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Protein

Carnitine O-palmitoyltransferase 1, brain isoform

Gene

Cpt1c

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

May play a role in lipid metabolic process.By similarity

Catalytic activityi

Palmitoyl-CoA + L-carnitine = CoA + L-palmitoylcarnitine.

Pathwayi: fatty acid beta-oxidation

This protein is involved in the pathway fatty acid beta-oxidation, which is part of Lipid metabolism.
View all proteins of this organism that are known to be involved in the pathway fatty acid beta-oxidation and in Lipid metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei469 – 4691Proton acceptorBy similarity
Binding sitei585 – 5851CarnitineBy similarity
Binding sitei587 – 5871CarnitineBy similarity
Binding sitei588 – 5881Coenzyme ABy similarity
Binding sitei598 – 5981CarnitineBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Enzyme and pathway databases

BRENDAi2.3.1.21. 3474.
UniPathwayiUPA00659.

Names & Taxonomyi

Protein namesi
Recommended name:
Carnitine O-palmitoyltransferase 1, brain isoform (EC:2.3.1.21)
Short name:
CPT1-B
Alternative name(s):
CPT IC
Carnitine O-palmitoyltransferase I, brain isoform
Short name:
CPTI-B
Carnitine palmitoyltransferase 1C
Gene namesi
Name:Cpt1c
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:2446526. Cpt1c.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 5252CytoplasmicSequence analysisAdd
BLAST
Transmembranei53 – 7523HelicalSequence analysisAdd
BLAST
Topological domaini76 – 10328Mitochondrial intermembraneSequence analysisAdd
BLAST
Transmembranei104 – 12623HelicalSequence analysisAdd
BLAST
Topological domaini127 – 798672CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • AMPA glutamate receptor complex Source: MGI
  • axon Source: UniProtKB
  • cell junction Source: UniProtKB-KW
  • dendrite Source: UniProtKB
  • endoplasmic reticulum Source: UniProtKB
  • endoplasmic reticulum membrane Source: Ensembl
  • mitochondrial outer membrane Source: UniProtKB-SubCell
  • mitochondrion Source: MGI
  • synapse Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell projection, Endoplasmic reticulum, Membrane, Mitochondrion, Mitochondrion outer membrane, Synapse

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 798798Carnitine O-palmitoyltransferase 1, brain isoformPRO_0000210167Add
BLAST

Proteomic databases

MaxQBiQ8BGD5.
PaxDbiQ8BGD5.
PRIDEiQ8BGD5.

PTM databases

PhosphoSiteiQ8BGD5.
SwissPalmiQ8BGD5.

Expressioni

Tissue specificityi

Predominantly expressed in brain (at protein level) and testis. Expressed in motor neurons (PubMed:25751282). Expressed in the ventral horn from spinal cords (PubMed:25751282).3 Publications

Gene expression databases

BgeeiQ8BGD5.
CleanExiMM_CPT1C.
GenevisibleiQ8BGD5. MM.

Interactioni

Subunit structurei

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. Interacts with ATL1 (By similarity).By similarity1 Publication

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000069539.

Structurei

3D structure databases

ProteinModelPortaliQ8BGD5.
SMRiQ8BGD5. Positions 1-50, 170-759.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni551 – 56313Coenzyme A bindingBy similarityAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3717. Eukaryota.
ENOG410XNZ9. LUCA.
GeneTreeiENSGT00760000119220.
HOGENOMiHOG000233542.
HOVERGENiHBG003458.
InParanoidiQ8BGD5.
KOiK19524.
OMAiIDCHVFP.
OrthoDBiEOG7J17ZQ.
PhylomeDBiQ8BGD5.
TreeFamiTF313836.

