ID   CPT1B_PIG               Reviewed;         772 AA.
AC   Q8HY46;
DT   05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 77.
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   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Skeletal muscle;
RA   Debata C., Penn D.;
RT   "Pig carnitine palmitoyltransferase IB muscle isoform.";
RL   Submitted (NOV-2002) 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; AY181062; AAO12153.1; -; mRNA.
DR   AlphaFoldDB; Q8HY46; -.
DR   SMR; Q8HY46; -.
DR   STRING; 9823.ENSSSCP00000027987; -.
DR   PaxDb; Q8HY46; -.
DR   PeptideAtlas; Q8HY46; -.
DR   PRIDE; Q8HY46; -.
DR   eggNOG; KOG3716; Eukaryota.
DR   InParanoid; Q8HY46; -.
DR   UniPathway; UPA00659; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
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..772
FT                   /note="Carnitine O-palmitoyltransferase 1, muscle isoform"
FT                   /id="PRO_0000210164"
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;  88230 MW;  EE3F20B9A406CDE1 CRC64;
     MAEAHQAVAF QFTVTPEGVD FRLSREALKH IYLSGINSWK KRLIRIKNGI LRGVYPGSPT
     SWLVVASATA GSSYYNVDIS MGLVNHIQRC LPERYGPYWT PQTRALLSMA VVSTGVWMIG
     IFFFRQTLKL LLSYHGWMFE MHGQSSRVTK VWAICVRLLS SRRPMLYSFQ TSLPKLPVPS
     VPATIHRYLE SVQHLLDDEE YSRKEMLAKE FQEKTAPRLQ KYLVLKSWWA TNYVSDWWEE
     YVYLRGRTPL MVNSNYYVMD LVLMRSTDVQ AARLGNAVHA MIMYRRKLDR EDIKPVMALG
     IVPMCSYQME RMFNTTRIPG KDTDTLQHLT DSRHVAVYHK GRFFKVWLYE GSRLLKPCEL
     ELQFQRILDD PSPPQPGEEK LAALTAGGRV EWAQARQAFF SSGKNKFALD AIERAAFFVA
     LDEESHHYDP EDEASLSLYG KALLHGNCYN RWFDKSFTLI AFKNGQLGLN TEHAWADAPI
     IGHLWEFVLG TDTFHLGYTE TGHCLGKPNP MLAPPQRLQW DIPEQCQAVI ESSYQVAKAL
     ADDVELYCFQ FLPFGKGLIK KCRTSPDAFV QIALQLAYFR DRGKFCLTYE ASMTRMFREG
     RTETVRSCTR ESTAFVQAMV EGRRVKADLQ DLFRKAAQKH QNMYRLAMTG AGIDRHLFCL
     YVVSKYLGVS SPFLAEVLSE PWRLSTSQIA QFQIRMFDPN KYPNHLGAGG GFGPVADDGY
     GVSYMIAGEN TIFFHVSSKF SSSETNAQRF GNHIRQALLD LADLFQVPKT DS