CPT2_HUMAN
ID CPT2_HUMAN Reviewed; 658 AA.
AC P23786; B2R6S0; Q5SW68; Q9BQ26;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 2.
DT 03-AUG-2022, entry version 213.
DE RecName: Full=Carnitine O-palmitoyltransferase 2, mitochondrial {ECO:0000305};
DE EC=2.3.1.21 {ECO:0000269|PubMed:20538056};
DE AltName: Full=Carnitine palmitoyltransferase II;
DE Short=CPT II;
DE Flags: Precursor;
GN Name=CPT2 {ECO:0000312|HGNC:HGNC:2330}; Synonyms=CPT1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Liver;
RX PubMed=1988962; DOI=10.1073/pnas.88.2.661;
RA Finocchiaro G., Taroni F., Rocchi M., Martin A.L., Colombo I.,
RA Tarelli G.T., Didonato S.;
RT "cDNA cloning, sequence analysis, and chromosomal localization of the gene
RT for human carnitine palmitoyltransferase.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:661-665(1991).
RN [2]
RP ERRATUM OF PUBMED:1988962, AND SEQUENCE REVISION TO 283 AND 375.
RX PubMed=1961767; DOI=10.1073/pnas.88.23.10981;
RA Finocchiaro G., Taroni F., Rocchi M., Martin A.L., Colombo I.,
RA Tarelli G.T., Didonato S.;
RL Proc. Natl. Acad. Sci. U.S.A. 88:10981-10981(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS CPT2D DEFICIENCY HIS-50 AND
RP ASN-553.
RX PubMed=7711730; DOI=10.1093/hmg/4.1.19;
RA Verderio E., Cavadini P., Montermini L., Wang H., Lamantea E.,
RA Finocchiaro G., Didonato S., Gellera C., Taroni F.;
RT "Carnitine palmitoyltransferase II deficiency: structure of the gene and
RT characterization of two novel disease-causing mutations.";
RL Hum. Mol. Genet. 4:19-29(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT CPT2D LEU-113, AND VARIANTS
RP ILE-368 AND VAL-647.
RC TISSUE=Skin, and Uterus;
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 [8]
RP PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Liver;
RX PubMed=2174799; DOI=10.1016/0014-5793(90)81354-q;
RA Finocchiaro G., Colombo I., Didonato S.;
RT "Purification, characterization and partial amino acid sequences of
RT carnitine palmitoyl-transferase from human liver.";
RL FEBS Lett. 274:163-166(1990).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=20538056; DOI=10.1016/j.bbadis.2010.06.002;
RA Violante S., Ijlst L., van Lenthe H., de Almeida I.T., Wanders R.J.,
RA Ventura F.V.;
RT "Carnitine palmitoyltransferase 2: New insights on the substrate
RT specificity and implications for acylcarnitine profiling.";
RL Biochim. Biophys. Acta 1802:728-732(2010).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [14]
RP VARIANT CPT2D LEU-227.
RA Taroni F., Gellera C., Cavadini P., Baratta S., Lamantea E., Dethlefs S.,
RA Didonato S., Reik R.A., Benke P.J.;
RT "Lethal carnitine palmitoyltransferase (CPT) II deficiency in newborns: a
RT molecular-genetic study.";
RL Am. J. Hum. Genet. 51:A245-A245(1992).
RN [15]
RP INVOLVEMENT IN CPT2DI, VARIANT CPT2DI CYS-631, AND VARIANTS ILE-368 AND
RP VAL-647.
RX PubMed=1528846; DOI=10.1073/pnas.89.18.8429;
RA Taroni F., Verderio E., Fiorucci S., Cavadini P., Finocchiaro G., Uziel G.,
RA Lamantea E., Gellera C., Didonato S.;
RT "Molecular characterization of inherited carnitine palmitoyltransferase II
RT deficiency.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:8429-8433(1992).
RN [16]
RP VARIANT CPT2D LEU-113.
RX PubMed=8358442; DOI=10.1038/ng0793-314;
RA Taroni F., Verderio E., Dworzak F., Willems P.J., Cavadini P., Didonato S.;
RT "Identification of a common mutation in the carnitine palmitoyltransferase
RT II gene in familial recurrent myoglobinuria patients.";
RL Nat. Genet. 4:314-320(1993).
RN [17]
RP INVOLVEMENT IN CPT2DI, AND VARIANT CPT2DI SER-628.
RX PubMed=8651281;
RA Bonnefont J.-P., Taroni F., Cavadini P., Cepanec C., Brivet M.,
RA Saudubray J.-M., Leroux J.-P., Demaugre F.;
RT "Molecular analysis of carnitine palmitoyltransferase II deficiency with
RT hepatocardiomuscular expression.";
RL Am. J. Hum. Genet. 58:971-978(1996).
RN [18]
RP VARIANTS CPT2D THR-214; LEU-448 AND PHE-479.
RA Wieser T., Deschauer M., Zierz S.;
RT "Carnitine palmityltransferase II deficiency: three novel mutations.";
RL Ann. Neurol. 42:414-415(1997).
RN [19]
RP VARIANTS CPT2D LYS-174 AND TYR-383, AND VARIANTS CYS-352; ILE-368 AND
RP VAL-647.
RX PubMed=9600456;
RX DOI=10.1002/(sici)1098-1004(1998)11:5<377::aid-humu5>3.0.co;2-e;
RA Wataya K., Akanuma J., Cavadini P., Aoki Y., Kure S., Invernizzi F.,
RA Yoshida I., Kira J., Taroni F., Matsubara Y., Narisawa K.;
RT "Two CPT2 mutations in three Japanese patients with carnitine
RT palmitoyltransferase II deficiency: functional analysis and association
RT with polymorphic haplotypes and two clinical phenotypes.";
RL Hum. Mutat. 11:377-386(1998).
RN [20]
RP VARIANTS CPT2D LEU-113; GLN-151; LEU-227; ARG-550 AND SER-604, AND VARIANTS
RP ILE-368 AND VAL-647.
RX PubMed=9758712; DOI=10.1006/mgme.1998.2711;
RA Yang B.-Z., Ding J.-H., Dewese T., Roe D., He G., Wilkinson J., Day D.W.,
RA Demaugre F., Rabier D., Brivet M., Roe C.;
RT "Identification of four novel mutations in patients with carnitine
RT palmitoyltransferase II (CPT II) deficiency.";
RL Mol. Genet. Metab. 64:229-236(1998).
RN [21]
RP VARIANTS CPT2D CYS-503 AND ASP-549.
RX PubMed=10090476;
RX DOI=10.1002/(sici)1098-1004(1999)13:3<210::aid-humu5>3.0.co;2-0;
RA Taggart R.T., Smail D., Apolito C., Vladutiu G.D.;
RT "Novel mutations associated with carnitine palmitoyltransferase II
RT deficiency.";
RL Hum. Mutat. 13:210-220(1999).
RN [22]
RP INVOLVEMENT IN CPT2DLN.
RX PubMed=11477613; DOI=10.1002/ajmg.1457;
RA Elpeleg O.N., Hammerman C., Saada A., Shaag A., Golzand E.,
RA Hochner-Celnikier D., Berger I., Nadjari M.;
RT "Antenatal presentation of carnitine palmitoyltransferase II deficiency.";
RL Am. J. Med. Genet. 102:183-187(2001).
RN [23]
RP VARIANTS CPT2D GLN-151; ASP-210; GLN-296 AND ARG-600, AND VARIANTS ILE-368
RP AND VAL-647.
RX PubMed=14605500; DOI=10.1023/a:1025947930752;
RA Olpin S.E., Afifi A., Clark S., Manning N.J., Bonham J.R., Dalton A.,
RA Leonard J.V., Land J.M., Andresen B.S., Morris A.A., Muntoni F.,
RA Turnbull D., Pourfarzam M., Rahman S., Pollitt R.J.;
RT "Mutation and biochemical analysis in carnitine palmitoyltransferase type
RT II (CPT II) deficiency.";
RL J. Inherit. Metab. Dis. 26:543-557(2003).
RN [24]
RP VARIANT CPT2D GLN-296.
RX PubMed=14615409; DOI=10.1097/01.lab.0000098428.51765.83;
RA Sigauke E., Rakheja D., Kitson K., Bennett M.J.;
RT "Carnitine palmitoyltransferase II deficiency: a clinical, biochemical, and
RT molecular review.";
RL Lab. Invest. 83:1543-1554(2003).
RN [25]
RP VARIANTS CPT2D HIS-50; LEU-113 AND GLY-213.
RX PubMed=15622536; DOI=10.1002/ana.20320;
RA Oerngreen M.C., Dunoe M., Ejstrup R., Christensen E., Schwartz M.,
RA Sacchetti M., Vissing J.;
RT "Fuel utilization in subjects with carnitine palmitoyltransferase 2 gene
RT mutations.";
RL Ann. Neurol. 57:60-66(2005).
RN [26]
RP ASSOCIATION OF VARIANTS CYS-352 AND ILE-368 WITH SUSCEPTIBILITY TO IIAE4.
RX PubMed=15811315; DOI=10.1016/j.febslet.2005.02.050;
RA Chen Y., Mizuguchi H., Yao D., Ide M., Kuroda Y., Shigematsu Y.,
RA Yamaguchi S., Yamaguchi M., Kinoshita M., Kido H.;
RT "Thermolabile phenotype of carnitine palmitoyltransferase II variations as
RT a predisposing factor for influenza-associated encephalopathy.";
RL FEBS Lett. 579:2040-2044(2005).
RN [27]
RP VARIANT VAL-647, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17488105; DOI=10.1021/pr0700908;
RA Bunger M.K., Cargile B.J., Sevinsky J.R., Deyanova E., Yates N.A.,
RA Hendrickson R.C., Stephenson J.L. Jr.;
RT "Detection and validation of non-synonymous coding SNPs from orthogonal
RT analysis of shotgun proteomics data.";
RL J. Proteome Res. 6:2331-2340(2007).
RN [28]
RP VARIANTS CYS-352; ILE-368; LEU-504; LEU-605 AND VAL-647, AND
RP CHARACTERIZATION OF VARIANTS CYS-352 AND ILE-368.
RX PubMed=18306170; DOI=10.1002/humu.20717;
RA Yao D., Mizuguchi H., Yamaguchi M., Yamada H., Chida J., Shikata K.,
RA Kido H.;
RT "Thermal instability of compound variants of carnitine palmitoyltransferase
RT II and impaired mitochondrial fuel utilization in influenza-associated
RT encephalopathy.";
RL Hum. Mutat. 29:718-727(2008).
RN [29]
RP ASSOCIATION OF VARIANTS CYS-352 AND ILE-368 WITH SUSCEPTIBILITY TO IIAE4.
RX PubMed=21697855; DOI=10.1038/jhg.2011.63;
RA Mak C.M., Lam C.W., Fong N.C., Siu W.K., Lee H.C., Siu T.S., Lai C.K.,
RA Law C.Y., Tong S.F., Poon W.T., Lam D.S., Ng H.L., Yuen Y.P., Tam S.,
RA Que T.L., Kwong N.S., Chan A.Y.;
RT "Fatal viral infection-associated encephalopathy in two Chinese boys: a
RT genetically determined risk factor of thermolabile carnitine
RT palmitoyltransferase II variants.";
RL J. Hum. Genet. 56:617-621(2011).
RN [30]
RP INVOLVEMENT IN CPT2D, FUNCTION, CATALYTIC ACTIVITY, AND VARIANT CPT2D
RP CYS-631.
RX PubMed=24780397; DOI=10.1016/j.bbrc.2014.04.084;
RA Yasuno T., Osafune K., Sakurai H., Asaka I., Tanaka A., Yamaguchi S.,
RA Yamada K., Hitomi H., Arai S., Kurose Y., Higaki Y., Sudo M., Ando S.,
RA Nakashima H., Saito T., Kaneoka H.;
RT "Functional analysis of iPSC-derived myocytes from a patient with carnitine
RT palmitoyltransferase II deficiency.";
RL Biochem. Biophys. Res. Commun. 448:175-181(2014).
