P23786 (CPT2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Carnitine O-palmitoyltransferase 2, mitochondrial
EC=2.3.1.21

Alternative name(s):
Carnitine palmitoyltransferase II
Short name=CPT II

Gene names

Name:	CPT2
Synonyms:	CPT1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	658 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	Palmitoyl-CoA + L-carnitine = CoA + L-palmitoylcarnitine.
Pathway	Lipid metabolism; fatty acid beta-oxidation.
Subcellular location	Mitochondrion inner membrane; Peripheral membrane protein; Matrix side.
Involvement in disease	Defects in CPT2 are the cause of carnitine palmitoyltransferase 2 deficiency late-onset (CPT2D) [MIM:255110]; also known as CPT-II deficiency or CPT2 deficiency. CPT2D is an autosomal recessive disorder characterized by recurrent myoglobinuria, episodes of muscle pain, stiffness, and rhabdomyolysis. These symptoms are triggered by prolonged exercise, fasting or viral infection and patients are usually young adults. In addition to this classical, late-onset, muscular type, a hepatic or hepatocardiomuscular form has been reported in infants. Clinical pictures in these children or neonates include hypoketotic hypoglycemia, liver dysfunction, cardiomyopathy and sudden death. Ref.3 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.20 Ref.21 Ref.22 Defects in CPT2 are the cause of carnitine palmitoyltransferase 2 deficiency infantile (CPT2DI) [MIM:600649]. A disorder of mitochondrial long-chain fatty acid oxidation characterized by hepatic or hepato-cardio-muscular manifestations with onset in infancy. Clinical features include hypoketotic hypoglycemia, lethargy, seizures, hepatomegaly, liver dysfunction, cardiomegaly and dilated cardiomyopathy. Defects in CPT2 are the cause of carnitine palmitoyltransferase 2 deficiency lethal neonatal (CPT2D-LN) [MIM:608836]; also known as lethal neonatal CPT-II deficiency. It is a lethal neonatal form of CPT2D. This rarely presentation is antenatal with cerebral periventricular cysts and cystic dysplastic kidneys. The clinical variability of the disease is likely attributed to the variable residual enzymatic activity. Defects in CPT2 are a cause of susceptibility to encephalopathy acute infection-induced type 4 (IIAE4) [MIM:614212]. A severe neurologic complication of an infection. It manifests within days in otherwise healthy children after common viral infections, without evidence of viral infection of the brain or inflammatory cell infiltration. In affected children, high-grade fever is accompanied within 12 to 48 hours by febrile convulsions, often leading to coma, multiple-organ failure, brain edema, and high morbidity and mortality. The infections are usually viral, particularly influenza, although other viruses and even mycoplasma have been found to cause the disorder. Note=Polymorphic variants in CPT2 can confer susceptibility to infection-induced encepalopathy. These variants do not cause classical carnitine palmitoyltransferase 2 deficiency, and patients harboring any of them are asymptomatic most of the time. However, they are prone to viral infection (high fever)-related encephalopathy (Ref.25). Ref.23 Ref.25
Sequence similarities	Belongs to the carnitine/choline acetyltransferase family.

