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Q8BGD5 (CPT1C_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 82. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length798 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. Ref.4

Subcellular location

Mitochondrion outer membrane; Multi-pass membrane protein By similarity. Cell junction › synapse Probable Ref.4.

Tissue specificity

Predominantly expressed in brain (at protein level) and testis. Ref.1 Ref.4

Sequence similarities

Belongs to the carnitine/choline acetyltransferase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 798798Carnitine O-palmitoyltransferase 1, brain isoform
PRO_0000210167

Regions

Topological domain1 – 5252Cytoplasmic Potential
Transmembrane53 – 7523Helical; Potential
Topological domain76 – 10328Mitochondrial intermembrane Potential
Transmembrane104 – 12623Helical; Potential
Topological domain127 – 798672Cytoplasmic Potential
Region551 – 56313Coenzyme A binding By similarity

Sites

Active site4691Proton acceptor By similarity
Binding site5851Carnitine By similarity
Binding site5871Carnitine By similarity
Binding site5881Coenzyme A By similarity
Binding site5981Carnitine By similarity

Experimental info

Sequence conflict1041F → L in AAH66155. Ref.3
Sequence conflict1951G → R in AAH66155. Ref.3
Sequence conflict3241R → C in AAH66155. Ref.3
Sequence conflict5591H → Q in AAH66155. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q8BGD5 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: A4886121168E8046

FASTA79890,030
        10         20         30         40         50         60 
MAEAHQASSL LSSLSSDGAE VELSSPVWQE IYLCALRSWK RHLWRVWNDF LAGVVPATPL 

        70         80         90        100        110        120 
SWLFLFSTIQ LACLLQLDPS LGLMEKIKEL LPDWGGQHHQ LQGFLSAAVF ASCLWGALIF 

       130        140        150        160        170        180 
TLHVALRLLL SHHGWLLEPH GAMSSPTKTW LALVRIFSGR HPRLFSFQRA LPRQPVPSAQ 

       190        200        210        220        230        240 
ETVRKYLESV RPVLGDDAFD RATALANDFL RLHAPRLQLY LQLKSWCTSN YVSDWWEEFV 

       250        260        270        280        290        300 
YLRSRGSLIN STYYMMDFLY VTPTPLQAAR AGNAVHTLLL YRHLLNRQEI SPTLLMGMRP 

       310        320        330        340        350        360 
LCSAQYERMF NTTRIPGVEK DHLRHLQDSR HVAVFHRGRF FRVGTHSPNG LLSPRALEQQ 

       370        380        390        400        410        420 
FQDILDDPSP ACPLEEHLAA LTAAPRSMWA QVRESVKTHA ATALEAVEGA AFFVSLDSEP 

       430        440        450        460        470        480 
AGLTREDPAA SLDAYAHALL AGRGHDRWFD KSFTLIVFSN GKLGLSVEHS WADCPVSGHL 

       490        500        510        520        530        540 
WEFTLATECF QLGYATDGHC KGHPDPTLPQ PQRLQWDLPE QIQPSISLAL RGAKTLSGNI 

       550        560        570        580        590        600 
DCHVFPFSHF GKSFIKCCHV SSDSFIQLVL QLAHFRDRGQ FCLTYESAMT RLFLEGRTET 

       610        620        630        640        650        660 
VRSCTREACQ FVRAMDNKET DQHCLALFRV AVDKHQALLK AAMSGQGIDR HLFALYIMSR 

       670        680        690        700        710        720 
LLHMQSPFLT QVQSQQWLLS TSQVPVQQTH LIDVHNYPDY VSSGGGFGPA HDHGYGISYI 

       730        740        750        760        770        780 
FMGENAITFH ISSKKSSTET DSHRLGQHIE NALLDVASLF RVGQHFKRQF RGENSDYRYN 

       790 
FLSCKTVDPN TPTSSTNL

« Hide

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], TISSUE SPECIFICITY.
Strain: C57BL/6J.
Tissue: Embryo.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Cerebellum and Medulla oblongata.
[3]"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].
Strain: CD-1.
Tissue: Neural stem cell.
[4]"High-resolution proteomics unravel architecture and molecular diversity of native AMPA receptor complexes."
Schwenk J., Harmel N., Brechet A., Zolles G., Berkefeld H., Muller C.S., Bildl W., Baehrens D., Huber B., Kulik A., Klocker N., Schulte U., Fakler B.
Neuron 74:621-633(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN AMPAR COMPLEX, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF320000 mRNA. Translation: AAN39013.1.
AK032101 mRNA. Translation: BAC27700.1.
AK035790 mRNA. Translation: BAC29187.1.
BC066155 mRNA. Translation: AAH66155.1.
IPIIPI00221577.
RefSeqNP_001239399.1. NM_001252470.1.
NP_710146.1. NM_153679.2.
UniGeneMm.231465.

3D structure databases

ProteinModelPortalQ8BGD5.
SMRQ8BGD5. Positions 170-759.
ModBaseSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000069539.

PTM databases

PhosphoSiteQ8BGD5.

Proteomic databases

PaxDbQ8BGD5.
PRIDEQ8BGD5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000063761; ENSMUSP00000069539; ENSMUSG00000007783.
GeneID78070.
KEGGmmu:78070.
UCSCuc009gsb.1. mouse.

Organism-specific databases

CTD126129.
MGIMGI:2446526. Cpt1c.

Phylogenomic databases

eggNOGNOG272759.
GeneTreeENSGT00550000074345.
HOGENOMHOG000233542.
HOVERGENHBG003458.
InParanoidQ8BGD5.
KOK08765.
OMAIDCHVFP.
OrthoDBEOG4X3H0Q.

Enzyme and pathway databases

UniPathwayUPA00659.

Gene expression databases

ArrayExpressQ8BGD5.
BgeeQ8BGD5.
CleanExMM_CPT1C.
GenevestigatorQ8BGD5.
GermOnlineENSMUSG00000007783. Mus musculus.

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

NextBio348140.
SOURCESearch...

Entry information

Entry nameCPT1C_MOUSE
AccessionPrimary (citable) accession number: Q8BGD5
Secondary accession number(s): Q6NZF8, Q8C071
Entry history
Integrated into UniProtKB/Swiss-Prot: July 5, 2004
Last sequence update: March 1, 2003
Last modified: May 1, 2013
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents