LOCUS NP_942133 2346 aa linear PRI 19-NOV-2023
DEFINITION acetyl-CoA carboxylase 1 isoform 2 [Homo sapiens].
ACCESSION NP_942133
VERSION NP_942133.1
DBSOURCE REFSEQ: accession NM_198836.3
KEYWORDS RefSeq.
SOURCE Homo sapiens (human)
ORGANISM Homo sapiens
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
REFERENCE 1 (residues 1 to 2346)
AUTHORS Shen Y, Wang X, Ni Z, Xu S, Qiu S, Zheng W and Zhang J.
TITLE Identification of acetyl-CoA carboxylase alpha as a prognostic and
targeted candidate for hepatocellular carcinoma
JOURNAL Clin Transl Oncol 25 (8), 2499-2513 (2023)
PUBMED 36976490
REMARK GeneRIF: Identification of acetyl-CoA carboxylase alpha as a
prognostic and targeted candidate for hepatocellular carcinoma.
REFERENCE 2 (residues 1 to 2346)
AUTHORS Saisomboon S, Kariya R, Boonnate P, Sawanyawisuth K, Cha'on U,
Luvira V, Chamgramol Y, Pairojkul C, Seubwai W, Silsirivanit A,
Wongkham S, Okada S, Jitrapakdee S and Vaeteewoottacharn K.
TITLE Diminishing acetyl-CoA carboxylase 1 attenuates CCA migration via
AMPK-NF-kappaB-snail axis
JOURNAL Biochim Biophys Acta Mol Basis Dis 1869 (5), 166694 (2023)
PUBMED 36972768
REMARK GeneRIF: Diminishing acetyl-CoA carboxylase 1 attenuates CCA
migration via AMPK-NF-kappaB-snail axis.
Erratum:[Biochim Biophys Acta Mol Basis Dis. 2024
Jan;1870(1):166886. PMID: 37743108]
REFERENCE 3 (residues 1 to 2346)
AUTHORS Huang YC, Hou MF, Tsai YM, Pan YC, Tsai PH, Lin YS, Chang CY, Tsai
EM and Hsu YL.
TITLE Involvement of ACACA (acetyl-CoA carboxylase alpha) in the lung
pre-metastatic niche formation in breast cancer by senescence
phenotypic conversion in fibroblasts
JOURNAL Cell Oncol (Dordr) 46 (3), 643-660 (2023)
PUBMED 36607556
REMARK GeneRIF: Involvement of ACACA (acetyl-CoA carboxylase alpha) in the
lung pre-metastatic niche formation in breast cancer by senescence
phenotypic conversion in fibroblasts.
REFERENCE 4 (residues 1 to 2346)
AUTHORS Cao H, Cai Q, Guo W, Su Q, Qin H, Wang T, Xian Y, Zeng L, Cai M,
Guan H, Chen S, Liang H and Xu F.
TITLE Malonylation of Acetyl-CoA carboxylase 1 promotes hepatic steatosis
and is attenuated by ketogenic diet in NAFLD
JOURNAL Cell Rep 42 (4), 112319 (2023)
PUBMED 37002924
REMARK GeneRIF: Malonylation of Acetyl-CoA carboxylase 1 promotes hepatic
steatosis and is attenuated by ketogenic diet in NAFLD.
REFERENCE 5 (residues 1 to 2346)
AUTHORS Liu S, Lai J, Feng Y, Zhuo Y, Zhang H, Chen Y, Li J, Mei X, Zeng Y,
Su J, Deng Y, Jiang F, Yang S, Tan H, Hon CT, Wei S, Han Z, Wang F
and Zhong W.
TITLE Acetyl-CoA carboxylase 1 depletion suppresses de novo fatty acid
synthesis and mitochondrial beta-oxidation in castration-resistant
prostate cancer cells
JOURNAL J Biol Chem 299 (1), 102720 (2023)
PUBMED 36410440
REMARK GeneRIF: Acetyl-CoA carboxylase 1 depletion suppresses de novo
fatty acid synthesis and mitochondrial beta-oxidation in
castration-resistant prostate cancer cells.