CC -!- FUNCTION: Involved in the intramitochondrial synthesis of
CC acylcarnitines from accumulated acyl-CoA metabolites (PubMed:20538056,
CC PubMed:24780397). Reconverts acylcarnitines back into the respective
CC acyl-CoA esters that can then undergo beta-oxidation, an essential step
CC for the mitochondrial uptake of long-chain fatty acids and their
CC subsequent beta-oxidation in the mitochondrion. Active with medium (C8-
CC C12) and long-chain (C14-C18) acyl-CoA esters (PubMed:20538056).
CC {ECO:0000269|PubMed:20538056, ECO:0000269|PubMed:24780397}.
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:0000269|PubMed:20538056, ECO:0000269|PubMed:24780397};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:12663;
CC Evidence={ECO:0000305|PubMed:24780397};
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:0000269|PubMed:20538056};
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:0000269|PubMed:20538056};
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:0000269|PubMed:20538056};
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:0000269|PubMed:20538056};
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:0000269|PubMed:20538056};
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:0000269|PubMed:20538056};
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:0000269|PubMed:20538056};
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:0000269|PubMed:20538056};
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:0000269|PubMed:20538056};
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:0000269|PubMed:20538056};
CC -!- ACTIVITY REGULATION: Inhibited by trans-2-hexadecanoyl-CoA.
CC {ECO:0000269|PubMed:20538056}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=7.1 uM for hexadecanoyl-CoA {ECO:0000269|PubMed:20538056};
CC KM=8.1 uM for trans-2-hexadecanoyl-CoA {ECO:0000269|PubMed:20538056};
CC Vmax=1156 pmol/min/mg enzyme toward {ECO:0000269|PubMed:20538056};
CC Vmax=77 pmol/min/mg enzyme toward trans-2-hexadecanoyl-CoA
CC {ECO:0000269|PubMed:20538056};
CC -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC {ECO:0000269|PubMed:20538056}.
CC -!- INTERACTION:
CC P23786; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-6269566, EBI-3867333;
CC P23786; P32242: OTX1; NbExp=3; IntAct=EBI-6269566, EBI-740446;
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane
CC protein; Matrix side.
CC -!- DISEASE: Carnitine palmitoyltransferase 2 deficiency, myopathic,
CC stress-induced (CPT2D) [MIM:255110]: An autosomal recessive disorder of
CC mitochondrial long-chain fatty acid oxidation, characterized by
CC recurrent myoglobinuria, episodes of muscle pain, stiffness, and
CC rhabdomyolysis. These symptoms are exacerbated by prolonged exercise,
CC fasting, cold, or viral infection. CPT2DM affects most frequently
CC children or young adults, and severity of attacks is highly variable.
CC Myoglobinuria can cause kidney failure and death.
CC {ECO:0000269|PubMed:10090476, ECO:0000269|PubMed:11477613,
CC ECO:0000269|PubMed:14605500, ECO:0000269|PubMed:14615409,
CC ECO:0000269|PubMed:1528846, ECO:0000269|PubMed:15489334,
CC ECO:0000269|PubMed:15622536, ECO:0000269|PubMed:24780397,
CC ECO:0000269|PubMed:7711730, ECO:0000269|PubMed:8358442,
CC ECO:0000269|PubMed:8651281, ECO:0000269|PubMed:9600456,
CC ECO:0000269|PubMed:9758712, ECO:0000269|Ref.14, ECO:0000269|Ref.18}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- DISEASE: Carnitine palmitoyltransferase 2 deficiency, infantile
CC (CPT2DI) [MIM:600649]: An autosomal recessive disorder of mitochondrial
CC long-chain fatty acid oxidation, characterized by hepatic or hepato-
CC cardio-muscular manifestations with onset in infancy. Clinical features
CC include hypoketotic hypoglycemia, lethargy, seizures, hepatomegaly,
CC liver dysfunction, cardiomegaly and dilated cardiomyopathy.
