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Acetyl-CoA carboxylase 1 (ACC1) (EC 6.4.1.2) (ACC-alpha) [Includes: Biotin carboxylase (EC 6.3.4.14)]

 ACACA_RAT               Reviewed;        2345 AA.
P11497; A1EC79; P97902;
01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
01-OCT-1989, sequence version 1.
22-NOV-2017, entry version 165.
RecName: Full=Acetyl-CoA carboxylase 1;
Short=ACC1;
EC=6.4.1.2;
AltName: Full=ACC-alpha;
Includes:
RecName: Full=Biotin carboxylase;
EC=6.3.4.14;
Name=Acaca; Synonyms=Acac;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=2901088; DOI=10.1073/pnas.85.16.5784;
Lopez-Casillas F., Bai D.-H., Luo X., Kong I.-S., Hermodson M.A.,
Kim K.-H.;
"Structure of the coding sequence and primary amino acid sequence of
acetyl-coenzyme A carboxylase.";
Proc. Natl. Acad. Sci. U.S.A. 85:5784-5788(1988).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2566999; DOI=10.1073/pnas.86.11.4042;
Luo X.N., Park K., Lopez-Casillas F., Kim K.-H.;
"Structural features of the acetyl-CoA carboxylase gene: mechanisms
for the generation of mRNAs with 5' end heterogeneity.";
Proc. Natl. Acad. Sci. U.S.A. 86:4042-4046(1989).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
STRAIN=Dahl salt-sensitive, and Lewis;
PubMed=17218081; DOI=10.1016/j.ygeno.2006.12.005;
Saad Y., Garrett M.R., Manickavasagam E., Yerga-Woolwine S., Farms P.,
Radecki T., Joe B.;
"Fine-mapping and comprehensive transcript analysis reveals
nonsynonymous variants within a novel 1.17 Mb blood pressure QTL
region on rat chromosome 10.";
Genomics 89:343-353(2007).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-33.
PubMed=2565337;
Lopez-Casillas F., Kim K.-H.;
"Heterogeneity at the 5' end of rat acetyl-coenzyme A carboxylase
mRNA. Lipogenic conditions enhance synthesis of a unique mRNA in
liver.";
J. Biol. Chem. 264:7176-7184(1989).
[5]
PROTEIN SEQUENCE OF 76-85 AND 1198-1201, AND PHOSPHORYLATION AT
SER-77; SER-79 AND SER-1200.
PubMed=2900138; DOI=10.1111/j.1432-1033.1988.tb14201.x;
Munday M.R., Campbell D.G., Carling D., Hardie D.G.;
"Identification by amino acid sequencing of three major regulatory
phosphorylation sites on rat acetyl-CoA carboxylase.";
Eur. J. Biochem. 175:331-338(1988).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 1167-1200 (ISOFORMS 1 AND 2), AND
PHOSPHORYLATION AT SER-1200.
PubMed=1974251;
Kong I.-S., Lopez-Casillas F., Kim K.-H.;
"Acetyl-CoA carboxylase mRNA species with or without inhibitory coding
sequence for Ser-1200 phosphorylation.";
J. Biol. Chem. 265:13695-13701(1990).
[7]
PARTIAL PROTEIN SEQUENCE, AND IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=Wistar; TISSUE=Liver;
PubMed=7910165;
Winz R., Hess D., Aebersold R., Brownsey R.W.;
"Unique structural features and differential phosphorylation of the
280-kDa component (isozyme) of rat liver acetyl-CoA carboxylase.";
J. Biol. Chem. 269:14438-14445(1994).
[8]
BIOTINYLATION AT LYS-785.
PubMed=2567668; DOI=10.1111/j.1432-1033.1989.tb14823.x;
Bai D.-H., Moon T.-W., Lopez-Casillas F., Andrews P.C., Kim K.-H.;
"Analysis of the biotin-binding site on acetyl-CoA carboxylase from
rat.";
Eur. J. Biochem. 182:239-245(1989).
[9]
PHOSPHORYLATION AT SER-79; SER-1200 AND SER-1215.
PubMed=1346520; DOI=10.1111/j.1432-1033.1992.tb16591.x;
Davies S.P., Carling D., Munday M.R., Hardie D.G.;
"Diurnal rhythm of phosphorylation of rat liver acetyl-CoA carboxylase
by the AMP-activated protein kinase, demonstrated using freeze-
clamping. Effects of high fat diets.";
Eur. J. Biochem. 203:615-623(1992).
[10]
PHOSPHORYLATION BY AMPK.
