Q8TCG5 (CPT1C_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Carnitine O-palmitoyltransferase 1, brain isoform
Short name=CPT1-B
EC=2.3.1.21

Alternative name(s):
CPT IC
Carnitine O-palmitoyltransferase I, brain isoform
Short name=CPTI-B
Carnitine palmitoyltransferase 1C

Gene names

Name:	CPT1C
Synonyms:	CATL1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	803 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Catalytic activity	Palmitoyl-CoA + L-carnitine = CoA + L-palmitoylcarnitine.
Pathway	Lipid metabolism; fatty acid beta-oxidation.
Subunit structure	Peripherally associated with AMPAR complex. AMPAR complex consists of an inner core made of 4 pore-forming GluA/GRIA proteins (GRIA1, GRIA2, GRIA3 and GRIA4) and 4 major auxiliary subunits arranged in a twofold symmetry. One of the two pairs of distinct binding sites is occupied either by CNIH2, CNIH3 or CACNG2, CACNG3. The other harbors CACNG2, CACNG3, CACNG4, CACNG8 or GSG1L. This inner core of AMPAR complex is complemented by outer core constituents binding directly to the GluA/GRIA proteins at sites distinct from the interaction sites of the inner core constituents. Outer core constituents include at least PRRT1, PRRT2, CKAMP44/SHISA9, FRRS1L and NRN1. The proteins of the inner and outer core serve as a platform for other, more peripherally associated AMPAR constituents, including CPT1C. Alone or in combination, these auxiliary subunits control the gating and pharmacology of the AMPAR complex and profoundly impact their biogenesis and protein processing By similarity.
Subcellular location	Mitochondrion outer membrane; Multi-pass membrane protein By similarity. Cell junction › synapse By similarity.
Tissue specificity	Expressed predominantly in brain and testis. Ref.1
Sequence similarities	Belongs to the carnitine/choline acetyltransferase family.
Sequence caution	The sequence BAB85068.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence CAD38561.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
Biological process	Fatty acid metabolism Lipid metabolism
Cellular component	Cell junction Membrane Mitochondrion Mitochondrion outer membrane Synapse
Coding sequence diversity	Alternative splicing
Domain	Transmembrane Transmembrane helix
Molecular function	Acyltransferase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	fatty acid beta-oxidation Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	cell junction Inferred from electronic annotation. Source: UniProtKB-KW integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW mitochondrial outer membrane Inferred from electronic annotation. Source: UniProtKB-SubCell synapse Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	carnitine O-palmitoyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q8TCG5-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q8TCG5-2)

The sequence of this isoform differs from the canonical sequence as follows:
     258-268: Missing.

Note: No experimental confirmation available.

Isoform 3 (identifier: Q8TCG5-3)

