CPT1B_BOVIN
ID CPT1B_BOVIN Reviewed; 771 AA.
AC Q58DK1; Q08DY3;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 102.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal muscle;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
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; BT021596; AAX46443.1; -; mRNA.
DR EMBL; BC123511; AAI23512.1; -; mRNA.
DR RefSeq; NP_001029521.1; NM_001034349.2.
DR AlphaFoldDB; Q58DK1; -.
DR SMR; Q58DK1; -.
DR STRING; 9913.ENSBTAP00000021357; -.
DR PaxDb; Q58DK1; -.
DR Ensembl; ENSBTAT00000021357; ENSBTAP00000021357; ENSBTAG00000016048.
DR GeneID; 509459; -.
DR KEGG; bta:509459; -.
DR CTD; 1375; -.
DR VEuPathDB; HostDB:ENSBTAG00000016048; -.
DR VGNC; VGNC:27677; CPT1B.
DR eggNOG; KOG3716; Eukaryota.
DR GeneTree; ENSGT01050000244830; -.
DR HOGENOM; CLU_013513_2_1_1; -.
DR InParanoid; Q58DK1; -.
DR OMA; GLVCCIQ; -.
DR OrthoDB; 559299at2759; -.
DR TreeFam; TF313836; -.
DR Reactome; R-BTA-200425; Carnitine metabolism.
DR Reactome; R-BTA-5362517; Signaling by Retinoic Acid.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000009136; Chromosome 5.
DR Bgee; ENSBTAG00000016048; Expressed in cardiac ventricle and 102 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0004095; F:carnitine O-palmitoyltransferase activity; IBA:GO_Central.
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; IBA:GO_Central.
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 2: Evidence at transcript 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..771
FT /note="Carnitine O-palmitoyltransferase 1, muscle isoform"
FT /id="PRO_0000245505"
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..101
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 102..121
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 122..771
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ACT_SITE 472
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P18886"
FT BINDING 554..566
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 588
FT /ligand="(R)-carnitine"
FT /ligand_id="ChEBI:CHEBI:16347"
FT /evidence="ECO:0000250|UniProtKB:P18886"
FT BINDING 601
FT /ligand="(R)-carnitine"
FT /ligand_id="ChEBI:CHEBI:16347"
FT /evidence="ECO:0000250|UniProtKB:P18886"
SQ SEQUENCE 771 AA; 88512 MW; 67FAB2B2531EDA85 CRC64;
MAEAHQAVAF QFTVTPEGVD FQLSREVLKH IYLSVIRSWK KRLIRIKNGI LRGVYPGSPT
SWLVVVMATA GSSYYNVDIS MGLVYYIQRW LPEGRPYRTP YTRTLFSMAI FSTGVWMMGI
FFFRQTLKLL LSYHGWMFEL HGQTSHLTRV WAVCVRLLSG RRPMLYSFQT SLPKLPVPSV
PATVHRYLES VEHLLDDEQY YRMETLAKEF EEKTAPRLQK YLVLKSWWAT NYVSDWWEEY
VYLRGRNPIV VNSNYYVMDL VLVKNTDVQA ARLGNAVHAM ITYRRKLDRE EIKPVMALGL
VPMCSYQMER MFNTTRIPGK DTDVLQHLPD SRHVAVYHKG RFFKVWLYEG SRLLKPRDLE
MQFQRILDDP SPPQPGEERL AALTAGGRVE WAQARQAFFS SGKNKAALDA IERAAFFVAL
DEESHHYDPE DEASLSLYGK ALLHGNCYNR WFDKSFTLIS FKNGQLGLNT EHAWADAPII
GHLWEFVLGT DSFHLGYTET GHCLGKPNPV LPPPQRLQWD IPKQCQAVIE SSYQVAKALA
DDVELYCFQF LPFGKGLIKK CRTSPDAFVQ IALQLAHFRD RGKFCLTYEA SMTRMFREGR
TETVRSCTRE STAFVQAMVQ GRHLNEDLQR LFRKAAEKHQ NMYRLAMTGA GIDRHLFCLY
VVSKYLGVES PFLAEVLSEP WRLSTSQIAQ FQIRMFDPNK YPKHLGAGGG FGPVADDGYG
VSYMIAGENT IFFHVSSKFS SSETNAQRFG NQIRQALLDI ANLFQVPKAD G
