Primary Information |
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BoMiProt ID | Bomi3613 |
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Protein Name | Acetyl-CoA carboxylase 1 |
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Organism | Bos taurus |
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Uniprot ID | Q9TTS3 |
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Milk Fraction | MFGM |
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Ref Sequence ID | NP_776649.1 |
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Aminoacid Length | 2346 |
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Molecular Weight | 265303 |
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FASTA Sequence |
Download |
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Gene Name | ACACA |
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Gene ID | 281590 |
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Protein Existence Status | reviewed |
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Secondary Information |
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Presence in other biological fluids/tissue/cells | Brain,adipose tissues and lactating mammary glands |
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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. |
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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 |
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Significance in milk | Fatty acid synthesis in the mammary glands. |
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PTMs | Phosphorylation on Ser-1263.Phosphorylation at Ser-80 |
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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
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Predicted Disorder Regions | NA |
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DisProt Annotation | |
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TM Helix Prediction | No TM helices |
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Significance of PTMs | hosphorylation on Ser-1263 is required for interaction with BRCA1 and Phosphorylation at Ser-80 by AMPK inactivates enzyme activity |
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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. |