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Database: UniProt
Entry: H2U487_TAKRU
LinkDB: H2U487_TAKRU
Original site: H2U487_TAKRU 
ID   H2U487_TAKRU            Unreviewed;       774 AA.
AC   H2U487;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 3.
DT   27-MAR-2024, entry version 60.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSTRUP00000031749.3};
OS   Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX   NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000031749.3, ECO:0000313|Proteomes:UP000005226};
RN   [1] {ECO:0000313|Ensembl:ENSTRUP00000031749.3, ECO:0000313|Proteomes:UP000005226}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21551351;
RA   Kai W., Kikuchi K., Tohari S., Chew A.K., Tay A., Fujiwara A., Hosoya S.,
RA   Suetake H., Naruse K., Brenner S., Suzuki Y., Venkatesh B.;
RT   "Integration of the genetic map and genome assembly of fugu facilitates
RT   insights into distinct features of genome evolution in teleosts and
RT   mammals.";
RL   Genome Biol. Evol. 3:424-442(2011).
RN   [2] {ECO:0000313|Ensembl:ENSTRUP00000031749.3}
RP   IDENTIFICATION.
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; H2U487; -.
DR   STRING; 31033.ENSTRUP00000068715; -.
DR   Ensembl; ENSTRUT00000031872.3; ENSTRUP00000031749.3; ENSTRUG00000012539.3.
DR   eggNOG; KOG3716; Eukaryota.
DR   GeneTree; ENSGT01060000248595; -.
DR   HOGENOM; CLU_013513_2_1_1; -.
DR   TreeFam; TF313836; -.
DR   UniPathway; UPA00659; -.
DR   Proteomes; UP000005226; Chromosome 1.
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:SF114; 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.
DR   PROSITE; PS00440; ACYLTRANSF_C_2; 1.
PE   3: Inferred from homology;
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   Reference proteome {ECO:0000313|Proteomes:UP000005226};
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        54..74
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        108..131
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          179..749
FT                   /note="Choline/carnitine acyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00755"
FT   ACT_SITE        478
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600542-1"
SQ   SEQUENCE   774 AA;  88413 MW;  DA32C2428C2C2584 CRC64;
     MAEAHQAVGF EFTVIPEGAD AQLSHQALTE IYLSAVNSWK KCIIRIKNSV IRGVYPASPF
     SWLFVVIAIL ATMYTRSDPS MGLIAKIQEN LPFFFYCFSL NSDTQCKVLL SAVIFSTMLW
     LLLIFTMRLC LKQLLSYHRW MFEPHGKMST TTKVWVALVR IFSGRKPRLY SYQASLPNLP
     VPAVKDTVKR YLESVRPLMD DAQYEHVTKL AAEFESSLGN RLQWYLKLKA LWVTNYVSDW
     WEEYVYLRGR NPIMVNSNYY VMDFLYVTPT PIQAARAGNT IYAMLLYRCK LNKEEIKPVG
     SALGTFPCCS YQFERMFNTC RIPGTLTDTI QHWKDSDFIV VYHKGRYFQL YVYQDGRLLC
     PREIEFQIQR ILDDPSPASK GEARLGALTA GDRIPWAKAR AKHFNSGINK KSLDCIEKAA
     FFVTLDDEEQ SIVGDNLGES LDCYIKSLLH GKCYNRWFDK SFSVVFYKNG KSGLNGEHSW
     GDAPVLTHLW EYTLATECFQ LGYNAEGHCK GEVDASLAEP QKLNWEISSE CEEQISQSLE
     VAQALANDVD MHVVVFRDFG KAKVKKCRVN PDAFIQIALQ LAYYRDQKRF SLTYESSMTR
     LFREGRTETV RSCTNESCAF IRALEGGETT DVCRRLFRTA SEKHQRLCRM ASTGAGIDRH
     LFCLYVVSKC LGVESPFLKE LESEAWRLSS SHIPYQMIDL FDTVNHPEYL CYGGGFGPVT
     DDGYGVCYLM LGGDVLTLHI SCKNSCPDTV IFYHLKAAFY DLGSLRLPSL PMFL
//
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