Q5SWU9 (ACACA_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Acetyl-CoA carboxylase 1
Short name=ACC1
EC=6.4.1.2

Alternative name(s):
ACC-alpha
Acetyl-CoA carboxylase 265

Including the following 1 domains:

1. Biotin carboxylase
   EC=6.3.4.14

Gene names

Name:	Acaca
Synonyms:	Acac, Gm738

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	2345 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.10 UniProtKB P11497
Catalytic activity	ATP + acetyl-CoA + HCO3- = ADP + phosphate + malonyl-CoA. Ref.10 UniProtKB P11497 ATP + biotin-[carboxyl-carrier-protein] + CO2 = ADP + phosphate + carboxy-biotin-[carboxyl-carrier-protein]. Ref.10
Cofactor	Biotin By similarity. Binds 2 manganese ions per subunit By similarity.
Enzyme regulation	By phosphorylation By similarity. Activity is increased by oligomerization. Citrate and MID1IP1 promote oligomerization. Ref.10 UniProtKB P11497
Pathway	Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1.
Subunit structure	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. Ref.6 Ref.10
Subcellular location	Cytoplasm Ref.6 Ref.10.
Post-translational modification	Phosphorylation on Ser-1262 is required for interaction with BRCA1 By similarity. UniProtKB Q13085
Sequence similarities	Contains 1 ATP-grasp domain. Contains 1 biotin carboxylation domain. Contains 1 biotinyl-binding domain. Contains 1 carboxyltransferase domain.

Ontologies

Keywords
Biological process	Fatty acid biosynthesis Fatty acid metabolism Lipid biosynthesis Lipid metabolism
Cellular component	Cytoplasm
Coding sequence diversity	Alternative promoter usage
Ligand	ATP-binding Biotin Manganese Metal-binding Nucleotide-binding
Molecular function	Ligase
PTM	Acetylation Phosphoprotein
Technical term	Allosteric enzyme Complete proteome Direct protein sequencing Multifunctional enzyme Reference proteome
Gene Ontology (GO)
Biological_process	acetyl-CoA metabolic process Inferred from direct assay Ref.10. Source: UniProtKB fatty acid biosynthetic process Inferred from direct assay Ref.10. Source: UniProtKB lipid homeostasis Inferred from mutant phenotype PubMed 17210641. Source: MGI lipid metabolic process Inferred from mutant phenotype PubMed 17210641. Source: MGI malonyl-CoA biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway multicellular organismal protein metabolic process Inferred from mutant phenotype PubMed 17210641. Source: MGI protein homotetramerization Inferred from direct assay Ref.10. Source: UniProtKB tissue homeostasis Inferred from mutant phenotype PubMed 17210641. Source: MGI
Cellular_component	cytosol Inferred from direct assay Ref.10. Source: UniProtKB mitochondrion Inferred from direct assay PubMed 18614015. Source: MGI
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW acetyl-CoA carboxylase activity Inferred from direct assay Ref.10. Source: UniProtKB biotin carboxylase activity Inferred from electronic annotation. Source: UniProtKB-EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative promoter usage. [Align] [Select]

Isoform 1 (identifier: Q5SWU9-1)

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.

Isoform 2 (identifier: Q5SWU9-2)

