UniProtKB - Q5SWU9 (ACACA_MOUSE)
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Protein
Acetyl-CoA carboxylase 1
Gene
Acaca
Organism
Mus musculus (Mouse)
Status
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 similarity1 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:Enzyme regulationi
By phosphorylation (By similarity). Activity is increased by oligomerization. Citrate and MID1IP1 promote oligomerization.By similarity1 Publication
: malonyl-CoA biosynthesis Pathwayi
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:
- Acetyl-CoA carboxylase 1 (Acaca), Acetyl-CoA carboxylase 2 (Acacb)
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 key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 423 | Manganese 1Sequence analysis | 1 | |
Metal bindingi | 436 | Manganese 1Sequence analysis | 1 | |
Metal bindingi | 436 | Manganese 2Sequence analysis | 1 | |
Metal bindingi | 438 | Manganese 2Sequence analysis | 1 | |
Active sitei | 440 | Sequence analysis | 1 | |
Binding sitei | 1822 | Coenzyme ABy similarity | 1 | |
Binding sitei | 2126 | Coenzyme ABy similarity | 1 | |
Binding sitei | 2128 | Coenzyme ABy similarity | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 300 – 357 | ATPPROSITE-ProRule annotationAdd BLAST | 58 |
GO - Molecular functioni
- acetyl-CoA carboxylase activity Source: UniProtKB
- ATP binding Source: UniProtKB-KW
- biotin carboxylase activity Source: UniProtKB-EC
- identical protein binding Source: MGI
- metal ion binding Source: UniProtKB-KW
GO - Biological processi
- acetyl-CoA metabolic process Source: UniProtKB
- cellular response to prostaglandin E stimulus Source: MGI
- fatty acid biosynthetic process Source: UniProtKB
- lipid homeostasis Source: MGI
- lipid metabolic process Source: MGI
- malonyl-CoA biosynthetic process Source: UniProtKB-UniPathway
- multicellular organismal protein metabolic process Source: MGI
- protein homotetramerization Source: UniProtKB
- tissue homeostasis Source: MGI
Keywordsi
Molecular function | Allosteric enzyme, Ligase, Multifunctional enzyme |
Biological process | Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism |
Ligand | ATP-binding, Biotin, Manganese, Metal-binding, Nucleotide-binding |
Enzyme and pathway databases
BRENDAi | 6.4.1.2. 3474. |
Reactomei | R-MMU-163765. ChREBP activates metabolic gene expression. R-MMU-196780. Biotin transport and metabolism. R-MMU-200425. Import of palmitoyl-CoA into the mitochondrial matrix. R-MMU-75105. Fatty acyl-CoA biosynthesis. |
UniPathwayi | UPA00655; UER00711. |
Names & Taxonomyi
Protein namesi | |
Gene namesi | |
Organismi | Mus musculus (Mouse) |
Taxonomic identifieri | 10090 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus |
Proteomesi |
|
Organism-specific databases
MGIi | MGI:108451. Acaca. |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000258040 | 1 – 2345 | Acetyl-CoA carboxylase 1Add BLAST | 2345 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 1 | N-acetylmethionineBy similarity | 1 | |
Modified residuei | 5 | PhosphoserineBy similarity | 1 | |
Modified residuei | 23 | PhosphoserineCombined sources | 1 | |
Modified residuei | 25 | PhosphoserineCombined sources | 1 | |
Modified residuei | 29 | PhosphoserineCombined sources | 1 | |
Modified residuei | 34 | PhosphoserineBy similarity | 1 | |
Modified residuei | 47 | PhosphoserineCombined sources | 1 | |
Modified residuei | 49 | PhosphoserineBy similarity | 1 | |
Modified residuei | 52 | PhosphoserineBy similarity | 1 | |
Modified residuei | 57 | PhosphothreonineCombined sources | 1 | |
Modified residuei | 77 | PhosphoserineBy similarity | 1 | |
Modified residuei | 79 | PhosphoserineCombined sources1 Publication | 1 | |
Modified residuei | 79 | Phosphoserine; by AMPKCombined sources1 Publication | 1 | |
Modified residuei | 609 | PhosphothreonineCombined sources | 1 | |
Modified residuei | 785 | N6-biotinyllysinePROSITE-ProRule annotationBy similarity | 1 | |
Modified residuei | 834 | PhosphoserineBy similarity | 1 | |
Modified residuei | 1200 | PhosphoserineBy similarity | 1 | |
Modified residuei | 1215 | PhosphoserineCombined sources | 1 | |
Modified residuei | 1217 | PhosphoserineCombined sources | 1 | |
Modified residuei | 1226 | PhosphothreonineCombined sources | 1 | |
Modified residuei | 1258 | PhosphoserineCombined sources | 1 | |
Modified residuei | 1262 | PhosphoserineCombined sources | 1 | |
Modified residuei | 1272 | PhosphoserineBy similarity | 1 | |
Modified residuei | 1333 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 2152 | PhosphothreonineBy similarity | 1 |
Post-translational modificationi
Phosphorylation on Ser-1262 is required for interaction with BRCA1.By similarity
Keywords - PTMi
Acetylation, PhosphoproteinProteomic databases