Ontologies

Keywords
Biological process	Fatty acid metabolism Lipid metabolism Transport
Cellular component	Membrane Mitochondrion Mitochondrion inner membrane
Coding sequence diversity	Polymorphism
Disease	Disease mutation
Domain	Transit peptide
Molecular function	Acyltransferase Transferase
PTM	Acetylation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	carnitine shuttle Traceable author statement. Source: Reactome fatty acid beta-oxidation Non-traceable author statement. Source: UniProtKB regulation of fatty acid oxidation Traceable author statement. Source: Reactome
Cellular component	mitochondrial inner membrane Non-traceable author statement Ref.1. Source: UniProtKB nucleolus Inferred from direct assay. Source: HPA
Molecular function	carnitine O-palmitoyltransferase activity Non-traceable author statement Ref.1. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 25	25	Mitochondrion
	Chain	26 – 658	633	Carnitine O-palmitoyltransferase 2, mitochondrial		PRO_0000004424
Regions
	Topological domain	26 – 178	153	Mitochondrial matrix By similarity
	Intramembrane	179 – 208	30	Note=Mitochondrial inner membrane; By similarity
	Topological domain	209 – 658	450	Mitochondrial matrix By similarity
	Region	452 – 464	13	Coenzyme A binding By similarity
Sites
	Active site	372	1	Proton acceptor By similarity
	Binding site	486	1	Carnitine By similarity
	Binding site	488	1	Carnitine By similarity
	Binding site	499	1	Carnitine By similarity
Amino acid modifications
	Modified residue	510	1	N6-acetyllysine Ref.9
	Modified residue	544	1	N6-acetyllysine Ref.9
Natural variations
	Natural variant	50	1	P → H in CPT2D; muscular type. Ref.3 Ref.22 Corresponds to variant rs28936674 [ dbSNP | Ensembl ].		VAR_001391
	Natural variant	113	1	S → L in CPT2D; muscular form. Frequent mutation, may be a polymorphism as it found in some 'normal' cDNA seqeuences. Ref.7 Ref.13 Ref.17 Ref.22		VAR_001392
	Natural variant	151	1	R → Q in CPT2D. Ref.17 Ref.20		VAR_020540
	Natural variant	174	1	E → K in CPT2D; muscular type. Ref.16 Corresponds to variant rs28936674 [ dbSNP | Ensembl ].		VAR_001393
	Natural variant	210	1	Y → D in CPT2D. Ref.20		VAR_020541
	Natural variant	213	1	D → G in CPT2D. Ref.22		VAR_037976
	Natural variant	214	1	M → T in CPT2D. Ref.15		VAR_007966
	Natural variant	227	1	P → L in CPT2D. Ref.11 Ref.17		VAR_007967
	Natural variant	296	1	R → Q in CPT2D. Ref.20 Ref.21		VAR_020542
	Natural variant	352	1	F → C Polymorphism associated with susceptibility to IIAE4; 3-fold decrease of affinity for L-carnitine; lower thermal stability compared to wild-type. Ref.16 Ref.23 Ref.24 Ref.25 Corresponds to variant rs2229291 [ dbSNP | Ensembl ].		VAR_001394
	Natural variant	368	1	V → I Common polymorphism associated with susceptibility to IIAE4; no effect on activity; does not affect affinity for L-carnitine; lower thermal stability compared to wild-type. Ref.7 Ref.12 Ref.16 Ref.17 Ref.20 Ref.23 Ref.24 Ref.25 Corresponds to variant rs1799821 [ dbSNP | Ensembl ].		VAR_001395
	Natural variant	383	1	F → Y in CPT2D; hepatocardiomuscular form. Ref.16 Corresponds to variant rs28936673 [ dbSNP | Ensembl ].		VAR_001396
	Natural variant	448	1	F → L in CPT2D. Ref.15		VAR_007968
	Natural variant	479	1	Y → F in CPT2D. Ref.15		VAR_007969
	Natural variant	503	1	R → C in CPT2D. Ref.18		VAR_007970
	Natural variant	504	1	P → L in a patient with IIAE4. Ref.24		VAR_066567
	Natural variant	549	1	G → D in CPT2D. Ref.18		VAR_007971
	Natural variant	550	1	Q → R in CPT2D. Ref.17		VAR_020543
	Natural variant	553	1	D → N in CPT2D. Ref.3 Corresponds to variant rs28936376 [ dbSNP | Ensembl ].		VAR_001397
	Natural variant	588	1	S → C. Corresponds to variant rs1871748 [ dbSNP | Ensembl ].		VAR_011741
	Natural variant	600	1	G → R in CPT2D. Ref.20		VAR_020544
	Natural variant	604	1	P → S in CPT2D. Ref.17		VAR_020545
	Natural variant	605	1	V → L in a patient with IIAE4. Ref.24		VAR_066568
	Natural variant	628	1	Y → S in CPT2D; hepatocardiomuscular form. Ref.14 Corresponds to variant rs28936673 [ dbSNP | Ensembl ].		VAR_001398
	Natural variant	631	1	R → C in CPT2D; early-onset hepatocardiomuscular form. Ref.12		VAR_001399
	Natural variant	647	1	M → V Common polymorphism. Ref.7 Ref.12 Ref.16 Ref.17 Ref.20 Ref.24 Corresponds to variant rs1799822 [ dbSNP | Ensembl ].		VAR_001400