CC {ECO:0000269|PubMed:1528846, ECO:0000269|PubMed:8651281}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Carnitine palmitoyltransferase 2 deficiency, lethal neonatal
CC (CPT2DLN) [MIM:608836]: An autosomal recessive disorder of
CC mitochondrial long-chain fatty acid oxidation with fatal outcome,
CC presenting shortly after birth. It is characterized by respiratory
CC distress, seizures, altered mental status, hepatomegaly, cardiomegaly,
CC cardiac arrhythmia, and, in many cases, dysmorphic features, renal
CC dysgenesis, and migration defects. recessive.
CC {ECO:0000269|PubMed:11477613}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Encephalopathy, acute, infection-induced, 4 (IIAE4)
CC [MIM:614212]: A severe neurologic complication of an infection. It
CC manifests within days in otherwise healthy children after common viral
CC infections, without evidence of viral infection of the brain or
CC inflammatory cell infiltration. In affected children, high-grade fever
CC is accompanied within 12 to 48 hours by febrile convulsions, often
CC leading to coma, multiple-organ failure, brain edema, and high
CC morbidity and mortality. The infections are usually viral, particularly
CC influenza, although other viruses and even mycoplasma have been found
CC to cause the disorder. {ECO:0000269|PubMed:15811315,
CC ECO:0000269|PubMed:21697855}. Note=Disease susceptibility is associated
CC with variants affecting the gene represented in this entry. CPT2
CC polymorphic variants do not cause classical carnitine
CC palmitoyltransferase 2 deficiency, and patients harboring any of them
CC are asymptomatic most of the time. However, they are prone to viral
CC infection (high fever)-related encephalopathy (PubMed:21697855).
CC {ECO:0000269|PubMed:21697855}.
CC -!- SIMILARITY: Belongs to the carnitine/choline acetyltransferase family.
CC {ECO:0000305}.
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DR EMBL; U09648; AAB60383.1; -; mRNA.
DR EMBL; M58581; AAB59462.1; -; mRNA.
DR EMBL; U09646; AAB60382.1; -; Genomic_DNA.
DR EMBL; U09642; AAB60382.1; JOINED; Genomic_DNA.
DR EMBL; U09643; AAB60382.1; JOINED; Genomic_DNA.
DR EMBL; U09644; AAB60382.1; JOINED; Genomic_DNA.
DR EMBL; U09645; AAB60382.1; JOINED; Genomic_DNA.
DR EMBL; AK312687; BAG35567.1; -; mRNA.
DR EMBL; AL606760; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471059; EAX06753.1; -; Genomic_DNA.
DR EMBL; BC002445; AAH02445.1; -; mRNA.
DR EMBL; BC005172; AAH05172.1; -; mRNA.
DR CCDS; CCDS575.1; -.
DR PIR; A39018; A39018.
DR RefSeq; NP_000089.1; NM_000098.2.
DR AlphaFoldDB; P23786; -.
DR SMR; P23786; -.
DR BioGRID; 107767; 63.
DR IntAct; P23786; 22.
DR MINT; P23786; -.
DR STRING; 9606.ENSP00000360541; -.
DR BindingDB; P23786; -.
DR ChEMBL; CHEMBL3238; -.
DR DrugBank; DB00583; Levocarnitine.
DR DrugBank; DB01074; Perhexiline.
DR DrugCentral; P23786; -.
DR SwissLipids; SLP:000001044; -.
DR GlyGen; P23786; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P23786; -.
DR MetOSite; P23786; -.
DR PhosphoSitePlus; P23786; -.
DR SwissPalm; P23786; -.
DR BioMuta; CPT2; -.
DR DMDM; 416836; -.
DR REPRODUCTION-2DPAGE; IPI00012912; -.
DR EPD; P23786; -.
DR jPOST; P23786; -.
DR MassIVE; P23786; -.
DR MaxQB; P23786; -.
DR PaxDb; P23786; -.
DR PeptideAtlas; P23786; -.
DR PRIDE; P23786; -.
DR ProteomicsDB; 54164; -.
DR Antibodypedia; 33067; 496 antibodies from 36 providers.
DR DNASU; 1376; -.
DR Ensembl; ENST00000371486.4; ENSP00000360541.3; ENSG00000157184.7.
DR GeneID; 1376; -.
DR KEGG; hsa:1376; -.
DR MANE-Select; ENST00000371486.4; ENSP00000360541.3; NM_000098.3; NP_000089.1.
