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Acetyl-CoA carboxylase 2 (EC 6.4.1.2) (ACC-beta) [Includes: Biotin carboxylase (EC 6.3.4.14)]

 ACACB_MOUSE             Reviewed;        2448 AA.
E9Q4Z2; Q6JIZ0;
29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
05-APR-2011, sequence version 1.
30-AUG-2017, entry version 59.
RecName: Full=Acetyl-CoA carboxylase 2 {ECO:0000250|UniProtKB:O00763};
EC=6.4.1.2 {ECO:0000250|UniProtKB:O00763};
AltName: Full=ACC-beta {ECO:0000250|UniProtKB:O00763};
Includes:
RecName: Full=Biotin carboxylase {ECO:0000250|UniProtKB:O00763};
EC=6.3.4.14;
Flags: Precursor;
Name=Acacb {ECO:0000312|MGI:MGI:2140940};
Synonyms=Acc2 {ECO:0000303|PubMed:10677481},
Accb {ECO:0000312|MGI:MGI:2140940};
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090 {ECO:0000312|Ensembl:ENSMUSP00000099642};
[1] {ECO:0000312|EMBL:AAS13686.1}
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=C57BL/6J {ECO:0000312|EMBL:AAS13686.1};
TISSUE=Heart {ECO:0000312|EMBL:AAS13686.1};
Mao J., Wakil S.J.;
"Alternative splicing in the mouse acetyl-CoA carboxylase 2 (ACC2)
gene.";
Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
[2] {ECO:0000312|Ensembl:ENSMUSP00000031583}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J {ECO:0000312|Ensembl:ENSMUSP00000031583};
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[3] {ECO:0000305}
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=10677481; DOI=10.1073/pnas.97.4.1444;
Abu-Elheiga L., Brinkley W.R., Zhong L., Chirala S.S.,
Woldegiorgis G., Wakil S.J.;
"The subcellular localization of acetyl-CoA carboxylase 2.";
Proc. Natl. Acad. Sci. U.S.A. 97:1444-1449(2000).
[4] {ECO:0000305}
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=11283375; DOI=10.1126/science.1056843;
Abu-Elheiga L., Matzuk M.M., Abo-Hashema K.A., Wakil S.J.;
"Continuous fatty acid oxidation and reduced fat storage in mice
lacking acetyl-CoA carboxylase 2.";
Science 291:2613-2616(2001).
[5] {ECO:0000305}
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=12920182; DOI=10.1073/pnas.1733877100;
Abu-Elheiga L., Oh W., Kordari P., Wakil S.J.;
"Acetyl-CoA carboxylase 2 mutant mice are protected against obesity
and diabetes induced by high-fat/high-carbohydrate diets.";
Proc. Natl. Acad. Sci. U.S.A. 100:10207-10212(2003).
[6] {ECO:0000305}
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=15677334; DOI=10.1073/pnas.0409451102;
Oh W., Abu-Elheiga L., Kordari P., Gu Z., Shaikenov T., Chirala S.S.,
Wakil S.J.;
"Glucose and fat metabolism in adipose tissue of acetyl-CoA
carboxylase 2 knockout mice.";
Proc. Natl. Acad. Sci. U.S.A. 102:1384-1389(2005).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[8] {ECO:0000305}
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=18487439; DOI=10.1152/ajpheart.91489.2007;
Essop M.F., Camp H.S., Choi C.S., Sharma S., Fryer R.M.,
Reinhart G.A., Guthrie P.H., Bentebibel A., Gu Z., Shulman G.I.,
Taegtmeyer H., Wakil S.J., Abu-Elheiga L.;
"Reduced heart size and increased myocardial fuel substrate oxidation
in ACC2 mutant mice.";
Am. J. Physiol. 295:H256-H265(2008).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47; THR-197; SER-459;
SER-1330; SER-1332 AND SER-1350, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, and Pancreas;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[10] {ECO:0000305}
DISRUPTION PHENOTYPE.
PubMed=20368432; DOI=10.1073/pnas.0913492107;
Olson D.P., Pulinilkunnil T., Cline G.W., Shulman G.I., Lowell B.B.;
"Gene knockout of Acc2 has little effect on body weight, fat mass, or
food intake.";
Proc. Natl. Acad. Sci. U.S.A. 107:7598-7603(2010).