REFERENCE 6 (residues 1 to 2346)
AUTHORS Abu-Elheiga L, Jayakumar A, Baldini A, Chirala SS and Wakil SJ.
TITLE Human acetyl-CoA carboxylase: characterization, molecular cloning,
and evidence for two isoforms
JOURNAL Proc Natl Acad Sci U S A 92 (9), 4011-4015 (1995)
PUBMED 7732023
REFERENCE 7 (residues 1 to 2346)
AUTHORS Ha J, Daniel S, Kong IS, Park CK, Tae HJ and Kim KH.
TITLE Cloning of human acetyl-CoA carboxylase cDNA
JOURNAL Eur J Biochem 219 (1-2), 297-306 (1994)
PUBMED 7905825
REFERENCE 8 (residues 1 to 2346)
AUTHORS Haystead TA, Campbell DG and Hardie DG.
TITLE Analysis of sites phosphorylated on acetyl-CoA carboxylase in
response to insulin in isolated adipocytes. Comparison with sites
phosphorylated by casein kinase-2 and the calmodulin-dependent
multiprotein kinase
JOURNAL Eur J Biochem 175 (2), 347-354 (1988)
PUBMED 2900140
REFERENCE 9 (residues 1 to 2346)
AUTHORS Munday MR, Campbell DG, Carling D and Hardie DG.
TITLE Identification by amino acid sequencing of three major regulatory
phosphorylation sites on rat acetyl-CoA carboxylase
JOURNAL Eur J Biochem 175 (2), 331-338 (1988)
PUBMED 2900138
REFERENCE 10 (residues 1 to 2346)
AUTHORS Milatovich A, Plattner R, Heerema NA, Palmer CG, Lopez-Casillas F
and Kim KH.
TITLE Localization of the gene for acetyl-CoA carboxylase to human
chromosome 17
JOURNAL Cytogenet Cell Genet 48 (3), 190-192 (1988)
PUBMED 2906852
COMMENT REVIEWED REFSEQ: This record has been curated by NCBI staff. The
reference sequence was derived from AY315621.1, AB371587.1 and
BC041598.1.
Summary: Acetyl-CoA carboxylase (ACC) is a complex multifunctional
enzyme system. ACC is a biotin-containing enzyme which catalyzes
the carboxylation of acetyl-CoA to malonyl-CoA, the rate-limiting
step in fatty acid synthesis. There are two ACC forms, alpha and
beta, encoded by two different genes. ACC-alpha is highly enriched
in lipogenic tissues. The enzyme is under long term control at the
transcriptional and translational levels and under short term
regulation by the phosphorylation/dephosphorylation of targeted
serine residues and by allosteric transformation by citrate or
palmitoyl-CoA. Multiple alternatively spliced transcript variants
divergent in the 5' sequence and encoding distinct isoforms have
been found for this gene. [provided by RefSeq, Jul 2008].
Transcript Variant: This variant (3) has an alternate 5' UTR exon,
and uses a downstream start codon, as compared to variant (1). The
resulting isoform (2) has a shorter N-terminus, as compared to
isoform 1.
Publication Note: This RefSeq record includes a subset of the
publications that are available for this gene. Please see the Gene
record to access additional publications.
##Evidence-Data-START##
Transcript exon combination :: AB371587.1, SRR14038192.1286999.1
[ECO:0000332]
RNAseq introns :: mixed sample support SAMEA1965299,
SAMEA1966682 [ECO:0006172]
##Evidence-Data-END##
FEATURES Location/Qualifiers
source 1..2346
/organism="Homo sapiens"
/db_xref="taxon:9606"
/chromosome="17"
/map="17q12"
Protein 1..2346
/product="acetyl-CoA carboxylase 1 isoform 2"
/EC_number="6.4.1.2"
/note="acetyl-Coenzyme A carboxylase alpha; acetyl-CoA
carboxylase 1; ACC-alpha"
/calculated_mol_wt=265424
Site 1
/site_type="acetylation"
/note="N-acetylmethionine. /evidence=ECO:0000269|Ref.9,
ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:20068231;
propagated from UniProtKB/Swiss-Prot (Q13085.2)"
Site 5
/site_type="phosphorylation"
/note="Phosphoserine.