DR UCSC; uc001cvb.4; human.
DR CTD; 1376; -.
DR DisGeNET; 1376; -.
DR GeneCards; CPT2; -.
DR GeneReviews; CPT2; -.
DR HGNC; HGNC:2330; CPT2.
DR HPA; ENSG00000157184; Tissue enhanced (liver).
DR MalaCards; CPT2; -.
DR MIM; 255110; phenotype.
DR MIM; 600649; phenotype.
DR MIM; 600650; gene.
DR MIM; 608836; phenotype.
DR MIM; 614212; phenotype.
DR neXtProt; NX_P23786; -.
DR OpenTargets; ENSG00000157184; -.
DR Orphanet; 263524; Acute necrotizing encephalopathy of childhood.
DR Orphanet; 228302; Carnitine palmitoyl transferase II deficiency, myopathic form.
DR Orphanet; 228308; Carnitine palmitoyl transferase II deficiency, neonatal form.
DR Orphanet; 228305; Carnitine palmitoyl transferase II deficiency, severe infantile form.
DR PharmGKB; PA26849; -.
DR VEuPathDB; HostDB:ENSG00000157184; -.
DR eggNOG; KOG3719; Eukaryota.
DR GeneTree; ENSGT01050000244969; -.
DR HOGENOM; CLU_013513_4_2_1; -.
DR InParanoid; P23786; -.
DR OrthoDB; 559299at2759; -.
DR PhylomeDB; P23786; -.
DR TreeFam; TF315202; -.
DR BioCyc; MetaCyc:HS08187-MON; -.
DR BRENDA; 2.3.1.21; 2681.
DR PathwayCommons; P23786; -.
DR Reactome; R-HSA-1989781; PPARA activates gene expression.
DR Reactome; R-HSA-200425; Carnitine metabolism.
DR SignaLink; P23786; -.
DR UniPathway; UPA00659; -.
DR BioGRID-ORCS; 1376; 16 hits in 1086 CRISPR screens.
DR ChiTaRS; CPT2; human.
DR GeneWiki; Carnitine_palmitoyltransferase_II; -.
DR GenomeRNAi; 1376; -.
DR Pharos; P23786; Tchem.
DR PRO; PR:P23786; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P23786; protein.
DR Bgee; ENSG00000157184; Expressed in mucosa of transverse colon and 175 other tissues.
DR ExpressionAtlas; P23786; baseline and differential.
DR Genevisible; P23786; HS.
DR GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0016746; F:acyltransferase activity; IDA:UniProtKB.
DR GO; GO:0008458; F:carnitine O-octanoyltransferase activity; IEA:RHEA.
DR GO; GO:0004095; F:carnitine O-palmitoyltransferase activity; IDA:UniProtKB.
DR GO; GO:0009437; P:carnitine metabolic process; IDA:UniProtKB.
DR GO; GO:0006853; P:carnitine shuttle; TAS:Reactome.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IDA:UniProtKB.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:0001676; P:long-chain fatty acid metabolic process; IDA:UniProtKB.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; ISS:YuBioLab.
DR Gene3D; 1.10.275.20; -; 1.
DR Gene3D; 3.30.559.10; -; 1.
DR Gene3D; 3.30.559.70; -; 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; PTHR22589; 1.
DR Pfam; PF00755; Carn_acyltransf; 1.
DR PROSITE; PS00439; ACYLTRANSF_C_1; 1.
DR PROSITE; PS00440; ACYLTRANSF_C_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Acyltransferase; Direct protein sequencing; Disease variant;
KW Fatty acid metabolism; Lipid metabolism; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Transferase;
KW Transit peptide; Transport.