[11] {ECO:0000305}
DISRUPTION PHENOTYPE.
PubMed=22730442; DOI=10.1161/CIRCRESAHA.112.268128;
Kolwicz S.C. Jr., Olson D.P., Marney L.C., Garcia-Menendez L.,
Synovec R.E., Tian R.;
"Cardiac-specific deletion of acetyl CoA carboxylase 2 prevents
metabolic remodeling during pressure-overload hypertrophy.";
Circ. Res. 111:728-738(2012).
[12]
INDUCTION BY ENDOCANNABINOID ANANDAMIDE.
PubMed=21987372; DOI=10.1002/hep.24733;
Jourdan T., Demizieux L., Gresti J., Djaouti L., Gaba L., Verges B.,
Degrace P.;
"Antagonism of peripheral hepatic cannabinoid receptor-1 improves
liver lipid metabolism in mice: evidence from cultured explants.";
Hepatology 55:790-799(2012).
[13] {ECO:0000305}
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=22362781; DOI=10.1074/jbc.M111.309559;
Abu-Elheiga L., Wu H., Gu Z., Bressler R., Wakil S.J.;
"Acetyl-CoA carboxylase 2-/- mutant mice are protected against fatty
liver under high-fat, high-carbohydrate dietary and de novo lipogenic
conditions.";
J. Biol. Chem. 287:12578-12588(2012).
[14] {ECO:0000305}
PHOSPHORYLATION AT SER-212, AND MUTAGENESIS OF SER-212.
PubMed=24913514; DOI=10.1007/s00125-014-3273-1;
O'Neill H.M., Lally J.S., Galic S., Thomas M., Azizi P.D.,
Fullerton M.D., Smith B.K., Pulinilkunnil T., Chen Z., Samaan M.C.,
Jorgensen S.B., Dyck J.R., Holloway G.P., Hawke T.J.,
van Denderen B.J., Kemp B.E., Steinberg G.R.;
"AMPK phosphorylation of ACC2 is required for skeletal muscle fatty
acid oxidation and insulin sensitivity in mice.";
Diabetologia 57:1693-1702(2014).
-!- FUNCTION: Catalyzes the ATP-dependent carboxylation of acetyl-CoA
to malonyl-CoA (By similarity). Carries out three functions:
biotin carboxyl carrier protein, biotin carboxylase and
carboxyltransferase (By similarity). Involved in inhibition of
fatty acid and glucose oxidation and enhancement of fat storage
(PubMed:11283375, PubMed:12920182, PubMed:15677334,
PubMed:18487439, PubMed:22362781). May play a role in regulation
of mitochondrial fatty acid oxidation through malonyl-CoA-
dependent inhibition of carnitine palmitoyltransferase 1
(PubMed:10677481). {ECO:0000250|UniProtKB:O00763,
ECO:0000269|PubMed:11283375, ECO:0000269|PubMed:12920182,
ECO:0000269|PubMed:15677334, ECO:0000269|PubMed:18487439,
ECO:0000269|PubMed:22362781, ECO:0000303|PubMed:10677481}.
-!- CATALYTIC ACTIVITY: ATP + acetyl-CoA + HCO(3)(-) = ADP + phosphate
+ malonyl-CoA. {ECO:0000250|UniProtKB:O00763}.
-!- CATALYTIC ACTIVITY: ATP + biotin-[carboxyl-carrier-protein] +
HCO(3)(-) = ADP + phosphate + carboxy-biotin-[carboxyl-carrier-
protein]. {ECO:0000250|UniProtKB:O00763}.
-!- COFACTOR:
Name=biotin; Xref=ChEBI:CHEBI:57586;
Evidence={ECO:0000250|UniProtKB:O00763};
-!- COFACTOR:
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000255|PROSITE-ProRule:PRU00409};
Note=Binds 2 manganese ions per subunit. {ECO:0000255|PROSITE-
ProRule:PRU00409};
-!- ENZYME REGULATION: Activity is increased by oligomerization.
Activated by citrate. Citrate and MID1IP1 promote oligomerization.
Inhibited by malonyl-CoA. {ECO:0000250|UniProtKB:O00763}.
-!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA
from acetyl-CoA: step 1/1.
