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Q8TCG5 (CPT1C_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 106. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length803 AA.
Sequence statusComplete.
Protein existenceEvidence at protein 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 junctionsynapse 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.

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 803803Carnitine O-palmitoyltransferase 1, brain isoform
PRO_0000210166

Regions

Topological domain1 – 5252Cytoplasmic Potential
Transmembrane53 – 7523Helical; Potential
Topological domain76 – 10328Mitochondrial intermembrane Potential
Transmembrane104 – 12623Helical; Potential
Topological domain127 – 803677Cytoplasmic Potential
Region552 – 56413Coenzyme A binding By similarity

Sites

Active site4701Proton acceptor By similarity
Binding site5861Carnitine By similarity
Binding site5881Carnitine By similarity
Binding site5891Coenzyme A By similarity
Binding site5991Carnitine By similarity

Natural variations

Alternative sequence258 – 26811Missing in isoform 2.
VSP_010677
Alternative sequence623 – 71189Missing in isoform 3.
VSP_012457

Experimental info

Sequence conflict581S → G in BAF82402. Ref.3
Sequence conflict375 – 3784HEEH → RTRG in CAD38561. Ref.6
Sequence conflict5421D → G in BAB85068. Ref.3

Secondary structure

..... 803
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: 96C2AE6ED0DEC705

FASTA80390,989
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 3420B3FE0457E895
Show »

FASTA79289,713
Isoform 3 [UniParc].

Checksum: 4435ECAA8502D6BA
Show »

FASTA71481,000

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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.
CCDSCCDS12779.1. [Q8TCG5-1]
CCDS46147.1. [Q8TCG5-2]
RefSeqNP_001129524.1. NM_001136052.2. [Q8TCG5-2]
NP_001186681.1. NM_001199752.2. [Q8TCG5-1]
NP_001186682.1. NM_001199753.1. [Q8TCG5-1]
NP_689572.1. NM_152359.2. [Q8TCG5-1]
XP_005258562.1. XM_005258505.2. [Q8TCG5-1]
XP_005258563.1. XM_005258506.2. [Q8TCG5-1]
UniGeneHs.112195.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2M76NMR-A1-50[»]
ProteinModelPortalQ8TCG5.
SMRQ8TCG5. Positions 1-50, 180-764.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid125958. 1 interaction.
MINTMINT-6631074.
STRING9606.ENSP00000319343.

PTM databases

PhosphoSiteQ8TCG5.

Polymorphism databases

DMDM57013809.

Proteomic databases

PaxDbQ8TCG5.
PRIDEQ8TCG5.

Protocols and materials databases

DNASU126129.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000323446; ENSP00000319343; ENSG00000169169. [Q8TCG5-1]
ENST00000354199; ENSP00000346138; ENSG00000169169. [Q8TCG5-3]
ENST00000392518; ENSP00000376303; ENSG00000169169. [Q8TCG5-1]
ENST00000405931; ENSP00000384465; ENSG00000169169. [Q8TCG5-2]
ENST00000598293; ENSP00000473028; ENSG00000169169. [Q8TCG5-1]
GeneID126129.
KEGGhsa:126129.
UCSCuc002ppi.3. human. [Q8TCG5-1]
uc002ppk.3. human. [Q8TCG5-2]
uc010eni.1. human. [Q8TCG5-3]

Organism-specific databases

CTD126129.
GeneCardsGC19P050199.
HGNCHGNC:18540. CPT1C.
HPAHPA014529.
MIM608846. gene.
neXtProtNX_Q8TCG5.
PharmGKBPA134922321.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG272759.
HOGENOMHOG000233542.
HOVERGENHBG003458.
InParanoidQ8TCG5.
KOK08765.
OMAIDCHVFP.
OrthoDBEOG7J17ZQ.
PhylomeDBQ8TCG5.
TreeFamTF313836.

Enzyme and pathway databases

BioCycMetaCyc:HS09892-MONOMER.
UniPathwayUPA00659.

Gene expression databases

ArrayExpressQ8TCG5.
BgeeQ8TCG5.
CleanExHS_CPT1C.
GenevestigatorQ8TCG5.

Family and domain databases

InterProIPR000542. Carn_acyl_trans.
[Graphical view]
PANTHERPTHR22589. PTHR22589. 1 hit.
PfamPF00755. Carn_acyltransf. 1 hit.
[Graphical view]
PROSITEPS00439. ACYLTRANSF_C_1. 1 hit.
PS00440. ACYLTRANSF_C_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi126129.
NextBio81696.
PROQ8TCG5.
SOURCESearch...

Entry information

Entry nameCPT1C_HUMAN
AccessionPrimary (citable) accession number: Q8TCG5
Secondary accession number(s): A8K0Z8 expand/collapse secondary AC list , Q5K6N5, Q8N6Q9, Q8NDS6, Q8TE84
Entry history
Integrated into UniProtKB/Swiss-Prot: July 5, 2004
Last sequence update: June 1, 2002
Last modified: July 9, 2014
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM