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Q5SWU9

- ACACA_MOUSE

UniProt

Q5SWU9 - ACACA_MOUSE

Protein

Acetyl-CoA carboxylase 1

Gene

Acaca

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 106 (01 Oct 2014)
      Sequence version 1 (21 Dec 2004)
      Previous versions | rss
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    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
    5. protein binding Source: UniProtKB

    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

    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. mitochondrion Source: MGI

    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

    ArrayExpressiQ5SWU9.
    BgeeiQ5SWU9.
    CleanExiMM_ACACA.
    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

    MDEPSPLAKT LELNQHSRFI IGSVSEDNSE DEISNLVKLD LEEKEGSLSP     50
    ASVSSDTLSD LGISGLQDGL AFHMRSSMSG LHLVKQGRDR KKIDSQRDFT 100
    VASPAEFVTR FGGNKVIEKV LIANNGIAAV KCMRSIRRWS YEMFRNERAI 150
    RFVVMVTPED LKANAEYIKM ADHYVPVPGG PNNNNYANVE LILDIAKRIP 200
    VQAVWAGWGH ASENPKLPEL LLKNGIAFMG PPSQAMWALG DKIASSIVAQ 250
    TAGIPTLPWS GSGLRVDWQE NDFSKRILNV PQDLYEKGYV KDVDDGLKAA 300
    EEVGYPVMIK ASEGGGGKGI RKVNNADDFP NLFRQVQAEV PGSPIFVMRL 350
    AKQSRHLEVQ ILADQYGNAI SLFGRDCSVQ RRHQKIIEEA PAAIATPAVF 400
    EHMEQCAVKL AKMVGYVSAG TVEYLYSQDG SFYFLELNPR LQVEHPCTEM 450
    VADVNLPAAQ LQIAMGIPLF RIKDIRMMYG VSPWGDAPID FENSAHVPCP 500
    RGHVIAARIT SENPDEGFKP SSGTVQELNF RSNKNVWGYF SVAAAGGLHE 550
    FADSQFGHCF SWGENREEAI SNMVVALKEL SIRGDFRTTV EYLIKLLETE 600
    SFQLNRIDTG WLDRLIAEKV QAERPDTMLG VVCGALHVAD VSLRNSISNF 650
    LHSLERGQVL PAHTLLNTVD VELIYEGIKY VLKVTRQSPN SYVVIMNGSC 700
    VEVDVHRLSD GGLLLSYDGS SYTTYMKEEV DRYRITIGNK TCVFEKENDP 750
    SVMRSPSAGK LIQYIVEDGG HVFAGQCYAE IEVMKMVMTL TAVESGCIHY 800
    VKRPGAALDP GCVIAKMQLD NPSKVQQAEL HTGSLPQIQS TALRGEKLHR 850
    VFHYVLDNLV NVMNGYCLPD PFFSSRVKDW VERLMKTLRD PSLPLLELQD 900
    IMTSVSGRIP LNVEKSIKKE MAQYASNITS VLCQFPSQQI ANILDSHAAT 950
    LNRKSEREVF FMNTQSIVQL VQRYRSGIRG HMKAVVMDLL RQYLRVETQF 1000
    QNGHYDKCVF ALREENKSDM NTVLNYIFSH AQVTKKNLLV TMLIDQLCGR 1050
    DPTLTDELLN ILTELTQLSK TTNAKVALRA RQVLIASHLP SYELRHNQVE 1100
    SIFLSAIDMY GHQFCIENLQ KLILSETSIF DVLPNFFYHS NQVVRMAALE 1150
    VYVRRAYIAY ELNSVQHRQL KDNTCVVEFQ FMLPTSHPNR GNIPTLNRMS 1200
    FASNLNHYGM THVASVSDVL LDNAFTPPCQ RMGGMVSFRT FEDFVRIFDE 1250
    IMGCFCDSPP QSPTFPESGH TSLYDEDKVP RDEPIHILNV AIKTDGDIED 1300
    DRLAAMFREF TQQNKATLVE HGIRRLTFLV AQKDFRKQVN CEVDQRFHRE 1350
    FPKFFTFRAR DKFEEDRIYR HLEPALAFQL ELNRMRNFDL TAIPCANHKM 1400
    HLYLGAAKVE VGTEVTDYRF FVRAIIRHSD LVTKEASFEY LQNEGERLLL 1450
    EAMDELEVAF NNTNVRTDCN HIFLNFVPTV IMDPSKIEES VRSMVMRYGS 1500
    RLWKLRVLQA ELKINIRLTT TGKAIPIRLF LTNESGYYLD ISLYKEVTDS 1550
    RTAQIMFQAY GDKQGPLHGM LINTPYVTKD LLQSKRFQAQ SLGTTYIYDI 1600
    PEMFRQSLIK LWESMSTQAF LPSPPLPSDI LTYTELVLDD QGQLVHMNRL 1650
    PGGNEIGMVA WKMSLKSPEY PDGRDIIVIG NDITYRIGSF GPQEDLLFLR 1700
    ASELARAEGI PRIYVAANSG ARIGLAEEIR HMFHVAWVDP EDPYKGYKYL 1750
    YLTPQDYKRV SALNSVHCEH VEDEGESRYK ITDIIGKEEG LGAENLRGSG 1800
    MIAGESSLAY DEVITISLVT CRAIGIGAYL VRLGQRTIQV ENSHLILTGA 1850
    GALNKVLGRE VYTSNNQLGG IQIMHNNGVT HSTVCDDFEG VFTVLHWLSY 1900
    MPKSVHSSVP LLNSKDPIDR IIEFVPTKAP YDPRWMLAGR PHPTQKGQWL 1950
    SGFFDYGSFS EIMQPWAQTV VVGRARLGGI PVGVVAVETR TVELSIPADP 2000
    ANLDSEAKII QQAGQVWFPD SAFKTYQAIK DFNREGLPLM VFANWRGFSG 2050
    GMKDMYDQVL KFGAYIVDGL RECSQPVMVY IPPQAELRGG SWVVIDPTIN 2100
    PRHMEMYADR ESRGSVLEPE GTVEIKFRKK DLVKTMRRVD PVYIRLAERL 2150
    GTPELSPTER KELESKLKER EEFLIPIYHQ VAVQFADLHD TPGRMQEKGV 2200
    INDILDWKTS RTFFYWRLRR LLLEDLVKKK IHNANPELTD GQIQAMLRRW 2250
    FVEVEGTVKA YVWDNNKDLV EWLEKQLTEE DGVRSVIEEN IKYISRDYVL 2300
    KQIRSLVQAN PEVAMDSIVH MTQHISPTQR AEVVRILSTM DSPST 2345
    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

    ArrayExpressi Q5SWU9.
    Bgeei Q5SWU9.
    CleanExi MM_ACACA.
    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

    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 1, 2014
    This is version 106 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