ID Q53FV7_HUMAN Unreviewed; 772 AA. AC Q53FV7; DT 24-MAY-2005, integrated into UniProtKB/TrEMBL. DT 24-MAY-2005, sequence version 1. DT 27-MAR-2024, entry version 95. DE RecName: Full=Carnitine O-palmitoyltransferase 1, muscle isoform {ECO:0000256|ARBA:ARBA00040569}; DE EC=2.3.1.21 {ECO:0000256|ARBA:ARBA00013243}; DE AltName: Full=Carnitine O-palmitoyltransferase I, muscle isoform {ECO:0000256|ARBA:ARBA00041685}; DE AltName: Full=Carnitine palmitoyltransferase 1B {ECO:0000256|ARBA:ARBA00042959}; DE Flags: Fragment; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606 {ECO:0000313|EMBL:BAD96894.1}; RN [1] {ECO:0000313|EMBL:BAD96894.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Human lung {ECO:0000313|EMBL:BAD96894.1}; RX PubMed=8125298; DOI=10.1016/0378-1119(94)90802-8; RA Maruyama K., Sugano S.; RT "Oligo-capping: a simple method to replace the cap structure of eukaryotic RT mRNAs with oligoribonucleotides."; RL Gene 138:171-174(1994). RN [2] {ECO:0000313|EMBL:BAD96894.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Human lung {ECO:0000313|EMBL:BAD96894.1}; RX PubMed=9373149; DOI=10.1016/S0378-1119(97)00411-3; RA Suzuki Y., Yoshitomo K., Maruyama K., Suyama A., Sugano S.; RT "Construction and characterization of a full length-enriched and a 5'-end- RT enriched cDNA library."; RL Gene 200:149-156(1997). RN [3] {ECO:0000313|EMBL:BAD96894.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Human lung {ECO:0000313|EMBL:BAD96894.1}; RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., RA Tanaka A., Yokoyama S.; RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the transfer of the acyl group of long-chain fatty CC acid-CoA conjugates onto carnitine, an essential step for the CC mitochondrial uptake of long-chain fatty acids and their subsequent CC beta-oxidation in the mitochondrion. {ECO:0000256|ARBA:ARBA00043926}. 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:0000256|ARBA:ARBA00043805}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12662; CC Evidence={ECO:0000256|ARBA:ARBA00043805}; CC -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation. CC {ECO:0000256|ARBA:ARBA00005005}. CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi- CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Mitochondrion CC outer membrane {ECO:0000256|ARBA:ARBA00004374}; Multi-pass membrane CC protein {ECO:0000256|ARBA:ARBA00004374}. CC -!- SIMILARITY: Belongs to the carnitine/choline acetyltransferase family. CC {ECO:0000256|ARBA:ARBA00005232, ECO:0000256|RuleBase:RU003801}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AK223174; BAD96894.1; -; mRNA. DR RefSeq; NP_001138607.1; NM_001145135.1. DR AlphaFoldDB; Q53FV7; -. DR PeptideAtlas; Q53FV7; -. DR DNASU; 1375; -. DR GeneID; 1375; -. DR KEGG; hsa:1375; -. DR CTD; 1375; -. DR PharmGKB; PA26848; -. DR OrthoDB; 1429709at2759; -. DR UniPathway; UPA00659; -. DR BioGRID-ORCS; 1375; 15 hits in 1154 CRISPR screens. DR GenomeRNAi; 1375; -. DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell. DR GO; GO:0004095; F:carnitine O-palmitoyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0006635; P:fatty acid beta-oxidation; IEA:UniProtKB-UniPathway. DR Gene3D; 6.10.250.1760; -; 1. DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1. DR Gene3D; 3.30.559.70; Choline/Carnitine o-acyltransferase, domain 2; 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; CARNITINE O-ACYLTRANSFERASE; 1. DR PANTHER; PTHR22589:SF69; CARNITINE O-PALMITOYLTRANSFERASE 1, MUSCLE ISOFORM; 1. DR Pfam; PF00755; Carn_acyltransf; 1. DR Pfam; PF16484; CPT_N; 1. DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 2. DR PROSITE; PS00439; ACYLTRANSF_C_1; 1. DR PROSITE; PS00440; ACYLTRANSF_C_2; 1. DR Genevisible; Q53FV7; HS. PE 2: Evidence at transcript level; KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315, KW ECO:0000256|RuleBase:RU003801}; KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832}; KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius}; KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128}; KW Mitochondrion outer membrane {ECO:0000256|ARBA:ARBA00022787}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003801}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}. FT TRANSMEM 62..84 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 105..124 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 1..47 FT /note="Carnitine O-palmitoyltransferase N-terminal" FT /evidence="ECO:0000259|Pfam:PF16484" FT DOMAIN 176..755 FT /note="Choline/carnitine acyltransferase" FT /evidence="ECO:0000259|Pfam:PF00755" FT ACT_SITE 473 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR600542-1" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:BAD96894.1" SQ SEQUENCE 772 AA; 87786 MW; 70B6F159BB023883 CRC64; MAEAHQAVAF QFTVTPDGVD FRLSREALKH VYLSGINSWK KRLIRIKNGI LRGVYPGSPT SWLVVIMATV GSSFCNVDIS LGLVSCIQRC LPQGCGPYQT PQTRALLSMA IFSTGVWVTG IFFFRQTLKL LLCYHGWMFE MHGKTSNLTR IWAMCIRLLS SRHPMLYSFQ TSLPKLPVPR VSATIQRYLE SVRPLLDDEE YYRMELLAKE FQDKTAPRLQ KYLVLKSWWA SNYVSDWWEE YIYLRGRSPL MVNSNYYVMD LVLIKNTDVQ AARLGNIIHA MIMYRRKLDR EEIKPVMALG IVPMCSYQME RMFNTTRIPG NDTDVLQHLS DSRHVAVYHK GRFFKLWLYE GARLLKPQDL EMQFQRILDD PSPPQPGEEK LAALTAGGRV EWAQARQAFF SSGKNKAALE AIERAAFFVA LDEESYSYDP EDEASLSLYG KALLHGNCYN RWFDKSFTLI SFKNGQLGLN AEHAWADAPI IGHLWEFVLG TDSFHLGYTE TGHCLGKPNP ALAPPTRLQW DIPKQCQAVI KSSYQVAKAL ADDVELYCFQ FLPFGKGLIK KCRTSPDAFV QIALQLAHFR DRGKFCLTYE ASMTRMFREG RTETVRSCTS ESTAFVQAMM EGSHTKADLR DLFQKAAKKH QNMYRLAMTG AGIDRHLFCL YLVSKYLGVS SPFLAEVLSE PWRLSTSQIP QSQIRMFDPE QHPNHLGAGG GFGPVADDGY GVSYMIAGEN TIFFHISSKF SSSETNAQRF GNHIRKALLD IADLFQVPKA YS //