ID   ACLY_RAT                Reviewed;        1100 AA.
AC   P16638; Q497C7; Q8VIQ1;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   27-MAR-2024, entry version 191.
DE   RecName: Full=ATP-citrate synthase;
DE            EC=2.3.3.8 {ECO:0000269|PubMed:9116495};
DE   AltName: Full=ATP-citrate (pro-S-)-lyase;
DE   AltName: Full=Citrate cleavage enzyme;
GN   Name=Acly;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PARTIAL PROTEIN SEQUENCE.
RC   TISSUE=Liver;
RX   PubMed=2295639; DOI=10.1016/s0021-9258(19)40033-1;
RA   Elshourbagy N.A., Near J.C., Kmetz P.J., Sathe G.M., Southan C.,
RA   Strickler J.E., Gross M., Young J.F., Wells T.N.C., Groot P.H.E.;
RT   "Rat ATP citrate-lyase. Molecular cloning and sequence analysis of a full-
RT   length cDNA and mRNA abundance as a function of diet, organ, and age.";
RL   J. Biol. Chem. 265:1430-1435(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Prostate;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 250-1100, ALTERNATIVE SPLICING, AND
RP   TISSUE SPECIFICITY.
RX   PubMed=8688462; DOI=10.1016/0167-4781(96)00067-x;
RA   Moon Y.-A., Kim K.-S., Park S.-W., Kim Y.-S.;
RT   "Cloning and identification of exon-intron organization of the rat ATP-
RT   citrate lyase gene.";
RL   Biochim. Biophys. Acta 1307:280-284(1996).
RN   [4]
RP   PROTEIN SEQUENCE OF 418-459, AND PHOSPHORYLATION AT THR-446 AND SER-450.
RX   PubMed=2176822; DOI=10.1021/bi00485a011;
RA   Ramakrishna S., D'Angelo G., Benjamin W.B.;
RT   "Sequence of sites on ATP-citrate lyase and phosphatase inhibitor 2
RT   phosphorylated by multifunctional protein kinase (a glycogen synthase
RT   kinase 3 like kinase).";
RL   Biochemistry 29:7617-7624(1990).
RN   [5]
RP   FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC   TISSUE=Liver;
RX   PubMed=9116495; DOI=10.1006/prep.1996.0668;
RA   Lord K.A., Wang X.M., Simmons S.J., Bruckner R.C., Loscig J., O'Connor B.,
RA   Bentley R., Smallwood A., Chadwick C.C., Stevis P.E., Ciccarelli R.B.;
RT   "Variant cDNA sequences of human ATP:citrate lyase: cloning, expression,
RT   and purification from baculovirus-infected insect cells.";
RL   Protein Expr. Purif. 9:133-141(1997).
RN   [6]
RP   PHOSPHORYLATION AT SER-454.
RX   PubMed=12107176; DOI=10.1074/jbc.m204681200;
RA   Berwick D.C., Hers I., Heesom K.J., Moule S.K., Tavare J.M.;
RT   "The identification of ATP-citrate lyase as a protein kinase B (Akt)
RT   substrate in primary adipocytes.";
RL   J. Biol. Chem. 277:33895-33900(2002).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=16396499; DOI=10.1021/pr0503073;
RA   Moser K., White F.M.;
RT   "Phosphoproteomic analysis of rat liver by high capacity IMAC and LC-
RT   MS/MS.";
RL   J. Proteome Res. 5:98-104(2006).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-454; SER-480 AND SER-662, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
RN   [9]
RP   PHOSPHORYLATION AT SER-454, AND PTM.
RX   PubMed=29779826; DOI=10.1016/j.cmet.2018.04.015;
RA   White P.J., McGarrah R.W., Grimsrud P.A., Tso S.C., Yang W.H.,
RA   Haldeman J.M., Grenier-Larouche T., An J., Lapworth A.L., Astapova I.,
RA   Hannou S.A., George T., Arlotto M., Olson L.B., Lai M., Zhang G.F.,
RA   Ilkayeva O., Herman M.A., Wynn R.M., Chuang D.T., Newgard C.B.;
RT   "The BCKDH Kinase and Phosphatase Integrate BCAA and Lipid Metabolism via
RT   Regulation of ATP-Citrate Lyase.";
RL   Cell Metab. 27:1281-1293.e7(2018).