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

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 2345	2345	Acetyl-CoA carboxylase 1		PRO_0000258040
Regions
	Domain	116 – 617	502	Biotin carboxylation
	Domain	274 – 465	192	ATP-grasp
	Domain	751 – 817	67	Biotinyl-binding
	Domain	1697 – 2193	497	Carboxyltransferase
	Nucleotide binding	300 – 357	58	ATP Potential
Sites
	Active site	440	1	By similarity
	Metal binding	423	1	Manganese 1 By similarity
	Metal binding	436	1	Manganese 1 By similarity
	Metal binding	436	1	Manganese 2 By similarity
	Metal binding	438	1	Manganese 2 By similarity
	Binding site	1822	1	Coenzyme A By similarity UniProtKB Q00955
	Binding site	2126	1	Coenzyme A By similarity UniProtKB Q00955
	Binding site	2128	1	Coenzyme A By similarity UniProtKB Q00955
Amino acid modifications
	Modified residue	1	1	N-acetylmethionine By similarity
	Modified residue	5	1	Phosphoserine By similarity
	Modified residue	23	1	Phosphoserine By similarity
	Modified residue	25	1	Phosphoserine Ref.7
	Modified residue	29	1	Phosphoserine Ref.7 Ref.8 UniProtKB Q13085
	Modified residue	52	1	Phosphoserine By similarity
	Modified residue	77	1	Phosphoserine By similarity UniProtKB P11497
	Modified residue	79	1	Phosphoserine; alternate Ref.8 Ref.9 Ref.10 UniProtKB P11497
	Modified residue	79	1	Phosphoserine; by AMPK; alternate Probable
	Modified residue	785	1	N6-biotinyllysine By similarity
	Modified residue	1200	1	Phosphoserine By similarity UniProtKB P11497
	Modified residue	1215	1	Phosphoserine By similarity
	Modified residue	1262	1	Phosphoserine By similarity UniProtKB Q13085
	Modified residue	1333	1	N6-acetyllysine By similarity
Natural variations
	Alternative sequence	1	1	M → MMWWSTLMSLLRASSFWRRI SAETIRIIRALRAYFERIM in isoform 2.		VSP_026101
Experimental info
	Sequence conflict	623	1	E → G in AAS13685. Ref.1
	Sequence conflict	906	1	S → P in AAS13685. Ref.1
	Sequence conflict	933	1	C → Y in AAS13685. Ref.1
	Sequence conflict	1456	1	L → S in AAS13685. Ref.1
	Sequence conflict	1995	1	S → G in AAS13685. Ref.1
	Sequence conflict	2077	1	V → I in AAS13685. Ref.1
	Sequence conflict	2169	1	E → K in AAS13685. Ref.1
	Sequence conflict	2251	1	F → S in AAS13685. Ref.1
	Sequence conflict	2257	1	T → A in AAS13685. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified December 21, 2004. Version 1. Checksum: 6995C534B054FE02	FASTA	2,345	265,257