-!- SUBUNIT: Monomer, homodimer, and homotetramer. Can form
filamentous polymers. Interacts with MID1IP1; interaction with
MID1IP1 promotes oligomerization and increases its activity.
{ECO:0000250|UniProtKB:O00763}.
-!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:10677481}.
Nucleus {ECO:0000250|UniProtKB:O00763}. Endomembrane system
{ECO:0000250|UniProtKB:O00763}. Note=May associate with membranes.
{ECO:0000250|UniProtKB:O00763}.
-!- INDUCTION: Up-regulated by endocannabinoid anandamide/AEA.
{ECO:0000269|PubMed:21987372}.
-!- PTM: Phosphorylated by AMPK, leading to inactivation of the
enzyme. Required for the maintenance of skeletal muscle lipid and
glucose homeostasis. {ECO:0000269|PubMed:24913514}.
-!- DISRUPTION PHENOTYPE: Normal morphology, fertility, growth rate
and lifespan but higher than normal food consumption and fatty
acid oxidation rate and decreased fat content in adipose tissue
and liver (PubMed:11283375). A high-fat/high-carbohydrate diet
results in maintenance of normal insulin and glucose levels with
less weight gain and less fat accumulation than wild-type mice
(PubMed:12920182). Elevated levels of Ucp2 in adipose tissue and
heart but not in skeletal muscle or liver, and elevated levels of
Ucp3 in skeletal muscle but not in heart or brown adipose tissue
(PubMed:12920182). Significant decrease in body weight, weight of
epidydimal fat pads and levels of hepatic triglycerides under a
range of dietary conditions including normal chow diet, fasting
and refeeding a fat-free high-carbohydrate diet, and a high-
fat/high-carbohydrate diet (PubMed:22362781). Up-regulation of
lipogenic enzymes under de novo lipogenic conditions but reduced
fat accumulation in liver (PubMed:22362781). Primary cultured
adipocytes show increased fatty acid and glucose oxidation rates
and increased lipolysis (PubMed:15677334). Reduced heart size,
reduced Mlycd and malonyl-CoA levels in mutant hearts, reduced
myocardial triglyceride levels, higher myocardial oleate and
glucose oxidation rates, reduced levels of Ppara and reduced
activation of Mtor (PubMed:18487439, PubMed:22730442). However, it
has also been reported that mutants show no differences in body
weight, food intake, body composition or glucose homeostasis as
compared with controls fed on chow or a high-fat diet
(PubMed:20368432). {ECO:0000269|PubMed:11283375,
ECO:0000269|PubMed:12920182, ECO:0000269|PubMed:15677334,
ECO:0000269|PubMed:18487439, ECO:0000269|PubMed:20368432,
ECO:0000269|PubMed:22362781, ECO:0000269|PubMed:22730442}.
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EMBL; AY451394; AAS13686.1; -; mRNA.
EMBL; AC122282; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS19561.1; -.
RefSeq; NP_598665.2; NM_133904.2.
RefSeq; XP_006530176.1; XM_006530113.3.
UniGene; Mm.81793; -.
ProteinModelPortal; E9Q4Z2; -.
SMR; E9Q4Z2; -.
BioGrid; 221514; 1.
MINT; MINT-1859452; -.
STRING; 10090.ENSMUSP00000031583; -.
BindingDB; E9Q4Z2; -.
ChEMBL; CHEMBL3108631; -.
iPTMnet; E9Q4Z2; -.
PhosphoSitePlus; E9Q4Z2; -.
SwissPalm; E9Q4Z2; -.
MaxQB; E9Q4Z2; -.
PaxDb; E9Q4Z2; -.
PeptideAtlas; E9Q4Z2; -.
PRIDE; E9Q4Z2; -.
Ensembl; ENSMUST00000031583; ENSMUSP00000031583; ENSMUSG00000042010.
Ensembl; ENSMUST00000102582; ENSMUSP00000099642; ENSMUSG00000042010.
GeneID; 100705; -.
KEGG; mmu:100705; -.
UCSC; uc008yzi.2; mouse.
CTD; 32; -.
MGI; MGI:2140940; Acacb.
eggNOG; KOG0368; Eukaryota.
eggNOG; COG0439; LUCA.
eggNOG; COG0511; LUCA.
eggNOG; COG4799; LUCA.
