Search by BoMiProt ID - Bomi3613


Primary Information

BoMiProt ID Bomi3613
Protein Name Acetyl-CoA carboxylase 1
Organism Bos taurus
Uniprot IdQ9TTS3
Milk FractionMFGM
Ref Sequence Id NP_776649.1
Aminoacid Length 2346
Molecular Weight 265303
Fasta Sequence https://www.uniprot.org/uniprot/Q9TTS3.fasta
Gene Name ACACA
Gene Id 281590
Protein Existence Status reviewed

Secondary Information

Presence in other biological fluids/tissue/cells Brain,adipose tissues and lactating mammary glands
Protein Function 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.
Biochemical Properties Consists of N-terminal biotin carboxylase (BC) domain and central biotin carboxyl carrier (BCC) domain.Biotin cofactor is covalently attached to the central biotinyl-binding domain which is important for the catalytic activity. Catalyses the following reaction- acetyl-CoA + ATP + hydrogencarbonate = ADP + H+ + malonyl-CoA + phosphate
Significance in milk Fatty acid synthesis in the mammary glands.
PTMs Phosphorylation on Ser-1263.Phosphorylation at Ser-80
Site(s) of PTM(s)

N-glycosylation, O-glycosylation,
Phosphorylation
>sp|Q9TTS3|ACACA_BOVIN Acetyl-CoA carboxylase 1 OS=Bos taurus OX=9913 GN=ACACA PE=2 SV=1 MDEPS*5SLAKPLELNQHSRFIIGS*23VS*25EDNS*29EDEIS*34NLVKLDLLEEKEGS*48LS*50PAS*53VSSDT*58LS DLGISSLQDGLALHMRSS*78MS*80GLHLVKQGRDRKKIDSQRDFTVASPAEFVTRFGGNKVIEK VLIANNGIAAVKCMRSIRRWSYEMFRNERAIRFVVMVTPEDLKANAEYIKMADHYVPVPG GPNNNNYANVELILDIAKRIPVQAVWAGWGHASENPKLPELLLKNGIAFMGPPSQAMWAL GDKIASSIVAQTAGIPTLPWSGSGLCVDWHENDFSKRILNVPQELYEKGYVKDVDDGLKA AEEVGYPVMIKASEGGGGKGIRKVNNADDFPNLFRQVQAEVPGSPIFVMRLAKQSRHLEV QILADQYGNAISLFGRDCSVQRRHQKIIEEAPAAIATPAVFEHMEQCAVKLARMVGYVSA GTVEYLYSQDGSFYFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPLYRIKDIRMMY GVSPWGDAPIDFENSAHVPCPRGHVIAARITSENPDEGFKPSSGTVQELNFRSNKNVWGY FSVAAAGGLHEFADSQFGHCFSWGENREEAISNMVVALKELSIRGDFRTTVEYLIKLLET ESFQLNRIGT*610GWLDRLIAEKVQAERPDTMLGVVCGALHVADVSLRNSISNFLHSLERGQV LTAHTLLNTVDVELIYEGVKYVLKVTRQSPNSYVVIMNGSCVEVDVHRLSDGGLLLSYDV SSYTTYMKEEVDRYRITIGNKTCVFEKENDPSVLRSPSAGKLIQYIVEDGGHVFAGQCYA EIEVMKMVMTLTAAESGCIHYVKRPGAALDPGCVIAKMQLDNPSKVQQAELHTGS*835LPRIQ STALRGEKLHRVFHYVLDNLVNVMNGYCLPDPFFSSRVKDWVERLMKTLRDPSLPLLELQ DIMTSVSGRIPPNVEKSIKKEMAQYASNITSVLCQFPSQQIANILDSHAATLNRKSEREV FFMNTQSIVQLVQRYRSGIRGHMKAVVMDLLRQYLRVETQFQNGHYDKCVFALREENKSD MNTVLNYIFSHAQVTRKNLLVTMLIDQLCGRGPTLTDELLNILTELTQLSKTTNAKVALR ARQVLIASHLPSYELRLNQVESIFLSAIDMYGHQFCIENLQKLILSETSIFDVLPNFFYH SNQVVRMAALEVYVRRAYIAYELNSVQHRQLKDNTCVVEFQFMLPTSHPNRGNIPTLNRM S*1201FSSNLNHYGMTHVAS*1216VS*1218DVLLDNAFT*1227PPCQRMGGMVSFRTFEDFVRIFDEVMGCFCDS*1259PPQS*1263PTFPEAGHTS*1273LYDEDKVPRDEPIHILNVAIKTDCDIEDDSLAAMFREFTQQNKATLVEHGIRRLTFLVAQKDFRKQVNYEVDQRFHREFPKFFTFRARDKFEEDRIYRHLEPALAFQ LELNRMRNFDLTAIPCANHKMHLYLGAAKVEVGTEVTDYRFFVRAIIRHSDLVTKEASFE YLQNEGERLLLEAMDELEVAFNNTNVRTDCNHIFLNFVPTVIMDPSKIEESVRSMVMRYG SRLWKLRVLQAELKINIRLTPTGKAIPIRLFLTNESGYYLDISLYKEVTDSRTAQIMFQA YGDKQGPLHGMLINTPYVTKDQLQSKRFQAQSLGTTYIYDIPEMFRQSLIKLWESMSSQA FLPPPPLPSDILTYTELVLDDQGQLVHMNRLPGGNEIGMVAWKMTLKSPEYPDGRDIIVI GNDITYRIGSFGPQEDLLFLRASELARAEGIPRIYVAANSGARIGLAEEIRHMFHVAWVD PEDPYKGYKYLYLTPQDYKRVSALNSVHCEHVEDEGESRYKITDIIGKEEGLGAENLRGS GMIAGESSLAYDEIITISLVTCRAIGIGAYLVRLGQRTIQVENSHLILTGAGALNKVLGR EVYTSNNQLGGIQIMHNNGVTHSTVCDDFEGVFTVLHWLSYMPKSVYSSVPLLNSKDPID RVIEFVPTKAPYDPRWMLAGRPHPTQKGQWLSGFFDYGSFSEIMQPWAQTVVVGRARLGG IPVGVVAVETRTVELSIPADPANLDSEAKIIQQAGQVWFPDSAFKTYQAIKDFNREGLPL MVFANWRGFSGGMKDMYDQVLKFGAYIVDGLRECSQPVMVYIPPQAELRGGSWVVIDPTI NPRHMEMYADRESRGSVLEPEGTVEIKFRRKDLVKTMRRVDPVYIHLAERLGT*2153PELSVAE RKELESKLKEREEFLLPIYHQVAVQFADLHDTPGRMQEKGVINDILDWKTSRTFFYWRLR RLLLEDLVKKKIHNANPELTDGQIQAMLRRWFVEVEGTVKAYVWDNNKDLVEWLEKQLTE EDGVRSVIEENIKYISRDYVLKQIRSLVQANPEVAMDSIVHMTQHISPTQRAEVVRILST MDSPST
Predicted Disorder Regions NA
DisProt Annotation
TM Helix Prediction No TM helices
Significance of PTMs hosphorylation on Ser-1263 is required for interaction with BRCA1 and Phosphorylation at Ser-80 by AMPK inactivates enzyme activity
Bibliography Hunkeler M, Hagmann A, Stuttfeld E, Chami M, Guri Y, Stahlberg H, Maier T. Structural basis for regulation of human acetyl-CoA carboxylase. Nature. 2018 Jun;558(7710):470-474. doi: 10.1038/s41586-018-0201-4. Epub 2018 Jun 13. PMID: 29899443.