CPT1C_MOUSE
ID CPT1C_MOUSE Reviewed; 798 AA.
AC Q8BGD5; Q6NZF8; Q8C071;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Carnitine O-palmitoyltransferase 1, brain isoform;
DE Short=CPT1-B;
DE EC=2.3.1.21;
DE AltName: Full=CPT IC;
DE AltName: Full=Carnitine O-palmitoyltransferase I, brain isoform;
DE Short=CPTI-B;
DE AltName: Full=Carnitine palmitoyltransferase 1C;
GN Name=Cpt1c;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=12376098; DOI=10.1006/geno.2002.6845;
RA Price N., van der Leij F.R., Jackson V., Corstorphine C., Thomson R.,
RA Sorensen A., Zammit V.;
RT "A novel brain-expressed protein related to carnitine palmitoyltransferase
RT I.";
RL Genomics 80:433-442(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, and Medulla oblongata;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CD-1; TISSUE=Neural stem cell;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP IDENTIFICATION IN AMPAR COMPLEX, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=22632720; DOI=10.1016/j.neuron.2012.03.034;
RA Schwenk J., Harmel N., Brechet A., Zolles G., Berkefeld H., Muller C.S.,
RA Bildl W., Baehrens D., Huber B., Kulik A., Klocker N., Schulte U.,
RA Fakler B.;
RT "High-resolution proteomics unravel architecture and molecular diversity of
RT native AMPA receptor complexes.";
RL Neuron 74:621-633(2012).
RN [6]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=25751282; DOI=10.1001/jamaneurol.2014.4769;
RA Rinaldi C., Schmidt T., Situ A.J., Johnson J.O., Lee P.R., Chen K.L.,
RA Bott L.C., Fado R., Harmison G.H., Parodi S., Grunseich C., Renvoise B.,
RA Biesecker L.G., De Michele G., Santorelli F.M., Filla A., Stevanin G.,
RA Duerr A., Brice A., Casals N., Traynor B.J., Blackstone C., Ulmer T.S.,
RA Fischbeck K.H.;
RT "Mutation in CPT1C Associated with pure autosomal dominant spastic
RT paraplegia.";
RL JAMA Neurol. 72:561-570(2015).
CC -!- FUNCTION: May play a role in lipid metabolic process.
CC {ECO:0000250|UniProtKB:Q8TCG5}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-carnitine + hexadecanoyl-CoA = CoA + O-hexadecanoyl-(R)-
CC carnitine; Xref=Rhea:RHEA:12661, ChEBI:CHEBI:16347,
CC ChEBI:CHEBI:17490, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379; EC=2.3.1.21;
CC -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC -!- SUBUNIT: Peripherally associated with AMPAR complex. AMPAR complex
CC consists of an inner core made of 4 pore-forming GluA/GRIA proteins
CC (GRIA1, GRIA2, GRIA3 and GRIA4) and 4 major auxiliary subunits arranged
CC in a twofold symmetry. One of the two pairs of distinct binding sites
CC is occupied either by CNIH2, CNIH3 or CACNG2, CACNG3. The other harbors
CC CACNG2, CACNG3, CACNG4, CACNG8 or GSG1L. This inner core of AMPAR
CC complex is complemented by outer core constituents binding directly to
CC the GluA/GRIA proteins at sites distinct from the interaction sites of
CC the inner core constituents. Outer core constituents include at least
CC PRRT1, PRRT2, CKAMP44/SHISA9, FRRS1L and NRN1. The proteins of the
CC inner and outer core serve as a platform for other, more peripherally
CC associated AMPAR constituents, including CPT1C. Alone or in
CC combination, these auxiliary subunits control the gating and
CC pharmacology of the AMPAR complex and profoundly impact their
CC biogenesis and protein processing. Interacts with ATL1 (By similarity).
