 630 640 650
VPLHRLKDIR LLYGESPWGV TPIPFETPLS PPIARGHVIA ARITSENPDE
660 670 680 690 700
GFKPSSGTVQ ELNFRSNKNV WGYFSVAAAG GLHEFADSQF GHCFSWGENR
710 720 730 740 750
EEAISNMVVA LKELSIRGDF RTTVEYLVNL LETESFQNND IDTGWLDHLI
760 770 780 790 800
AQRVQAEKPD IMLGVVCGAL NVADAMFRTC MTEFLHSLER GQVLPADSLL
810 820 830 840 850
NIVDVELIYG GIKYALKVAR QSLTMFVLIM NGCHIEIDAH RLNDGGLLLS
860 870 880 890 900
YNGSSYTTYM KEEVDSYRIT IGNKTCVFEK ENDPTVLRSP SAGKLMQYTV
910 920 930 940 950
EDGDHVEAGS SYAEMEVMKM IMTLNVQESG RVKYIKRPGV ILEAGCVVAR
960 970 980 990 1000
LELDDPSKVH AAQPFTGELP AQQTLPILGE KLHQVFHGVL ENLTNVMSGY
1010 1020 1030 1040 1050
CLPEPFFSMK LKDWVQKLMM TLRHPSLPLL ELQEIMTSVA GRIPAPVEKA
1060 1070 1080 1090 1100
VRRVMAQYAS NITSVLCQFP SQQIATILDC HAATLQRKAD REVFFMNTQS
1110 1120 1130 1140 1150
IVQLVQRYRS GTRGYMKAVV LDLLRKYLNV EHHFQQAHYD KCVINLREQF
1160 1170 1180 1190 1200
KPDMTQVLDC IFSHSQVAKK NQLVTMLIDE LCGPDPTLSD ELTSILCELT
1210 1220 1230 1240 1250
QLSRSEHCKV ALRARQVLIA SHLPSYELRH NQVESIFLSA IDMYGHQFCP
1260 1270 1280 1290 1300
ENLKKLILSE TTIFDVLPTF FYHENKVVCM ASLEVYVRRG YIAYELNSLQ
1310 1320 1330 1340 1350
HRELPDGTCV VEFQFMLPSS HPNRMAVPIS VSNPDLLRHS TELFMDSGFS
1360 1370 1380 1390 1400
PLCQRMGAMV AFRRFEEFTR NFDEVISCFA NVQTDTLLFS KACTSLYSEE
1410 1420 1430 1440 1450
DSKSLREEPI HILNVAIQCA DHMEDEALVP VFRAFVQSKK HILVDYGLRR
1460 1470 1480 1490 1500
ITFLVAQERE FPKFFTFRAR DEFAEDRIYR HLEPALAFQL ELSRMRNFDL
1510 1520 1530 1540 1550
TAVPCANHKM HLYLGAAKVK EGLEVTDHRF FIRAIIRHSD LITKEASFEY
1560 1570 1580 1590 1600
LQNEGERLLL EAMDELEVAF NNTSVRTDCN HIFLNFVPTV IMDPLKIEES
1610 1620 1630 1640 1650
VRDMVMRYGS RLWKLRVLQA EVKINIRQTT SDSAIPIRLF ITNESGYYLD
1660 1670 1680 1690 1700
ISLYREVTDS RSGNIMFHSF GNKQGSLHGM LINTPYVTKD LLQAKRFQAQ
1710 1720 1730 1740 1750
SLGTTYVYDF PEMFRQALFK LWGSPEKYPK DILTYTELVL DSQGQLVEMN
1760 1770 1780 1790 1800
RLPGCNEVGM VAFKMRFKTP EYPEGRDAVV IGNDITFQIG SFGIGEDFLY
1810 1820 1830 1840 1850
LRASEMARTE GIPQIYLAAN SGARMGLAEE IKQIFQVAWV DPEDPHKGFR
1860 1870 1880 1890 1900
YLYLTPQDYT QISSQNSVHC KHIEDEGESR YVIVDVIGKD ANLGVENLRG
1910 1920 1930 1940 1950
SGMIAGEASL AYEKTVTISM VTCRALGIGA YLVRLGQRVI QVENSHIILT
1960 1970 1980 1990 2000
GAGALNKVLG REVYTSNNQL GGVQIMHTNG VSHVTVPDDF EGVCTILEWL
2010 2020 2030 2040 2050
SFIPKDNRSP VPITTPSDPI DREIEFTPTK APYDPRWMLA GRPHPTLKGT
2060 2070 2080 2090 2100
WQSGFFDHGS FKEIMAPWAQ TVVTGRARLG GIPVGVIAVE TRTVEVAVPA
2110 2120 2130 2140 2150
DPANLDSEAK IIQQAGQVWF PDSAYKTAQV IRDFNKERLP LMIFANWRGF
2160 2170 2180 2190 2200
SGGMKDMYEQ MLKFGAYIVD GLRLYEQPIL IYIPPCAELR GGSWVVLDST
2210 2220 2230 2240 2250
INPLCIEMYA DKESRGGVLE PEGTVEIKFR KKDLVKTIRR IDPVCKKLVG
2260 2270 2280 2290 2300
QLGKAQLPDK DRKELEGQLK AREELLLPIY HQVAVQFADL HDTPGHMLEK
2310 2320 2330 2340 2350
GIISDVLEWK TARTFFYWRL RRLLLEAQVK QEILRASPEL NHEHTQSMLR
2360 2370 2380 2390 2400
RWFVETEGAV KAYLWDSNQV VVQWLEQHWS AKDGLRSTIR ENINYLKRDS
2410 2420 2430 2440
VLKTIQSLVQ EHPEVIMDCV AYLSQHLTPA ERIQVAQLLS TTESPASS
Length:2,448
Mass (Da):275,750
Last modified:April 5, 2011 - v1
Checksum:i6CD686C7AF012A5E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti124 – 1241S → P in AAS13686 (Ref. 1) Curated
Sequence conflicti534 – 5341F → S in AAS13686 (Ref. 1) Curated
Sequence conflicti562 – 5621Q → R in AAS13686 (Ref. 1) Curated
Sequence conflicti1315 – 13151F → S in AAS13686 (Ref. 1) Curated
Sequence conflicti1402 – 14021S → N in AAS13686 (Ref. 1) Curated
Sequence conflicti2341 – 23411N → S in AAS13686 (Ref. 1) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY451394 mRNA. Translation: AAS13686.1.
AC122282 Genomic DNA. No translation available.
CCDSiCCDS19561.1.
RefSeqiNP_598665.2. NM_133904.2.
XP_006530176.1. XM_006530113.2.
UniGeneiMm.81793.

