ID   CPT2_MOUSE              Reviewed;         658 AA.
AC   P52825; Q3TFS0;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   27-MAR-2024, entry version 164.
DE   RecName: Full=Carnitine O-palmitoyltransferase 2, mitochondrial {ECO:0000305};
DE            EC=2.3.1.21 {ECO:0000250|UniProtKB:P23786};
DE   AltName: Full=Carnitine palmitoyltransferase II;
DE            Short=CPT II;
DE   Flags: Precursor;
GN   Name=Cpt2 {ECO:0000312|MGI:MGI:109176}; Synonyms=Cpt-2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC   STRAIN=129/Sv;
RX   PubMed=8307575; DOI=10.1016/s0888-7543(05)80368-4;
RA   Gelb B.D.;
RT   "Genomic structure of and a cardiac promoter for the mouse carnitine
RT   palmitoyltransferase II gene.";
RL   Genomics 18:651-655(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Stomach;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [7]
RP   SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-69; LYS-85; LYS-239; LYS-418;
RP   LYS-424; LYS-439; LYS-510 AND LYS-544, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic fibroblast, and Liver;
RX   PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA   Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA   Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT   "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT   pathways.";
RL   Mol. Cell 50:919-930(2013).
RN   [8]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-79; LYS-239; LYS-305; LYS-418;
RP   LYS-510 AND LYS-544, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA   Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA   Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT   "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT   identifies substrates of SIRT3 in metabolic pathways.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
CC   -!- FUNCTION: Involved in the intramitochondrial synthesis of
CC       acylcarnitines from accumulated acyl-CoA metabolites. Reconverts
CC       acylcarnitines back into the respective acyl-CoA esters that can then
CC       undergo beta-oxidation, an essential step for the mitochondrial uptake
CC       of long-chain fatty acids and their subsequent beta-oxidation in the
CC       mitochondrion. Active with medium (C8-C12) and long-chain (C14-C18)
CC       acyl-CoA esters. {ECO:0000250|UniProtKB:P23786}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-carnitine + hexadecanoyl-CoA = CoA + O-hexadecanoyl-(R)-
CC         carnitine; Xref=Rhea:RHEA:12661, ChEBI:CHEBI:16347,
CC         ChEBI:CHEBI:17490, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379; EC=2.3.1.21;
CC         Evidence={ECO:0000250|UniProtKB:P23786};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:12663;
CC         Evidence={ECO:0000250|UniProtKB:P23786};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-carnitine + octanoyl-CoA = CoA + O-octanoyl-(R)-carnitine;
CC         Xref=Rhea:RHEA:17177, ChEBI:CHEBI:16347, ChEBI:CHEBI:18102,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57386;
CC         Evidence={ECO:0000250|UniProtKB:P23786};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-carnitine + decanoyl-CoA = CoA + O-decanoyl-(R)-carnitine;
CC         Xref=Rhea:RHEA:44828, ChEBI:CHEBI:16347, ChEBI:CHEBI:28717,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:61430;
CC         Evidence={ECO:0000250|UniProtKB:P23786};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-carnitine + dodecanoyl-CoA = CoA + O-dodecanoyl-R-
CC         carnitine; Xref=Rhea:RHEA:40279, ChEBI:CHEBI:16347,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57375, ChEBI:CHEBI:77086;
CC         Evidence={ECO:0000250|UniProtKB:P23786};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-carnitine + tetradecanoyl-CoA = CoA + O-tetradecanoyl-(R)-
CC         carnitine; Xref=Rhea:RHEA:44832, ChEBI:CHEBI:16347,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57385, ChEBI:CHEBI:84634;
CC         Evidence={ECO:0000250|UniProtKB:P23786};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-carnitine + octadecanoyl-CoA = CoA + O-octadecanoyl-(R)-
CC         carnitine; Xref=Rhea:RHEA:44840, ChEBI:CHEBI:16347,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57394, ChEBI:CHEBI:84644;
CC         Evidence={ECO:0000250|UniProtKB:P23786};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-carnitine + eicosanoyl-CoA = CoA + O-eicosanoyl-(R)-
CC         carnitine; Xref=Rhea:RHEA:44844, ChEBI:CHEBI:16347,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57380, ChEBI:CHEBI:84645;
CC         Evidence={ECO:0000250|UniProtKB:P23786};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(9Z)-tetradecenoyl-CoA + (R)-carnitine = CoA + O-(9Z)-
CC         tetradecenoyl-(R)-carnitine; Xref=Rhea:RHEA:44848, ChEBI:CHEBI:16347,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:65060, ChEBI:CHEBI:84647;
CC         Evidence={ECO:0000250|UniProtKB:P23786};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(5Z)-tetradecenoyl-CoA + (R)-carnitine = CoA + O-(5Z)-
CC         tetradecenoyl-(R)-carnitine; Xref=Rhea:RHEA:44852, ChEBI:CHEBI:16347,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:84649, ChEBI:CHEBI:84650;
CC         Evidence={ECO:0000250|UniProtKB:P23786};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(9Z)-octadecenoyl-CoA + (R)-carnitine = CoA + O-(9Z)-
CC         octadecenoyl-(R)-carnitine; Xref=Rhea:RHEA:44856, ChEBI:CHEBI:16347,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:84651;
CC         Evidence={ECO:0000250|UniProtKB:P23786};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-carnitine + 4,8-dimethylnonanoyl-CoA = CoA + O-4,8-
CC         dimethylnonanoyl-(R)-carnitine; Xref=Rhea:RHEA:44860,
CC         ChEBI:CHEBI:16347, ChEBI:CHEBI:57287, ChEBI:CHEBI:77061,
CC         ChEBI:CHEBI:84654; Evidence={ECO:0000250|UniProtKB:P23786};
CC   -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC       {ECO:0000250|UniProtKB:P23786}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250};
CC       Peripheral membrane protein {ECO:0000250}; Matrix side {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the carnitine/choline acetyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; U01170; AAA18922.1; -; Unassigned_DNA.
