CPT1B_RAT
ID CPT1B_RAT Reviewed; 772 AA.
AC Q63704;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Carnitine O-palmitoyltransferase 1, muscle isoform;
DE Short=CPT1-M;
DE EC=2.3.1.21 {ECO:0000269|PubMed:8636126};
DE AltName: Full=Carnitine O-palmitoyltransferase I, muscle isoform;
DE Short=CPT I;
DE Short=CPTI-M;
DE AltName: Full=Carnitine palmitoyltransferase 1B;
DE AltName: Full=Carnitine palmitoyltransferase I-like protein;
GN Name=Cpt1b;
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 [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=Wistar; TISSUE=Brown adipose tissue;
RX PubMed=7729550; DOI=10.1016/0014-5793(95)00277-g;
RA Yamazaki N., Shinohara Y., Shima A., Terada H.;
RT "High expression of a novel carnitine palmitoyltransferase I like protein
RT in rat brown adipose tissue and heart: isolation and characterization of
RT its cDNA clone.";
RL FEBS Lett. 363:41-45(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, TISSUE SPECIFICITY,
RP SUBCELLULAR LOCATION, AND ACTIVITY REGULATION.
RC STRAIN=Sprague-Dawley; TISSUE=Heart;
RX PubMed=8636126; DOI=10.1074/jbc.271.12.6972;
RA Esser V., Brown N.F., Cowan A.T., Foster D.W., McGarry J.D.;
RT "Expression of a cDNA isolated from rat brown adipose tissue and heart
RT identifies the product as the muscle isoform of carnitine
RT palmitoyltransferase I (M-CPT I). M-CPT I is the predominant CPT I isoform
RT expressed in both white (epididymal) and brown adipocytes.";
RL J. Biol. Chem. 271:6972-6977(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
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).
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 Evidence={ECO:0000269|PubMed:8636126};
CC -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000305|PubMed:8636126}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: High expression in heart, skeletal muscle and brown
CC adipose tissue. Also expressed in white adipose tissue, but not in
CC liver. {ECO:0000269|PubMed:7729550, ECO:0000269|PubMed:8636126}.
CC -!- SIMILARITY: Belongs to the carnitine/choline acetyltransferase family.
CC {ECO:0000305}.
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DR EMBL; D43623; BAA07733.1; -; mRNA.
DR EMBL; BC085761; AAH85761.1; -; mRNA.
DR PIR; S65532; S65532.
DR RefSeq; NP_037332.1; NM_013200.1.
DR AlphaFoldDB; Q63704; -.
DR SMR; Q63704; -.
DR STRING; 10116.ENSRNOP00000013985; -.
DR BindingDB; Q63704; -.
DR ChEMBL; CHEMBL3216; -.
DR DrugCentral; Q63704; -.
DR iPTMnet; Q63704; -.
DR PhosphoSitePlus; Q63704; -.
DR PaxDb; Q63704; -.
DR PRIDE; Q63704; -.
DR Ensembl; ENSRNOT00000013985; ENSRNOP00000013985; ENSRNOG00000010438.
DR GeneID; 25756; -.
DR KEGG; rno:25756; -.
DR CTD; 1375; -.
DR RGD; 2397; Cpt1b.
DR eggNOG; KOG3716; Eukaryota.
DR GeneTree; ENSGT01050000244830; -.
DR HOGENOM; CLU_013513_2_1_1; -.
DR InParanoid; Q63704; -.
DR OMA; GLVCCIQ; -.
DR PhylomeDB; Q63704; -.
DR TreeFam; TF313836; -.
DR BRENDA; 2.3.1.21; 5301.
DR Reactome; R-RNO-200425; Carnitine metabolism.
DR Reactome; R-RNO-5362517; Signaling by Retinoic Acid.
DR SABIO-RK; Q63704; -.
DR UniPathway; UPA00659; -.
DR PRO; PR:Q63704; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000010438; Expressed in heart and 19 other tissues.
DR Genevisible; Q63704; RN.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0004095; F:carnitine O-palmitoyltransferase activity; IDA:RGD.
DR GO; GO:0009437; P:carnitine metabolic process; IBA:GO_Central.
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:0015909; P:long-chain fatty acid transport; IDA:RGD.
DR GO; GO:0009637; P:response to blue light; ISS:UniProtKB.
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; Fatty acid metabolism; Lipid metabolism; Membrane;
KW Mitochondrion; Mitochondrion outer membrane; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..772
FT /note="Carnitine O-palmitoyltransferase 1, muscle isoform"
FT /id="PRO_0000210165"
FT TOPO_DOM 1..47
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 48..73
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 74..102
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 103..122
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 123..772
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ACT_SITE 473
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P18886"
FT BINDING 555..567
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 589
FT /ligand="(R)-carnitine"
FT /ligand_id="ChEBI:CHEBI:16347"
FT /evidence="ECO:0000250|UniProtKB:P18886"
FT BINDING 602
FT /ligand="(R)-carnitine"
FT /ligand_id="ChEBI:CHEBI:16347"
FT /evidence="ECO:0000250|UniProtKB:P18886"
SQ SEQUENCE 772 AA; 88217 MW; AFBB4BC67B47FA47 CRC64;
MAEAHQAVAF QFTVTPDGVD FRLSREALRH IYLSGINSWK KRLIRIKNGI LRGVYPGSPT
SWLVVVMATV GSNYCKVDIS MGLVHCIQRC LPTRYGSYGT PQTETLLSMV IFSTGVWATG
IFLFRQTLKL LLSYHGWMFE MHSKTSHATK IWAICVRLLS SRRPMLYSFQ TSLPKLPVPS
VPATIHRYLD SVRPLLDDEA YFRMESLAKE FQDKIAPRLQ KYLVLKSWWA TNYVSDWWEE
YVYLRGRSPI MVNSNYYAMD FVLIKNTSQQ AARLGNTVHA MIMYRRKLDR EEIKPVMALG
MVPMCSYQME RMFNTTRIPG KETDLLQHLS ESRHVAVYHK GRFFKVWLYE GSCLLKPRDL
EMQFQRILDD TSPPQPGEEK LAALTAGGRV EWAEARQKFF SSGKNKMSLD TIERAAFFVA
LDEDSHCYNP DDEASLSLYG KSLLHGNCYN RWFDKSFTLI SCKNGQLGLN TEHSWADAPI
IGHLWEFVLA TDTFHLGYTE TGHCVGEPNT KLPPPQRMQW DIPEQCQTAI ENSYQVAKAL
ADDVELYCFQ FLPFGKGLIK KCRTSPDAFV QIALQLAHFR DKGKFCLTYE ASMTRMFREG
RTETVRSCTS ESTAFVRAMM TGSHKKQDLQ DLFRKASEKH QNMYRLAMTG AGIDRHLFCL
YIVSKYLGVR SPFLDEVLSE PWSLSTSQIP QFQICMFDPK QYPNHLGAGG GFGPVADHGY
GVSYMIAGEN TMFFHVSSKL SSSETNALRF GNHIRQALLD IADLFKISKT DS