Sequences

	Sequence		Length	Mass (Da)
	P23786 [UniParc]. Last modified October 1, 1993. Version 2. Checksum: 6444B75ACD57140F	FASTA	658	73,777
	10 20 30 40 50 60 MVPRLLLRAW PRGPAVGPGA PSRPLSAGSG PGQYLQRSIV PTMHYQDSLP RLPIPKLEDT 70 80 90 100 110 120 IRRYLSAQKP LLNDGQFRKT EQFCKSFENG IGKELHEQLV ALDKQNKHTS YISGPWFDMY 130 140 150 160 170 180 LSARDSVVLN FNPFMAFNPD PKSEYNDQLT RATNMTVSAI RFLKTLRAGL LEPEVFHLNP 190 200 210 220 230 240 AKSDTITFKR LIRFVPSSLS WYGAYLVNAY PLDMSQYFRL FNSTRLPKPS RDELFTDDKA 250 260 270 280 290 300 RHLLVLRKGN FYIFDVLDQD GNIVSPSEIQ AHLKYILSDS SPAPEFPLAY LTSENRDIWA 310 320 330 340 350 360 ELRQKLMSSG NEESLRKVDS AVFCLCLDDF PIKDLVHLSH NMLHGDGTNR WFDKSFNLII 370 380 390 400 410 420 AKDGSTAVHF EHSWGDGVAV LRFFNEVFKD STQTPAVTPQ SQPATTDSTV TVQKLNFELT 430 440 450 460 470 480 DALKTGITAA KEKFDATMKT LTIDCVQFQR GGKEFLKKQK LSPDAVAQLA FQMAFLRQYG 490 500 510 520 530 540 QTVATYESCS TAAFKHGRTE TIRPASVYTK RCSEAFVREP SRHSAGELQQ MMVECSKYHG 550 560 570 580 590 600 QLTKEAAMGQ GFDRHLFALR HLAAAKGIIL PELYLDPAYG QINHNVLSTS TLSSPAVNLG 610 620 630 640 650 GFAPVVSDGF GVGYAVHDNW IGCNVSSYPG RNAREFLQCV EKALEDMFDA LEGKSIKS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"cDNA cloning, sequence analysis, and chromosomal localization of the gene for human carnitine palmitoyltransferase." Finocchiaro G., Taroni F., Rocchi M., Martin A.L., Colombo I., Tarelli G.T., Didonato S. Proc. Natl. Acad. Sci. U.S.A. 88:661-665(1991) [PubMed: 1988962] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE. Tissue: Liver.
[2]	Erratum Finocchiaro G., Taroni F., Rocchi M., Martin A.L., Colombo I., Tarelli G.T., Didonato S. Proc. Natl. Acad. Sci. U.S.A. 88:10981-10981(1991) [PubMed: 1961767] [Abstract] Cited for: SEQUENCE REVISION TO 283 AND 375.
[3]	"Carnitine palmitoyltransferase II deficiency: structure of the gene and characterization of two novel disease-causing mutations." Verderio E., Cavadini P., Montermini L., Wang H., Lamantea E., Finocchiaro G., Didonato S., Gellera C., Taroni F. Hum. Mol. Genet. 4:19-29(1995) [PubMed: 7711730] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS CPT2D DEFICIENCY HIS-50 AND ASN-553.
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed: 16710414] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS LEU-113; ILE-368 AND VAL-647. Tissue: Skin and Uterus.
[8]	"Purification, characterization and partial amino acid sequences of carnitine palmitoyl-transferase from human liver." Finocchiaro G., Colombo I., Didonato S. FEBS Lett. 274:163-166(1990) [PubMed: 2174799] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE. Tissue: Liver.
[9]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-510 AND LYS-544, MASS SPECTROMETRY.
[10]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]	"Lethal carnitine palmitoyltransferase (CPT) II deficiency in newborns: a molecular-genetic study." Taroni F., Gellera C., Cavadini P., Baratta S., Lamantea E., Dethlefs S., Didonato S., Reik R.A., Benke P.J. Am. J. Hum. Genet. 51:A245-A245(1992) Cited for: VARIANT CPT2D LEU-227.
[12]	"Molecular characterization of inherited carnitine palmitoyltransferase II deficiency." Taroni F., Verderio E., Fiorucci S., Cavadini P., Finocchiaro G., Uziel G., Lamantea E., Gellera C., Didonato S. Proc. Natl. Acad. Sci. U.S.A. 89:8429-8433(1992) [PubMed: 1528846] [Abstract] Cited for: VARIANT CPT2D CYS-631, VARIANTS ILE-368 AND VAL-647.