DR   EMBL; U01166; AAA18922.1; JOINED; Unassigned_DNA.
DR   EMBL; U01167; AAA18922.1; JOINED; Unassigned_DNA.
DR   EMBL; U01168; AAA18922.1; JOINED; Unassigned_DNA.
DR   EMBL; U01169; AAA18922.1; JOINED; Unassigned_DNA.
DR   EMBL; U01163; AAA18921.1; -; mRNA.
DR   EMBL; AK169038; BAE40828.1; -; mRNA.
DR   EMBL; AL611936; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH466527; EDL30761.1; -; Genomic_DNA.
DR   EMBL; BC138514; AAI38515.1; -; mRNA.
DR   EMBL; BC145859; AAI45860.1; -; mRNA.
DR   CCDS; CCDS18443.1; -.
DR   PIR; A49362; A49362.
DR   RefSeq; NP_034079.2; NM_009949.2.
DR   AlphaFoldDB; P52825; -.
DR   SMR; P52825; -.
DR   BioGRID; 198865; 25.
DR   IntAct; P52825; 1.
DR   STRING; 10090.ENSMUSP00000030345; -.
DR   GlyGen; P52825; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P52825; -.
DR   PhosphoSitePlus; P52825; -.
DR   SwissPalm; P52825; -.
DR   EPD; P52825; -.
DR   jPOST; P52825; -.
DR   MaxQB; P52825; -.
DR   PaxDb; 10090-ENSMUSP00000030345; -.
DR   PeptideAtlas; P52825; -.
DR   ProteomicsDB; 284004; -.
DR   Pumba; P52825; -.
DR   Antibodypedia; 33067; 559 antibodies from 36 providers.
DR   DNASU; 12896; -.
DR   Ensembl; ENSMUST00000030345.15; ENSMUSP00000030345.9; ENSMUSG00000028607.17.
DR   GeneID; 12896; -.
DR   KEGG; mmu:12896; -.
DR   UCSC; uc008uan.2; mouse.
DR   AGR; MGI:109176; -.
DR   CTD; 1376; -.
DR   MGI; MGI:109176; Cpt2.
DR   VEuPathDB; HostDB:ENSMUSG00000028607; -.
DR   eggNOG; KOG3719; Eukaryota.
DR   GeneTree; ENSGT01060000248556; -.
DR   HOGENOM; CLU_013513_4_2_1; -.
DR   InParanoid; P52825; -.
DR   OMA; HILVMRR; -.
DR   OrthoDB; 1429709at2759; -.
DR   PhylomeDB; P52825; -.
DR   TreeFam; TF315202; -.
DR   Reactome; R-MMU-200425; Carnitine metabolism.
DR   UniPathway; UPA00659; -.
DR   BioGRID-ORCS; 12896; 4 hits in 79 CRISPR screens.
DR   PRO; PR:P52825; -.
DR   Proteomes; UP000000589; Chromosome 4.
DR   RNAct; P52825; Protein.
DR   Bgee; ENSMUSG00000028607; Expressed in brown adipose tissue and 259 other cell types or tissues.
DR   ExpressionAtlas; P52825; baseline and differential.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR   GO; GO:0005730; C:nucleolus; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0016746; F:acyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0008458; F:carnitine O-octanoyltransferase activity; IEA:RHEA.
DR   GO; GO:0004095; F:carnitine O-palmitoyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0009437; P:carnitine metabolic process; ISS:UniProtKB.