	10 20 30 40 50 60 MDEPSPLAKT LELNQHSRFI IGSVSEDNSE DEISNLVKLD LEEKEGSLSP ASVSSDTLSD 70 80 90 100 110 120 LGISGLQDGL AFHMRSSMSG LHLVKQGRDR KKIDSQRDFT VASPAEFVTR FGGNKVIEKV 130 140 150 160 170 180 LIANNGIAAV KCMRSIRRWS YEMFRNERAI RFVVMVTPED LKANAEYIKM ADHYVPVPGG 190 200 210 220 230 240 PNNNNYANVE LILDIAKRIP VQAVWAGWGH ASENPKLPEL LLKNGIAFMG PPSQAMWALG 250 260 270 280 290 300 DKIASSIVAQ TAGIPTLPWS GSGLRVDWQE NDFSKRILNV PQDLYEKGYV KDVDDGLKAA 310 320 330 340 350 360 EEVGYPVMIK ASEGGGGKGI RKVNNADDFP NLFRQVQAEV PGSPIFVMRL AKQSRHLEVQ 370 380 390 400 410 420 ILADQYGNAI SLFGRDCSVQ RRHQKIIEEA PAAIATPAVF EHMEQCAVKL AKMVGYVSAG 430 440 450 460 470 480 TVEYLYSQDG SFYFLELNPR LQVEHPCTEM VADVNLPAAQ LQIAMGIPLF RIKDIRMMYG 490 500 510 520 530 540 VSPWGDAPID FENSAHVPCP RGHVIAARIT SENPDEGFKP SSGTVQELNF RSNKNVWGYF 550 560 570 580 590 600 SVAAAGGLHE FADSQFGHCF SWGENREEAI SNMVVALKEL SIRGDFRTTV EYLIKLLETE 610 620 630 640 650 660 SFQLNRIDTG WLDRLIAEKV QAERPDTMLG VVCGALHVAD VSLRNSISNF LHSLERGQVL 670 680 690 700 710 720 PAHTLLNTVD VELIYEGIKY VLKVTRQSPN SYVVIMNGSC VEVDVHRLSD GGLLLSYDGS 730 740 750 760 770 780 SYTTYMKEEV DRYRITIGNK TCVFEKENDP SVMRSPSAGK LIQYIVEDGG HVFAGQCYAE 790 800 810 820 830 840 IEVMKMVMTL TAVESGCIHY VKRPGAALDP GCVIAKMQLD NPSKVQQAEL HTGSLPQIQS 850 860 870 880 890 900 TALRGEKLHR VFHYVLDNLV NVMNGYCLPD PFFSSRVKDW VERLMKTLRD PSLPLLELQD 910 920 930 940 950 960 IMTSVSGRIP LNVEKSIKKE MAQYASNITS VLCQFPSQQI ANILDSHAAT LNRKSEREVF 970 980 990 1000 1010 1020 FMNTQSIVQL VQRYRSGIRG HMKAVVMDLL RQYLRVETQF QNGHYDKCVF ALREENKSDM 1030 1040 1050 1060 1070 1080 NTVLNYIFSH AQVTKKNLLV TMLIDQLCGR DPTLTDELLN ILTELTQLSK TTNAKVALRA 1090 1100 1110 1120 1130 1140 RQVLIASHLP SYELRHNQVE SIFLSAIDMY GHQFCIENLQ KLILSETSIF DVLPNFFYHS 1150 1160 1170 1180 1190 1200 NQVVRMAALE VYVRRAYIAY ELNSVQHRQL KDNTCVVEFQ FMLPTSHPNR GNIPTLNRMS 1210 1220 1230 1240 1250 1260 FASNLNHYGM THVASVSDVL LDNAFTPPCQ RMGGMVSFRT FEDFVRIFDE IMGCFCDSPP 1270 1280 1290 1300 1310 1320 QSPTFPESGH TSLYDEDKVP RDEPIHILNV AIKTDGDIED DRLAAMFREF TQQNKATLVE 1330 1340 1350 1360 1370 1380 HGIRRLTFLV AQKDFRKQVN CEVDQRFHRE FPKFFTFRAR DKFEEDRIYR HLEPALAFQL 1390 1400 1410 1420 1430 1440 ELNRMRNFDL TAIPCANHKM HLYLGAAKVE VGTEVTDYRF FVRAIIRHSD LVTKEASFEY 1450 1460 1470 1480 1490 1500 LQNEGERLLL EAMDELEVAF NNTNVRTDCN HIFLNFVPTV IMDPSKIEES VRSMVMRYGS 1510 1520 1530 1540 1550 1560 RLWKLRVLQA ELKINIRLTT TGKAIPIRLF LTNESGYYLD ISLYKEVTDS RTAQIMFQAY 1570 1580 1590 1600 1610 1620 GDKQGPLHGM LINTPYVTKD LLQSKRFQAQ SLGTTYIYDI PEMFRQSLIK LWESMSTQAF 1630 1640 1650 1660 1670 1680 LPSPPLPSDI