/evidence=ECO:0007744|PubMed:19369195,
ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
propagated from UniProtKB/Swiss-Prot (Q13085.2)"
Site 23
/site_type="phosphorylation"
/note="Phosphoserine.
/evidence=ECO:0007744|PubMed:18669648,
ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231;
propagated from UniProtKB/Swiss-Prot (Q13085.2)"
Site 25
/site_type="phosphorylation"
/note="Phosphoserine.
/evidence=ECO:0007744|PubMed:18669648,
ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163,
ECO:0007744|PubMed:24275569; propagated from
UniProtKB/Swiss-Prot (Q13085.2)"
Site 29
/site_type="phosphorylation"
/note="Phosphoserine.
/evidence=ECO:0007744|PubMed:17081983,
ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:19690332,
ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
propagated from UniProtKB/Swiss-Prot (Q13085.2)"
Site 34
/site_type="phosphorylation"
/note="Phosphoserine.
/evidence=ECO:0000250|UniProtKB:P11497; propagated from
UniProtKB/Swiss-Prot (Q13085.2)"
Site 48
/site_type="phosphorylation"
/note="Phosphoserine.
/evidence=ECO:0007744|PubMed:20068231; propagated from
UniProtKB/Swiss-Prot (Q13085.2)"
Site 50
/site_type="phosphorylation"
/note="Phosphoserine.
/evidence=ECO:0000250|UniProtKB:P11497; propagated from
UniProtKB/Swiss-Prot (Q13085.2)"
Site 53
/site_type="phosphorylation"
/note="Phosphoserine.
/evidence=ECO:0007744|PubMed:17081983; propagated from
UniProtKB/Swiss-Prot (Q13085.2)"
Site 58
/site_type="phosphorylation"
/note="Phosphothreonine.
/evidence=ECO:0000250|UniProtKB:Q5SWU9; propagated from
UniProtKB/Swiss-Prot (Q13085.2)"
Site 78
/site_type="phosphorylation"
/note="Phosphoserine.
/evidence=ECO:0000250|UniProtKB:P11497; propagated from
UniProtKB/Swiss-Prot (Q13085.2)"
Site 80
/site_type="phosphorylation"
/note="Phosphoserine.
/evidence=ECO:0000269|PubMed:29899443, ECO:0000269|Ref.9,
ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
propagated from UniProtKB/Swiss-Prot (Q13085.2)"
Region 118..620
/region_name="AccC"
/note="Biotin carboxylase [Lipid transport and
metabolism]; COG0439"
/db_xref="CDD:223516"
Site 488
/site_type="phosphorylation"
/note="Phosphoserine.
/evidence=ECO:0007744|PubMed:18220336; propagated from
UniProtKB/Swiss-Prot (Q13085.2)"
Site 610
/site_type="phosphorylation"
/note="Phosphothreonine.
/evidence=ECO:0007744|PubMed:23186163; propagated from
UniProtKB/Swiss-Prot (Q13085.2)"
Region 671..818
/region_name="AccB"
/note="Biotin carboxyl carrier protein [Coenzyme transport
and metabolism, Lipid transport and metabolism]; COG0511"
/db_xref="CDD:223585"
Region 753..818
/region_name="Biotin_lipoyl"
/note="Biotin-requiring enzyme; pfam00364"
/db_xref="CDD:395290"
Site order(776,785..787,794)
/site_type="active"
/note="carboxyltransferase (CT) interaction site [active]"
/db_xref="CDD:133459"
Site 786
/site_type="other"
/note="biotinylation site [posttranslational
modification]"
/db_xref="CDD:133459"
Region 820..1569
/region_name="ACC_central"
/note="Acetyl-CoA carboxylase, central region; pfam08326"
/db_xref="CDD:429920"
Site 835
/site_type="phosphorylation"
/note="Phosphoserine.
