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Database: UniProt
Entry: A0A1I8NSM4_STOCA
LinkDB: A0A1I8NSM4_STOCA
Original site: A0A1I8NSM4_STOCA 
ID   A0A1I8NSM4_STOCA        Unreviewed;       785 AA.
AC   A0A1I8NSM4;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=carnitine O-palmitoyltransferase {ECO:0000256|ARBA:ARBA00013243};
DE            EC=2.3.1.21 {ECO:0000256|ARBA:ARBA00013243};
GN   Name=106096031 {ECO:0000313|EnsemblMetazoa:SCAU001666-PB};
OS   Stomoxys calcitrans (Stable fly) (Conops calcitrans).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Muscoidea;
OC   Muscidae; Stomoxys.
OX   NCBI_TaxID=35570 {ECO:0000313|EnsemblMetazoa:SCAU001666-PB, ECO:0000313|Proteomes:UP000095300};
RN   [1] {ECO:0000313|EnsemblMetazoa:SCAU001666-PB}
RP   IDENTIFICATION.
RC   STRAIN=USDA {ECO:0000313|EnsemblMetazoa:SCAU001666-PB};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) to UniProtKB.
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   RefSeq; XP_013119002.1; XM_013263548.1.
DR   AlphaFoldDB; A0A1I8NSM4; -.
DR   EnsemblMetazoa; SCAU001666-RB; SCAU001666-PB; SCAU001666.
DR   GeneID; 106096031; -.
DR   VEuPathDB; VectorBase:SCAU001666; -.
DR   OrthoDB; 1429709at2759; -.
DR   UniPathway; UPA00659; -.
DR   Proteomes; UP000095300; 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.
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   Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW   Mitochondrion outer membrane {ECO:0000256|ARBA:ARBA00022787};
KW   Transferase {ECO:0000256|ARBA:ARBA00023315};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        55..76
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        96..122
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1..45
FT                   /note="Carnitine O-palmitoyltransferase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16484"
FT   DOMAIN          175..750
FT                   /note="Choline/carnitine acyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00755"
FT   REGION          764..785
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        770..785
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        471
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600542-1"
SQ   SEQUENCE   785 AA;  89749 MW;  CEB92A04DB8445A0 CRC64;
     MAEAHQAVAF SFAITHEGFD INYDQEVLNL VWNSGFRSWK KRVARARNGV RNGVYPAHIQ
     SLWLITAIAL GLHFAGLRTP FNIVNRILVN LPANTINWQV TACFLASLVI WLSICFTMRY
     TLKLLLMYKG WMYESRAPGS KTSLRTKLWA GAVKVFSSWN KPGLYSFQGS LPRLTLPSVT
     ATTQRYLRSV RPLLDDEKYK RMEGLAHEFE TTIGKKLQWY LILKSWWSTN YVSDWWEEYV
     YLRGRSPLMI NSNFYGTDAI FMDLSHNQAA RAANVVYLLL GFRRLIERQE LQPIMVQGIV
     PLCSWQYERT FNTVRVPGME TDRIVHYRDS NHIVVLHKGC YYKVLIYYKG RQLRPCEIQV
     QMEEILNSKA TPLPGEEHLA ALTAWNRSKW AEVRNTYFTR GVNRVSLHTV ESAAFVVSLD
     DIPFEFDLNR PELLDNFGKT LLHGNGYNRW FDKSFTVCVG TNGRVGFNAE HTWADAPVMG
     HTWEYIFGDE IDGYDENGNT RGTPEFQPPS PTRLSWKLEP CLTQIEEATL DANKLINDID
     LRILVHNQYG KGFMKKCRLS PDAFIQMALQ LAYYRDAGRF SLTYEASMTR LFREGRTETV
     RPCTIESAAW VKAMEDKTKT NDERVALIKA ACDRHQLGYQ DAMCGHGIDR HLFCLYVVSK
     YLEVDSPFLN EVLSEPWRLS TSQTPHGQTP KMDLKKHPQC ISSGGGFGPV ADDGYGVSYI
     IAGEDLIFFH ISAKNSCDTT NVHRFADNIC KALADIRSMF EEHMKKNPPK SKAVSSNGNQ
     ASASK
//
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