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Q5SWU9

- ACACA_MOUSE

UniProt

Q5SWU9 - ACACA_MOUSE

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Protein

Acetyl-CoA carboxylase 1

Gene

Acaca

Organism
Mus musculus (Mouse)
Status
Reviewed - 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 (By similarity).By similarity

Catalytic activityi

ATP + acetyl-CoA + HCO3- = ADP + phosphate + malonyl-CoA.By similarity1 Publication
ATP + biotin-[carboxyl-carrier-protein] + CO2 = ADP + phosphate + carboxy-biotin-[carboxyl-carrier-protein].1 Publication

Cofactori

Biotin.By similarity
Binds 2 manganese ions per subunit.By similarity

Enzyme regulationi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi423 – 4231Manganese 1Sequence Analysis
Metal bindingi436 – 4361Manganese 1Sequence Analysis
Metal bindingi436 – 4361Manganese 2Sequence Analysis
Metal bindingi438 – 4381Manganese 2Sequence Analysis
Active sitei440 – 4401Sequence Analysis
Binding sitei1822 – 18221Coenzyme ABy similarity
Binding sitei2126 – 21261Coenzyme ABy similarity
Binding sitei2128 – 21281Coenzyme ABy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi300 – 35758ATPPROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. acetyl-CoA carboxylase activity Source: UniProtKB
  2. ATP binding Source: UniProtKB-KW
  3. biotin carboxylase activity Source: UniProtKB-EC
  4. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. acetyl-CoA metabolic process Source: UniProtKB
  2. fatty acid biosynthetic process Source: UniProtKB
  3. lipid homeostasis Source: MGI
  4. lipid metabolic process Source: MGI
  5. malonyl-CoA biosynthetic process Source: UniProtKB-UniPathway
  6. multicellular organismal protein metabolic process Source: MGI
  7. protein homotetramerization Source: UniProtKB
  8. tissue homeostasis 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

ReactomeiREACT_189100. Defective HLCS causes multiple carboxylase deficiency.
REACT_198969. Activation of gene expression by SREBF (SREBP).
REACT_206176. Biotin transport and metabolism.
UniPathwayiUPA00655; UER00711.

Names & Taxonomyi

Protein namesi
Recommended name:
Acetyl-CoA carboxylase 1 (EC:6.4.1.2)
Short name:
ACC1
Alternative name(s):
ACC-alpha
Acetyl-CoA carboxylase 265
Including the following 1 domains:
Biotin carboxylase (EC:6.3.4.14)
Gene namesi
Name:AcacaImported
Synonyms:AcacImported, Gm738
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 11

Organism-specific databases

MGIiMGI:108451. Acaca.

Subcellular locationi

Cytoplasm 2 Publications

GO - Cellular componenti

  1. cytosol Source: UniProtKB
  2. extracellular vesicular exosome Source: Ensembl
  3. mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 23452345Acetyl-CoA carboxylase 1PRO_0000258040Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei5 – 51PhosphoserineBy similarity
Modified residuei23 – 231PhosphoserineBy similarity
Modified residuei25 – 251Phosphoserine1 Publication
Modified residuei29 – 291Phosphoserine2 Publications
Modified residuei52 – 521PhosphoserineBy similarity
Modified residuei77 – 771PhosphoserineBy similarity
Modified residuei79 – 791Phosphoserine; alternate3 Publications
Modified residuei79 – 791Phosphoserine; by AMPK; alternate3 Publications
Modified residuei785 – 7851N6-biotinyllysineBy similarity
Modified residuei1200 – 12001PhosphoserineBy similarity
Modified residuei1215 – 12151PhosphoserineBy similarity
Modified residuei1262 – 12621PhosphoserineBy similarity
Modified residuei1333 – 13331N6-acetyllysineBy similarity

Post-translational modificationi

Phosphorylation on Ser-1262 is required for interaction with BRCA1.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ5SWU9.
PaxDbiQ5SWU9.
PRIDEiQ5SWU9.

PTM databases

PhosphoSiteiQ5SWU9.

Expressioni

Gene expression databases

BgeeiQ5SWU9.
CleanExiMM_ACACA.
ExpressionAtlasiQ5SWU9. baseline and differential.
GenevestigatoriQ5SWU9.

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.2 Publications

Protein-protein interaction databases

BioGridi223322. 2 interactions.
DIPiDIP-32276N.
IntActiQ5SWU9. 8 interactions.
MINTiMINT-4091386.