[13]	"Identification of a common mutation in the carnitine palmitoyltransferase II gene in familial recurrent myoglobinuria patients." Taroni F., Verderio E., Dworzak F., Willems P.J., Cavadini P., Didonato S. Nat. Genet. 4:314-320(1993) [PubMed: 8358442] [Abstract] Cited for: VARIANT CPT2D LEU-113.
[14]	"Molecular analysis of carnitine palmitoyltransferase II deficiency with hepatocardiomuscular expression." Bonnefont J.-P., Taroni F., Cavadini P., Cepanec C., Brivet M., Saudubray J.-M., Leroux J.-P., Demaugre F. Am. J. Hum. Genet. 58:971-978(1996) [PubMed: 8651281] [Abstract] Cited for: VARIANT CPT2D SER-628.
[15]	"Carnitine palmityltransferase II deficiency: three novel mutations." Wieser T., Deschauer M., Zierz S. Ann. Neurol. 42:414-415(1997) Cited for: VARIANTS CPT2D THR-214; LEU-448 AND PHE-479.
[16]	"Two CPT2 mutations in three Japanese patients with carnitine palmitoyltransferase II deficiency: functional analysis and association with polymorphic haplotypes and two clinical phenotypes." Wataya K., Akanuma J., Cavadini P., Aoki Y., Kure S., Invernizzi F., Yoshida I., Kira J., Taroni F., Matsubara Y., Narisawa K. Hum. Mutat. 11:377-386(1998) [PubMed: 9600456] [Abstract] Cited for: VARIANTS CPT2D LYS-174 AND TYR-383, VARIANTS CYS-352; ILE-368 AND VAL-647.
[17]	"Identification of four novel mutations in patients with carnitine palmitoyltransferase II (CPT II) deficiency." Yang B.-Z., Ding J.-H., Dewese T., Roe D., He G., Wilkinson J., Day D.W., Demaugre F., Rabier D., Brivet M., Roe C. Mol. Genet. Metab. 64:229-236(1998) [PubMed: 9758712] [Abstract] Cited for: VARIANTS CPT2D LEU-113; GLN-151; LEU-227; ARG-550 AND SER-604, VARIANTS ILE-368 AND VAL-647.
[18]	"Novel mutations associated with carnitine palmitoyltransferase II deficiency." Taggart R.T., Smail D., Apolito C., Vladutiu G.D. Hum. Mutat. 13:210-220(1999) [PubMed: 10090476] [Abstract] Cited for: VARIANTS CPT2D CYS-503 AND ASP-549.
[19]	"Antenatal presentation of carnitine palmitoyltransferase II deficiency." Elpeleg O.N., Hammerman C., Saada A., Shaag A., Golzand E., Hochner-Celnikier D., Berger I., Nadjari M. Am. J. Med. Genet. 102:183-187(2001) [PubMed: 11477613] [Abstract] Cited for: INVOLVEMENT IN LN-CPT2D.
[20]	"Mutation and biochemical analysis in carnitine palmitoyltransferase type II (CPT II) deficiency." Olpin S.E., Afifi A., Clark S., Manning N.J., Bonham J.R., Dalton A., Leonard J.V., Land J.M., Andresen B.S., Morris A.A., Muntoni F., Turnbull D., Pourfarzam M., Rahman S., Pollitt R.J. J. Inherit. Metab. Dis. 26:543-557(2003) [PubMed: 14605500] [Abstract] Cited for: VARIANTS CPT2D GLN-151; ASP-210; GLN-296 AND ARG-600, VARIANTS ILE-368 AND VAL-647.
[21]	"Carnitine palmitoyltransferase II deficiency: a clinical, biochemical, and molecular review." Sigauke E., Rakheja D., Kitson K., Bennett M.J. Lab. Invest. 83:1543-1554(2003) [PubMed: 14615409] [Abstract] Cited for: VARIANT CPT2D GLN-296.
[22]	"Fuel utilization in subjects with carnitine palmitoyltransferase 2 gene mutations." Oerngreen M.C., Dunoe M., Ejstrup R., Christensen E., Schwartz M., Sacchetti M., Vissing J. Ann. Neurol. 57:60-66(2005) [PubMed: 15622536] [Abstract] Cited for: VARIANTS CPT2D HIS-50; LEU-113 AND GLY-213.
[23]	"Thermolabile phenotype of carnitine palmitoyltransferase II variations as a predisposing factor for influenza-associated encephalopathy." Chen Y., Mizuguchi H., Yao D., Ide M., Kuroda Y., Shigematsu Y., Yamaguchi S., Yamaguchi M., Kinoshita M., Kido H. FEBS Lett. 579:2040-2044(2005) [PubMed: 15811315] [Abstract] Cited for: ASSOCIATION OF VARIANTS CYS-352 AND ILE-368 WITH SUSCEPTIBILITY TO IIAE4.