LTYTELVLDD QGQLVHMNRL PGGNEIGMVA WKMSLKSPEY PDGRDIIVIG 1690 1700 1710 1720 1730 1740 NDITYRIGSF GPQEDLLFLR ASELARAEGI PRIYVAANSG ARIGLAEEIR HMFHVAWVDP 1750 1760 1770 1780 1790 1800 EDPYKGYKYL YLTPQDYKRV SALNSVHCEH VEDEGESRYK ITDIIGKEEG LGAENLRGSG 1810 1820 1830 1840 1850 1860 MIAGESSLAY DEVITISLVT CRAIGIGAYL VRLGQRTIQV ENSHLILTGA GALNKVLGRE 1870 1880 1890 1900 1910 1920 VYTSNNQLGG IQIMHNNGVT HSTVCDDFEG VFTVLHWLSY MPKSVHSSVP LLNSKDPIDR 1930 1940 1950 1960 1970 1980 IIEFVPTKAP YDPRWMLAGR PHPTQKGQWL SGFFDYGSFS EIMQPWAQTV VVGRARLGGI 1990 2000 2010 2020 2030 2040 PVGVVAVETR TVELSIPADP ANLDSEAKII QQAGQVWFPD SAFKTYQAIK DFNREGLPLM 2050 2060 2070 2080 2090 2100 VFANWRGFSG GMKDMYDQVL KFGAYIVDGL RECSQPVMVY IPPQAELRGG SWVVIDPTIN 2110 2120 2130 2140 2150 2160 PRHMEMYADR ESRGSVLEPE GTVEIKFRKK DLVKTMRRVD PVYIRLAERL GTPELSPTER 2170 2180 2190 2200 2210 2220 KELESKLKER EEFLIPIYHQ VAVQFADLHD TPGRMQEKGV INDILDWKTS RTFFYWRLRR 2230 2240 2250 2260 2270 2280 LLLEDLVKKK IHNANPELTD GQIQAMLRRW FVEVEGTVKA YVWDNNKDLV EWLEKQLTEE 2290 2300 2310 2320 2330 2340 DGVRSVIEEN IKYISRDYVL KQIRSLVQAN PEVAMDSIVH MTQHISPTQR AEVVRILSTM DSPST
	Isoform 2 [UniParc]. Checksum: 57B7FB88C694692E	FASTA	2,383	269,958
	10 20 30 40 50 60 MMWWSTLMSL LRASSFWRRI SAETIRIIRA LRAYFERIMD EPSPLAKTLE LNQHSRFIIG 70 80 90 100 110 120 SVSEDNSEDE ISNLVKLDLE EKEGSLSPAS VSSDTLSDLG ISGLQDGLAF HMRSSMSGLH 130 140 150 160 170 180 LVKQGRDRKK IDSQRDFTVA SPAEFVTRFG GNKVIEKVLI ANNGIAAVKC MRSIRRWSYE 190 200 210 220 230 240 MFRNERAIRF VVMVTPEDLK ANAEYIKMAD HYVPVPGGPN NNNYANVELI LDIAKRIPVQ 250 260 270 280 290 300 AVWAGWGHAS ENPKLPELLL KNGIAFMGPP SQAMWALGDK IASSIVAQTA GIPTLPWSGS 310 320 330 340 350 360 GLRVDWQEND FSKRILNVPQ DLYEKGYVKD VDDGLKAAEE VGYPVMIKAS EGGGGKGIRK 370 380 390 400 410 420 VNNADDFPNL FRQVQAEVPG SPIFVMRLAK QSRHLEVQIL ADQYGNAISL FGRDCSVQRR 430 440 450 460 470 480 HQKIIEEAPA AIATPAVFEH MEQCAVKLAK MVGYVSAGTV EYLYSQDGSF YFLELNPRLQ 490 500 510 520 530 540 VEHPCTEMVA DVNLPAAQLQ IAMGIPLFRI KDIRMMYGVS PWGDAPIDFE NSAHVPCPRG 550 560 570 580 590 600 HVIAARITSE NPDEGFKPSS GTVQELNFRS NKNVWGYFSV AAAGGLHEFA DSQFGHCFSW 610 620 630 640 650 660 GENREEAISN MVVALKELSI RGDFRTTVEY LIKLLETESF QLNRIDTGWL DRLIAEKVQA 670 680 690 700 710 720 ERPDTMLGVV CGALHVADVS LRNSISNFLH SLERGQVLPA HTLLNTVDVE LIYEGIKYVL 730 740 750 760 770 780 KVTRQSPNSY VVIMNGSCVE VDVHRLSDGG LLLSYDGSSY TTYMKEEVDR YRITIGNKTC 790 800 810 820 830 840 VFEKENDPSV MRSPSAGKLI QYIVEDGGHV FAGQCYAEIE VMKMVMTLTA VESGCIHYVK 850 860 