FT TRANSIT 1..25
FT /note="Mitochondrion"
FT CHAIN 26..658
FT /note="Carnitine O-palmitoyltransferase 2, mitochondrial"
FT /id="PRO_0000004424"
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:0000250|UniProtKB:P52825"
FT MOD_RES 79
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P52825"
FT MOD_RES 85
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P52825"
FT MOD_RES 239
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P52825"
FT MOD_RES 239
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P52825"
FT MOD_RES 305
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P52825"
FT MOD_RES 424
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P52825"
FT MOD_RES 439
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P52825"
FT MOD_RES 510
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P52825"
FT MOD_RES 510
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P52825"
FT MOD_RES 544
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P52825"
FT MOD_RES 544
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P52825"
FT VARIANT 50
FT /note="P -> H (in CPT2D; muscular type; dbSNP:rs28936375)"
FT /evidence="ECO:0000269|PubMed:15622536,
FT ECO:0000269|PubMed:7711730"
FT /id="VAR_001391"
FT VARIANT 113
FT /note="S -> L (in CPT2D; muscular form; frequent mutation;
FT dbSNP:rs74315294)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:15622536, ECO:0000269|PubMed:8358442,
FT ECO:0000269|PubMed:9758712"
FT /id="VAR_001392"
FT VARIANT 151
FT /note="R -> Q (in CPT2D; dbSNP:rs515726177)"
FT /evidence="ECO:0000269|PubMed:14605500,
FT ECO:0000269|PubMed:9758712"
FT /id="VAR_020540"
FT VARIANT 174
FT /note="E -> K (in CPT2D; muscular type; dbSNP:rs28936674)"
FT /evidence="ECO:0000269|PubMed:9600456"
FT /id="VAR_001393"
FT VARIANT 210
FT /note="Y -> D (in CPT2D)"
FT /evidence="ECO:0000269|PubMed:14605500"
FT /id="VAR_020541"
FT VARIANT 213
FT /note="D -> G (in CPT2D; dbSNP:rs74315300)"
FT /evidence="ECO:0000269|PubMed:15622536"
FT /id="VAR_037976"
FT VARIANT 214
FT /note="M -> T (in CPT2D; dbSNP:rs515726174)"
FT /evidence="ECO:0000269|Ref.18"
FT /id="VAR_007966"
FT VARIANT 227
FT /note="P -> L (in CPT2D; dbSNP:rs74315298)"
FT /evidence="ECO:0000269|PubMed:9758712, ECO:0000269|Ref.14"
FT /id="VAR_007967"
FT VARIANT 296
FT /note="R -> Q (in CPT2D; dbSNP:rs764849762)"
FT /evidence="ECO:0000269|PubMed:14605500,
FT ECO:0000269|PubMed:14615409"
FT /id="VAR_020542"
FT VARIANT 352
FT /note="F -> C (associated with susceptibility to IIAE4; 3-
FT fold decrease of affinity for L-carnitine; lower thermal
FT stability compared to wild-type; dbSNP:rs2229291)"
FT /evidence="ECO:0000269|PubMed:15811315,
FT ECO:0000269|PubMed:18306170, ECO:0000269|PubMed:21697855,
FT ECO:0000269|PubMed:9600456"
FT /id="VAR_001394"
FT VARIANT 368
FT /note="V -> I (associated with susceptibility to IIAE4; no
FT effect on activity; does not affect affinity for L-
FT carnitine; lower thermal stability compared to wild-type;
FT dbSNP:rs1799821)"
FT /evidence="ECO:0000269|PubMed:14605500,