GeneTree; ENSGT00550000074703; -.
HOGENOM; HOG000214115; -.
HOVERGEN; HBG005371; -.
InParanoid; E9Q4Z2; -.
KO; K01946; -.
OMA; QAHYDKC; -.
OrthoDB; EOG091G02ND; -.
TreeFam; TF300061; -.
BRENDA; 6.4.1.2; 3474.
Reactome; R-MMU-163765; ChREBP activates metabolic gene expression.
Reactome; R-MMU-196780; Biotin transport and metabolism.
Reactome; R-MMU-200425; Import of palmitoyl-CoA into the mitochondrial matrix.
UniPathway; UPA00655; UER00711.
ChiTaRS; Acacb; mouse.
PRO; PR:E9Q4Z2; -.
Proteomes; UP000000589; Chromosome 5.
Bgee; ENSMUSG00000042010; -.
ExpressionAtlas; E9Q4Z2; baseline and differential.
Genevisible; E9Q4Z2; MM.
GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:0003989; F:acetyl-CoA carboxylase activity; IDA:MGI.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0009374; F:biotin binding; IEA:Ensembl.
GO; GO:0004075; F:biotin carboxylase activity; IEA:UniProtKB-EC.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0006084; P:acetyl-CoA metabolic process; ISO:MGI.
GO; GO:0097009; P:energy homeostasis; IMP:UniProtKB.
GO; GO:0006633; P:fatty acid biosynthetic process; IMP:MGI.
GO; GO:2001295; P:malonyl-CoA biosynthetic process; IMP:UniProtKB.
GO; GO:0043086; P:negative regulation of catalytic activity; IDA:UniProtKB.
GO; GO:0031999; P:negative regulation of fatty acid beta-oxidation; IMP:UniProtKB.
GO; GO:0046322; P:negative regulation of fatty acid oxidation; IMP:UniProtKB.
GO; GO:0010629; P:negative regulation of gene expression; IMP:UniProtKB.
GO; GO:0050995; P:negative regulation of lipid catabolic process; IMP:UniProtKB.
GO; GO:0060421; P:positive regulation of heart growth; IMP:UniProtKB.
GO; GO:0010884; P:positive regulation of lipid storage; IMP:UniProtKB.
GO; GO:0051289; P:protein homotetramerization; ISO:MGI.
GO; GO:0010906; P:regulation of glucose metabolic process; IMP:UniProtKB.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:0031667; P:response to nutrient levels; IMP:UniProtKB.
GO; GO:0014070; P:response to organic cyclic compound; IEA:Ensembl.
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; 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.
InterPro; IPR011763; COA_CT_C.
InterPro; IPR011762; COA_CT_N.
InterPro; IPR016185; PreATP-grasp_dom.
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; 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;
Allosteric enzyme; ATP-binding; Biotin; Complete proteome;
Fatty acid biosynthesis; Fatty acid metabolism; Ligase;
Lipid biosynthesis; Lipid metabolism; Manganese; Membrane;
Metal-binding; Mitochondrion; Multifunctional enzyme;
Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
Transit peptide.
TRANSIT 1 ? Mitochondrion.
{ECO:0000303|PubMed:10677481}.
CHAIN ? 2448 Acetyl-CoA carboxylase 2.
{ECO:0000303|PubMed:10677481}.
/FTId=PRO_0000430774.
DOMAIN 249 751 Biotin carboxylation. {ECO:0000255}.
DOMAIN 408 599 ATP-grasp. {ECO:0000255|PROSITE-
ProRule:PRU00409}.
DOMAIN 878 952 Biotinyl-binding. {ECO:0000255|PROSITE-
ProRule:PRU01066}.
DOMAIN 1685 2015 CoA carboxyltransferase N-terminal.
{ECO:0000255|PROSITE-ProRule:PRU01136}.
DOMAIN 2019 2335 CoA carboxyltransferase C-terminal.
{ECO:0000255|PROSITE-ProRule:PRU01137}.
NP_BIND 434 491 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00409}.
REGION 1685 2335 Carboxyltransferase.
{ECO:0000255|PROSITE-ProRule:PRU01138}.
ACT_SITE 574 574 {ECO:0000250|UniProtKB:P24182}.
METAL 557 557 Manganese 1. {ECO:0000255|PROSITE-
ProRule:PRU00409}.