PubMed=9029219;
Winder W.W., Wilson H.A., Hardie D.G., Rasmussen B.B., Hutber C.A.,
Call G.B., Clayton R.D., Conley L.M., Yoon S., Zhou B.;
"Phosphorylation of rat muscle acetyl-CoA carboxylase by AMP-activated
protein kinase and protein kinase A.";
J. Appl. Physiol. 82:219-225(1997).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=16396499; DOI=10.1021/pr0503073;
Moser K., White F.M.;
"Phosphoproteomic analysis of rat liver by high capacity IMAC and LC-
MS/MS.";
J. Proteome Res. 5:98-104(2006).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23; SER-25; SER-29;
SER-34; SER-47; SER-49; SER-79; THR-609 AND SER-1258, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: Catalyzes the rate-limiting reaction in the biogenesis
of long-chain fatty acids. Carries out three functions: biotin
carboxyl carrier protein, biotin carboxylase and
carboxyltransferase. {ECO:0000250|UniProtKB:Q13085}.
-!- CATALYTIC ACTIVITY: ATP + acetyl-CoA + HCO(3)(-) = ADP + phosphate
+ malonyl-CoA. {ECO:0000250|UniProtKB:Q5SWU9}.
-!- CATALYTIC ACTIVITY: ATP + biotin-[carboxyl-carrier-protein] +
HCO(3)(-) = ADP + phosphate + carboxy-biotin-[carboxyl-carrier-
protein]. {ECO:0000250|UniProtKB:Q5SWU9}.
-!- COFACTOR:
Name=biotin; Xref=ChEBI:CHEBI:57586;
-!- COFACTOR:
Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
Note=Binds 2 manganese ions per subunit. {ECO:0000250};
-!- ENZYME REGULATION: Activity is increased by oligomerization.
Citrate and MID1IP1 promote oligomerization (By similarity).
Activity is increased by phosphorylation. {ECO:0000250}.
-!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA
from acetyl-CoA: step 1/1.
-!- SUBUNIT: Monomer, homodimer, and homotetramer. Can form
filamentous polymers. Interacts in its inactive phosphorylated
form with the BRCT domains of BRCA1 which prevents ACACA
dephosphorylation and inhibits lipid synthesis. Interacts with
MID1IP1; interaction with MID1IP1 promotes oligomerization and
increases its activity (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P11497-1; Sequence=Displayed;
Name=2;
IsoId=P11497-2; Sequence=VSP_011753;
-!- 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}.
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EMBL; J03808; AAA40653.1; -; mRNA.
EMBL; M26731; AAA40652.1; -; Genomic_DNA.
EMBL; EF121986; ABL63425.1; -; mRNA.
EMBL; EF121987; ABL63426.1; -; mRNA.
EMBL; M26195; AAA40654.1; -; mRNA.
EMBL; M26196; AAA40655.1; -; mRNA.
EMBL; M26197; AAA40656.1; -; mRNA.
EMBL; M55315; -; NOT_ANNOTATED_CDS; mRNA.
PIR; A35578; A35578.
RefSeq; NP_071529.1; NM_022193.1. [P11497-1]
UniGene; Rn.163753; -.
UniGene; Rn.217177; -.
UniGene; Rn.44372; -.
ProteinModelPortal; P11497; -.
SMR; P11497; -.
BioGrid; 248868; 1.
STRING; 10116.ENSRNOP00000049438; -.
BindingDB; P11497; -.
ChEMBL; CHEMBL2397; -.
iPTMnet; P11497; -.
PhosphoSitePlus; P11497; -.
PaxDb; P11497; -.
PRIDE; P11497; -.
GeneID; 60581; -.
KEGG; rno:60581; -.
CTD; 31; -.
RGD; 621248; Acaca.
eggNOG; ENOG410ISCX; Eukaryota.
eggNOG; COG0439; LUCA.
eggNOG; COG0511; LUCA.
eggNOG; COG4799; LUCA.
HOGENOM; HOG000214115; -.
HOVERGEN; HBG005371; -.
InParanoid; P11497; -.
KO; K11262; -.
PhylomeDB; P11497; -.
UniPathway; UPA00655; UER00711.
PRO; PR:P11497; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005829; C:cytosol; ISS:UniProtKB.
GO; GO:0070062; C:extracellular exosome; ISO:RGD.
GO; GO:0005739; C:mitochondrion; ISO:RGD.
GO; GO:0003989; F:acetyl-CoA carboxylase activity; IDA:CACAO.
GO; GO:0005524; F:ATP binding; IDA:RGD.
GO; GO:0009374; F:biotin binding; IMP:RGD.
