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Database: UniProt
Entry: A0A3P8WP90_CYNSE
LinkDB: A0A3P8WP90_CYNSE
Original site: A0A3P8WP90_CYNSE 
ID   A0A3P8WP90_CYNSE        Unreviewed;       640 AA.
AC   A0A3P8WP90;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Carnitine O-acetyltransferase {ECO:0000313|Ensembl:ENSCSEP00000028297.1};
OS   Cynoglossus semilaevis (Tongue sole).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Carangaria; Pleuronectiformes; Pleuronectoidei; Cynoglossidae;
OC   Cynoglossinae; Cynoglossus.
OX   NCBI_TaxID=244447 {ECO:0000313|Ensembl:ENSCSEP00000028297.1, ECO:0000313|Proteomes:UP000265120};
RN   [1] {ECO:0000313|Ensembl:ENSCSEP00000028297.1, ECO:0000313|Proteomes:UP000265120}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=24487278;
RA   Chen S., Zhang G., Shao C., Huang Q., Liu G., Zhang P., Song W., An N.,
RA   Chalopin D., Volff J.N., Hong Y., Li Q., Sha Z., Zhou H., Xie M., Yu Q.,
RA   Liu Y., Xiang H., Wang N., Wu K., Yang C., Zhou Q., Liao X., Yang L.,
RA   Hu Q., Zhang J., Meng L., Jin L., Tian Y., Lian J., Yang J., Miao G.,
RA   Liu S., Liang Z., Yan F., Li Y., Sun B., Zhang H., Zhang J., Zhu Y., Du M.,
RA   Zhao Y., Schartl M., Tang Q., Wang J.;
RT   "Whole-genome sequence of a flatfish provides insights into ZW sex
RT   chromosome evolution and adaptation to a benthic lifestyle.";
RL   Nat. Genet. 46:253-260(2014).
RN   [2] {ECO:0000313|Ensembl:ENSCSEP00000028297.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the carnitine/choline acetyltransferase family.
CC       {ECO:0000256|ARBA:ARBA00005232, ECO:0000256|RuleBase:RU003801}.
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DR   RefSeq; XP_008322671.1; XM_008324449.2.
DR   AlphaFoldDB; A0A3P8WP90; -.
DR   STRING; 244447.ENSCSEP00000028297; -.
DR   Ensembl; ENSCSET00000028675.1; ENSCSEP00000028297.1; ENSCSEG00000018060.1.
DR   GeneID; 103389153; -.
DR   KEGG; csem:103389153; -.
DR   CTD; 449545; -.
DR   GeneTree; ENSGT01060000248556; -.
DR   InParanoid; A0A3P8WP90; -.
DR   OMA; TTQHRDT; -.
DR   OrthoDB; 1429709at2759; -.
DR   Proteomes; UP000265120; Chromosome 14.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
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   PANTHER; PTHR22589:SF50; CARNITINE O-ACETYLTRANSFERASE; 1.
DR   PANTHER; PTHR22589; CARNITINE O-ACYLTRANSFERASE; 1.
DR   Pfam; PF00755; Carn_acyltransf; 1.
DR   SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
DR   PROSITE; PS00440; ACYLTRANSF_C_2; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW   ECO:0000256|RuleBase:RU003801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000265120};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003801}.
FT   DOMAIN          49..622
FT                   /note="Choline/carnitine acyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00755"
FT   ACT_SITE        354
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600542-1"
FT   BINDING         433
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600542-2"
FT   BINDING         437..444
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600542-2"
FT   BINDING         466
FT                   /ligand="(R)-carnitine"
FT                   /ligand_id="ChEBI:CHEBI:16347"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600542-2"
FT   BINDING         468
FT                   /ligand="(R)-carnitine"
FT                   /ligand_id="ChEBI:CHEBI:16347"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600542-2"
FT   BINDING         470
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600542-2"
FT   BINDING         479
FT                   /ligand="(R)-carnitine"
FT                   /ligand_id="ChEBI:CHEBI:16347"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600542-2"
FT   BINDING         518
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600542-2"
FT   BINDING         569
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600542-2"
SQ   SEQUENCE   640 AA;  71871 MW;  18652731860FDB77 CRC64;
     MWGICSRTAV KLGMAKPCSL VKTNHLVKPV SATRVAGRYL THQQGLPCLP VPPLQQTCER
     YITALEPIVE VDELKHTKEL VQEFQKSGGV GEKLQKGLEE RAKSTENWLS EWWVQLAYLE
     YRLPVVVHSS PGLVLPRMNF RDKQGQIRFA AKLIAGVLDF KTMIDNETLP VEYLGGKALC
     MNQYYEVLSS CRVPGLKRDM VVNHAKSTPP PKHIIVVHNF QFFALDVYNA DDSPLTVEQL
     CSQLERICSS SNQNMVEPVG ILTTQHRDAW GQAYVNLIKD ATNKASVSTI QRSIFTLCMD
     GVMPQESEQT YRSSAAIQML HGGGSRWNSA NRWFDKTLQF IVGEDGTCGA NYEHAPAEGP
     PIVALIDHVV EYTRKEKDEE VLQPPEEPLP GPQKLHFNIT PEVKKSIEEA KQSMNTLAQD
     LDMKVIVFEH FGKNVPKVHK MSPDAFIQMA LQLAYYRLYQ RCCATYESAS LRMFRLGRTD
     TIRSASNASA AFIRAFDDSS RQNTEKLELM EKAVHAHRSY TNMAINGQAI DRHLLGLRMQ
     AVEEKLTVPE IFKDAAYAKA LHYQLSTSQV PSKTDCVMCF GPVVQNGYGV CYNPMNDHIN
     FALSSFNTCK ETNSAHLAQA VESALLDMRA LLEQTPRAKL
//
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