CC {ECO:0000250|UniProtKB:Q8TCG5, ECO:0000269|PubMed:22632720}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}. Synapse
CC {ECO:0000305|PubMed:22632720}. Cell projection, axon
CC {ECO:0000269|PubMed:25751282}. Cell projection, dendrite
CC {ECO:0000269|PubMed:25751282}. Endoplasmic reticulum
CC {ECO:0000269|PubMed:25751282}. Note=Localized in the soma and dendritic
CC and axonal projections. {ECO:0000269|PubMed:25751282}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in brain (at protein level)
CC and testis. Expressed in motor neurons (PubMed:25751282). Expressed in
CC the ventral horn from spinal cords (PubMed:25751282).
CC {ECO:0000269|PubMed:12376098, ECO:0000269|PubMed:22632720,
CC ECO:0000269|PubMed:25751282}.
CC -!- SIMILARITY: Belongs to the carnitine/choline acetyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AF320000; AAN39013.1; -; mRNA.
DR EMBL; AK032101; BAC27700.1; -; mRNA.
DR EMBL; AK035790; BAC29187.1; -; mRNA.
DR EMBL; BC066155; AAH66155.1; -; mRNA.
DR CCDS; CCDS21221.1; -.
DR RefSeq; NP_001239399.1; NM_001252470.1.
DR RefSeq; NP_710146.1; NM_153679.2.
DR AlphaFoldDB; Q8BGD5; -.
DR SMR; Q8BGD5; -.
DR BioGRID; 219139; 2.
DR STRING; 10090.ENSMUSP00000069539; -.
DR iPTMnet; Q8BGD5; -.
DR PhosphoSitePlus; Q8BGD5; -.
DR SwissPalm; Q8BGD5; -.
DR MaxQB; Q8BGD5; -.
DR PaxDb; Q8BGD5; -.
DR PeptideAtlas; Q8BGD5; -.
DR PRIDE; Q8BGD5; -.
DR ProteomicsDB; 285260; -.
DR Antibodypedia; 3052; 273 antibodies from 33 providers.
DR DNASU; 78070; -.
DR Ensembl; ENSMUST00000063761; ENSMUSP00000069539; ENSMUSG00000007783.
DR Ensembl; ENSMUST00000212836; ENSMUSP00000148815; ENSMUSG00000007783.
DR GeneID; 78070; -.
DR KEGG; mmu:78070; -.
DR UCSC; uc009gsb.2; mouse.
DR CTD; 126129; -.
DR MGI; MGI:2446526; Cpt1c.
DR VEuPathDB; HostDB:ENSMUSG00000007783; -.
DR eggNOG; KOG3716; Eukaryota.
DR GeneTree; ENSGT01050000244830; -.
DR HOGENOM; CLU_013513_2_1_1; -.
DR InParanoid; Q8BGD5; -.
DR OMA; VYSEQWQ; -.
DR OrthoDB; 559299at2759; -.
DR PhylomeDB; Q8BGD5; -.
DR TreeFam; TF313836; -.
DR BRENDA; 2.3.1.21; 3474.
DR UniPathway; UPA00659; -.
DR BioGRID-ORCS; 78070; 8 hits in 76 CRISPR screens.
DR ChiTaRS; Cpt1c; mouse.
DR PRO; PR:Q8BGD5; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q8BGD5; protein.
DR Bgee; ENSMUSG00000007783; Expressed in humerus cartilage element and 227 other tissues.
DR ExpressionAtlas; Q8BGD5; baseline and differential.
DR Genevisible; Q8BGD5; MM.
DR GO; GO:0032281; C:AMPA glutamate receptor complex; IDA:MGI.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; IDA:UniProtKB.
DR GO; GO:0030425; C:dendrite; IDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA:SynGO.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0098794; C:postsynapse; IDA:SynGO.
DR GO; GO:0004095; F:carnitine O-palmitoyltransferase activity; ISO:MGI.
DR GO; GO:0009437; P:carnitine metabolic process; ISO:MGI.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IEA:UniProtKB-UniPathway.
DR GO; GO:0006631; P:fatty acid metabolic process; IBA:GO_Central.
DR GO; GO:0099072; P:regulation of postsynaptic membrane neurotransmitter receptor levels; IDA:SynGO.
DR Gene3D; 3.30.559.10; -; 1.
DR Gene3D; 3.30.559.70; -; 1.