GO; GO:0004075; F:biotin carboxylase activity; IEA:UniProtKB-EC.
GO; GO:0019900; F:kinase binding; IPI:RGD.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0006084; P:acetyl-CoA metabolic process; IDA:RGD.
GO; GO:0071380; P:cellular response to prostaglandin E stimulus; ISO:RGD.
GO; GO:0006633; P:fatty acid biosynthetic process; IDA:RGD.
GO; GO:0055088; P:lipid homeostasis; ISO:RGD.
GO; GO:0006629; P:lipid metabolic process; ISO:RGD.
GO; GO:2001295; P:malonyl-CoA biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0044268; P:multicellular organismal protein metabolic process; ISO:RGD.
GO; GO:0051289; P:protein homotetramerization; ISS:UniProtKB.
GO; GO:0042493; P:response to drug; IEP:RGD.
GO; GO:0014070; P:response to organic cyclic compound; IMP:RGD.
GO; GO:0001894; P:tissue homeostasis; ISO:RGD.
Gene3D; 3.30.1490.20; -; 1.
InterPro; IPR034733; AcCoA_carboxyl.
InterPro; IPR013537; AcCoA_COase_cen.
InterPro; IPR011761; ATP-grasp.
InterPro; IPR013815; ATP_grasp_subdomain_1.
InterPro; IPR005481; BC-like_N.
InterPro; IPR001882; Biotin_BS.
InterPro; IPR011764; Biotin_carboxylation_dom.
InterPro; IPR005482; Biotin_COase_C.
InterPro; IPR000089; Biotin_lipoyl.
InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
InterPro; IPR011763; COA_CT_C.
InterPro; IPR011762; COA_CT_N.
InterPro; IPR016185; PreATP-grasp_dom_sf.
InterPro; IPR011054; Rudment_hybrid_motif.
InterPro; IPR011053; Single_hybrid_motif.
Pfam; PF08326; ACC_central; 1.
Pfam; PF02785; Biotin_carb_C; 1.
Pfam; PF00289; Biotin_carb_N; 1.
Pfam; PF00364; Biotin_lipoyl; 1.
Pfam; PF01039; Carboxyl_trans; 1.
Pfam; PF02786; CPSase_L_D2; 1.
SMART; SM00878; Biotin_carb_C; 1.
SUPFAM; SSF51230; SSF51230; 1.
SUPFAM; SSF51246; SSF51246; 1.
SUPFAM; SSF52096; SSF52096; 2.
SUPFAM; SSF52440; SSF52440; 1.
PROSITE; PS50975; ATP_GRASP; 1.
PROSITE; PS50979; BC; 1.
PROSITE; PS00188; BIOTIN; 1.
PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
PROSITE; PS50989; COA_CT_CTER; 1.
PROSITE; PS50980; COA_CT_NTER; 1.
PROSITE; PS00866; CPSASE_1; 1.
PROSITE; PS00867; CPSASE_2; 1.
1: Evidence at protein level;
Acetylation; Allosteric enzyme; Alternative splicing; ATP-binding;
Biotin; Complete proteome; Cytoplasm; Direct protein sequencing;
Fatty acid biosynthesis; Fatty acid metabolism; Ligase;
Lipid biosynthesis; Lipid metabolism; Manganese; Metal-binding;
Multifunctional enzyme; Nucleotide-binding; Phosphoprotein;
Reference proteome.
CHAIN 1 2345 Acetyl-CoA carboxylase 1.
/FTId=PRO_0000146765.
DOMAIN 116 617 Biotin carboxylation.
DOMAIN 274 465 ATP-grasp. {ECO:0000255|PROSITE-
ProRule:PRU00409}.
DOMAIN 744 818 Biotinyl-binding. {ECO:0000255|PROSITE-
ProRule:PRU01066}.
DOMAIN 1575 1913 CoA carboxyltransferase N-terminal.
{ECO:0000255|PROSITE-ProRule:PRU01136}.
DOMAIN 1917 2233 CoA carboxyltransferase C-terminal.
{ECO:0000255|PROSITE-ProRule:PRU01137}.
NP_BIND 314 319 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00409}.
REGION 1575 2233 Carboxyltransferase.
{ECO:0000255|PROSITE-ProRule:PRU01138}.
ACT_SITE 440 440 {ECO:0000250}.
METAL 423 423 Manganese 1. {ECO:0000250}.
METAL 436 436 Manganese 1. {ECO:0000250}.
METAL 436 436 Manganese 2. {ECO:0000250}.
METAL 438 438 Manganese 2. {ECO:0000250}.
BINDING 1822 1822 Coenzyme A. {ECO:0000250}.
BINDING 2126 2126 Coenzyme A. {ECO:0000250}.
BINDING 2128 2128 Coenzyme A. {ECO:0000250}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:Q13085}.
MOD_RES 5 5 Phosphoserine.
{ECO:0000250|UniProtKB:Q13085}.
MOD_RES 23 23 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 25 25 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 29 29 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 34 34 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 47 47 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 49 49 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 52 52 Phosphoserine.
{ECO:0000250|UniProtKB:Q13085}.
MOD_RES 57 57 Phosphothreonine.
{ECO:0000250|UniProtKB:Q5SWU9}.
MOD_RES 77 77 Phosphoserine.
{ECO:0000269|PubMed:2900138}.
MOD_RES 79 79 Phosphoserine; by AMPK.
{ECO:0000244|PubMed:22673903,
ECO:0000269|PubMed:1346520,
ECO:0000269|PubMed:2900138}.
MOD_RES 609 609 Phosphothreonine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 785 785 N6-biotinyllysine. {ECO:0000255|PROSITE-
ProRule:PRU01066,
ECO:0000269|PubMed:2567668}.
MOD_RES 834 834 Phosphoserine.
{ECO:0000250|UniProtKB:Q13085}.
MOD_RES 1200 1200 Phosphoserine; by AMPK; in vitro.
{ECO:0000269|PubMed:1346520,
ECO:0000269|PubMed:1974251,
ECO:0000269|PubMed:2900138}.
MOD_RES 1215 1215 Phosphoserine; by AMPK; in vitro.
{ECO:0000269|PubMed:1346520}.
MOD_RES 1217 1217 Phosphoserine.
{ECO:0000250|UniProtKB:Q5SWU9}.
MOD_RES 1226 1226 Phosphothreonine.
{ECO:0000250|UniProtKB:Q5SWU9}.
MOD_RES 1258 1258 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 1262 1262 Phosphoserine.
{ECO:0000250|UniProtKB:Q13085}.
MOD_RES 1272 1272 Phosphoserine.
{ECO:0000250|UniProtKB:Q13085}.
MOD_RES 1333 1333 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q13085}.
MOD_RES 2152 2152 Phosphothreonine.
{ECO:0000250|UniProtKB:Q13085}.
VAR_SEQ 1189 1196 Missing (in isoform 2).
{ECO:0000303|PubMed:1974251}.
/FTId=VSP_011753.
SEQUENCE 2345 AA; 265194 MW; 78E9CF9ADE1E8771 CRC64;
MDEPSPLAKT LELNQHSRFI IGSVSEDNSE DEISNLVKLD LEEKEGSLSP ASVSSDTLSD
LGISALQDGL AFHMRSSMSG LHLVKQGRDR KKIDSQRDFT VASPAEFVTR FGGNKVIEKV
LIANNGIAAV KCMRSIRRWS YEMFRNERAI RFVVMVTPED LKANAEYIKM ADHYVPVPGG
ANNNNYANVE LILDIAKRIP VQAVWAGWGH ASENPKLPEL LLKNGIAFMG PPSQAMWALG
DKIASSIVAQ TAGIPTLPWS GSGLRVDWQE NDFSKRILNV PQDLYEKGYV KDVDDGLKAA
EEVGYPVMIK ASEGGGGKGI RKVNNADDFP NLFRQVQAEV PGSPIFVMRL AKQSRHLEVQ
ILADQYGNAI SLFGRDCSVQ RRHQKIIEEA PAAIATPAVF EHMEQCAVKL AKMVGYVSAG
TVEYLYSQDG SFYFLELNPR LQVEHPCTEM VADVNLPAAQ LQIAMGIPLF RIKDIRMMYG
VSPWGDAPID FENSAHVPCP RGHVIAARIT SENPDEGFKP SSGTVQELNF RSNKNVWGYF