DR   GO; GO:0006635; P:fatty acid beta-oxidation; ISS:UniProtKB.
DR   GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR   GO; GO:0001676; P:long-chain fatty acid metabolic process; ISS:UniProtKB.
DR   GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; IMP:YuBioLab.
DR   Gene3D; 1.20.1280.180; -; 1.
DR   Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR   Gene3D; 1.10.275.20; Choline/Carnitine o-acyltransferase; 1.
DR   Gene3D; 3.30.559.70; Choline/Carnitine o-acyltransferase, domain 2; 1.
DR   InterPro; IPR000542; Carn_acyl_trans.
DR   InterPro; IPR042572; Carn_acyl_trans_N.
DR   InterPro; IPR023213; CAT-like_dom_sf.
DR   InterPro; IPR039551; Cho/carn_acyl_trans.
DR   InterPro; IPR042231; Cho/carn_acyl_trans_2.
DR   PANTHER; PTHR22589; CARNITINE O-ACYLTRANSFERASE; 1.
DR   PANTHER; PTHR22589:SF51; CARNITINE O-PALMITOYLTRANSFERASE 2, MITOCHONDRIAL; 1.
DR   Pfam; PF00755; Carn_acyltransf; 1.
DR   SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
DR   PROSITE; PS00439; ACYLTRANSF_C_1; 1.
DR   PROSITE; PS00440; ACYLTRANSF_C_2; 1.
DR   Genevisible; P52825; MM.
PE   1: Evidence at protein level;
KW   Acetylation; Acyltransferase; Fatty acid metabolism; Lipid metabolism;
KW   Membrane; Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW   Transferase; Transit peptide; Transport.
FT   TRANSIT         1..25
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000250"
FT   CHAIN           26..658
FT                   /note="Carnitine O-palmitoyltransferase 2, mitochondrial"
FT                   /id="PRO_0000004426"
FT   TOPO_DOM        26..178
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000250"
FT   INTRAMEM        179..208
FT                   /note="Note=Mitochondrial inner membrane"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        209..658
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        372
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         452..464
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250"
FT   BINDING         486
FT                   /ligand="(R)-carnitine"
FT                   /ligand_id="ChEBI:CHEBI:16347"
FT                   /evidence="ECO:0000250"
FT   BINDING         488
FT                   /ligand="(R)-carnitine"
FT                   /ligand_id="ChEBI:CHEBI:16347"
FT                   /evidence="ECO:0000250"
FT   BINDING         499
FT                   /ligand="(R)-carnitine"
FT                   /ligand_id="ChEBI:CHEBI:16347"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         69
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         79
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23576753"
FT   MOD_RES         85
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         239
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23576753"
FT   MOD_RES         239
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         305
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23576753"
FT   MOD_RES         418
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23576753"
FT   MOD_RES         418
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         424
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         439
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         510
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23576753"
FT   MOD_RES         510
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         544
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23576753"
FT   MOD_RES         544
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   CONFLICT        503
FT                   /note="R -> C (in Ref. 1; AAA18921/AAA18922)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   658 AA;  73981 MW;  3A02DA887DF1D3A1 CRC64;
     MMPRLLLRDW PRCPSLVLGA PSRPLSAVSG PAEYLQHSIV PTMHYQDSLP RLPIPKLEDT
     MKRYLSAQKP LLNDSQFRKT EVLCKDFENG IGKELHAHLL AQDKQNKHTS YISGPWFDMY
     LTARDSVVLN FNPFMAFNPD PKSEYNDQLT RATNLTVSAV RFLKTLRAGL LEPEVFHLNP
     ARSDTDAFKR LIRFVPSSLS WYGAYLVNAY PLDMSQYFRL FNSTRIPKPS RDELFTDTKA
     RHLLVLRKGH FYVFDVLDQD GNIVNPSEIQ AHLKYILSDS SPVPEFPLAY LTSENRDVWA
     ELRQKLIHGG NEETLRKVDS AVFCLCLDDF PMKDLVHLSH TMLHGDGTNR WFDKSFNLIV
     AKDGTAAVHF EHAWGDGVAV LRFFNEVFRD STQTPAIAPQ SQPAATDSSV SVQKLSFKLS
     SALKAGVTAA KEKFDATMKT LTIDAIQFQR GGKEFLKKKK LSPDAVAQLA FQMAFLRQYG
     QTVATYESCS TAAFKHGRTE TIRPASIFTK RCSEAFVREP SKHSVGELQH MMAECSKYHG
     QLTKEAAMGQ GFDRHLFALR YLAAARGVTL PELYQDPAYQ RINHNILSTS TLSSPAVSLG
     GFAPVVPDGF GIAYAVHDDW IGCNVSSYSG RNAREFLHCV QKCLEDMFDA LEGKAIKT
//