870 880 890 900 RPGAALDPGC VIAKMQLDNP SKVQQAELHT GSLPQIQSTA LRGEKLHRVF HYVLDNLVNV 910 920 930 940 950 960 MNGYCLPDPF FSSRVKDWVE RLMKTLRDPS LPLLELQDIM TSVSGRIPLN VEKSIKKEMA 970 980 990 1000 1010 1020 QYASNITSVL CQFPSQQIAN ILDSHAATLN RKSEREVFFM NTQSIVQLVQ RYRSGIRGHM 1030 1040 1050 1060 1070 1080 KAVVMDLLRQ YLRVETQFQN GHYDKCVFAL REENKSDMNT VLNYIFSHAQ VTKKNLLVTM 1090 1100 1110 1120 1130 1140 LIDQLCGRDP TLTDELLNIL TELTQLSKTT NAKVALRARQ VLIASHLPSY ELRHNQVESI 1150 1160 1170 1180 1190 1200 FLSAIDMYGH QFCIENLQKL ILSETSIFDV LPNFFYHSNQ VVRMAALEVY VRRAYIAYEL 1210 1220 1230 1240 1250 1260 NSVQHRQLKD NTCVVEFQFM LPTSHPNRGN IPTLNRMSFA SNLNHYGMTH VASVSDVLLD 1270 1280 1290 1300 1310 1320 NAFTPPCQRM GGMVSFRTFE DFVRIFDEIM GCFCDSPPQS PTFPESGHTS LYDEDKVPRD 1330 1340 1350 1360 1370 1380 EPIHILNVAI KTDGDIEDDR LAAMFREFTQ QNKATLVEHG IRRLTFLVAQ KDFRKQVNCE 1390 1400 1410 1420 1430 1440 VDQRFHREFP KFFTFRARDK FEEDRIYRHL EPALAFQLEL NRMRNFDLTA IPCANHKMHL 1450 1460 1470 1480 1490 1500 YLGAAKVEVG TEVTDYRFFV RAIIRHSDLV TKEASFEYLQ NEGERLLLEA MDELEVAFNN 1510 1520 1530 1540 1550 1560 TNVRTDCNHI FLNFVPTVIM DPSKIEESVR SMVMRYGSRL WKLRVLQAEL KINIRLTTTG 1570 1580 1590 1600 1610 1620 KAIPIRLFLT NESGYYLDIS LYKEVTDSRT AQIMFQAYGD KQGPLHGMLI NTPYVTKDLL 1630 1640 1650 1660 1670 1680 QSKRFQAQSL GTTYIYDIPE MFRQSLIKLW ESMSTQAFLP SPPLPSDILT YTELVLDDQG 1690 1700 1710 1720 1730 1740 QLVHMNRLPG GNEIGMVAWK MSLKSPEYPD GRDIIVIGND ITYRIGSFGP QEDLLFLRAS 1750 1760 1770 1780 1790 1800 ELARAEGIPR IYVAANSGAR IGLAEEIRHM FHVAWVDPED PYKGYKYLYL TPQDYKRVSA 1810 1820 1830 1840 1850 1860 LNSVHCEHVE DEGESRYKIT DIIGKEEGLG AENLRGSGMI AGESSLAYDE VITISLVTCR 1870 1880 1890 1900 1910 1920 AIGIGAYLVR LGQRTIQVEN SHLILTGAGA LNKVLGREVY TSNNQLGGIQ IMHNNGVTHS 1930 1940 1950 1960 1970 1980 TVCDDFEGVF TVLHWLSYMP KSVHSSVPLL NSKDPIDRII EFVPTKAPYD PRWMLAGRPH 1990 2000 2010 2020 2030 2040 PTQKGQWLSG FFDYGSFSEI MQPWAQTVVV GRARLGGIPV GVVAVETRTV ELSIPADPAN 2050 2060 2070 2080 2090 2100 LDSEAKIIQQ AGQVWFPDSA FKTYQAIKDF NREGLPLMVF ANWRGFSGGM KDMYDQVLKF 2110 2120 2130 2140 2150 2160 GAYIVDGLRE CSQPVMVYIP PQAELRGGSW VVIDPTINPR HMEMYADRES RGSVLEPEGT 2170 2180 2190 2200 2210 2220 VEIKFRKKDL VKTMRRVDPV YIRLAERLGT PELSPTERKE LESKLKEREE FLIPIYHQVA 2230 2240 2250 2260 2270 2280 VQFADLHDTP GRMQEKGVIN DILDWKTSRT FFYWRLRRLL LEDLVKKKIH NANPELTDGQ 2290 2300 2310 2320 2330 2340 IQAMLRRWFV EVEGTVKAYV WDNNKDLVEW LEKQLTEEDG VRSVIEENIK YISRDYVLKQ 2350 2360 2370 2380 IRSLVQANPE VAMDSIVHMT QHISPTQRAE VVRILSTMDS PST

