ID   A5PLL0_HUMAN            Unreviewed;       772 AA.
AC   A5PLL0;
DT   10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT   10-JUL-2007, sequence version 1.
DT   02-SEP-2026, entry version 86.
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};
GN   Name=CPT1B {ECO:0000313|EMBL:AAI42955.1};
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:AAI42955.1};
RN   [1] {ECO:0000313|EMBL:AAI42955.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RA   Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H.,
RA   Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., Peck A.M.,
RA   Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M.,
RA   Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F.,
RA   Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T.,
RA   Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F.,
RA   Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E.,
RA   Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y.,
RA   Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E.,
RA   Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y.,
RA   Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W.,
RA   Fuh E., Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J.,
RA   Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S.,
RA   Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., Granite S.J.,
RA   Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W.,
RA   Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J.,
RA   Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I.,
RA   Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U.,
RA   Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A.,
RA   Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.;
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   -!- 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 = O-hexadecanoyl-(R)-
CC         carnitine + CoA; 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:ARBA00048480};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12662;
CC         Evidence={ECO:0000256|ARBA:ARBA00048480};
CC   -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC       {ECO:0000256|ARBA:ARBA00005005}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC       {ECO:0000256|ARBA:ARBA00004374}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004374}.
CC   -!- SIMILARITY: Belongs to the carnitine/choline acetyltransferase family.
CC       {ECO:0000256|ARBA:ARBA00005232, ECO:0000256|RuleBase:RU003801}.
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DR   EMBL; BC142954; AAI42955.1; -; mRNA.
DR   RefSeq; NP_001138607.1; NM_001145135.2.
DR   RefSeq; NP_001138609.1; NM_001145137.2.
DR   AlphaFoldDB; A5PLL0; -.
DR   PeptideAtlas; A5PLL0; -.
DR   DNASU; 1375; -.
DR   GeneID; 1375; -.
DR   KEGG; hsa:1375; -.
DR   ClinPGx; PA26848; -.
DR   CTD; 1375; -.
DR   DisGeNET; 1375; -.
DR   OrthoDB; 240216at2759; -.
DR   UniPathway; UPA00659; -.
DR   BioGRID-ORCS; 1375; 15 hits in 1154 CRISPR screens.
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:0006853; P:carnitine shuttle; IEA:UniProtKB-ARBA.
DR   GO; GO:0006635; P:fatty acid beta-oxidation; IEA:UniProtKB-UniPathway.
DR   FunFam; 3.30.559.10:FF:000002; carnitine O-palmitoyltransferase 1, liver isoform; 1.
DR   FunFam; 3.30.559.70:FF:000001; Carnitine O-palmitoyltransferase 1, liver isoform; 1.
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_1_2.
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.
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 o-acyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00755"
FT   ACT_SITE        473
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600542-1"
SQ   SEQUENCE   772 AA;  87702 MW;  887E0F85537222C6 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 GMFNTTRIPG KDTDVLQHLS DSRHVAVYHK GRFFKLWLYE GARLLKPQDL
     EMQFQRILDD PSPPQPGEEK LAALTAGGRV EWAQARQAFF SSGKNKAALE AIERAAFFVA
     LDEESYSYDP EDEASLSLYG KALLHGNCYN RWFDKSFTLI SFKNGQLGLN AEHAWADAPI
     IGHLWEFVLG TDSFHLGYTE TGHCLGKPNP ALAPPTRLQW DIPKQCQAVI ESSYQVAKAL
     ADDVELYCFQ FLPFGKGLIK KCRTSPDAFV QIALQLAHFR DRGKFCLTYE ASMTRMFREG
     RTETVRSCTS ESTAFVQAMM EGSHTKADLR DLFQKAAKKH QNMYRLAMTG AGIDRHLFCL
     YLVSKYLGVS SPFLAEVLSE PWRLSTSQIP QSQIRMFDPE QHPNHLGAGG GFGPVADDGY
     GVSYMIAGEN TIFFHISSKF SSSETNAQRF GNHIRKALLD IADLFQVPKA YS
//