FT ECO:0000269|PubMed:1528846, ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:18306170, ECO:0000269|PubMed:9600456,
FT ECO:0000269|PubMed:9758712"
FT /id="VAR_001395"
FT VARIANT 383
FT /note="F -> Y (in CPT2D; hepatocardiomuscular form;
FT dbSNP:rs74315295)"
FT /evidence="ECO:0000269|PubMed:9600456"
FT /id="VAR_001396"
FT VARIANT 448
FT /note="F -> L (in CPT2D; dbSNP:rs74315297)"
FT /evidence="ECO:0000269|Ref.18"
FT /id="VAR_007968"
FT VARIANT 479
FT /note="Y -> F (in CPT2D; dbSNP:rs749895856)"
FT /evidence="ECO:0000269|Ref.18"
FT /id="VAR_007969"
FT VARIANT 503
FT /note="R -> C (in CPT2D; dbSNP:rs74315296)"
FT /evidence="ECO:0000269|PubMed:10090476"
FT /id="VAR_007970"
FT VARIANT 504
FT /note="P -> L (in a patient with IIAE4; dbSNP:rs368311455)"
FT /evidence="ECO:0000269|PubMed:18306170"
FT /id="VAR_066567"
FT VARIANT 549
FT /note="G -> D (in CPT2D; dbSNP:rs186044004)"
FT /evidence="ECO:0000269|PubMed:10090476"
FT /id="VAR_007971"
FT VARIANT 550
FT /note="Q -> R (in CPT2D)"
FT /evidence="ECO:0000269|PubMed:9758712"
FT /id="VAR_020543"
FT VARIANT 553
FT /note="D -> N (in CPT2D; dbSNP:rs28936376)"
FT /evidence="ECO:0000269|PubMed:7711730"
FT /id="VAR_001397"
FT VARIANT 588
FT /note="S -> C (in dbSNP:rs1871748)"
FT /id="VAR_011741"
FT VARIANT 600
FT /note="G -> R (in CPT2D)"
FT /evidence="ECO:0000269|PubMed:14605500"
FT /id="VAR_020544"
FT VARIANT 604
FT /note="P -> S (in CPT2D)"
FT /evidence="ECO:0000269|PubMed:9758712"
FT /id="VAR_020545"
FT VARIANT 605
FT /note="V -> L (in a patient with IIAE4; dbSNP:rs751557097)"
FT /evidence="ECO:0000269|PubMed:18306170"
FT /id="VAR_066568"
FT VARIANT 628
FT /note="Y -> S (in CPT2DI; hepatocardiomuscular form;
FT dbSNP:rs28936673)"
FT /evidence="ECO:0000269|PubMed:8651281"
FT /id="VAR_001398"
FT VARIANT 631
FT /note="R -> C (in CPT2DI and CPT2D; early-onset
FT hepatocardiomuscular form; dbSNP:rs74315293)"
FT /evidence="ECO:0000269|PubMed:1528846,
FT ECO:0000269|PubMed:24780397"
FT /id="VAR_001399"
FT VARIANT 647
FT /note="M -> V (confirmed at protein level;
FT dbSNP:rs1799822)"
FT /evidence="ECO:0000269|PubMed:14605500,
FT ECO:0000269|PubMed:1528846, ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:17488105, ECO:0000269|PubMed:18306170,
FT ECO:0000269|PubMed:9600456, ECO:0000269|PubMed:9758712"
FT /id="VAR_001400"
SQ SEQUENCE 658 AA; 73777 MW; 6444B75ACD57140F CRC64;
MVPRLLLRAW PRGPAVGPGA PSRPLSAGSG PGQYLQRSIV PTMHYQDSLP RLPIPKLEDT
IRRYLSAQKP LLNDGQFRKT EQFCKSFENG IGKELHEQLV ALDKQNKHTS YISGPWFDMY
LSARDSVVLN FNPFMAFNPD PKSEYNDQLT RATNMTVSAI RFLKTLRAGL LEPEVFHLNP
AKSDTITFKR LIRFVPSSLS WYGAYLVNAY PLDMSQYFRL FNSTRLPKPS RDELFTDDKA
RHLLVLRKGN FYIFDVLDQD GNIVSPSEIQ AHLKYILSDS SPAPEFPLAY LTSENRDIWA
ELRQKLMSSG NEESLRKVDS AVFCLCLDDF PIKDLVHLSH NMLHGDGTNR WFDKSFNLII
AKDGSTAVHF EHSWGDGVAV LRFFNEVFKD STQTPAVTPQ SQPATTDSTV TVQKLNFELT
DALKTGITAA KEKFDATMKT LTIDCVQFQR GGKEFLKKQK LSPDAVAQLA FQMAFLRQYG
QTVATYESCS TAAFKHGRTE TIRPASVYTK RCSEAFVREP SRHSAGELQQ MMVECSKYHG
QLTKEAAMGQ GFDRHLFALR HLAAAKGIIL PELYLDPAYG QINHNVLSTS TLSSPAVNLG
GFAPVVSDGF GVGYAVHDNW IGCNVSSYPG RNAREFLQCV EKALEDMFDA LEGKSIKS