The sequence of this isoform differs from the canonical sequence as follows:
     623-711: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 803	803	Carnitine O-palmitoyltransferase 1, brain isoform		PRO_0000210166
Regions
	Topological domain	1 – 52	52	Cytoplasmic Potential
	Transmembrane	53 – 75	23	Helical; Potential
	Topological domain	76 – 103	28	Mitochondrial intermembrane Potential
	Transmembrane	104 – 126	23	Helical; Potential
	Topological domain	127 – 803	677	Cytoplasmic Potential
	Region	552 – 564	13	Coenzyme A binding By similarity
Sites
	Active site	470	1	Proton acceptor By similarity
	Binding site	586	1	Carnitine By similarity
	Binding site	588	1	Carnitine By similarity
	Binding site	589	1	Coenzyme A By similarity
	Binding site	599	1	Carnitine By similarity
Natural variations
	Alternative sequence	258 – 268	11	Missing in isoform 2.		VSP_010677
	Alternative sequence	623 – 711	89	Missing in isoform 3.		VSP_012457
Experimental info
	Sequence conflict	58	1	S → G in BAF82402. Ref.3
	Sequence conflict	375 – 378	4	HEEH → RTRG in CAD38561. Ref.6
	Sequence conflict	542	1	D → G in BAB85068. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified June 1, 2002. Version 1. Checksum: 96C2AE6ED0DEC705	FASTA	803	90,989
	10 20 30 40 50 60 MAEAHQAVGF RPSLTSDGAE VELSAPVLQE IYLSGLRSWK RHLSRFWNDF LTGVFPASPL 70 80 90 100 110 120 SWLFLFSAIQ LAWFLQLDPS LGLMEKIKEL LPDWGGQHHG LRGVLAAALF ASCLWGALIF 130 140 150 160 170 180 TLHVALRLLL SYHGWLLEPH GAMSSPTKTW LALVRIFSGR HPMLFSYQRS LPRQPVPSVQ 190 200 210 220 230 240 DTVRKYLESV RPILSDEDFD WTAVLAQEFL RLQASLLQWY LRLKSWWASN YVSDWWEEFV 250 260 270 280 290 300 YLRSRNPLMV NSNYYMMDFL YVTPTPLQAA RAGNAVHALL LYRHRLNRQE IPPTLLMGMR 310 320 330 340 350 360 PLCSAQYEKI FNTTRIPGVQ KDYIRHLHDS QHVAVFHRGR FFRMGTHSRN SLLSPRALEQ 370 380 390 400 410 420 QFQRILDDPS PACPHEEHLA ALTAAPRGTW AQVRTSLKTQ AAEALEAVEG AAFFVSLDAE 430 440 450 460 470 480 PAGLTREDPA ASLDAYAHAL LAGRGHDRWF DKSFTLIVFS NGKLGLSVEH SWADCPISGH 490 500 510 520 530 540 MWEFTLATEC FQLGYSTDGH CKGHPDPTLP QPQRLQWDLP DQIHSSISLA LRGAKILSEN 550 560 570 580 590 600 VDCHVVPFSL FGKSFIRRCH LSSDSFIQIA LQLAHFRDRG QFCLTYESAM TRLFLEGRTE 610 620 630 640 650 660 TVRSCTREAC NFVRAMEDKE KTDPQCLALF RVAVDKHQAL LKAAMSGQGV DRHLFALYIV 670 680 690 700 710 720 SRFLHLQSPF LTQVHSEQWQ LSTSQIPVQQ MHLFDVHNYP DYVSSGGGFG PADDHGYGVS 730 740 750 760 770 780 YIFMGDGMIT FHISSKKSST KTDSHRLGQH IEDALLDVAS LFQAGQHFKR RFRGSGKENS 790 800 RHRCGFLSRQ TGASKASMTS TDF
	Isoform 2 [UniParc]. Checksum: 3420B3FE0457E895	FASTA	792	89,713
	10 20 30 40 50 60 MAEAHQAVGF RPSLTSDGAE VELSAPVLQE IYLSGLRSWK RHLSRFWNDF LTGVFPASPL 70 80 90 100 110 120 SWLFLFSAIQ LAWFLQLDPS LGLMEKIKEL LPDWGGQHHG LRGVLAAALF ASCLWGALIF 130 140 150 160 170 180 TLHVALRLLL SYHGWLLEPH GAMSSPTKTW LALVRIFSGR HPMLFSYQRS LPRQPVPSVQ 190 200 210 220 230 240 DTVRKYLESV RPILSDEDFD WTAVLAQEFL RLQASLLQWY LRLKSWWASN YVSDWWEEFV 250 260 270 280 290 300 YLRSRNPLMV NSNYYMMAAR AGNAVHALLL YRHRLNRQEI PPTLLMGMRP LCSAQYEKIF 310 320 330 340 350 360 NTTRIPGVQK DYIRHLHDSQ HVAVFHRGRF FRMGTHSRNS LLSPRALEQQ FQRILDDPSP 370 380 390 400 410 420 ACPHEEHLAA LTAAPRGTWA QVRTSLKTQA AEALEAVEGA AFFVSLDAEP AGLTREDPAA 430 440 450 460 470 480 SLDAYAHALL AGRGHDRWFD KSFTLIVFSN GKLGLSVEHS WADCPISGHM WEFTLATECF 490 500 510 520 530 540 QLGYSTDGHC KGHPDPTLPQ PQRLQWDLPD QIHSSISLAL RGAKILSENV DCHVVPFSLF 550 560 570 580 590 600 GKSFIRRCHL SSDSFIQIAL QLAHFRDRGQ FCLTYESAMT RLFLEGRTET VRSCTREACN 610 620 630 640 650 660 FVRAMEDKEK TDPQCLALFR VAVDKHQALL KAAMSGQGVD RHLFALYIVS RFLHLQSPFL 670 680 690 700 710 720 TQVHSEQWQL STSQIPVQQM HLFDVHNYPD YVSSGGGFGP ADDHGYGVSY IFMGDGMITF 730 740 750 760 770 780 HISSKKSSTK TDSHRLGQHI EDALLDVASL FQAGQHFKRR FRGSGKENSR HRCGFLSRQT 790 GASKASMTST DF
	Isoform 3 [UniParc]. Checksum: 4435ECAA8502D6BA	FASTA	714	81,000