Family and domain databases

InterProiIPR000542. Carn_acyl_trans.
IPR032476. CPT_N.
[Graphical view]
PANTHERiPTHR22589. PTHR22589. 1 hit.
PfamiPF00755. Carn_acyltransf. 1 hit.
PF16484. CPT_N. 1 hit.
[Graphical view]
PROSITEiPS00439. ACYLTRANSF_C_1. 1 hit.
PS00440. ACYLTRANSF_C_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8BGD5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAEAHQASSL LSSLSSDGAE VELSSPVWQE IYLCALRSWK RHLWRVWNDF
60 70 80 90 100
LAGVVPATPL SWLFLFSTIQ LACLLQLDPS LGLMEKIKEL LPDWGGQHHQ
110 120 130 140 150
LQGFLSAAVF ASCLWGALIF TLHVALRLLL SHHGWLLEPH GAMSSPTKTW
160 170 180 190 200
LALVRIFSGR HPRLFSFQRA LPRQPVPSAQ ETVRKYLESV RPVLGDDAFD
210 220 230 240 250
RATALANDFL RLHAPRLQLY LQLKSWCTSN YVSDWWEEFV YLRSRGSLIN
260 270 280 290 300
STYYMMDFLY VTPTPLQAAR AGNAVHTLLL YRHLLNRQEI SPTLLMGMRP
310 320 330 340 350
LCSAQYERMF NTTRIPGVEK DHLRHLQDSR HVAVFHRGRF FRVGTHSPNG
360 370 380 390 400
LLSPRALEQQ FQDILDDPSP ACPLEEHLAA LTAAPRSMWA QVRESVKTHA
410 420 430 440 450
ATALEAVEGA AFFVSLDSEP AGLTREDPAA SLDAYAHALL AGRGHDRWFD
460 470 480 490 500
KSFTLIVFSN GKLGLSVEHS WADCPVSGHL WEFTLATECF QLGYATDGHC
510 520 530 540 550
KGHPDPTLPQ PQRLQWDLPE QIQPSISLAL RGAKTLSGNI DCHVFPFSHF
560 570 580 590 600
GKSFIKCCHV SSDSFIQLVL QLAHFRDRGQ FCLTYESAMT RLFLEGRTET
610 620 630 640 650
VRSCTREACQ FVRAMDNKET DQHCLALFRV AVDKHQALLK AAMSGQGIDR
660 670 680 690 700
HLFALYIMSR LLHMQSPFLT QVQSQQWLLS TSQVPVQQTH LIDVHNYPDY
710 720 730 740 750
VSSGGGFGPA HDHGYGISYI FMGENAITFH ISSKKSSTET DSHRLGQHIE
760 770 780 790
NALLDVASLF RVGQHFKRQF RGENSDYRYN FLSCKTVDPN TPTSSTNL
Length:798
Mass (Da):90,030
Last modified:March 1, 2003 - v1
Checksum:iA4886121168E8046
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti104 – 1041F → L in AAH66155 (PubMed:15489334).Curated
Sequence conflicti195 – 1951G → R in AAH66155 (PubMed:15489334).Curated
Sequence conflicti324 – 3241R → C in AAH66155 (PubMed:15489334).Curated
Sequence conflicti559 – 5591H → Q in AAH66155 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF320000 mRNA. Translation: AAN39013.1.
AK032101 mRNA. Translation: BAC27700.1.
AK035790 mRNA. Translation: BAC29187.1.
BC066155 mRNA. Translation: AAH66155.1.
CCDSiCCDS21221.1.
RefSeqiNP_001239399.1. NM_001252470.1.
NP_710146.1. NM_153679.2.
UniGeneiMm.231465.

Genome annotation databases

EnsembliENSMUST00000063761; ENSMUSP00000069539; ENSMUSG00000007783.
GeneIDi78070.
KEGGimmu:78070.
UCSCiuc009gsb.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF320000 mRNA. Translation: AAN39013.1.
AK032101 mRNA. Translation: BAC27700.1.
AK035790 mRNA. Translation: BAC29187.1.
BC066155 mRNA. Translation: AAH66155.1.
CCDSiCCDS21221.1.
RefSeqiNP_001239399.1. NM_001252470.1.
NP_710146.1. NM_153679.2.
UniGeneiMm.231465.

3D structure databases

ProteinModelPortaliQ8BGD5.
SMRiQ8BGD5. Positions 1-50, 170-759.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000069539.

PTM databases

PhosphoSiteiQ8BGD5.
SwissPalmiQ8BGD5.

Proteomic databases

MaxQBiQ8BGD5.
PaxDbiQ8BGD5.
PRIDEiQ8BGD5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000063761; ENSMUSP00000069539; ENSMUSG00000007783.
GeneIDi78070.
KEGGimmu:78070.
UCSCiuc009gsb.2. mouse.

Organism-specific databases

CTDi126129.
MGIiMGI:2446526. Cpt1c.

Phylogenomic databases

eggNOGiKOG3717. Eukaryota.
ENOG410XNZ9. LUCA.
GeneTreeiENSGT00760000119220.
HOGENOMiHOG000233542.
HOVERGENiHBG003458.
InParanoidiQ8BGD5.
KOiK19524.
OMAiIDCHVFP.
OrthoDBiEOG7J17ZQ.
PhylomeDBiQ8BGD5.
TreeFamiTF313836.

Enzyme and pathway databases

UniPathwayiUPA00659.
BRENDAi2.3.1.21. 3474.

Miscellaneous databases

NextBioi348140.
PROiQ8BGD5.
SOURCEiSearch...

Gene expression databases

BgeeiQ8BGD5.
CleanExiMM_CPT1C.
GenevisibleiQ8BGD5. MM.

Family and domain databases

InterProiIPR000542. Carn_acyl_trans.
IPR032476. CPT_N.
[Graphical view]
PANTHERiPTHR22589. PTHR22589. 1 hit.
PfamiPF00755. Carn_acyltransf. 1 hit.
PF16484. CPT_N. 1 hit.
[Graphical view]
PROSITEiPS00439. ACYLTRANSF_C_1. 1 hit.
PS00440. ACYLTRANSF_C_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain and Testis.
  5. "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.
  6. Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.

Entry informationi

Entry nameiCPT1C_MOUSE
AccessioniPrimary (citable) accession number: Q8BGD5
Secondary accession number(s): Q6NZF8, Q8C071
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 5, 2004
Last sequence update: March 1, 2003
Last modified: February 17, 2016
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.