CC   -!- FUNCTION: Catalyzes the cleavage of citrate into oxaloacetate and
CC       acetyl-CoA, the latter serving as common substrate for de novo
CC       cholesterol and fatty acid synthesis. {ECO:0000269|PubMed:9116495}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + ADP + oxaloacetate + phosphate = ATP + citrate +
CC         CoA; Xref=Rhea:RHEA:21160, ChEBI:CHEBI:16452, ChEBI:CHEBI:16947,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57288, ChEBI:CHEBI:456216; EC=2.3.3.8;
CC         Evidence={ECO:0000269|PubMed:9116495};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:21162;
CC         Evidence={ECO:0000305|PubMed:9116495};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P53396};
CC   -!- ACTIVITY REGULATION: Phosphorylation results in activation of its
CC       activity (By similarity). Glucose 6-phosphate, fructose 6-phosphate,
CC       fructose 2,6-bisphosphate, ribulose 5-phosphate, and fructose 1,6-
CC       bisphosphate also act as activators (By similarity).
CC       {ECO:0000250|UniProtKB:P53396}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=155 uM for citrate {ECO:0000269|PubMed:9116495};
CC         KM=103 uM for ATP {ECO:0000269|PubMed:9116495};
CC         KM=15 uM for CoA {ECO:0000269|PubMed:9116495};
CC         Vmax=1.9 umol/h/ug enzyme {ECO:0000269|PubMed:9116495};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P53396}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:P53396}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P16638-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P16638-2; Sequence=VSP_026273, VSP_026274;
CC   -!- TISSUE SPECIFICITY: Expressed in the brain, kidney, mammary gland, lung
CC       and liver. {ECO:0000269|PubMed:8688462}.
CC   -!- PTM: Phosphorylated by PKA and GSK3 in a sequential manner;
CC       phosphorylation results in activation of its activity (By similarity).
CC       Phosphorylation on Thr-446 and Ser-450 depends on the phosphorylation
CC       state of Ser-454 (PubMed:12107176, PubMed:2176822). Phosphorylation on
CC       Ser-454 is decreased by prior phosphorylation on the other 2 residues
CC       (PubMed:12107176, PubMed:2176822). Phosphorylated at Ser-454 by BCKDK
CC       and dephosphorylated by protein phosphatase PPM1K.
CC       {ECO:0000250|UniProtKB:P53396, ECO:0000269|PubMed:12107176,
CC       ECO:0000269|PubMed:2176822, ECO:0000269|PubMed:29779826}.
CC   -!- PTM: The N-terminus is blocked. {ECO:0000269|PubMed:2295639}.
CC   -!- PTM: ISGylated. {ECO:0000250|UniProtKB:P53396}.
CC   -!- PTM: Acetylated at Lys-539, Lys-545 and Lys-553 by KAT2B/PCAF (By
CC       similarity). Acetylation is promoted by glucose and stabilizes the
CC       protein, probably by preventing ubiquitination at the same sites (By
CC       similarity). Acetylation promotes de novo lipid synthesis (By
CC       similarity). Deacetylated by SIRT2 (By similarity).
CC       {ECO:0000250|UniProtKB:P53396}.
CC   -!- PTM: Ubiquitinated at Lys-539, Lys-545 and Lys-553 by the BCR(KLHL25)
CC       E3 ubiquitin ligase complex and UBR4, leading to its degradation (By
CC       similarity). Ubiquitination is probably inhibited by acetylation at
CC       same site (By similarity). BCR(KLHL25)-mediated degradation of ACLY
CC       promotes fatty acid oxidation and is required for differentiation of
CC       inducible regulatory T (iTreg) cells (By similarity).
CC       {ECO:0000250|UniProtKB:P53396, ECO:0000250|UniProtKB:Q91V92}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the succinate/malate
CC       CoA ligase beta subunit family. {ECO:0000305}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the succinate/malate
CC       CoA ligase alpha subunit family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; J05210; AAA74463.1; -; mRNA.
DR   EMBL; BC100618; AAI00619.1; -; mRNA.
DR   EMBL; AH011205; AAL34316.1; -; Genomic_DNA.
DR   PIR; A35007; A35007.
DR   RefSeq; NP_001104565.1; NM_001111095.1.
DR   RefSeq; NP_058683.2; NM_016987.2.
DR   AlphaFoldDB; P16638; -.
DR   SMR; P16638; -.
DR   BioGRID; 246351; 6.
DR   IntAct; P16638; 3.
DR   MINT; P16638; -.
DR   STRING; 10116.ENSRNOP00000023447; -.
DR   BindingDB; P16638; -.
DR   ChEMBL; CHEMBL2745; -.
DR   GlyGen; P16638; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P16638; -.
DR   PhosphoSitePlus; P16638; -.
DR   jPOST; P16638; -.
DR   PaxDb; 10116-ENSRNOP00000023447; -.
DR   PeptideAtlas; P16638; -.
DR   GeneID; 24159; -.
DR   KEGG; rno:24159; -.
DR   AGR; RGD:2018; -.
DR   CTD; 47; -.
DR   RGD; 2018; Acly.
DR   eggNOG; KOG1254; Eukaryota.
DR   InParanoid; P16638; -.
DR   OrthoDB; 536at2759; -.
DR   PhylomeDB; P16638; -.
DR   Reactome; R-RNO-6798695; Neutrophil degranulation.
DR   Reactome; R-RNO-75105; Fatty acyl-CoA biosynthesis.
DR   PRO; PR:P16638; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003878; F:ATP citrate synthase activity; IDA:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006085; P:acetyl-CoA biosynthetic process; ISO:RGD.
DR   GO; GO:0006084; P:acetyl-CoA metabolic process; IDA:RGD.
DR   GO; GO:0006101; P:citrate metabolic process; IDA:RGD.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IDA:RGD.
DR   GO; GO:0008610; P:lipid biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0006107; P:oxaloacetate metabolic process; ISO:RGD.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR   CDD; cd06100; CCL_ACL-C; 1.
DR   Gene3D; 3.30.470.110; -; 1.
DR   Gene3D; 1.10.580.10; Citrate Synthase, domain 1; 1.
DR   Gene3D; 1.10.230.10; Cytochrome P450-Terp, domain 2; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   Gene3D; 3.40.50.261; Succinyl-CoA synthetase domains; 2.
DR   InterPro; IPR014608; ATP-citrate_synthase.
DR   InterPro; IPR017440; Cit_synth/succinyl-CoA_lig_AS.
DR   InterPro; IPR032263; Citrate-bd.
DR   InterPro; IPR016142; Citrate_synth-like_lrg_a-sub.
DR   InterPro; IPR016143; Citrate_synth-like_sm_a-sub.
DR   InterPro; IPR002020; Citrate_synthase.
DR   InterPro; IPR036969; Citrate_synthase_sf.
DR   InterPro; IPR033847; Citrt_syn/SCS-alpha_CS.
DR   InterPro; IPR003781; CoA-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR017866; Succ-CoA_synthase_bsu_CS.
DR   InterPro; IPR005811; SUCC_ACL_C.
DR   InterPro; IPR016102; Succinyl-CoA_synth-like.
DR   PANTHER; PTHR23118; ATP-CITRATE SYNTHASE; 1.
DR   PANTHER; PTHR23118:SF42; ATP-CITRATE SYNTHASE; 1.
DR   Pfam; PF16114; Citrate_bind; 1.
DR   Pfam; PF00285; Citrate_synt; 1.
DR   Pfam; PF02629; CoA_binding; 1.
DR   Pfam; PF00549; Ligase_CoA; 1.
DR   PIRSF; PIRSF036511; ATP_citrt_syn; 1.
DR   SMART; SM00881; CoA_binding; 1.
DR   SUPFAM; SSF48256; Citrate synthase; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   SUPFAM; SSF52210; Succinyl-CoA synthetase domains; 1.
DR   PROSITE; PS01216; SUCCINYL_COA_LIG_1; 1.
DR   PROSITE; PS00399; SUCCINYL_COA_LIG_2; 1.
DR   PROSITE; PS01217; SUCCINYL_COA_LIG_3; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; ATP-binding; Cytoplasm;
KW   Direct protein sequencing; Isopeptide bond; Lipid biosynthesis;
KW   Lipid metabolism; Magnesium; Metal-binding; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome; Transferase; Ubl conjugation.