Structurei

3D structure databases

ProteinModelPortaliQ5SWU9.
SMRiQ5SWU9. Positions 101-615, 747-816, 1580-2337.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini116 – 617502Biotin carboxylationSequence AnalysisAdd
BLAST
Domaini274 – 465192ATP-graspPROSITE-ProRule annotationAdd
BLAST
Domaini751 – 81767Biotinyl-bindingSequence AnalysisAdd
BLAST
Domaini1697 – 2193497CarboxyltransferaseSequence AnalysisAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0511.
GeneTreeiENSGT00550000074703.
HOVERGENiHBG005371.
InParanoidiQ5SWU9.
KOiK11262.
OMAiHVFSGQC.
OrthoDBiEOG7HXCPW.
PhylomeDBiQ5SWU9.
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.
IPR001882. Biotin_BS.
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.
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 (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative promoter usage. Align

Isoform 1 (identifier: Q5SWU9-1) [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
MDEPSPLAKT LELNQHSRFI IGSVSEDNSE DEISNLVKLD LEEKEGSLSP
60 70 80 90 100
ASVSSDTLSD LGISGLQDGL AFHMRSSMSG LHLVKQGRDR KKIDSQRDFT
110 120 130 140 150
VASPAEFVTR FGGNKVIEKV LIANNGIAAV KCMRSIRRWS YEMFRNERAI
160 170 180 190 200
RFVVMVTPED LKANAEYIKM ADHYVPVPGG PNNNNYANVE LILDIAKRIP
210 220 230 240 250
VQAVWAGWGH ASENPKLPEL LLKNGIAFMG PPSQAMWALG DKIASSIVAQ
260 270 280 290 300
TAGIPTLPWS GSGLRVDWQE NDFSKRILNV PQDLYEKGYV KDVDDGLKAA
310 320 330 340 350
EEVGYPVMIK ASEGGGGKGI RKVNNADDFP NLFRQVQAEV PGSPIFVMRL
360 370 380 390 400
AKQSRHLEVQ ILADQYGNAI SLFGRDCSVQ RRHQKIIEEA PAAIATPAVF
410 420 430 440 450
EHMEQCAVKL AKMVGYVSAG TVEYLYSQDG SFYFLELNPR LQVEHPCTEM
460 470 480 490 500
VADVNLPAAQ LQIAMGIPLF RIKDIRMMYG VSPWGDAPID FENSAHVPCP
510 520 530 540 550
RGHVIAARIT SENPDEGFKP SSGTVQELNF RSNKNVWGYF SVAAAGGLHE
560 570 580 590 600
FADSQFGHCF SWGENREEAI SNMVVALKEL SIRGDFRTTV EYLIKLLETE
610 620 630 640 650
SFQLNRIDTG WLDRLIAEKV QAERPDTMLG VVCGALHVAD VSLRNSISNF
660 670 680 690 700
LHSLERGQVL PAHTLLNTVD VELIYEGIKY VLKVTRQSPN SYVVIMNGSC
710 720 730 740 750
VEVDVHRLSD GGLLLSYDGS SYTTYMKEEV DRYRITIGNK TCVFEKENDP
760 770 780 790 800
SVMRSPSAGK LIQYIVEDGG HVFAGQCYAE IEVMKMVMTL TAVESGCIHY
810 820 830 840 850
VKRPGAALDP GCVIAKMQLD NPSKVQQAEL HTGSLPQIQS TALRGEKLHR
860 870 880 890 900
VFHYVLDNLV NVMNGYCLPD PFFSSRVKDW VERLMKTLRD PSLPLLELQD
910 920 930 940 950
IMTSVSGRIP LNVEKSIKKE MAQYASNITS VLCQFPSQQI ANILDSHAAT
960 970 980 990 1000
LNRKSEREVF FMNTQSIVQL VQRYRSGIRG HMKAVVMDLL RQYLRVETQF
1010 1020 1030 1040 1050
QNGHYDKCVF ALREENKSDM NTVLNYIFSH AQVTKKNLLV TMLIDQLCGR
1060 1070 1080 1090 1100
DPTLTDELLN ILTELTQLSK TTNAKVALRA RQVLIASHLP SYELRHNQVE
1110 1120 1130 1140 1150
SIFLSAIDMY GHQFCIENLQ KLILSETSIF DVLPNFFYHS NQVVRMAALE
1160 1170 1180 1190 1200
VYVRRAYIAY ELNSVQHRQL KDNTCVVEFQ FMLPTSHPNR GNIPTLNRMS
1210 1220 1230 1240 1250
