ID A0A3P9ALA7_ESOLU Unreviewed; 1257 AA.
AC A0A3P9ALA7;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 2.
DT 27-MAR-2024, entry version 28.
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};
OS Esox lucius (Northern pike).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Esociformes;
OC Esocidae; Esox.
OX NCBI_TaxID=8010 {ECO:0000313|Ensembl:ENSELUP00000041480.2, ECO:0000313|Proteomes:UP000265140};
RN [1] {ECO:0000313|Ensembl:ENSELUP00000041480.2, ECO:0000313|Proteomes:UP000265140}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25069045;
RA Rondeau E.B., Minkley D.R., Leong J.S., Messmer A.M., Jantzen J.R.,
RA von Schalburg K.R., Lemon C., Bird N.H., Koop B.F.;
RT "The genome and linkage map of the northern pike (Esox lucius): conserved
RT synteny revealed between the salmonid sister group and the Neoteleostei.";
RL PLoS ONE 9:e102089-e102089(2014).
RN [2] {ECO:0000313|Ensembl:ENSELUP00000041480.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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}.
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DR AlphaFoldDB; A0A3P9ALA7; -.
DR STRING; 8010.ENSELUP00000041480; -.
DR Ensembl; ENSELUT00000042715.2; ENSELUP00000041480.2; ENSELUG00000022369.2.
DR GeneTree; ENSGT01060000248595; -.
DR InParanoid; A0A3P9ALA7; -.
DR OMA; RQHTHRE; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000265140; LG19.
DR Bgee; ENSELUG00000022369; Expressed in bone element and 7 other cell types or tissues.
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 CDD; cd01165; BTB_POZ; 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 Gene3D; 2.120.10.80; Kelch-type beta propeller; 1.
DR InterPro; IPR000210; BTB/POZ_dom.
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 InterPro; IPR015915; Kelch-typ_b-propeller.
DR InterPro; IPR006652; Kelch_1.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR PANTHER; PTHR22589; CARNITINE O-ACYLTRANSFERASE; 1.
DR PANTHER; PTHR22589:SF69; CARNITINE O-PALMITOYLTRANSFERASE 1, MUSCLE ISOFORM; 1.
DR Pfam; PF00651; BTB; 1.
DR Pfam; PF00755; Carn_acyltransf; 1.
DR Pfam; PF16484; CPT_N; 1.
DR Pfam; PF01344; Kelch_1; 1.
DR SMART; SM00225; BTB; 1.
DR SMART; SM00612; Kelch; 2.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
DR SUPFAM; SSF117281; Kelch motif; 1.
DR SUPFAM; SSF54695; POZ domain; 1.
DR PROSITE; PS00439; ACYLTRANSF_C_1; 1.
DR PROSITE; PS00440; ACYLTRANSF_C_2; 1.
DR PROSITE; PS50097; BTB; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Kelch repeat {ECO:0000256|ARBA:ARBA00022441};
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 Reference proteome {ECO:0000313|Proteomes:UP000265140};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
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 SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..1257
FT /note="Carnitine O-palmitoyltransferase 1, muscle isoform"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5027550141"
FT TRANSMEM 538..563
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 592..614
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 72..141
FT /note="BTB"
FT /evidence="ECO:0000259|PROSITE:PS50097"
FT ACT_SITE 959
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600542-1"
SQ SEQUENCE 1257 AA; 144005 MW; A9945ABC11839FCF CRC64;
MISLLRRRVS VVLLWICRWL QYALGRVWGT SFSVPHSLVT SPCNSGYGLY ERLPEEWKTK
EVNRIYHSGD GSGTMITVQT STHTFYVDLG RLSECSEYFR ALSQSSMRET TERRILLDHI
PSSVFHALLE FCFRNDFAVT QEEMGEHIQV GTYLLAETFV SRCLLALSSV LTPDTCLSYL
DQARNICSTE METTVFSYLS RNLLELPHVN RRLPSEDKTL LIRLRGQGDL RLCSVRKENL
TSWKDLETEA ARHLFAQDGS ETTSDWRPIT ELPFIADKWC FTTVVLLNYL YLIGGYRQQA
RRGWEFKMAS FRYNPFTNTW VSIAPLIKHR RHFSAVPCNG SIYAVGGWYL GSLVTPDSST
ALYTAVERYD PWDDRWTFVS SLPMTDFQFT MSLSHDLPLA TSMGPCLYVL GNIQRTGEKL
LLQYDTRQDL WSELLPTLTR ADADLPSLYF LGATDQLFVI GGNNSENVIT SFCVESGQWG
QGCLDVIAMA EAHQAVGFQF TVTPDGIDLH LSREVLKHIY HAGVTSWRKR AIRFKNGILT
GVYPASPSSW LFVVIAIMST MYARIDPSMG MIDTIKRTLP VSDYMTMQSH TVLSAVLFAT
GLWFSLILML RYILKALLSY HAWIFESHGK MSFSTKLWLN LLKMFSGRRP LLYSFQASLP
RLPVPSVDDT IRRYLESVHP LLDDKQYNQM EVLANEFKTD QSPRLQKYLI LKSWWATNYV
SDWWEEYIYL RGRNPIMVNS NFYAMDLLYV TPTHRQAARA GNVVHAMLQY RRKLERGELA
PLRALGVVPM CSCQMERMFN TTRIPGIETD FVQHLSDRKH LVVYHKGRFF KVWLYYGGRH
LSPSELETQF RKIIDDNTQP QPGELKLAAL TAGNRVPWAQ ARLKYFNQGV NKASLDAIET
SAFFLTLDDE AHGYDPDKLR SLDLYAKSLL HGKCYDRWFD KSFTLIAYTN GKLGVNAEHS
WADAPIVGHM WEYVLATDCF HLGYTDEGHC RGESTKGLPA PVKLQWDIPL ECQEVIEDSY
MVAKEIADDV DFYGYLFDEF GKGLIKKSRT SPDAFIQLAL QLAQFRDKGK FCLTYEASMT
RMFREGRTET VRSCTSDSTA FVRAMEDKST TNTLRLDLFR KAADKHQNMY RLAMTGSGID
RHLFCLYIVS KYLNIDSPFL KKVLSEPWRL STSQTPQQQL NMVDLNKFPR YVGAGGGFGP
VADDGYGVSY IIVGENLITF HISSKFSSPE TDSYRFGQNI RQAMLDIRAL FDQKEKN
//