/evidence=ECO:0007744|PubMed:23186163; propagated from
UniProtKB/Swiss-Prot (Q13085.2)"
Site 1201
/site_type="phosphorylation"
/note="Phosphoserine.
/evidence=ECO:0000250|UniProtKB:P11497; propagated from
UniProtKB/Swiss-Prot (Q13085.2)"
Site 1216
/site_type="phosphorylation"
/note="Phosphoserine.
/evidence=ECO:0000250|UniProtKB:P11497; propagated from
UniProtKB/Swiss-Prot (Q13085.2)"
Site 1218
/site_type="phosphorylation"
/note="Phosphoserine.
/evidence=ECO:0000250|UniProtKB:Q5SWU9; propagated from
UniProtKB/Swiss-Prot (Q13085.2)"
Site 1227
/site_type="phosphorylation"
/note="Phosphothreonine.
/evidence=ECO:0000250|UniProtKB:Q5SWU9; propagated from
UniProtKB/Swiss-Prot (Q13085.2)"
Site 1259
/site_type="phosphorylation"
/note="Phosphoserine.
/evidence=ECO:0000250|UniProtKB:Q5SWU9; propagated from
UniProtKB/Swiss-Prot (Q13085.2)"
Site 1263
/site_type="phosphorylation"
/note="Phosphoserine.
/evidence=ECO:0000269|PubMed:16698035,
ECO:0000269|PubMed:29899443; propagated from
UniProtKB/Swiss-Prot (Q13085.2)"
Site 1273
/site_type="phosphorylation"
/note="Phosphoserine.
/evidence=ECO:0007744|PubMed:24275569; propagated from
UniProtKB/Swiss-Prot (Q13085.2)"
Site 1334
/site_type="acetylation"
/note="N6-acetyllysine.
/evidence=ECO:0007744|PubMed:19608861; propagated from
UniProtKB/Swiss-Prot (Q13085.2)"
Region 1576..2234
/region_name="Carboxyltransferase.
/evidence=ECO:0000255|PROSITE-ProRule:PRU01138"
/note="propagated from UniProtKB/Swiss-Prot (Q13085.2)"
Region 1669..2217
/region_name="Carboxyl_trans"
/note="Carboxyl transferase domain; pfam01039"
/db_xref="CDD:426008"
Site 2153
/site_type="phosphorylation"
/note="Phosphothreonine.
/evidence=ECO:0007744|PubMed:23186163; propagated from
UniProtKB/Swiss-Prot (Q13085.2)"
CDS 1..2346
/gene="ACACA"
/gene_synonym="ACAC; Acac1; ACACAD; ACACalpha; ACC; ACC1;
ACCA; ACCalpha; hACC1"
/coded_by="NM_198836.3:172..7212"
/note="isoform 2 is encoded by transcript variant 3"
/db_xref="CCDS:CCDS11317.1"
/db_xref="GeneID:31"
/db_xref="HGNC:HGNC:84"
/db_xref="MIM:200350"
ORIGIN
1 mdepsplaqp lelnqhsrfi igsvsednse deisnlvkld lleekegsls pasvgsdtls
61 dlgisslqdg lalhirssms glhlvkqgrd rkkidsqrdf tvaspaefvt rfggnkviek
121 vlianngiaa vkcmrsirrw syemfrnera irfvvmvtpe dlkanaeyik madhyvpvpg
181 gpnnnnyanv elildiakri pvqavwagwg hasenpklpe lllkngiafm gppsqamwal
241 gdkiassiva qtagiptlpw sgsglrvdwq endfskriln vpqelyekgy vkdvddglqa
