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Database: UniProt/TrEMBL
Entry: E2A6C2_CAMFO
LinkDB: E2A6C2_CAMFO
Original site: E2A6C2_CAMFO 
ID   E2A6C2_CAMFO            Unreviewed;       795 AA.
AC   E2A6C2;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   SubName: Full=Carnitine O-palmitoyltransferase I, liver isoform {ECO:0000313|EMBL:EFN71007.1};
GN   ORFNames=EAG_09896 {ECO:0000313|EMBL:EFN71007.1};
OS   Camponotus floridanus (Florida carpenter ant).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Formicinae; Camponotus.
OX   NCBI_TaxID=104421 {ECO:0000313|Proteomes:UP000000311};
RN   [1] {ECO:0000313|EMBL:EFN71007.1, ECO:0000313|Proteomes:UP000000311}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C129 {ECO:0000313|Proteomes:UP000000311};
RX   PubMed=20798317; DOI=10.1126/science.1192428;
RA   Bonasio R., Zhang G., Ye C., Mutti N.S., Fang X., Qin N., Donahue G.,
RA   Yang P., Li Q., Li C., Zhang P., Huang Z., Berger S.L., Reinberg D.,
RA   Wang J., Liebig J.;
RT   "Genomic comparison of the ants Camponotus floridanus and Harpegnathos
RT   saltator.";
RL   Science 329:1068-1071(2010).
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   EMBL; GL437123; EFN71007.1; -; Genomic_DNA.
DR   RefSeq; XP_011252290.1; XM_011253988.2.
DR   AlphaFoldDB; E2A6C2; -.
DR   STRING; 104421.E2A6C2; -.
DR   EnsemblMetazoa; XM_011253988.3; XP_011252290.1; LOC105248916.
DR   GeneID; 105248916; -.
DR   KEGG; cfo:105248916; -.
DR   InParanoid; E2A6C2; -.
DR   OMA; NTEHSWG; -.
DR   OrthoDB; 1429709at2759; -.
DR   UniPathway; UPA00659; -.
DR   Proteomes; UP000000311; Unassembled WGS sequence.
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:SF31; CARNITINE O-PALMITOYLTRANSFERASE; 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   Coiled coil {ECO:0000256|SAM:Coils};
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:UP000000311};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EFN71007.1};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        54..76
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        96..118
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1..46
FT                   /note="Carnitine O-palmitoyltransferase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16484"
FT   DOMAIN          174..774
FT                   /note="Choline/carnitine acyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00755"
FT   COILED          765..792
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   ACT_SITE        471
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600542-1"
SQ   SEQUENCE   795 AA;  90962 MW;  D13A8DB5DF5C4329 CRC64;
     MAEAHSAVAF SFAITHEGWD VNFDREVLHL VWLSGVRSWK KRFFRFLNNL KSGVYPASLE
     SLWITIMLVT AVHFAGYKVP YDLVGKVSPY LSGTSILAHL AGSFLVALFL WLAVIYAIRY
     TLKLLLMYKG WIYESRGKTY KPSSLTKIWL LMVKLFSGWH KPMLYSFQGS LPRLPLPSVA
     DTMTRYLRTV RPLLDDENYA RMERLATEFQ NGIGVKLQRY LILKSWWSTN YVSDWWEEYV
     YLRGRSPLMV NSNFYGIDAI LSHPTNLQSA RAAAVIYSCL KYRRLIERQE LEPILVQGLV
     PLCSWQYERV FNTTRIPGIE VDKIVHYQDA KHIVVYHKGR YFKVLIYYRN RILQACEIEL
     QIQQILNDDS TPAEGEEKLA ALTAGERTIW AQTRKDFFAK GVNKASLDII EKAAFVVALD
     DVAYEYDPNH PEKLDHYGRI LLHGKGYDRW FDKSFTLCIG TNGRIGFNAE HSWADAAVMS
     HLWEYVICSE FLDREADAPV MGTLWEFIMA ADNEIGYQDG HNIGTPEFTP PAPLRLQWDL
     NAKCIEAIEQ SYQVAHNILN DVELRIYVHD AYGKGLMKAN SVSPDAYIQM ALQLAYYRDA
     GKFSLTYEAS MTRLFREGRT ETVRPCTIES SKWVKAMENK TITIDEKVKL LMDAVARHQK
     SYQDAMCGKG IDRHLFCLYV VSKYLEVDSP FLKEVLSEPW RLSTSQTPHG QTAKLDLKKY
     PNCISAGGGF GPVAHDGYGV SYIIAGENLI FFHVSSKRSS SKTDAARFAK EIEKALDDMK
     NLLGQKKKIH QNGSA
//
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