ID   A0A2K5C0P2_AOTNA        Unreviewed;       706 AA.
AC   A0A2K5C0P2;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Carnitine palmitoyltransferase 1A {ECO:0000313|Ensembl:ENSANAP00000002252.1};
GN   Name=CPT1A {ECO:0000313|Ensembl:ENSANAP00000002252.1};
OS   Aotus nancymaae (Ma's night monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Aotidae;
OC   Aotus.
OX   NCBI_TaxID=37293 {ECO:0000313|Ensembl:ENSANAP00000002252.1, ECO:0000313|Proteomes:UP000233020};
RN   [1] {ECO:0000313|Ensembl:ENSANAP00000002252.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-carnitine + 4,8-dimethylnonanoyl-CoA = CoA + O-4,8-
CC         dimethylnonanoyl-(R)-carnitine; Xref=Rhea:RHEA:44860,
CC         ChEBI:CHEBI:16347, ChEBI:CHEBI:57287, ChEBI:CHEBI:77061,
CC         ChEBI:CHEBI:84654; Evidence={ECO:0000256|ARBA:ARBA00024283};
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}.
CC   -!- SIMILARITY: Belongs to the carnitine/choline acetyltransferase family.
CC       {ECO:0000256|ARBA:ARBA00005232}.
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DR   AlphaFoldDB; A0A2K5C0P2; -.
DR   Ensembl; ENSANAT00000018646.1; ENSANAP00000002252.1; ENSANAG00000017356.1.
DR   GeneTree; ENSGT01060000248595; -.
DR   UniPathway; UPA00659; -.
DR   Proteomes; UP000233020; Unplaced.
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; 1.10.275.20; Choline/Carnitine o-acyltransferase; 1.
DR   Gene3D; 3.30.559.70; Choline/Carnitine o-acyltransferase, domain 2; 2.
DR   InterPro; IPR000542; Carn_acyl_trans.
DR   InterPro; IPR042572; Carn_acyl_trans_N.
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:SF74; CARNITINE O-PALMITOYLTRANSFERASE 1, LIVER 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.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
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   Reference proteome {ECO:0000313|Proteomes:UP000233020};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
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        104..126
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          174..695
FT                   /note="Choline/carnitine acyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00755"
SQ   SEQUENCE   706 AA;  80520 MW;  4C9BE7B41C9D6BFB CRC64;
     MAEAHQAVAF QFTVTPDGID LRLSHEALKQ IYLSGLHSWK KKFIRFKNGI ITGVYPASPS
     SWLIVVVGVM TTMYAKIDPS LGIIAKINRT LERTDCMSSQ TKNVVSGVLF GTGLWVALIV
     TMRFSLKVLL SYHGWMFAEH GKMSRATKIW MGMVKLFSGR KPMLYSFQTS LPRLPVPAVK
     DTVNRYLESV RPLMKEEDFK RMTALAQDFA VSLGPRLQWY LRLKSWWATN YVSLYTHCWL
     QYSMDLLYIL PTHIQAARAG NAIHAILLYR RKLDREEIKP IRLLGSTIPL CSAQWERMFN
     TSRIPGEETD TIQHMRDSKH IVVYHRGRYF KVWLYHDGRL LKPREMEQQM QRILDDTSEP
     QPGEARLAAL TAGDRVPWAR CRQAYFGRGK NKQSLDAVEK AAFFVTLDET EQGYRREDPD
     TSMDSYAKSL LHGRCYDRGS PLTGALWEGI LGLQMGYAED GHCKGDTNPN IPYPTRLQWD
     IPGECQEVIE TSLNTANLLA NDVDFHSFPF EDFGKGIIKK CRTSPDAFVQ LALQLAHYKD
     MGKFCLTYEA SMTRLFREGR TETVRSCTTE SCDFVRAMVD PAQTVEQRLK LFKLASEKHQ
     LMYRLAMTGS GIDRHLFCLY VVSKYLAVES PFLKEVLSEP WRLSTSQTPQ QQVELNPEYV
     RSGGVADDGY GVSYILVGEN LINFHISSKF SCPETGIVSQ GQVQIL
//