CPT1B_MOUSE
ID CPT1B_MOUSE Reviewed; 772 AA.
AC Q924X2; O35287; Q9QYP4;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Carnitine O-palmitoyltransferase 1, muscle isoform;
DE Short=CPT1-M;
DE EC=2.3.1.21 {ECO:0000250|UniProtKB:Q92523};
DE AltName: Full=Carnitine O-palmitoyltransferase I, muscle isoform;
DE Short=CPT I;
DE Short=CPTI-M;
DE AltName: Full=Carnitine palmitoyltransferase 1B;
GN Name=Cpt1b;
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 [GENOMIC DNA].
RX PubMed=12015320; DOI=10.1074/jbc.m203189200;
RA van der Leij F.R., Cox K.B., Jackson V.N., Huijkman N.C., Bartelds B.,
RA Kuipers J.R., Dijkhuizen T., Terpstra P., Wood P.A., Zammit V.A.,
RA Price N.T.;
RT "Structural and functional genomics of the CPT1B gene for muscle-type
RT carnitine palmitoyltransferase I in mammals.";
RL J. Biol. Chem. 277:26994-27005(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ICR; TISSUE=Heart;
RA Cox K.B., Johnson K.R., Wood P.A.;
RL Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=ddY;
RA Yamazaki N.;
RT "cDNA encoding mouse muscle type carnitine palmitoyltransferase I.";
RL Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Salivary gland;
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Lung, 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).
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:0000250|UniProtKB:Q92523};
CC -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000250|UniProtKB:Q92523}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the carnitine/choline acetyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AJ278284; CAC40150.1; -; Genomic_DNA.
DR EMBL; AF017174; AAC31640.2; -; mRNA.
DR EMBL; AB010826; BAA88685.1; -; mRNA.
DR EMBL; BC018270; AAH18270.1; -; mRNA.
DR CCDS; CCDS27749.1; -.
DR RefSeq; NP_034078.2; NM_009948.2.
DR AlphaFoldDB; Q924X2; -.
DR SMR; Q924X2; -.
DR BioGRID; 198864; 4.
DR IntAct; Q924X2; 2.
DR STRING; 10090.ENSMUSP00000104936; -.
DR iPTMnet; Q924X2; -.
DR PhosphoSitePlus; Q924X2; -.
DR jPOST; Q924X2; -.
DR MaxQB; Q924X2; -.
DR PaxDb; Q924X2; -.
DR PRIDE; Q924X2; -.
DR ProteomicsDB; 285259; -.
DR Antibodypedia; 28758; 426 antibodies from 35 providers.
DR DNASU; 12895; -.
DR Ensembl; ENSMUST00000109313; ENSMUSP00000104936; ENSMUSG00000078937.
DR GeneID; 12895; -.
DR KEGG; mmu:12895; -.
DR UCSC; uc007xgr.1; mouse.
DR CTD; 1375; -.
DR MGI; MGI:1098297; Cpt1b.
DR VEuPathDB; HostDB:ENSMUSG00000078937; -.
DR eggNOG; KOG3716; Eukaryota.
DR GeneTree; ENSGT01050000244830; -.
DR HOGENOM; CLU_013513_2_1_1; -.
DR InParanoid; Q924X2; -.
DR OMA; GLVCCIQ; -.
DR OrthoDB; 559299at2759; -.
DR PhylomeDB; Q924X2; -.
DR TreeFam; TF313836; -.
DR BRENDA; 2.3.1.21; 3474.
DR Reactome; R-MMU-200425; Carnitine metabolism.
DR Reactome; R-MMU-5362517; Signaling by Retinoic Acid.
DR UniPathway; UPA00659; -.
DR BioGRID-ORCS; 12895; 1 hit in 77 CRISPR screens.
DR PRO; PR:Q924X2; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q924X2; protein.
DR Bgee; ENSMUSG00000078937; Expressed in hindlimb stylopod muscle and 57 other tissues.
DR ExpressionAtlas; Q924X2; baseline and differential.
DR Genevisible; Q924X2; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005741; C:mitochondrial outer membrane; TAS:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0004095; F:carnitine O-palmitoyltransferase activity; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0009637; P:response to blue light; IDA: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_0000210163"
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"
FT CONFLICT 528
FT /note="E -> K (in Ref. 3; BAA88685)"
FT /evidence="ECO:0000305"
FT CONFLICT 761
FT /note="I -> V (in Ref. 2; AAC31640)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 772 AA; 88217 MW; B53F7002141EFA7F CRC64;
MAEAHQAVAF QFTVTPDGVD FRLSREALRH IYLSGINSWK KRLIRIKNGI LRGVYPGSPT
SWLVVVMATV GSNYCKVDIS MGLVDCIQRC LPERYGHFGT PQTEALLSMV IFSTGVWATG
IFFFRQTLKL LLSYHGWMFE MHSKTSHATK IWAICVRLLS SRRPMLYSFQ TSLPKLPVPS
VPATIHRYLD SVRPLLDDEA YYRMETLAKE FQDKTAPRLQ KYLVLKSWWA TNYVSDWWEE
YVYLRSRSPL MVNSNYYAMD FVLIKNTNVQ AARLGNAVHA MIMYRRKLDR EEIKPVMALG
MVPMCSYQME RMFNTTRIPG KETDLLQHLS ESRHVAVYHK GRFFKVWLYE GSRLLKPRDL
EMQFQRILDD PSPPQPGEEK LAALTAGGRV EWAEARQTFF SSGKNKMSLD AIERAAFFVT
LDEDSHCYNP DDETSLSLYG KALLHGNCYN RWFDKSFTLI SCKNGLLGLN TEHSWADAPI
IGHLWEFVLG TDTFHLGYTE TGHCVGEPNT TLPPPQRLPW DIPEQCREAI ENSYQVAKAL
ADDVELYCFQ FLPFGKGLIK KCRTSPDAFV QIALQLAHFR DKGKFCLTYE ASMTRMFREG
RTETVRSCTN ESAAFVQAMM KGSHKKQDLQ DLFRKASEKH QNMYRLAMTG AGIDRHLFCL
YIVSKYLGVS SPFLAEVLSE PWSLSTSQIP QFQICMFDPK QYPNHLGAGG GFGPVADDGY
GVSYMIAGEN TMFFHISSKY SSSETNAQRF GNHIRQALLD IAELFKISKT DS