Genome annotation databases

EnsembliENSMUST00000031583; ENSMUSP00000031583; ENSMUSG00000042010.
ENSMUST00000102582; ENSMUSP00000099642; ENSMUSG00000042010.
GeneIDi100705.
KEGGimmu:100705.
UCSCiuc008yzi.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY451394 mRNA. Translation: AAS13686.1.
AC122282 Genomic DNA. No translation available.
CCDSiCCDS19561.1.
RefSeqiNP_598665.2. NM_133904.2.
XP_006530176.1. XM_006530113.2.
UniGeneiMm.81793.

3D structure databases

ProteinModelPortaliE9Q4Z2.
SMRiE9Q4Z2. Positions 227-748, 881-950, 1687-2435.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi221514. 1 interaction.
MINTiMINT-1859452.
STRINGi10090.ENSMUSP00000031583.

Chemistry

ChEMBLiCHEMBL3108631.

PTM databases

PhosphoSiteiQ6JIZ0.

Proteomic databases

MaxQBiE9Q4Z2.
PRIDEiE9Q4Z2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000031583; ENSMUSP00000031583; ENSMUSG00000042010.
ENSMUST00000102582; ENSMUSP00000099642; ENSMUSG00000042010.
GeneIDi100705.
KEGGimmu:100705.
UCSCiuc008yzi.2. mouse.