301 aeevgypvmi kaseggggkg irkvnnaddf pnlfrqvqae vpgspifvmr lakqsrhlev
361 qiladqygna islfgrdcsv qrrhqkiiee apatiatpav fehmeqcavk lakmvgyvsa
421 gtveylysqd gsfyflelnp rlqvehpcte mvadvnlpaa qlqiamgipl yrikdirmmy
481 gvspwgdspi dfedsahvpc prghviaari tsenpdegfk pssgtvqeln frsnknvwgy
541 fsvaaagglh efadsqfghc fswgenreea isnmvvalke lsirgdfrtt veylikllet
601 esfqmnridt gwldrliaek vqaerpdtml gvvcgalhva dvslrnsvsn flhslergqv
661 lpahtllntv dveliyegvk yvlkvtrqsp nsyvvimngs cvevdvhrls dgglllsydg
721 ssyttymkee vdryritign ktcvfekend psvmrspsag kliqyivedg ghvfagqcya
781 eievmkmvmt ltavesgcih yvkrpgaald pgcvlakmql dnpskvqqae lhtgslpriq
841 stalrgeklh rvfhyvldnl vnvmngyclp dpffsskvkd wverlmktlr dpslpllelq
901 dimtsvsgri ppnveksikk emaqyasnit svlcqfpsqq ianildshaa tlnrkserev
961 ffmntqsivq lvqryrsgir ghmkavvmdl lrqylrvetq fqnghydkcv falreenksd
1021 mntvlnyifs haqvtkknll vtmlidqlcg rdptltdell nilteltqls kttnakvalr
1081 arqvliashl psyelrhnqv esiflsaidm yghqfcienl qklilsetsi fdvlpnffyh
1141 snqvvrmaal evyvrrayia yelnsvqhrq lkdntcvvef qfmlptshpn rgniptlnrm
1201 sfssnlnhyg mthvasvsdv lldnsftppc qrmggmvsfr tfedfvrifd evmgcfsdsp
1261 pqsptfpeag htslydedkv prdepihiln vaiktdcdie ddrlaamfre ftqqnkatlv
1321 dhgirrltfl vaqkdfrkqv nyevdrrfhr efpkfftfra rdkfeedriy rhlepalafq
1381 lelnrmrnfd ltaipcanhk mhlylgaakv evgtevtdyr ffvraiirhs dlvtkeasfe
1441 ylqnegerll leamdeleva fnntnvrtdc nhiflnfvpt vimdpskiee svrsmvmryg
1501 srlwklrvlq aelkinirlt ptgkaipirl fltnesgyyl dislykevtd srtaqimfqa
1561 ygdkqgplhg mlintpyvtk dllqskrfqa qslgttyiyd ipemfrqsli klwesmstqa
1621 flpspplpsd mltytelvld dqgqlvhmnr lpggneigmv awkmtfkspe ypegrdiivi
1681 gndityrigs fgpqedllfl raselaraeg ipriyvsans gariglaeei rhmfhvawvd
1741 pedpykgyry lyltpqdykr vsalnsvhce hvedegesry kitdiigkee gigpenlrgs
1801 gmiagessla yneiitislv tcraigigay lvrlgqrtiq venshliltg agalnkvlgr
1861 evytsnnqlg giqimhnngv thctvcddfe gvftvlhwls ympksvhssv pllnskdpid
1921 riiefvptkt pydprwmlag rphptqkgqw lsgffdygsf seimqpwaqt vvvgrarlgg
1981 ipvgvvavet rtvelsipad panldseaki iqqagqvwfp dsafktyqai kdfnreglpl
2041 mvfanwrgfs ggmkdmydqv lkfgayivdg lreccqpvlv yippqaelrg gswvvidssi
2101 nprhmemyad resrgsvlep egtveikfrr kdlvktmrrv dpvyihlaer lgtpelstae
2161 rkelenklke reeflipiyh qvavqfadlh dtpgrmqekg visdildwkt srtffywrlr
2221 rllledlvkk kihnanpelt dgqiqamlrr wfvevegtvk ayvwdnnkdl aewlekqlte
2281 edgvhsviee nikcisrdyv lkqirslvqa npevamdsii hmtqhisptq raevirilst
2341 mdspst
//