FASNLNHYGM THVASVSDVL LDNAFTPPCQ RMGGMVSFRT FEDFVRIFDE
1260 1270 1280 1290 1300
IMGCFCDSPP QSPTFPESGH TSLYDEDKVP RDEPIHILNV AIKTDGDIED
1310 1320 1330 1340 1350
DRLAAMFREF TQQNKATLVE HGIRRLTFLV AQKDFRKQVN CEVDQRFHRE
1360 1370 1380 1390 1400
FPKFFTFRAR DKFEEDRIYR HLEPALAFQL ELNRMRNFDL TAIPCANHKM
1410 1420 1430 1440 1450
HLYLGAAKVE VGTEVTDYRF FVRAIIRHSD LVTKEASFEY LQNEGERLLL
1460 1470 1480 1490 1500
EAMDELEVAF NNTNVRTDCN HIFLNFVPTV IMDPSKIEES VRSMVMRYGS
1510 1520 1530 1540 1550
RLWKLRVLQA ELKINIRLTT TGKAIPIRLF LTNESGYYLD ISLYKEVTDS
1560 1570 1580 1590 1600
RTAQIMFQAY GDKQGPLHGM LINTPYVTKD LLQSKRFQAQ SLGTTYIYDI
1610 1620 1630 1640 1650
PEMFRQSLIK LWESMSTQAF LPSPPLPSDI LTYTELVLDD QGQLVHMNRL
1660 1670 1680 1690 1700
PGGNEIGMVA WKMSLKSPEY PDGRDIIVIG NDITYRIGSF GPQEDLLFLR
1710 1720 1730 1740 1750
ASELARAEGI PRIYVAANSG ARIGLAEEIR HMFHVAWVDP EDPYKGYKYL
1760 1770 1780 1790 1800
YLTPQDYKRV SALNSVHCEH VEDEGESRYK ITDIIGKEEG LGAENLRGSG
1810 1820 1830 1840 1850
MIAGESSLAY DEVITISLVT CRAIGIGAYL VRLGQRTIQV ENSHLILTGA
1860 1870 1880 1890 1900
GALNKVLGRE VYTSNNQLGG IQIMHNNGVT HSTVCDDFEG VFTVLHWLSY
1910 1920 1930 1940 1950
MPKSVHSSVP LLNSKDPIDR IIEFVPTKAP YDPRWMLAGR PHPTQKGQWL
1960 1970 1980 1990 2000
SGFFDYGSFS EIMQPWAQTV VVGRARLGGI PVGVVAVETR TVELSIPADP
2010 2020 2030 2040 2050
ANLDSEAKII QQAGQVWFPD SAFKTYQAIK DFNREGLPLM VFANWRGFSG
2060 2070 2080 2090 2100
GMKDMYDQVL KFGAYIVDGL RECSQPVMVY IPPQAELRGG SWVVIDPTIN
2110 2120 2130 2140 2150
PRHMEMYADR ESRGSVLEPE GTVEIKFRKK DLVKTMRRVD PVYIRLAERL
2160 2170 2180 2190 2200
GTPELSPTER KELESKLKER EEFLIPIYHQ VAVQFADLHD TPGRMQEKGV
2210 2220 2230 2240 2250
INDILDWKTS RTFFYWRLRR LLLEDLVKKK IHNANPELTD GQIQAMLRRW
2260 2270 2280 2290 2300
FVEVEGTVKA YVWDNNKDLV EWLEKQLTEE DGVRSVIEEN IKYISRDYVL
2310 2320 2330 2340
KQIRSLVQAN PEVAMDSIVH MTQHISPTQR AEVVRILSTM DSPST
Length:2,345
Mass (Da):265,257
Last modified:December 21, 2004 - v1
Checksum:i6995C534B054FE02
GO
Isoform 2 (identifier: Q5SWU9-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:2,383
Mass (Da):269,958
Checksum:i57B7FB88C694692E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti623 – 6231E → G in AAS13685. 1 PublicationCurated
Sequence conflicti906 – 9061S → P in AAS13685. 1 PublicationCurated
Sequence conflicti933 – 9331C → Y in AAS13685. 1 PublicationCurated
Sequence conflicti1456 – 14561L → S in AAS13685. 1 PublicationCurated
Sequence conflicti1995 – 19951S → G in AAS13685. 1 PublicationCurated
Sequence conflicti2077 – 20771V → I in AAS13685. 1 PublicationCurated
Sequence conflicti2169 – 21691E → K in AAS13685. 1 PublicationCurated
Sequence conflicti2251 – 22511F → S in AAS13685. 1 PublicationCurated
Sequence conflicti2257 – 22571T → A in AAS13685. 1 PublicationCurated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MMWWSTLMSLLRASSFWRRI SAETIRIIRALRAYFERIM in isoform 2. 1 PublicationVSP_026101

