ID Q08DN5_BOVIN Unreviewed; 626 AA.
AC Q08DN5;
DT 31-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 131.
DE SubName: Full=Carnitine O-acetyltransferase {ECO:0000313|Ensembl:ENSBTAP00000002513.5};
DE SubName: Full=Carnitine acetyltransferase {ECO:0000313|EMBL:AAI23650.1};
GN Name=CRAT {ECO:0000313|EMBL:ABS45027.1,
GN ECO:0000313|Ensembl:ENSBTAP00000002513.5,
GN ECO:0000313|VGNC:VGNC:27687};
GN Synonyms=MGC142781 {ECO:0000313|EMBL:AAI23650.1};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913 {ECO:0000313|EMBL:AAI23650.1};
RN [1] {ECO:0000313|EMBL:ABS45027.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Pooled {ECO:0000313|EMBL:ABS45027.1};
RX PubMed=12140684; DOI=10.1007/s00335-001-2145-4;
RA Sonstegard T.S., Capuco A.V., White J., Van Tassell C.P., Connor E.E.,
RA Cho J., Sultana R., Shade L., Wray J.E., Wells K.D., Quackenbush J.;
RT "Analysis of bovine mammary gland EST and functional annotation of the Bos
RT taurus gene index.";
RL Mamm. Genome 13:373-379(2002).
RN [2] {ECO:0000313|EMBL:ABS45027.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Pooled {ECO:0000313|EMBL:ABS45027.1};
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [3] {ECO:0000313|EMBL:AAI23650.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=L1 Hereford {ECO:0000313|EMBL:AAI23650.1};
RC TISSUE=Hippocampus {ECO:0000313|EMBL:AAI23650.1};
RA Moore S., Alexander L., Brownstein M., Guan L., Lobo S., Meng Y.,
RA Tanaguchi M., Wang Z., Yu J., Prange C., Schreiber K., Shenmen C.,
RA Wagner L., Bala M., Barbazuk S., Barber S., Babakaiff R., Beland J.,
RA Chun E., Del Rio L., Gibson S., Hanson R., Kirkpatrick R., Liu J.,
RA Matsuo C., Mayo M., Santos R.R., Stott J., Tsai M., Wong D., Siddiqui A.,
RA Holt R., Jones S.J., Marra M.A.;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:ABS45027.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Pooled {ECO:0000313|EMBL:ABS45027.1};
RA Harhay G.P., Sonstegard T.S., Van Tassell C.P., Clawson M.L., Heaton M.P.,
RA Keele J.W., Snelling W.M., Weidmann R.T., Smith T.P.L.;
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000313|Ensembl:ENSBTAP00000002513.5, ECO:0000313|Proteomes:UP000009136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000002513.5,
RC ECO:0000313|Proteomes:UP000009136};
RA Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT "ARS-UCD1.2.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [6] {ECO:0000313|Ensembl:ENSBTAP00000002513.5}
RP IDENTIFICATION.
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000002513.5};
RG Ensembl;
RL Submitted (NOV-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 EMBL; BC123649; AAI23650.1; -; mRNA.
DR EMBL; BT030711; ABS45027.1; -; mRNA.
DR RefSeq; NP_001069055.1; NM_001075587.1.
DR IntAct; Q08DN5; 1.
DR PaxDb; 9913-ENSBTAP00000002513; -.
DR Ensembl; ENSBTAT00000002513.6; ENSBTAP00000002513.5; ENSBTAG00000001932.6.
DR GeneID; 512902; -.
DR KEGG; bta:512902; -.
DR CTD; 1384; -.
DR VEuPathDB; HostDB:ENSBTAG00000001932; -.
DR VGNC; VGNC:27687; CRAT.
DR eggNOG; KOG3717; Eukaryota.
DR GeneTree; ENSGT01060000248556; -.
DR HOGENOM; CLU_013513_5_0_1; -.
DR OMA; ENHSKGP; -.
DR OrthoDB; 1429709at2759; -.
DR TreeFam; TF313836; -.
DR Proteomes; UP000009136; Chromosome 11.
DR Bgee; ENSBTAG00000001932; Expressed in corpus luteum and 106 other cell types or tissues.
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; PS00439; ACYLTRANSF_C_1; 1.
DR PROSITE; PS00440; ACYLTRANSF_C_2; 1.
PE 1: Evidence at protein level;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW ECO:0000256|RuleBase:RU003801};
KW Proteomics identification {ECO:0007829|PeptideAtlas:Q08DN5};
KW Reference proteome {ECO:0000313|Proteomes:UP000009136};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003801}.
FT DOMAIN 38..609
FT /note="Choline/carnitine acyltransferase"
FT /evidence="ECO:0000259|Pfam:PF00755"
FT ACT_SITE 343
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600542-1"
FT BINDING 419
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000256|PIRSR:PIRSR600542-2"
FT BINDING 423..430
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000256|PIRSR:PIRSR600542-2"
FT BINDING 452
FT /ligand="(R)-carnitine"
FT /ligand_id="ChEBI:CHEBI:16347"
FT /evidence="ECO:0000256|PIRSR:PIRSR600542-2"
FT BINDING 454
FT /ligand="(R)-carnitine"
FT /ligand_id="ChEBI:CHEBI:16347"
FT /evidence="ECO:0000256|PIRSR:PIRSR600542-2"
FT BINDING 456
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000256|PIRSR:PIRSR600542-2"
FT BINDING 465
FT /ligand="(R)-carnitine"
FT /ligand_id="ChEBI:CHEBI:16347"
FT /evidence="ECO:0000256|PIRSR:PIRSR600542-2"
FT BINDING 504
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000256|PIRSR:PIRSR600542-2"
FT BINDING 555
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000256|PIRSR:PIRSR600542-2"
SQ SEQUENCE 626 AA; 71017 MW; 48D8B2AF96880FB1 CRC64;
MLAFAARTVV KPLGLLKPSS LMKVSSRFKA HQDSLPRLPV PPLQQTLDHY LKALQPIVSE
EEWAQTKQLV EEFQTAGGVG ERLQKGLERR ARKMENWLSD WWLKTAYLQY RQPLVIYSSP
GVMLPKQDFV DRQGQLRFAA KLIEGVLDFK AMIDNETLPV EYLGGKPLCM NQYYQILSSC
RVPGPKQDLV TKFSRTKKPP MHITVVHNYQ FFELDVYHSD GTPLTSDQIF MQLEKVWNSS
LQTNKEPVGI LTSNHRNSWA KAYSTLIKDK VNRESVHSIQ RSIFTVCLDA PMPRVSEDTY
RSQVAGQMLH GGGSKLNSGN RWFDKTLQFI VAEDGACGLI YEHAAAEGPP IVSLLDHVIE
FTKRPELVRS PMVPLPMPKK LRFNITPEIK SDIEKAKQNL SIMIQDLDIT VMVFHHFGKD
FPKSEKLSPD AFIQMALQLA YYRIYGQACA TYESASLRMF HLGRTDTIRS ASMDSLTFVK
AMDDPNVTEH EKVELLRKAV QAHRAYTDRA IRGEAFDRHL LGLKLQAIED LVSMPDIFMD
TSYAIAMHFN LSTSQVPAKT DCVMFFGPVV PDGYGVCYNP METHINFSVS AYNSCAETNA
VHLAHYLEKA LLDMRALLQS HPRAKL
//