	10 20 30 40 50 60 MAEAHQAVGF RPSLTSDGAE VELSAPVLQE IYLSGLRSWK RHLSRFWNDF LTGVFPASPL 70 80 90 100 110 120 SWLFLFSAIQ LAWFLQLDPS LGLMEKIKEL LPDWGGQHHG LRGVLAAALF ASCLWGALIF 130 140 150 160 170 180 TLHVALRLLL SYHGWLLEPH GAMSSPTKTW LALVRIFSGR HPMLFSYQRS LPRQPVPSVQ 190 200 210 220 230 240 DTVRKYLESV RPILSDEDFD WTAVLAQEFL RLQASLLQWY LRLKSWWASN YVSDWWEEFV 250 260 270 280 290 300 YLRSRNPLMV NSNYYMMDFL YVTPTPLQAA RAGNAVHALL LYRHRLNRQE IPPTLLMGMR 310 320 330 340 350 360 PLCSAQYEKI FNTTRIPGVQ KDYIRHLHDS QHVAVFHRGR FFRMGTHSRN SLLSPRALEQ 370 380 390 400 410 420 QFQRILDDPS PACPHEEHLA ALTAAPRGTW AQVRTSLKTQ AAEALEAVEG AAFFVSLDAE 430 440 450 460 470 480 PAGLTREDPA ASLDAYAHAL LAGRGHDRWF DKSFTLIVFS NGKLGLSVEH SWADCPISGH 490 500 510 520 530 540 MWEFTLATEC FQLGYSTDGH CKGHPDPTLP QPQRLQWDLP DQIHSSISLA LRGAKILSEN 550 560 570 580 590 600 VDCHVVPFSL FGKSFIRRCH LSSDSFIQIA LQLAHFRDRG QFCLTYESAM TRLFLEGRTE 610 620 630 640 650 660 TVRSCTREAC NFVRAMEDKE KTADDHGYGV SYIFMGDGMI TFHISSKKSS TKTDSHRLGQ 670 680 690 700 710 HIEDALLDVA SLFQAGQHFK RRFRGSGKEN SRHRCGFLSR QTGASKASMT STDF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A novel brain-expressed protein related to carnitine palmitoyltransferase I." Price N., van der Leij F.R., Jackson V., Corstorphine C., Thomson R., Sorensen A., Zammit V. Genomics 80:433-442(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY. Tissue: Eye.
[2]	"Molecular characterization, chromosomal localization and expression analysis of a gene, CATL1, encoding for a new member of the human carnitine acyltransferase family." Scorilas A., Katsaros N. Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Brain, Kidney epithelium and Subthalamic nucleus.
[4]	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].
[5]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Eye.
[6]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 375-803 (ISOFORM 3). Tissue: Brain.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF357970 mRNA. Translation: AAL99615.1. AF331918 Genomic DNA. Translation: AAQ14875.1. AK074389 mRNA. Translation: BAB85068.1. Different initiation. AK289713 mRNA. Translation: BAF82402.1. AK290092 mRNA. Translation: BAF82781.1. CH471177 Genomic DNA. Translation: EAW52524.1. BC029104 mRNA. Translation: AAH29104.1. AL831876 mRNA. Translation: CAD38561.2. Different initiation.
IPI	IPI00152358. IPI00168584. IPI00418747.
RefSeq	NP_001129524.1. NM_001136052.2. NP_001186681.1. NM_001199752.1. NP_001186682.1. NM_001199753.1. NP_689572.1. NM_152359.2.
UniGene	Hs.112195.
3D structure databases
ProteinModelPortal	Q8TCG5.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000319343.
PTM databases
PhosphoSite	Q8TCG5.
Polymorphism databases
DMDM	57013809.
Proteomic databases
PaxDb	Q8TCG5.
PRIDE	Q8TCG5.
Protocols and materials databases
DNASU	126129.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000323446; ENSP00000319343; ENSG00000169169. ENST00000354199; ENSP00000346138; ENSG00000169169. ENST00000392518; ENSP00000376303; ENSG00000169169. ENST00000405931; ENSP00000384465; ENSG00000169169. ENST00000598293; ENSP00000473028; ENSG00000169169.
GeneID	126129.
KEGG	hsa:126129.
UCSC	uc002ppi.3. human. uc002ppk.3. human. uc010eni.1. human.
Organism-specific databases
CTD	126129.
GeneCards	GC19P050195.
HGNC	HGNC:18540. CPT1C.
HPA	HPA014529.
MIM	608846. gene.
neXtProt	NX_Q8TCG5.
PharmGKB	PA134922321.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG272759.
HOGENOM	HOG000233542.
HOVERGEN	HBG003458.
InParanoid	Q8TCG5.
KO	K08765.
OMA	IDCHVFP.
PhylomeDB	Q8TCG5.
Enzyme and pathway databases
Pathway_Interaction_DB	hnf3bpathway. FOXA2 and FOXA3 transcription factor networks.
UniPathway	UPA00659.
Gene expression databases
ArrayExpress	Q8TCG5.
Bgee	Q8TCG5.
CleanEx	HS_CPT1C.
Genevestigator	Q8TCG5.
GermOnline	ENSG00000169169. Homo sapiens.
Family and domain databases
InterPro	IPR000542. Carn_acyl_trans. [Graphical view]
PANTHER	PTHR22589. PTHR22589. 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
GenomeRNAi	126129.
NextBio	81696.
SOURCE	Search...

Entry information

Entry name

CPT1C_HUMAN

Accession

Primary (citable) accession number: Q8TCG5
Secondary accession number(s): A8K0Z8 , Q5K6N5, Q8N6Q9, Q8NDS6, Q8TE84

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 5, 2004
Last sequence update:	June 1, 2002
Last modified:	May 1, 2013
This is version 94 of the entry and version 1 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.