ID G3VLF8_SARHA Unreviewed; 774 AA.
AC G3VLF8;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=Carnitine O-palmitoyltransferase 1, muscle isoform {ECO:0000256|ARBA:ARBA00040569};
DE EC=2.3.1.21 {ECO:0000256|ARBA:ARBA00013243};
DE AltName: Full=Carnitine O-palmitoyltransferase I, muscle isoform {ECO:0000256|ARBA:ARBA00041685};
DE AltName: Full=Carnitine palmitoyltransferase 1B {ECO:0000256|ARBA:ARBA00042959};
GN Name=CPT1B {ECO:0000313|Ensembl:ENSSHAP00000004013.1};
OS Sarcophilus harrisii (Tasmanian devil) (Sarcophilus laniarius).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Metatheria; Dasyuromorphia; Dasyuridae; Sarcophilus.
OX NCBI_TaxID=9305 {ECO:0000313|Ensembl:ENSSHAP00000004013.1, ECO:0000313|Proteomes:UP000007648};
RN [1] {ECO:0000313|Ensembl:ENSSHAP00000004013.1, ECO:0000313|Proteomes:UP000007648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21709235; DOI=10.1073/pnas.1102838108;
RA Miller W., Hayes V.M., Ratan A., Petersen D.C., Wittekindt N.E., Miller J.,
RA Walenz B., Knight J., Qi J., Zhao F., Wang Q., Bedoya-Reina O.C.,
RA Katiyar N., Tomsho L.P., Kasson L.M., Hardie R.A., Woodbridge P.,
RA Tindall E.A., Bertelsen M.F., Dixon D., Pyecroft S., Helgen K.M.,
RA Lesk A.M., Pringle T.H., Patterson N., Zhang Y., Kreiss A., Woods G.M.,
RA Jones M.E., Schuster S.C.;
RT "Genetic diversity and population structure of the endangered marsupial
RT Sarcophilus harrisii (Tasmanian devil).";
RL Proc. Natl. Acad. Sci. U.S.A. 108:12348-12353(2011).
RN [2] {ECO:0000313|Ensembl:ENSSHAP00000004013.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Catalyzes the transfer of the acyl group of long-chain fatty
CC acid-CoA conjugates onto carnitine, an essential step for the
CC mitochondrial uptake of long-chain fatty acids and their subsequent
CC beta-oxidation in the mitochondrion. {ECO:0000256|ARBA:ARBA00043926}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-carnitine + hexadecanoyl-CoA = CoA + O-hexadecanoyl-(R)-
CC carnitine; Xref=Rhea:RHEA:12661, ChEBI:CHEBI:16347,
CC ChEBI:CHEBI:17490, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379; EC=2.3.1.21;
CC Evidence={ECO:0000256|ARBA:ARBA00043805};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12662;
CC Evidence={ECO:0000256|ARBA:ARBA00043805};
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, ECO:0000256|RuleBase:RU003801}.
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DR RefSeq; XP_003770854.1; XM_003770806.2.
DR AlphaFoldDB; G3VLF8; -.
DR STRING; 9305.ENSSHAP00000004013; -.
DR Ensembl; ENSSHAT00000004053.2; ENSSHAP00000004013.1; ENSSHAG00000003537.2.
DR eggNOG; KOG3716; Eukaryota.
DR GeneTree; ENSGT01060000248595; -.
DR HOGENOM; CLU_013513_2_1_1; -.
DR InParanoid; G3VLF8; -.
DR OMA; PERCGPY; -.
DR OrthoDB; 1429709at2759; -.
DR TreeFam; TF313836; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000007648; 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 GO; GO:0009637; P:response to blue light; IEA:Ensembl.
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:SF69; CARNITINE O-PALMITOYLTRANSFERASE 1, MUSCLE ISOFORM; 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 Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Mitochondrion outer membrane {ECO:0000256|ARBA:ARBA00022787};
KW Reference proteome {ECO:0000313|Proteomes:UP000007648};
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}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 105..124
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 176..756
FT /note="Choline/carnitine acyltransferase"
FT /evidence="ECO:0000259|Pfam:PF00755"
FT ACT_SITE 473
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600542-1"
SQ SEQUENCE 774 AA; 88655 MW; 694EA9B73258B7CD CRC64;
MAEAHQAVAF QFTVTPDGVD FQLSREALKH VYLSGINSWK KRFIRIKNGI LRGVYPGSPT
SWLVVVMATM GSSYCNVDIS MGMICHIRKY IPEGCSNYLT LQTRTLISVG IFSTGVWVTG
IFLFRQTLKL LLSYHGWMFE MHGQTSRITK IWAICVRLLS NRRPMLYTFQ TSLPKLPVPK
VSATIKRYLE SVRPLLDDEE YYRMEMLAKD FQERTAPRLQ KYLVLKSWWA TNYVSDWWEE
YIYLRSRGPI MVNSNYYVMD FVLTPHTEVQ AARLGNVVHA MIMYRRKLDR EEIKPVMALG
IVPMCSYQME RMFNTTRIPG KESDVLQHLV DSRHVAVYHK GRFYKVWLYQ GTQLLKPRDL
EMQFQRILDD TCPIQPGEEK LAALTAGGRV QWAEARQTYF NTGKNKASLE AIEKAAFFVT
LDEESHGYDP EDEASLSLYG KALLHGNCYN RWFDKSFTLV AFKNGKLGLN TEHAWADAPV
VGHLWEFVLA TDAFHLDYNE SGHCQGKPNH SLAPPQRLQW EIPEECQKII ESSYEVAKAL
ADDVELYCFQ FLPFGKGLIK KCRSSPDAFV QIALQLAHFR DKGNFCLTYE ASMTRMFRDG
RTETVRSCTA ETTAFVRAMT DSGYMKPDLQ DLFRKAAEKH QHLYRLAMTG AGIDRHLFCL
YVVSKYLGLH SPFLAQVLSE PWRLSTSQTA QFQIRMFDPE KYPNHLAAGG GFGPVADDGY
GVSYMIAGEN TIFFHISSKF SSSETNAQRF GNHIHQALED IAALFELPSP KPES
//