[24]	"Thermal instability of compound variants of carnitine palmitoyltransferase II and impaired mitochondrial fuel utilization in influenza-associated encephalopathy." Yao D., Mizuguchi H., Yamaguchi M., Yamada H., Chida J., Shikata K., Kido H. Hum. Mutat. 29:718-727(2008) [PubMed: 18306170] [Abstract] Cited for: VARIANTS CYS-352; ILE-368; LEU-504; LEU-605 AND VAL-647, CHARACTERIZATION OF VARIANTS CYS-352 AND ILE-368.
[25]	"Fatal viral infection-associated encephalopathy in two Chinese boys: a genetically determined risk factor of thermolabile carnitine palmitoyltransferase II variants." Mak C.M., Lam C.W., Fong N.C., Siu W.K., Lee H.C., Siu T.S., Lai C.K., Law C.Y., Tong S.F., Poon W.T., Lam D.S., Ng H.L., Yuen Y.P., Tam S., Que T.L., Kwong N.S., Chan A.Y. J. Hum. Genet. 56:617-621(2011) [PubMed: 21697855] [Abstract] Cited for: ASSOCIATION OF VARIANTS CYS-352 AND ILE-368 WITH SUSCEPTIBILITY TO IIAE4.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases
EMBL GenBank DDBJ	U09648 mRNA. Translation: AAB60383.1. M58581 mRNA. Translation: AAB59462.1. U09646 , U09642, U09643, U09644, U09645 Genomic DNA. Translation: AAB60382.1. AK312687 mRNA. Translation: BAG35567.1. AL606760 Genomic DNA. Translation: CAI18907.1. CH471059 Genomic DNA. Translation: EAX06753.1. BC002445 mRNA. Translation: AAH02445.1. BC005172 mRNA. Translation: AAH05172.1.
IPI	IPI00012912.
PIR	A39018.
RefSeq	NP_000089.1. NM_000098.2.
UniGene	Hs.713535.
3D structure databases
ProteinModelPortal	P23786.
SMR	P23786. Positions 34-657.
ModBase	Search...
Protein-protein interaction databases
STRING	P23786.
PTM databases
PhosphoSite	P23786.
Polymorphism databases
DMDM	416836.
2D gel databases
REPRODUCTION-2DPAGE	IPI00012912.
Proteomic databases
PeptideAtlas	P23786.
PRIDE	P23786.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000371486; ENSP00000360541; ENSG00000157184.
GeneID	1376.
KEGG	hsa:1376.
NMPDR	fig|9606.3.peg.1184.
UCSC	uc001cvb.2. human.
Organism-specific databases
CTD	1376.
GeneCards	GC01P053662.
H-InvDB	HIX0000594.
HGNC	HGNC:2330. CPT2.
HPA	HPA028201. HPA028202. HPA028214.
MIM	255110. phenotype. 600649. phenotype. 600650. gene. 608836. phenotype. 614212. phenotype.
neXtProt	NX_P23786.
Orphanet	228302. Carnitine palmitoyl transferase II deficiency, myopathic form.
PharmGKB	PA26849.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG06915.
HOGENOM	HBG522304.
HOVERGEN	HBG098001.
InParanoid	P23786.
OMA	YNDQLTR.
OrthoDB	EOG4WM4TB.
PhylomeDB	P23786.
Enzyme and pathway databases
BRENDA	2.3.1.21. 2681.
Reactome	REACT_11163. Activated AMPK stimulates fatty-acid oxidation in muscle. REACT_22258. Metabolism of lipids and lipoproteins.
Gene expression databases
ArrayExpress	P23786.
Bgee	P23786.
CleanEx	HS_CPT2.
Genevestigator	P23786.
GermOnline	ENSG00000157184. Homo sapiens.
Family and domain databases
InterPro	IPR000542. Carn_acyl_trans. [Graphical view]
KO	K08766.
PANTHER	PTHR22589. Carn_acyl_trans. 1 hit.
Pfam	PF00755. Carn_acyltransf. 1 hit. [Graphical view]
PROSITE	PS00439. ACYLTRANSF_C_1. 1 hit. PS00440. ACYLTRANSF_C_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
DrugBank	DB00583. L-Carnitine. DB01074. Perhexiline.
NextBio	5585.
SOURCE	Search...

Entry information

Entry name

CPT2_HUMAN

Accession

Primary (citable) accession number: P23786
Secondary accession number(s): B2R6S0, Q5SW68, Q9BQ26

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1991
Last sequence update:	October 1, 1993
Last modified:	January 25, 2012
This is version 127 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.