EPDi | Q5SWU9. |
PaxDbi | Q5SWU9. |
PeptideAtlasi | Q5SWU9. |
PRIDEi | Q5SWU9. |
PTM databases
iPTMneti | Q5SWU9. |
PhosphoSitePlusi | Q5SWU9. |
SwissPalmi | Q5SWU9. |
Expressioni
Inductioni
Up-regulated by endocannabinoid anandamide/AEA.1 Publication
Gene expression databases
Bgeei | ENSMUSG00000020532. |
CleanExi | MM_ACACA. |
ExpressionAtlasi | Q5SWU9. baseline and differential. |
Genevisiblei | Q5SWU9. MM. |
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
Binary interactionsi
With | Entry | #Exp. | IntAct | Notes |
---|---|---|---|---|
Mid1ip1 | Q9CQ20 | 2 | EBI-773043,EBI-473024 |
GO - Molecular functioni
- identical protein binding Source: MGI
Protein-protein interaction databases
BioGridi | 223322. 5 interactors. |
DIPi | DIP-32276N. |
IntActi | Q5SWU9. 12 interactors. |
MINTi | Q5SWU9. |
STRINGi | 10090.ENSMUSP00000020843. |
Chemistry databases
BindingDBi | Q5SWU9. |
Structurei
3D structure databases
ProteinModelPortali | Q5SWU9. |
SMRi | Q5SWU9. |
ModBasei | Search... |
MobiDBi | Search... |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 116 – 617 | Biotin carboxylationSequence analysisAdd BLAST | 502 | |
Domaini | 274 – 465 | ATP-graspPROSITE-ProRule annotationAdd BLAST | 192 | |
Domaini | 744 – 818 | Biotinyl-bindingPROSITE-ProRule annotationAdd BLAST | 75 | |
Domaini | 1575 – 1913 | CoA carboxyltransferase N-terminalPROSITE-ProRule annotationAdd BLAST | 339 | |
Domaini | 1917 – 2233 | CoA carboxyltransferase C-terminalPROSITE-ProRule annotationAdd BLAST | 317 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 1575 – 2233 | CarboxyltransferasePROSITE-ProRule annotationAdd BLAST | 659 |
Phylogenomic databases
eggNOGi | KOG0368. Eukaryota. COG0439. LUCA. COG0511. LUCA. COG4799. LUCA. |
GeneTreei | ENSGT00550000074703. |
HOVERGENi | HBG005371. |
InParanoidi | Q5SWU9. |
KOi | K11262. |
OMAi | IPTLNRM. |
OrthoDBi | EOG091G02ND. |
PhylomeDBi | Q5SWU9. |
TreeFami | TF300061. |
Family and domain databases
Gene3Di | 3.30.1490.20. 1 hit. |
InterProi | View protein in InterPro IPR034733. AcCoA_carboxyl. IPR013537. AcCoA_COase_cen. IPR011761. ATP-grasp. IPR013815. ATP_grasp_subdomain_1. IPR005481. BC-like_N. IPR001882. Biotin_BS. IPR011764. Biotin_carboxylation_dom. IPR005482. Biotin_COase_C. IPR000089. Biotin_lipoyl. IPR005479. CbamoylP_synth_lsu-like_ATP-bd. IPR029045. ClpP/crotonase-like_dom_sf. IPR011763. COA_CT_C. IPR011762. COA_CT_N. IPR016185. PreATP-grasp_dom_sf. IPR011054. Rudment_hybrid_motif. IPR011053. Single_hybrid_motif. |
Pfami | View protein in Pfam PF08326. 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. |
SMARTi | View protein in SMART SM00878. Biotin_carb_C. 1 hit. |
SUPFAMi | SSF51230. SSF51230. 1 hit. SSF51246. SSF51246. 1 hit. SSF52096. SSF52096. 2 hits. SSF52440. SSF52440. 1 hit. |
PROSITEi | View protein in PROSITE 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. |
s (2)i Sequence
Sequence statusi: Complete.
This entry describes 2 produced by isoformsialternative promoter usage. AlignAdd to basket
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.
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
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 623 | E → G in AAS13685 (Ref. 1) Curated | 1 | |
Sequence conflicti | 906 | S → P in AAS13685 (Ref. 1) Curated | 1 | |
Sequence conflicti | 933 | C → Y in AAS13685 (Ref. 1) Curated | 1 | |
Sequence conflicti | 1456 | L → S in AAS13685 (Ref. 1) Curated | 1 | |
Sequence conflicti | 1995 | S → G in AAS13685 (Ref. 1) Curated | 1 | |
Sequence conflicti | 2077 | V → I in AAS13685 (Ref. 1) Curated | 1 | |
Sequence conflicti | 2169 | E → K in AAS13685 (Ref. 1) Curated | 1 | |
Sequence conflicti | 2251 | F → S in AAS13685 (Ref. 1) Curated | 1 | |
Sequence conflicti | 2257 | T → A in AAS13685 (Ref. 1) Curated | 1 |
Alternative sequence
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Alternative sequenceiVSP_026101 | 1 | M → MMWWSTLMSLLRASSFWRRI SAETIRIIRALRAYFERIM in isoform 2. 1 Publication | 1 |
Sequence databases
Genome annotation databases
Ensembli | ENSMUST00000020843; ENSMUSP00000020843; ENSMUSG00000020532. [Q5SWU9-1] ENSMUST00000103201; ENSMUSP00000099490; ENSMUSG00000020532. [Q5SWU9-1] |
GeneIDi | 107476. |
KEGGi | mmu:107476. |
UCSCi | uc007kql.1. mouse. [Q5SWU9-1] |
Keywords - Coding sequence diversityi
Alternative promoter usageSimilar proteinsi
Entry informationi
Entry namei | ACACA_MOUSE | |
Accessioni | Q5SWU9Primary (citable) accession number: Q5SWU9 Secondary accession number(s): A2A6H4 Q925C5 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | October 31, 2006 |
Last sequence update: | December 21, 2004 | |
Last modified: | March 28, 2018 | |
This is version 139 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |