ID E1BKY3_BOVIN Unreviewed; 769 AA.
AC E1BKY3;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 3.
DT 27-MAR-2024, entry version 87.
DE SubName: Full=Carnitine palmitoyltransferase 1A {ECO:0000313|Ensembl:ENSBTAP00000029336.6};
GN Name=CPT1A {ECO:0000313|Ensembl:ENSBTAP00000029336.6,
GN ECO:0000313|VGNC:VGNC:27676};
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 {ECO:0000313|Ensembl:ENSBTAP00000029336.6, ECO:0000313|Proteomes:UP000009136};
RN [1] {ECO:0000313|Ensembl:ENSBTAP00000029336.6, ECO:0000313|Proteomes:UP000009136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000029336.6,
RC ECO:0000313|Proteomes:UP000009136};
RA Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT "ARS-UCD1.2.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSBTAP00000029336.6}
RP IDENTIFICATION.
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000029336.6};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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, ECO:0000256|RuleBase:RU003801}.
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DR AlphaFoldDB; E1BKY3; -.
DR Ensembl; ENSBTAT00000029336.6; ENSBTAP00000029336.6; ENSBTAG00000021999.6.
DR VEuPathDB; HostDB:ENSBTAG00000021999; -.
DR VGNC; VGNC:27676; CPT1A.
DR eggNOG; KOG3716; Eukaryota.
DR GeneTree; ENSGT01060000248595; -.
DR HOGENOM; CLU_013513_2_1_1; -.
DR TreeFam; TF313836; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000009136; Chromosome 29.
DR Bgee; ENSBTAG00000021999; Expressed in adult mammalian kidney and 106 other cell types or tissues.
DR ExpressionAtlas; E1BKY3; baseline and differential.
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: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.
DR PROSITE; PS00440; ACYLTRANSF_C_2; 1.
PE 1: Evidence at protein 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 Proteomics identification {ECO:0007829|PeptideAtlas:E1BKY3};
KW Reference proteome {ECO:0000313|Proteomes:UP000009136};
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}.
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..675
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"
SQ SEQUENCE 769 AA; 87734 MW; CEC1B90DF9ED54DE CRC64;
MAEAHQAVAF QFTVTPDGID LRMSHEALRQ IYLSGLHSWK KKFIRFKNGI ITGVYPASPS
SWLIVVVGVM STMYAKIDPS LGIIAKINRT LDTTGCMSSQ TKKVVSGVIF GTGLWVALIV
TMRYSLKVLL SYHGWMFTQH GRLSRTTKIW MFMVKIFSGR KPMLYSFQTS LPRLPVPAVQ
DTVNRYLESV KPLMKEGDFT RMTALAQDFA VNLGPRLQWY LKLKSWWATN YVSDWWEEYI
YLRGRGPLMV NSNYFAMDLL YIIPTHIQAA RAGNGIHAIL LYRRKLDREE IKPILLLGST
IPLCSAQWER MFNTSRIPGE ETDTIQHLRD SKHIVVFHRG RYFKVWLYHD GRLLRPREIE
QQVQRILEDP SEPQPGEAKL AALTAADRVP WARCRQAYFG HGKNKQSLDA VEKAAFFVTL
DETEQGYREE DPETSMDSYA KSLLHGRCFD RWFDKSFTFI VFKNGKMGIN AEHSWADAPI
MGHLWEYVMA TDSFQLGYTE DGHCKGDTNP NIPYPTRLQW DIPEECQEVI ETSLSSANLL
ANDVDFHSFP FRTFGKGLIK KCKTSPDAFV QLSLQLAHYK DMGKFSLTYE ASMTRLFREG
RTETVRSCTA ESCSFVLAMV DPTQTVEQKL KLFRIASEKH QLLYRLAMTG AGIDRHLFCL
YVVSKYLAVD SPFLKEVRPF CAAHSAFLAK PNLVNLRTKF STALPVRTGL TDGFQGSAVL
TLENLSHISS TPGMPLLFSR QDSHRFGKNL REAMTDIISL FGFSPNSKK
//
