CPT1C_RAT
ID CPT1C_RAT Reviewed; 801 AA.
AC F1LN46;
DT 09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 63.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
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:Q8BGD5}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}. Synapse
CC {ECO:0000250|UniProtKB:Q8BGD5}. Cell projection, dendrite
CC {ECO:0000250|UniProtKB:Q8BGD5}. Cell projection, axon
CC {ECO:0000250|UniProtKB:Q8BGD5}. Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:Q8BGD5}. Note=Localized in the soma and
CC dendritic and axonal projections. {ECO:0000250|UniProtKB:Q8BGD5}.
CC -!- TISSUE SPECIFICITY: Expressed in brain (at protein level).
CC -!- SIMILARITY: Belongs to the carnitine/choline acetyltransferase family.
CC {ECO:0000305}.
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DR RefSeq; NP_001030097.2; NM_001034925.2.
DR AlphaFoldDB; F1LN46; -.
DR SMR; F1LN46; -.
DR CORUM; F1LN46; -.
DR STRING; 10116.ENSRNOP00000032802; -.
DR PaxDb; F1LN46; -.
DR PRIDE; F1LN46; -.
DR GeneID; 308579; -.
DR KEGG; rno:308579; -.
DR CTD; 126129; -.
DR RGD; 1305384; Cpt1c.
DR VEuPathDB; HostDB:ENSRNOG00000026163; -.
DR eggNOG; KOG3716; Eukaryota.
DR HOGENOM; CLU_013513_2_1_1; -.
DR InParanoid; F1LN46; -.
DR OMA; VYSEQWQ; -.
DR OrthoDB; 559299at2759; -.
DR TreeFam; TF313836; -.
DR UniPathway; UPA00659; -.
DR PRO; PR:F1LN46; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000026163; Expressed in frontal cortex and 20 other tissues.
DR Genevisible; F1LN46; RN.
DR GO; GO:0032281; C:AMPA glutamate receptor complex; ISO:RGD.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; ISS:UniProtKB.
DR GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISO:RGD.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0098794; C:postsynapse; ISO:RGD.
DR GO; GO:0004095; F:carnitine O-palmitoyltransferase activity; IDA:RGD.
DR GO; GO:0009437; P:carnitine metabolic process; IDA:RGD.
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; ISO:RGD.
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..801
FT /note="Carnitine O-palmitoyltransferase 1, brain isoform"
FT /id="PRO_0000420690"
FT TOPO_DOM 1..49
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 50..70
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 71..103
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 104..124
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 125..801
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"
SQ SEQUENCE 801 AA; 90170 MW; C2ED0FC31EABBF8B CRC64;
MAEAHQASSL LSSLSSDGAE VELSSSVWQE IYLSALRSWK RNLWRVWNDF LAGVVPATPL
SWLFLFSTIQ LACLLQLDPS LGLMEKIKEL LPDWGGQHHQ LQGLLAAAVF ASCLWGTLIF
TLHVALRLLL SHHGWLLEPH GTMSSPTKTW LALVRIFSGR HPRLFSFQRA LPRQPVPGAQ
ETVRKYLESM RPVLRDDAFD SVVALANDFL RLQAPRLQLY LQLKSWCASN YVSDWWEEFV
YLRSRGSLVN STYYMMDFLY VTPTPLQAAR AGNAVHTLLL YRHLLNRQEI PPTLLMGMRP
LCSAQYERMF NTTRIPGVEK DYLCHLQDSQ HVAVFHQGRF FRVGTHSSNG LLSPRALEQQ
FQYILDDPSP ACPLEEHLAA LTAAPRSMWA QVRESVKTHA ATALETVEGA AFFVSLDSEP
AGLTRENPAA SLDTYAHTLL TGQGHDRWFD KSFTLIVFSN GKLGLSVEHS WADCPVAGHL
WEFTLATECF QLGYATDGHC KGHPDPALPK PQRLQWDLPK QIQPSISLAL RGAKTLSGNI
DCHVFPFFHF GKSFIKGCHV SSDSFIQLVL QLAHFRDRGQ FCLTYESAMT RLFLEGRTET
VRSCTREACQ FVRAMENKER TDQQCLALFR EAVDKHQALL KAAMSGQGID RHLFALYIMS
RLLHMQSPFL TQVQSQQWLL STSQIPVQQT HLFDVHNYPD YVSSGGGFGP AHDHGYGVSY
IFMGENAISF HISSKQSSTE TDSHRLGQHI EDALLDVASL FQAGQQFKRQ FTGLGESSGW
KYSNLSCKTV DPNIPKSSTN L