SVAAAGGLHE FADSQFGHCF SWGENREEAI SNMVVALKEL SIRGDFRTTV EYLIKLLETE
SFQLNRIDTG WLDRLIAEKV QAERPDTMLG VVCGALHVAD VNLRNSISNF LHSLERGQVL
PAHTLLNTVD VELIYEGIKY VLKVTRQSPN SYVVIMNGSC VEVDVHRLSD GGLLLSYDGS
SYTTYMKEEV DRYRITIGNK TCVFEKENDP SVMRSPSAGK LIQYIVEDGG HVFAGQCYAE
IEVMKMVMTL TAVESGCIHY VKRPGAALDP GCVIAKMQLD NPSKVQQAEL HTGSLPQIQS
TALRGEKLHR VFHYVLDNLV NVMNGYCLPD PFFSSKVKDW VERLMKTLRD PSLPLLELQD
IMTSVSGRIP LNVEKSIKKE MAQYASNITS VLCQFPSQQI ANILDSHAAT LNRKSEREVF
FMNTQSIVQL VQRYRSGIRG HMKAVVMDLL RQYLRVETQF QNGHYDKCVF ALREENKSDM
NTVLNYIFSH AQVTKKNLLV TMLIDQLCGR DPTLTDELLN ILTELTQLSK TTNAKVALRA
RQVLIASHLP SYDVRHNQVE SIFLSAIDMY GHQFCIENLQ KLILSETSIF DVLPNFFYHS
NQVVRMAALE VYVRRAYIAY ELNSVQHRQL KDNTCVVEFQ FMLPTSHPNR GNIPTLNRMS
FASNLNHYGM THVASVSDVL LDNAFTPPCQ RMGGMVSFRT FEDFVRIFDE VMGCFCDSPP
QSPTFPESGH TSLYDEDKVP RDEPIHILNV AIKTDGDIED DRLAAMFREF TQQNKATLVE
HGIRRLTFLV AQKDFRKQVN CEVDQRFHRE FPKFFTFRAR DKFEEDRIYR HLEPALAFQL
ELNRMRNFDL TAIPCANHKM HLYLGAAKVE VGTEVTDYRF FVRAIIRHSD LVTKEASFEY
LQNEGERLLL EAMDELEVAF NNTNVRTDCN HIFLNFVPTV IMDPSKIEES VRSMVMRYGS
RLWKLRVLQA ELKINIRLTT TGKAIPIRLF LTNESGYYLD ISLYKEVTDS RTAQIMFQAY
GDKQGPLHGM LINTPYVTKD LLQSKRFQAQ SLGTTYIYDI PEMFRQSLIK LWESMSTQAF
LPSPPLPSDI LTYTELVLDD QGQLVHMNRL PGGNEIGMVA WKMSLKSPEY PDGRDVIVIG
NDITYRIGSF GPQEDLLFLR ASELARAEGI PRIYVAANSG ARIGLAEEIR HMFHVAWVDS
EDPYKGYKYL YLTPQDYKRV SALNSVHCEH VEDEGESRYK ITDIIGKEEG LGAENLRGSG
MIAGESSLAY DEIITISLVT CRAIGIGAYL VRLGQRTIQV ENSHLILTGA GALNKVLGRE
VYTSNNQLGG IQIMHNNGVT HCTVCDDFEG VFTVLHWLSY MPKNVHSSVP LLNSKDPIDR
IIEFVPTKAP YDPRWMLAGR PHPTQKGQWL SGFFDYGSFS EIMQPWAQTV VVGRARLGGI
PVGVVAVETR TVELSVPADP ANLDSEAKII QQAGQVWFPD SAFKTYQAIK DFNREGLPLM
VFANWRGFSG GMKDMYDQVL KFGAYIVDGL RECSQPVMVY IPPQAELRGG SWVVIDPTIN
PRHMEMYADR ESRGSVLEPE GTVEIKFRKK DLVKTMRRVD PVYIRLAERL GTPELSPTER
KELESKLKER EEFLIPIYHQ VAVQFADLHD TPGRMQEKGV INDILDWKTS RTFFYWRLRR
LLLEDLVKKK IHSANPELTD GQIQAMLRRW FVEVEGTVKA YVWDNNKDLV EWLEKQLTEE
DGVRSVIEEN IKYISRDYVL KQIRSLVQAN PEVAMDSIVH MTQHISPTQR AEVVRILSTM
DSPST


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EIAAB45820 Gamma-glutamyl carboxylase,Ggcx,Mouse,Mus musculus,Peptidyl-glutamate 4-carboxylase,Vitamin K gamma glutamyl carboxylase,Vitamin K-dependent gamma-carboxylase
bs-2745R-Biotin Rabbit Anti-Acetyl CoA Carboxylase Polyclonal Antibody, Biotin Conjugated 100ul
bs-2745R-Biotin Rabbit Anti-Acetyl CoA Carboxylase Polyclonal Antibody, Biotin Conjugated 100ug
bs-2745R-Biotin Rabbit Anti-Acetyl CoA Carboxylase Polyclonal Antibody, Biotin conjugated, Isotype: IgG 100ug Lyophilized
E02A0639 Rat Acetyl Coenzyme A Carboxylase Alpha ELISA 96T/kit


 

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