METAL 570 570 Manganese 1. {ECO:0000255|PROSITE-
ProRule:PRU00409}.
METAL 570 570 Manganese 2. {ECO:0000255|PROSITE-
ProRule:PRU00409}.
METAL 572 572 Manganese 2. {ECO:0000255|PROSITE-
ProRule:PRU00409}.
BINDING 1924 1924 Coenzyme A.
{ECO:0000250|UniProtKB:Q00955}.
BINDING 2228 2228 Coenzyme A.
{ECO:0000250|UniProtKB:Q00955}.
BINDING 2230 2230 Coenzyme A.
{ECO:0000250|UniProtKB:Q00955}.
MOD_RES 35 35 Phosphoserine.
{ECO:0000250|UniProtKB:O00763}.
MOD_RES 47 47 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 81 81 Phosphoserine.
{ECO:0000250|UniProtKB:O00763}.
MOD_RES 85 85 Phosphoserine.
{ECO:0000250|UniProtKB:O00763}.
MOD_RES 190 190 Phosphoserine.
{ECO:0000250|UniProtKB:O00763}.
MOD_RES 197 197 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 212 212 Phosphoserine; by AMPK.
{ECO:0000269|PubMed:24913514}.
MOD_RES 459 459 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 919 919 N6-biotinyllysine.
{ECO:0000250|UniProtKB:P11497,
ECO:0000255|PROSITE-ProRule:PRU01066}.
MOD_RES 1330 1330 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1332 1332 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1350 1350 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MUTAGEN 212 212 S->A: No phosphorylation by AMPK, reduced
fatty acid oxidation in skeletal muscle,
increased lipid deposition in skeletal
muscle, and development of insulin
resistance.
{ECO:0000269|PubMed:24913514}.
CONFLICT 124 124 S -> P (in Ref. 1; AAS13686).
{ECO:0000305}.
CONFLICT 534 534 F -> S (in Ref. 1; AAS13686).
{ECO:0000305}.
CONFLICT 562 562 Q -> R (in Ref. 1; AAS13686).
{ECO:0000305}.
CONFLICT 1315 1315 F -> S (in Ref. 1; AAS13686).
{ECO:0000305}.
CONFLICT 1402 1402 S -> N (in Ref. 1; AAS13686).
{ECO:0000305}.
CONFLICT 2341 2341 N -> S (in Ref. 1; AAS13686).
{ECO:0000305}.
SEQUENCE 2448 AA; 275750 MW; 6CD686C7AF012A5E CRC64;
MVLLLFLTCL VFSCLTFSWL KIWGKMTDSK PLTNSKVEAN LLSSEESLSA SELSGEQLQE
HGDHSCLSYR GPRDASQQRN SLPSSCQRPP RNPLSSNDTW PSPELQTNWT AAPGPEVPDA
NGLSFPARPP SQRTVSPSRE DRKQAHIKRQ LMTSFILGSL DDNSSDEDPS AGSFQNSSRK
SSRASLGTLS QEAALNTSDP ESHAPTMRPS MSGLHLVKRG REHKKLDLHR DFTVASPAEF
VTRFGGNRVI EKVLIANNGI AAVKCMRSIR RWAYEMFRNE RAIRFVVMVT PEDLKANAEY
IKMADQYVPV PGGPNNNNYA NVELIIDIAK RIPVQAVWAG WGHASENPKL PELLCKHEIA
FLGPPSEAMW ALGDKIASTI VAQTLQIPTL PWSGSGLTVE WTEDSRHQGK CISVPEDVYE