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY451393 mRNA. Translation: AAS13685.1.
AL596252, AL596447 Genomic DNA. Translation: CAI24019.1.
AL596447, AL596252 Genomic DNA. Translation: CAI25271.1.
AL596447 Genomic DNA. Translation: CAI25272.1.
AL596447 Genomic DNA. Translation: CAI25273.1.
AL596447 Genomic DNA. Translation: CAI25274.1.
AL596447 Genomic DNA. Translation: CAM21560.1.
AJ619664 mRNA. Translation: CAF02251.1.
AJ619665 Genomic DNA. Translation: CAF02252.1.
AF374167 mRNA. Translation: AAK57389.1.
AF374168 mRNA. Translation: AAK57390.1.
AF374169 mRNA. Translation: AAK57391.1.
AF374170 mRNA. Translation: AAK57392.1.
BC056500 mRNA. Translation: AAH56500.1.
CCDSiCCDS25185.1. [Q5SWU9-1]
RefSeqiNP_579938.2. NM_133360.2. [Q5SWU9-1]
XP_006532016.1. XM_006531953.1. [Q5SWU9-2]
XP_006532017.1. XM_006531954.1. [Q5SWU9-1]
XP_006532018.1. XM_006531955.1. [Q5SWU9-1]
XP_006532019.1. XM_006531956.1. [Q5SWU9-1]
XP_006532020.1. XM_006531957.1. [Q5SWU9-1]
UniGeneiMm.31374.

Genome annotation databases

EnsembliENSMUST00000020843; ENSMUSP00000020843; ENSMUSG00000020532. [Q5SWU9-1]
ENSMUST00000103201; ENSMUSP00000099490; ENSMUSG00000020532. [Q5SWU9-1]
ENSMUST00000133811; ENSMUSP00000116174; ENSMUSG00000020532.
GeneIDi107476.
KEGGimmu:107476.
UCSCiuc007kql.1. mouse. [Q5SWU9-1]

Keywords - Coding sequence diversityi

Alternative promoter usage

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY451393 mRNA. Translation: AAS13685.1 .
AL596252 , AL596447 Genomic DNA. Translation: CAI24019.1 .
AL596447 , AL596252 Genomic DNA. Translation: CAI25271.1 .
AL596447 Genomic DNA. Translation: CAI25272.1 .
AL596447 Genomic DNA. Translation: CAI25273.1 .
AL596447 Genomic DNA. Translation: CAI25274.1 .
AL596447 Genomic DNA. Translation: CAM21560.1 .
AJ619664 mRNA. Translation: CAF02251.1 .
AJ619665 Genomic DNA. Translation: CAF02252.1 .
AF374167 mRNA. Translation: AAK57389.1 .
AF374168 mRNA. Translation: AAK57390.1 .
AF374169 mRNA. Translation: AAK57391.1 .
AF374170 mRNA. Translation: AAK57392.1 .
BC056500 mRNA. Translation: AAH56500.1 .
CCDSi CCDS25185.1. [Q5SWU9-1 ]
RefSeqi NP_579938.2. NM_133360.2. [Q5SWU9-1 ]
XP_006532016.1. XM_006531953.1. [Q5SWU9-2 ]
XP_006532017.1. XM_006531954.1. [Q5SWU9-1 ]
XP_006532018.1. XM_006531955.1. [Q5SWU9-1 ]
XP_006532019.1. XM_006531956.1. [Q5SWU9-1 ]
XP_006532020.1. XM_006531957.1. [Q5SWU9-1 ]
UniGenei Mm.31374.

3D structure databases

ProteinModelPortali Q5SWU9.
SMRi Q5SWU9. Positions 101-615, 747-816, 1580-2337.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 223322. 2 interactions.
DIPi DIP-32276N.
IntActi Q5SWU9. 8 interactions.
MINTi MINT-4091386.

Chemistry

ChEMBLi CHEMBL3086.