Organism-specific databases

CTDi32.
MGIiMGI:2140940. Acacb.

Phylogenomic databases

GeneTreeiENSGT00550000074703.
HOGENOMiHOG000214115.
HOVERGENiHBG005371.
InParanoidiE9Q4Z2.
KOiK11262.
OMAiWYEENKK.
TreeFamiTF300061.

Enzyme and pathway databases

UniPathwayiUPA00655; UER00711.
BRENDAi6.4.1.2. 3474.
ReactomeiREACT_293784. Import of palmitoyl-CoA into the mitochondrial matrix.
REACT_303828. Activation of gene expression by SREBF (SREBP).
REACT_333418. Biotin transport and metabolism.
REACT_333964. ChREBP activates metabolic gene expression.

Miscellaneous databases

ChiTaRSiAcacb. mouse.
NextBioi354598.
PROiE9Q4Z2.
SOURCEiSearch...

Gene expression databases

ExpressionAtlasiE9Q4Z2. baseline and differential.
GenevisibleiE9Q4Z2. MM.

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.
IPR011764. Biotin_carboxylation_dom.
IPR005482. Biotin_COase_C.
IPR000089. Biotin_lipoyl.
IPR005481. CarbamoylP_synth_lsu_N.
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.
PF00364. Biotin_lipoyl. 1 hit.
PF01039. Carboxyl_trans. 1 hit.
PF00289. CPSase_L_chain. 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.
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...

Publicationsi

« Hide 'large scale' publications
  1. "Alternative splicing in the mouse acetyl-CoA carboxylase 2 (ACC2) gene."
    Mao J., Wakil S.J.
    Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C57BL/6JImported.
    Tissue: HeartImported.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6JImported.
  3. Cited for: FUNCTION, SUBCELLULAR LOCATION.
  4. "Continuous fatty acid oxidation and reduced fat storage in mice lacking acetyl-CoA carboxylase 2."
    Abu-Elheiga L., Matzuk M.M., Abo-Hashema K.A., Wakil S.J.
    Science 291:2613-2616(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  5. "Acetyl-CoA carboxylase 2 mutant mice are protected against obesity and diabetes induced by high-fat/high-carbohydrate diets."
    Abu-Elheiga L., Oh W., Kordari P., Wakil S.J.
    Proc. Natl. Acad. Sci. U.S.A. 100:10207-10212(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  6. "Glucose and fat metabolism in adipose tissue of acetyl-CoA carboxylase 2 knockout mice."
    Oh W., Abu-Elheiga L., Kordari P., Gu Z., Shaikenov T., Chirala S.S., Wakil S.J.
    Proc. Natl. Acad. Sci. U.S.A. 102:1384-1389(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  8. Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  9. "Gene knockout of Acc2 has little effect on body weight, fat mass, or food intake."
    Olson D.P., Pulinilkunnil T., Cline G.W., Shulman G.I., Lowell B.B.
    Proc. Natl. Acad. Sci. U.S.A. 107:7598-7603(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  10. "Cardiac-specific deletion of acetyl CoA carboxylase 2 prevents metabolic remodeling during pressure-overload hypertrophy."
    Kolwicz S.C. Jr., Olson D.P., Marney L.C., Garcia-Menendez L., Synovec R.E., Tian R.
    Circ. Res. 111:728-738(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  11. "Acetyl-CoA carboxylase 2-/- mutant mice are protected against fatty liver under high-fat, high-carbohydrate dietary and de novo lipogenic conditions."
    Abu-Elheiga L., Wu H., Gu Z., Bressler R., Wakil S.J.
    J. Biol. Chem. 287:12578-12588(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  12. Cited for: PHOSPHORYLATION AT SER-212, MUTAGENESIS OF SER-212.

Entry informationi

Entry nameiACACB_MOUSE
AccessioniPrimary (citable) accession number: E9Q4Z2
Secondary accession number(s): Q6JIZ0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 29, 2014
Last sequence update: April 5, 2011
Last modified: July 22, 2015
This is version 41 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Allosteric enzyme, Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.