FT   CHAIN           1..1100
FT                   /note="ATP-citrate synthase"
FT                   /id="PRO_0000102783"
FT   DOMAIN          4..265
FT                   /note="ATP-grasp"
FT   REGION          442..485
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        442..457
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        759
FT                   /note="Tele-phosphohistidine intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:P53396"
FT   BINDING         58
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P53396"
FT   BINDING         66
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P53396"
FT   BINDING         67
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P53396"
FT   BINDING         109
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P53396"
FT   BINDING         111
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P53396"
FT   BINDING         118
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P53396"
FT   BINDING         216
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P53396"
FT   BINDING         257
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P53396"
FT   BINDING         260
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P53396"
FT   BINDING         262
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P53396"
FT   BINDING         309
FT                   /ligand="citrate"
FT                   /ligand_id="ChEBI:CHEBI:16947"
FT                   /evidence="ECO:0000250|UniProtKB:P53396"
FT   BINDING         346
FT                   /ligand="citrate"
FT                   /ligand_id="ChEBI:CHEBI:16947"
FT                   /evidence="ECO:0000250|UniProtKB:P53396"
FT   BINDING         348
FT                   /ligand="citrate"
FT                   /ligand_id="ChEBI:CHEBI:16947"
FT                   /evidence="ECO:0000250|UniProtKB:P53396"
FT   BINDING         364
FT                   /ligand="citrate"
FT                   /ligand_id="ChEBI:CHEBI:16947"
FT                   /evidence="ECO:0000250|UniProtKB:P53396"
FT   BINDING         379
FT                   /ligand="citrate"
FT                   /ligand_id="ChEBI:CHEBI:16947"
FT                   /evidence="ECO:0000250|UniProtKB:P53396"
FT   BINDING         778..788
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         131
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P53396"
FT   MOD_RES         263
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q91V92"
FT   MOD_RES         446
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000269|PubMed:2176822"
FT   MOD_RES         450
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:2176822"
FT   MOD_RES         454
FT                   /note="Phosphoserine; by PKA and PKB/AKT1 or PKB/AKT2 or
FT                   BCKDK"
FT                   /evidence="ECO:0000269|PubMed:12107176,
FT                   ECO:0000269|PubMed:29779826, ECO:0007744|PubMed:22673903"
FT   MOD_RES         458
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P53396"
FT   MOD_RES         480
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         539
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P53396"
FT   MOD_RES         545
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P53396"
FT   MOD_RES         553
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P53396"
FT   MOD_RES         638
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P53396"
FT   MOD_RES         662
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         681
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P53396"
FT   MOD_RES         838
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P53396"
FT   MOD_RES         947
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P53396"
FT   MOD_RES         967
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P53396"
FT   MOD_RES         977
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q91V92"
FT   MOD_RES         1076
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P53396"
FT   MOD_RES         1099
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P53396"
FT   CROSSLNK        539
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P53396"
FT   CROSSLNK        545
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P53396"
FT   CROSSLNK        553
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P53396"
FT   VAR_SEQ         419..422
FT                   /note="WAPA -> LGHRP (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_026273"
FT   VAR_SEQ         475..484
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_026274"
FT   CONFLICT        116
FT                   /note="A -> V (in Ref. 2; AAI00619)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        367
FT                   /note="S -> P (in Ref. 2; AAI00619)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1100 AA;  120636 MW;  2C6BE4BC1F53BDD2 CRC64;
     MSAKAISEQT GKELLYKYIC TTSAIQNRFK YARVTPDTDW AHLLQDHPWL LSQSLVVKPD
     QLIKRRGKLG LVGVNLSLDG VKSWLKPRLG HEATVGKAKG FLKNFLIEPF VPHSQAEEFY
     VCIYATREGD YVLFHHEGGV DVGDVDTKAQ KLLVGVDEKL NAEDIKRHLL VHAPEDKKEI
     LASFISGLFN FYEDLYFTYL EINPLVVTKD GVYILDLAAK VDATADYICK VKWGDIEFPP
     PFGREAYPEE AYIADLDAKS GASLKLTLLN PKGRIWTMVA GGGASVVYSD TICDLGGVNE
     LANYGEYSGA PSEQQTYDYA KTILSLMTRE KHPDGKILII GGSIANFTNV AATFKGIVRA
     IRDYQGSLKE HEVTIFVRRG GPNYQEGLRV MGEVGKTTGI PIHVFGTETH MTAIVGMAWA
     PAIPNQPPTA AHTANFLLNA SGSTSTPAPS RTASFSESRA DEVAPAKKAK PAMPQDSVPS
     PRSLQGKSAT LFSRHTKAIV WGMQTRAVQG MLDFDYVCSR DEPSVAAMVY PFTGDHKQKF
     YWGHKEILIP VFKNMADAMK KHPEVDVLIN FASLRSAYDS TMETMNYAQI RTIAIIAEGI
     PEALTRKLIK KADQKGVTII GPATVGGIKP GCFKIGNTGG MLDNILASKL YRPGSVAYVS
     RSGGMSNELN NIISRTTDGV YEGVAIGGDR YPGSTFMDHV LRYQDTPGVK MIVVLGEIGG
     TEEYKICRGI KEGRLTKPVV CWCIGTCATM FSSEVQFGHA GACANQASET AVAKNQALKE
     AGVFVPRSFD ELGEIIQSVY EDLVAKGAIV PAQEVPPPTV PMDYSWAREL GLIRKPASFM
     TSICDERGQE LIYAGMPITE VFKEEMGIGG VLGLLWFQRR LPKYSCQFIE MCLMVTADHG
     PAVSGAHNTI ICARAGKDLV SSLTSGLLTI GDRFGGALDA AAKMFSKAFD SGIIPMEFVN
     KMKKEGKLIM GIGHRVKSIN NPDMRVQILK DFVKQHFPAT PLLDYALEVE KITTSKKPNL
     ILNVDGFIGV AFVDMLRNCG SFTREEADEY VDIGALNGVF VLGRSMGFIG HYLDQKRLKQ
     GLYRHPWDDI SYVLPEHMSM
//