Acaca
entrez
60581
canonical
uniprot
P11497
canonical
ensembl
ENSRNOG00000034013
resolver
ensp
ENSRNOP00000086394
resolver
ensp
ENSRNOP00000094595
resolver
enst
ENSRNOT00000116202
resolver
genesymbol
Acaca
resolver
genesymbol_syn
Acac
resolver
uniprot
A0A8I6A239
resolver
uniprot
A1EC79
resolver
uniprot
P97902
resolver
uniprot_entry
A0A8I6A239_RAT
resolver
uniprot_entry
ACACA_RAT
resolver
uniprot_sec
A1EC79
resolver
uniprot_sec
P97902
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited by phosphorylation (By similarity). Citrate promotes oligomerization of the protein into filaments that correspond to the most active form of the carboxylase (By similarity). {ECO:0000250|UniProtKB:Q13085}.
uniprot
proteins
amino_acid_sequence
MDEPSPLAKTLELNQHSRFIIGSVSEDNSEDEISNLVKLDLEEKEGSLSPASVSSDTLSDLGISALQDGLAFHMRSSMSGLHLVKQGRDRKKIDSQRDFTVASPAEFVTRFGGNKVIEKVLIANNGIAAVKCMRSIRRWSYEMFRNERAIRFVVMVTPEDLKANAEYIKMADHYVPVPGGANNNNYANVELILDIAKRIPVQAVWAGWGHASENPKLPELLLKNGIAFMGPPSQAMWALGDKIASSIVAQTAGIPTLPWSGSGLRVDWQENDFSKRILNVPQDLYEKGYVKDVDDGLKAAEEVGYPVMIKASEGGGGKGIRKVNNADDFPNLFRQVQAEVPGSPIFVMRLAKQSRHLEVQILADQYGNAISLFGRDCSVQRRHQKIIEEAPAAIATPAVFEHMEQCAVKLAKMVGYVSAGTVEYLYSQDGSFYFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPLFRIKDIRMMYGVSPWGDAPIDFENSAHVPCPRGHVIAARITSENPDEGFKPSSGTVQELNFRSNKNVWGYFSVAAAGGLHEFADSQFGHCFSWGENREEAISNMVVALKELSIRGDFRTTVEYLIKLLETESFQLNRIDTGWLDRLIAEKVQAERPDTMLGVVCGALHVADVNLRNSISNFLHSLERGQVLPAHTLLNTVDVELIYEGIKYVLKVTRQSPNSYVVIMNGSCVEVDVHRLSDGGLLLSYDGSSYTTYMKEEVDRYRITIGNKTCVFEKENDPSVMRSPSAGKLIQYIVEDGGHVFAGQCYAEIEVMKMVMTLTAVESGCIHYVKRPGAALDPGCVIAKMQLDNPSKVQQAELHTGSLPQIQSTALRGEKLHRVFHYVLDNLVNVMNGYCLPDPFFSSKVKDWVERLMKTLRDPSLPLLELQDIMTSVSGRIPLNVEKSIKKEMAQYASNITSVLCQFPSQQIANILDSHAATLNRKSEREVFFMNTQSIVQLVQRYRSGIRGHMKAVVMDLLRQYLRVETQFQNGHYDKCVFALREENKSDMNTVLNYIFSHAQVTKKNLLVTMLIDQLCGRDPTLTDELLNILTELTQLSKTTNAKVALRARQVLIASHLPSYDVRHNQVESIFLSAIDMYGHQFCIENLQKLILSETSIFDVLPNFFYHSNQVVRMAALEVYVRRAYIAYELNSVQHRQLKDNTCVVEFQFMLPTSHPNRGNIPTLNRMSFASNLNHYGMTHVASVSDVLLDNAFTPPCQRMGGMVSFRTFEDFVRIFDEVMGCFCDSPPQSPTFPESGHTSLYDEDKVPRDEPIHILNVAIKTDGDIEDDRLAAMFREFTQQNKATLVEHGIRRLTFLVAQKDFRKQVNCEVDQRFHREFPKFFTFRARDKFEEDRIYRHLEPALAFQLELNRMRNFDLTAIPCANHKMHLYLGAAKVEVGTEVTDYRFFVRAIIRHSDLVTKEASFEYLQNEGERLLLEAMDELEVAFNNTNVRTDCNHIFLNFVPTVIMDPSKIEESVRSMVMRYGSRLWKLRVLQAELKINIRLTTTGKAIPIRLFLTNESGYYLDISLYKEVTDSRTAQIMFQAYGDKQGPLHGMLINTPYVTKDLLQSKRFQAQSLGTTYIYDIPEMFRQSLIKLWESMSTQAFLPSPPLPSDILTYTELVLDDQGQLVHMNRLPGGNEIGMVAWKMSLKSPEYPDGRDVIVIGNDITYRIGSFGPQEDLLFLRASELARAEGIPRIYVAANSGARIGLAEEIRHMFHVAWVDSEDPYKGYKYLYLTPQDYKRVSALNSVHCEHVEDEGESRYKITDIIGKEEGLGAENLRGSGMIAGESSLAYDEIITISLVTCRAIGIGAYLVRLGQRTIQVENSHLILTGAGALNKVLGREVYTSNNQLGGIQIMHNNGVTHCTVCDDFEGVFTVLHWLSYMPKNVHSSVPLLNSKDPIDRIIEFVPTKAPYDPRWMLAGRPHPTQKGQWLSGFFDYGSFSEIMQPWAQTVVVGRARLGGIPVGVVAVETRTVELSVPADPANLDSEAKIIQQAGQVWFPDSAFKTYQAIKDFNREGLPLMVFANWRGFSGGMKDMYDQVLKFGAYIVDGLRECSQPVMVYIPPQAELRGGSWVVIDPTINPRHMEMYADRESRGSVLEPEGTVEIKFRKKDLVKTMRRVDPVYIRLAERLGTPELSPTERKELESKLKEREEFLIPIYHQVAVQFADLHDTPGRMQEKGVINDILDWKTSRTFFYWRLRRLLLEDLVKKKIHSANPELTDGQIQAMLRRWFVEVEGTVKAYVWDNNKDLVEWLEKQLTEEDGVRSVIEENIKYISRDYVLKQIRSLVQANPEVAMDSIVHMTQHISPTQRAEVVRILSTMDSPST
uniprot
proteins
ec_number
6.4.1.2
uniprot
proteins
function
FUNCTION: Cytosolic enzyme that catalyzes the carboxylation of acetyl-CoA to malonyl-CoA, the first and rate-limiting step of de novo fatty acid biosynthesis. This is 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. {ECO:0000250|UniProtKB:Q13085}.
uniprot
proteins
mass_dalton
265194
uniprot
proteins
pathway_participation
PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. {ECO:0000250|UniProtKB:Q13085}.
uniprot
proteins
post_translational_modification
PTM: The N-terminus is blocked.; PTM: Phosphorylation on Ser-1262 is required for interaction with BRCA1. {ECO:0000250}.; PTM: Phosphorylation at Ser-79 by AMPK inactivates enzyme activity. Phosphorylated in vitro at Ser-1200 and Ser-1215 by AMPK; the relevance of phosphorylation of these sites in vivo is however unclear. {ECO:0000269|PubMed:1346520, ECO:0000269|PubMed:1974251, ECO:0000269|PubMed:2900138, ECO:0000269|PubMed:9029219}.; PTM: The biotin cofactor is covalently attached to the central biotinyl-binding domain and is required for the catalytic activity. {ECO:0000305|PubMed:2567668}.
uniprot
proteins
pubmed
1346520
uniprot
proteins
pubmed
16396499
uniprot
proteins
pubmed
17218081
uniprot
proteins
pubmed
1974251
uniprot
proteins
pubmed
22673903
uniprot
proteins
pubmed
2565337
uniprot
proteins
pubmed
2566999
uniprot
proteins
pubmed
2567668
uniprot
proteins
pubmed
2900138
uniprot
proteins
pubmed
2901088
uniprot
proteins
pubmed
7910165
uniprot
proteins
pubmed
9029219
uniprot
proteins
sequence_length
2345
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q5SWU9}.
uniprot
proteins