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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/6J. Tissue: Liver.
[2]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] 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/6.
[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/6. Tissue: Brain.
[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]	"Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract] 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]	"Crystal structure of Spot 14, a modulator of fatty acid synthesis." Colbert C.L., Kim C.W., Moon Y.A., Henry L., Palnitkar M., McKean W.B., Fitzgerald K., Deisenhofer J., Horton J.D., Kwon H.J. Proc. Natl. Acad. Sci. U.S.A. 107:18820-18825(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, ENZYME REGULATION, INTERACTION WITH MID1IP1, PHOSPHORYLATION AT SER-79, SUBCELLULAR LOCATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
RefSeq	NP_579938.2. NM_133360.2. XP_006532016.1. XM_006531953.1. XP_006532017.1. XM_006531954.1. XP_006532018.1. XM_006531955.1. XP_006532019.1. XM_006531956.1. XP_006532020.1. XM_006531957.1.
UniGene	Mm.31374.
3D structure databases
ProteinModelPortal	Q5SWU9.
SMR	Q5SWU9. Positions 101-615, 747-816, 1580-2337.
ModBase	Search...
MobiDB	Search...
Protein-protein interaction databases
BioGrid	223322. 1 interaction.
DIP	DIP-32276N.
IntAct	Q5SWU9. 8 interactions.
MINT	MINT-4091386.
Chemistry
ChEMBL	CHEMBL3086.
PTM databases
PhosphoSite	Q5SWU9.
Proteomic databases
PaxDb	Q5SWU9.
PRIDE	Q5SWU9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000020843; ENSMUSP00000020843; ENSMUSG00000020532. [Q5SWU9-1] ENSMUST00000103201; ENSMUSP00000099490; ENSMUSG00000020532. [Q5SWU9-1] ENSMUST00000133811; ENSMUSP00000116174; ENSMUSG00000020532.
GeneID	107476.
KEGG	mmu:107476.
UCSC	uc007kql.1. mouse. [Q5SWU9-1]
Organism-specific databases
CTD	31.
MGI	MGI:108451. Acaca.
Phylogenomic databases
eggNOG	COG0511.
GeneTree	ENSGT00550000074703.
HOVERGEN	HBG005371.
InParanoid	Q5SWU9.
KO	K11262.
OMA	ETESFQM.
OrthoDB	EOG7HXCPW.
PhylomeDB	Q5SWU9.
TreeFam	TF300061.
Enzyme and pathway databases
UniPathway	UPA00655; UER00711.
Gene expression databases
ArrayExpress	Q5SWU9.
Bgee	Q5SWU9.
CleanEx	MM_ACACA.
Genevestigator	Q5SWU9.
Family and domain databases
Gene3D	3.30.1490.20. 1 hit. 3.30.470.20. 1 hit. 3.40.50.20. 1 hit.
InterPro	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. IPR011763. COA_CT_C. IPR011762. COA_CT_N. IPR016185. PreATP-grasp_dom. IPR011054. Rudment_hybrid_motif. IPR011053. Single_hybrid_motif. [Graphical view]
Pfam	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]
SMART	SM00878. Biotin_carb_C. 1 hit. [Graphical view]
SUPFAM	SSF51230. SSF51230. 1 hit. SSF51246. SSF51246. 1 hit. SSF52440. SSF52440. 1 hit.
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. [Graphical view]
ProtoNet	Search...
Other
NextBio	358872.
PRO	Q5SWU9.
SOURCE	Search...

Entry information

Entry name

ACACA_MOUSE

Accession

Primary (citable) accession number: Q5SWU9
Secondary accession number(s): A2A6H4 , Q5SWU6, Q5SWU7, Q5SWU8, Q6JIZ1, Q6PHL9, Q705X8, Q705X9, Q91VC8, Q925C4, Q925C5

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 31, 2006
Last sequence update:	December 21, 2004
Last modified:	April 16, 2014
This is version 101 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program