DR InterPro; IPR000542; Carn_acyl_trans.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR039551; Cho/carn_acyl_trans.
DR InterPro; IPR042231; Cho/carn_acyl_trans_2.
DR InterPro; IPR032476; CPT_N.
DR PANTHER; PTHR22589; PTHR22589; 1.
DR Pfam; PF00755; Carn_acyltransf; 1.
DR Pfam; PF16484; CPT_N; 1.
DR PROSITE; PS00439; ACYLTRANSF_C_1; 1.
DR PROSITE; PS00440; ACYLTRANSF_C_2; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Cell projection; Endoplasmic reticulum;
KW Fatty acid metabolism; Lipid metabolism; Membrane; Mitochondrion;
KW Mitochondrion outer membrane; Reference proteome; Synapse; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..798
FT /note="Carnitine O-palmitoyltransferase 1, brain isoform"
FT /id="PRO_0000210167"
FT TOPO_DOM 1..52
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 53..75
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 76..103
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 104..126
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 127..798
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ACT_SITE 469
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 551..563
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 585
FT /ligand="(R)-carnitine"
FT /ligand_id="ChEBI:CHEBI:16347"
FT /evidence="ECO:0000250"
FT BINDING 587
FT /ligand="(R)-carnitine"
FT /ligand_id="ChEBI:CHEBI:16347"
FT /evidence="ECO:0000250"
FT BINDING 598
FT /ligand="(R)-carnitine"
FT /ligand_id="ChEBI:CHEBI:16347"
FT /evidence="ECO:0000250"
FT CONFLICT 104
FT /note="F -> L (in Ref. 3; AAH66155)"
FT /evidence="ECO:0000305"
FT CONFLICT 195
FT /note="G -> R (in Ref. 3; AAH66155)"
FT /evidence="ECO:0000305"
FT CONFLICT 324
FT /note="R -> C (in Ref. 3; AAH66155)"
FT /evidence="ECO:0000305"
FT CONFLICT 559
FT /note="H -> Q (in Ref. 3; AAH66155)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 798 AA; 90030 MW; A4886121168E8046 CRC64;
MAEAHQASSL LSSLSSDGAE VELSSPVWQE IYLCALRSWK RHLWRVWNDF LAGVVPATPL
SWLFLFSTIQ LACLLQLDPS LGLMEKIKEL LPDWGGQHHQ LQGFLSAAVF ASCLWGALIF
TLHVALRLLL SHHGWLLEPH GAMSSPTKTW LALVRIFSGR HPRLFSFQRA LPRQPVPSAQ
ETVRKYLESV RPVLGDDAFD RATALANDFL RLHAPRLQLY LQLKSWCTSN YVSDWWEEFV
YLRSRGSLIN STYYMMDFLY VTPTPLQAAR AGNAVHTLLL YRHLLNRQEI SPTLLMGMRP
LCSAQYERMF NTTRIPGVEK DHLRHLQDSR HVAVFHRGRF FRVGTHSPNG LLSPRALEQQ
FQDILDDPSP ACPLEEHLAA LTAAPRSMWA QVRESVKTHA ATALEAVEGA AFFVSLDSEP
AGLTREDPAA SLDAYAHALL AGRGHDRWFD KSFTLIVFSN GKLGLSVEHS WADCPVSGHL
WEFTLATECF QLGYATDGHC KGHPDPTLPQ PQRLQWDLPE QIQPSISLAL RGAKTLSGNI
DCHVFPFSHF GKSFIKCCHV SSDSFIQLVL QLAHFRDRGQ FCLTYESAMT RLFLEGRTET
VRSCTREACQ FVRAMDNKET DQHCLALFRV AVDKHQALLK AAMSGQGIDR HLFALYIMSR
LLHMQSPFLT QVQSQQWLLS TSQVPVQQTH LIDVHNYPDY VSSGGGFGPA HDHGYGISYI
FMGENAITFH ISSKKSSTET DSHRLGQHIE NALLDVASLF RVGQHFKRQF RGENSDYRYN
FLSCKTVDPN TPTSSTNL