PTM databases

PhosphoSitei Q5SWU9.

Proteomic databases

MaxQBi Q5SWU9.
PaxDbi Q5SWU9.
PRIDEi Q5SWU9.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000020843 ; ENSMUSP00000020843 ; ENSMUSG00000020532 . [Q5SWU9-1 ]
ENSMUST00000103201 ; ENSMUSP00000099490 ; ENSMUSG00000020532 . [Q5SWU9-1 ]
ENSMUST00000133811 ; ENSMUSP00000116174 ; ENSMUSG00000020532 .
GeneIDi 107476.
KEGGi mmu:107476.
UCSCi uc007kql.1. mouse. [Q5SWU9-1 ]

Organism-specific databases

CTDi 31.
MGIi MGI:108451. Acaca.

Phylogenomic databases

eggNOGi COG0511.
GeneTreei ENSGT00550000074703.
HOVERGENi HBG005371.
InParanoidi Q5SWU9.
KOi K11262.
OMAi HVFSGQC.
OrthoDBi EOG7HXCPW.
PhylomeDBi Q5SWU9.
TreeFami TF300061.

Enzyme and pathway databases

UniPathwayi UPA00655 ; UER00711 .
Reactomei REACT_189100. Defective HLCS causes multiple carboxylase deficiency.
REACT_198969. Activation of gene expression by SREBF (SREBP).
REACT_206176. Biotin transport and metabolism.

Miscellaneous databases

NextBioi 358872.
PROi Q5SWU9.
SOURCEi Search...

Gene expression databases

Bgeei Q5SWU9.
CleanExi MM_ACACA.
ExpressionAtlasi Q5SWU9. baseline and differential.
Genevestigatori Q5SWU9.

Family and domain databases

Gene3Di 3.30.1490.20. 1 hit.
3.30.470.20. 1 hit.
3.40.50.20. 1 hit.
3.90.226.10. 3 hits.
InterProi IPR013537. 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.
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 ]
Pfami PF08326. 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 ]
SMARTi SM00878. Biotin_carb_C. 1 hit.
[Graphical view ]
SUPFAMi SSF51230. SSF51230. 1 hit.
SSF51246. SSF51246. 1 hit.
SSF52096. SSF52096. 2 hits.
SSF52440. SSF52440. 1 hit.
PROSITEi 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.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of the mouse acetyl-CoA carboxylase 1 (ACC1) gene and identification of an intronless pseudogene."
    Mao J., Wakil S.J.
    Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Strain: C57BL/6JImported.
    Tissue: LiverImported.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "Asymmetric expression of transcripts derived from the shared promoter between the divergently oriented ACACA and TADA2L genes."
    Travers M.T., Cambot M., Kennedy H.T., Lenoir G.M., Barber M.C., Joulin V.
    Genomics 85:71-84(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 1-119 (ISOFORM 2).
    Strain: Swiss.
    Tissue: Brain.
  4. "Acetyl-CoA carboxylase and SREBP expression during peripheral nervous system myelination."
    Salles J., Sargueil F., Knoll-Gellida A., Witters L.A., Cassagne C., Garbay B.
    Biochim. Biophys. Acta 1631:229-238(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-38; 1221-1348 AND 1681-1891.
    Strain: C57BL/6Imported.
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1501-2345.
    Strain: C57BL/6Imported.
    Tissue: BrainImported.
  6. "BRCA1 interacts with acetyl-CoA carboxylase through its tandem of BRCT domains."
    Magnard C., Bachelier R., Vincent A., Jaquinod M., Kieffer S., Lenoir G.M., Venezia N.D.
    Oncogene 21:6729-6739(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 298-306 AND 2267-2275, INTERACTION WITH BRCA1, SUBCELLULAR LOCATION.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25 AND SER-29, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  8. "Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis."
    Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.
    J. Proteome Res. 7:3957-3967(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29 AND SER-79, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  9. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
    Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
    Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  10. Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, ENZYME REGULATION, INTERACTION WITH MID1IP1, PHOSPHORYLATION AT SER-79, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiACACA_MOUSE
AccessioniPrimary (citable) accession number: Q5SWU9
Secondary accession number(s): A2A6H4
, Q5SWU6, Q5SWU7, Q5SWU8, Q6JIZ1, Q6PHL9, Q705X8, Q705X9, Q91VC8, Q925C4, Q925C5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: December 21, 2004
Last modified: October 29, 2014
This is version 107 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, Direct protein sequencing, 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