Acacb
entrez
100705
canonical
uniprot
E9Q4Z2
canonical
ensembl
ENSMUSG00000042010
resolver
ensp
ENSMUSP00000031583
resolver
ensp
ENSMUSP00000099642
resolver
ensp
ENSMUSP00000254511
resolver
ensp
ENSMUSP00000254514
resolver
enst
ENSMUST00000031583
resolver
enst
ENSMUST00000102582
resolver
genesymbol
Acacb
resolver
genesymbol_syn
ACC2
resolver
genesymbol_syn
Acc2
resolver
genesymbol_syn
Accb
resolver
uniprot
Q3UHC8
resolver
uniprot
Q6JIZ0
resolver
uniprot
Q9ESZ2
resolver
uniprot
Q9ESZ3
resolver
uniprot_entry
ACACB_MOUSE
resolver
uniprot_entry
Q3UHC8_MOUSE
resolver
uniprot_entry
Q9ESZ3_MOUSE
resolver
uniprot_sec
Q6JIZ0
resolver
uniprot_sec
Q9ESZ2
resolver
activity_regulation
ACTIVITY REGULATION: Activity is increased by oligomerization of the protein into filaments that correspond to the most active form of the carboxylase. The oligomerization and the activity of the enzyme are inhibited by phosphorylation at Ser-212 (PubMed:24913514). Inhibited by its own product malonyl-CoA. Activation by MID1IP1 is citrate dependent. {ECO:0000250|UniProtKB:O00763, ECO:0000269|PubMed:24913514}.
uniprot
proteins
amino_acid_sequence
MVLLLFLTCLVFSCLTFSWLKIWGKMTDSKPLTNSKVEANLLSSEESLSASELSGEQLQEHGDHSCLSYRGPRDASQQRNSLPSSCQRPPRNPLSSNDTWPSPELQTNWTAAPGPEVPDANGLSFPARPPSQRTVSPSREDRKQAHIKRQLMTSFILGSLDDNSSDEDPSAGSFQNSSRKSSRASLGTLSQEAALNTSDPESHAPTMRPSMSGLHLVKRGREHKKLDLHRDFTVASPAEFVTRFGGNRVIEKVLIANNGIAAVKCMRSIRRWAYEMFRNERAIRFVVMVTPEDLKANAEYIKMADQYVPVPGGPNNNNYANVELIIDIAKRIPVQAVWAGWGHASENPKLPELLCKHEIAFLGPPSEAMWALGDKIASTIVAQTLQIPTLPWSGSGLTVEWTEDSRHQGKCISVPEDVYEQGCVKDVDEGLQAAEKIGFPLMIKASEGGGGKGIRKAESAEDFPMLFRQVQSEIPGSPIFLMKLAQNARHLEVQVLADQYGNAVSLFGRDCSIQRRHQKIIEEAPATIAAPAVFEFMEQCAVLLAKMVGYVSAGTVEYLYSQDGSFHFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGVPLHRLKDIRLLYGESPWGVTPIPFETPLSPPIARGHVIAARITSENPDEGFKPSSGTVQELNFRSNKNVWGYFSVAAAGGLHEFADSQFGHCFSWGENREEAISNMVVALKELSIRGDFRTTVEYLVNLLETESFQNNDIDTGWLDHLIAQRVQAEKPDIMLGVVCGALNVADAMFRTCMTEFLHSLERGQVLPADSLLNIVDVELIYGGIKYALKVARQSLTMFVLIMNGCHIEIDAHRLNDGGLLLSYNGSSYTTYMKEEVDSYRITIGNKTCVFEKENDPTVLRSPSAGKLMQYTVEDGDHVEAGSSYAEMEVMKMIMTLNVQESGRVKYIKRPGVILEAGCVVARLELDDPSKVHAAQPFTGELPAQQTLPILGEKLHQVFHGVLENLTNVMSGYCLPEPFFSMKLKDWVQKLMMTLRHPSLPLLELQEIMTSVAGRIPAPVEKAVRRVMAQYASNITSVLCQFPSQQIATILDCHAATLQRKADREVFFMNTQSIVQLVQRYRSGTRGYMKAVVLDLLRKYLNVEHHFQQAHYDKCVINLREQFKPDMTQVLDCIFSHSQVAKKNQLVTMLIDELCGPDPTLSDELTSILCELTQLSRSEHCKVALRARQVLIASHLPSYELRHNQVESIFLSAIDMYGHQFCPENLKKLILSETTIFDVLPTFFYHENKVVCMASLEVYVRRGYIAYELNSLQHRELPDGTCVVEFQFMLPSSHPNRMAVPISVSNPDLLRHSTELFMDSGFSPLCQRMGAMVAFRRFEEFTRNFDEVISCFANVQTDTLLFSKACTSLYSEEDSKSLREEPIHILNVAIQCADHMEDEALVPVFRAFVQSKKHILVDYGLRRITFLVAQEREFPKFFTFRARDEFAEDRIYRHLEPALAFQLELSRMRNFDLTAVPCANHKMHLYLGAAKVKEGLEVTDHRFFIRAIIRHSDLITKEASFEYLQNEGERLLLEAMDELEVAFNNTSVRTDCNHIFLNFVPTVIMDPLKIEESVRDMVMRYGSRLWKLRVLQAEVKINIRQTTSDSAIPIRLFITNESGYYLDISLYREVTDSRSGNIMFHSFGNKQGSLHGMLINTPYVTKDLLQAKRFQAQSLGTTYVYDFPEMFRQALFKLWGSPEKYPKDILTYTELVLDSQGQLVEMNRLPGCNEVGMVAFKMRFKTPEYPEGRDAVVIGNDITFQIGSFGIGEDFLYLRASEMARTEGIPQIYLAANSGARMGLAEEIKQIFQVAWVDPEDPHKGFRYLYLTPQDYTQISSQNSVHCKHIEDEGESRYVIVDVIGKDANLGVENLRGSGMIAGEASLAYEKTVTISMVTCRALGIGAYLVRLGQRVIQVENSHIILTGAGALNKVLGREVYTSNNQLGGVQIMHTNGVSHVTVPDDFEGVCTILEWLSFIPKDNRSPVPITTPSDPIDREIEFTPTKAPYDPRWMLAGRPHPTLKGTWQSGFFDHGSFKEIMAPWAQTVVTGRARLGGIPVGVIAVETRTVEVAVPADPANLDSEAKIIQQAGQVWFPDSAYKTAQVIRDFNKERLPLMIFANWRGFSGGMKDMYEQMLKFGAYIVDGLRLYEQPILIYIPPCAELRGGSWVVLDSTINPLCIEMYADKESRGGVLEPEGTVEIKFRKKDLVKTIRRIDPVCKKLVGQLGKAQLPDKDRKELEGQLKAREELLLPIYHQVAVQFADLHDTPGHMLEKGIISDVLEWKTARTFFYWRLRRLLLEAQVKQEILRASPELNHEHTQSMLRRWFVETEGAVKAYLWDSNQVVVQWLEQHWSAKDGLRSTIRENINYLKRDSVLKTIQSLVQEHPEVIMDCVAYLSQHLTPAERIQVAQLLSTTESPASS
uniprot
proteins
ec_number
6.4.1.2
uniprot
proteins
function
FUNCTION: Mitochondrial enzyme that catalyzes the carboxylation of acetyl-CoA to malonyl-CoA and plays a central role in fatty acid metabolism (By similarity). Catalyzes a 2 steps reaction starting with the ATP-dependent carboxylation of the biotin carried by the biotin carboxyl carrier (BCC) domain followed by the transfer of the carboxyl group from carboxylated biotin to acetyl-CoA (By similarity). Through the production of malonyl-CoA that allosterically inhibits carnitine palmitoyltransferase 1 at the mitochondria, negatively regulates fatty acid oxidation (PubMed:24913514). Together with its cytosolic isozyme ACACA, which is involved in de novo fatty acid biosynthesis, promotes lipid storage (PubMed:24913514). {ECO:0000250|UniProtKB:O00763, ECO:0000269|PubMed:24913514}.
uniprot
proteins
mass_dalton
275750
uniprot
proteins
mutagenesis
MUTAGEN 212; /note="S->A: No phosphorylation by AMPK, reduced fatty acid oxidation in skeletal muscle, increased lipid deposition in skeletal muscle, and development of insulin resistance."; /evidence="ECO:0000269|PubMed:24913514
uniprot
proteins
pathway_participation
PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. {ECO:0000250|UniProtKB:O00763}.
uniprot
proteins
post_translational_modification
PTM: The biotin cofactor is covalently attached to the central biotinyl-binding domain and is required for the catalytic activity. {ECO:0000250|UniProtKB:O00763}.; PTM: Phosphorylated by AMPK at Ser-212 inactivates the enzyme (PubMed:24913514). Required for the maintenance of skeletal muscle lipid and glucose homeostasis (PubMed:24913514). {ECO:0000269|PubMed:24913514}.
uniprot
proteins
pubmed
10677481
uniprot
proteins
pubmed
11283375
uniprot
proteins
pubmed
12920182
uniprot
proteins
pubmed
15677334
uniprot
proteins
pubmed
17242355
uniprot
proteins
pubmed
18487439
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
20368432
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
21987372
uniprot
proteins
pubmed
22362781
uniprot
proteins
pubmed
22730442
uniprot
proteins
pubmed
24913514
uniprot
proteins
sequence_length
2448
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:10677481}.
uniprot
proteins