QGCVKDVDEG LQAAEKIGFP LMIKASEGGG GKGIRKAESA EDFPMLFRQV QSEIPGSPIF
LMKLAQNARH LEVQVLADQY GNAVSLFGRD CSIQRRHQKI IEEAPATIAA PAVFEFMEQC
AVLLAKMVGY VSAGTVEYLY SQDGSFHFLE LNPRLQVEHP CTEMIADVNL PAAQLQIAMG
VPLHRLKDIR LLYGESPWGV TPIPFETPLS PPIARGHVIA ARITSENPDE GFKPSSGTVQ
ELNFRSNKNV WGYFSVAAAG GLHEFADSQF GHCFSWGENR EEAISNMVVA LKELSIRGDF
RTTVEYLVNL LETESFQNND IDTGWLDHLI AQRVQAEKPD IMLGVVCGAL NVADAMFRTC
MTEFLHSLER GQVLPADSLL NIVDVELIYG GIKYALKVAR QSLTMFVLIM NGCHIEIDAH
RLNDGGLLLS YNGSSYTTYM KEEVDSYRIT IGNKTCVFEK ENDPTVLRSP SAGKLMQYTV
EDGDHVEAGS SYAEMEVMKM IMTLNVQESG RVKYIKRPGV ILEAGCVVAR LELDDPSKVH
AAQPFTGELP AQQTLPILGE KLHQVFHGVL ENLTNVMSGY CLPEPFFSMK LKDWVQKLMM
TLRHPSLPLL ELQEIMTSVA GRIPAPVEKA VRRVMAQYAS NITSVLCQFP SQQIATILDC
HAATLQRKAD REVFFMNTQS IVQLVQRYRS GTRGYMKAVV LDLLRKYLNV EHHFQQAHYD
KCVINLREQF KPDMTQVLDC IFSHSQVAKK NQLVTMLIDE LCGPDPTLSD ELTSILCELT
QLSRSEHCKV ALRARQVLIA SHLPSYELRH NQVESIFLSA IDMYGHQFCP ENLKKLILSE
TTIFDVLPTF FYHENKVVCM ASLEVYVRRG YIAYELNSLQ HRELPDGTCV VEFQFMLPSS
HPNRMAVPIS VSNPDLLRHS TELFMDSGFS PLCQRMGAMV AFRRFEEFTR NFDEVISCFA
NVQTDTLLFS KACTSLYSEE DSKSLREEPI HILNVAIQCA DHMEDEALVP VFRAFVQSKK
HILVDYGLRR ITFLVAQERE FPKFFTFRAR DEFAEDRIYR HLEPALAFQL ELSRMRNFDL
TAVPCANHKM HLYLGAAKVK EGLEVTDHRF FIRAIIRHSD LITKEASFEY LQNEGERLLL
EAMDELEVAF NNTSVRTDCN HIFLNFVPTV IMDPLKIEES VRDMVMRYGS RLWKLRVLQA
EVKINIRQTT SDSAIPIRLF ITNESGYYLD ISLYREVTDS RSGNIMFHSF GNKQGSLHGM
LINTPYVTKD LLQAKRFQAQ SLGTTYVYDF PEMFRQALFK LWGSPEKYPK DILTYTELVL
DSQGQLVEMN RLPGCNEVGM VAFKMRFKTP EYPEGRDAVV IGNDITFQIG SFGIGEDFLY
LRASEMARTE GIPQIYLAAN SGARMGLAEE IKQIFQVAWV DPEDPHKGFR YLYLTPQDYT
QISSQNSVHC KHIEDEGESR YVIVDVIGKD ANLGVENLRG SGMIAGEASL AYEKTVTISM
VTCRALGIGA YLVRLGQRVI QVENSHIILT GAGALNKVLG REVYTSNNQL GGVQIMHTNG
VSHVTVPDDF EGVCTILEWL SFIPKDNRSP VPITTPSDPI DREIEFTPTK APYDPRWMLA
GRPHPTLKGT WQSGFFDHGS FKEIMAPWAQ TVVTGRARLG GIPVGVIAVE TRTVEVAVPA
DPANLDSEAK IIQQAGQVWF PDSAYKTAQV IRDFNKERLP LMIFANWRGF SGGMKDMYEQ
MLKFGAYIVD GLRLYEQPIL IYIPPCAELR GGSWVVLDST INPLCIEMYA DKESRGGVLE
PEGTVEIKFR KKDLVKTIRR IDPVCKKLVG QLGKAQLPDK DRKELEGQLK AREELLLPIY
HQVAVQFADL HDTPGHMLEK GIISDVLEWK TARTFFYWRL RRLLLEAQVK QEILRASPEL
NHEHTQSMLR RWFVETEGAV KAYLWDSNQV VVQWLEQHWS AKDGLRSTIR ENINYLKRDS
VLKTIQSLVQ EHPEVIMDCV AYLSQHLTPA ERIQVAQLLS TTESPASS


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