UniProt/TrEMBL: S9XQ06

Database: UniProt/TrEMBL
Entry: S9XQ06_CAMFR

LinkDB:  S9XQ06_CAMFR 
Original site:  S9XQ06_CAMFR

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Ontology (3)   
   GO (3)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (9)   
   InterPro (5)   
   Pfam (2)   
   PROSITE (2)   
Literature (1)   
   PubMed (1)   
All databases (16)   

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ID   S9XQ06_CAMFR            Unreviewed;       772 AA.
AC   S9XQ06;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 37.
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   ORFNames=CB1_000079011 {ECO:0000313|EMBL:EPY89739.1};
OS   Camelus ferus (Wild bactrian camel) (Camelus bactrianus ferus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Tylopoda; Camelidae; Camelus.
OX   NCBI_TaxID=419612 {ECO:0000313|EMBL:EPY89739.1, ECO:0000313|Proteomes:UP000030684};
RN   [1] {ECO:0000313|EMBL:EPY89739.1, ECO:0000313|Proteomes:UP000030684}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=bactrian camel {ECO:0000313|Proteomes:UP000030684};
RX   PubMed=23149746;
RG   Bactrian Camels Genome Sequencing and Analysis Consortium;
RA   Jirimutu, Wang Z., Ding G., Chen G., Sun Y., Sun Z., Zhang H., Wang L.,
RA   Hasi S., Zhang Y., Li J., Shi Y., Xu Z., He C., Yu S., Li S., Zhang W.,
RA   Batmunkh M., Ts B., Narenbatu, Unierhu, Bat-Ireedui S., Gao H.,
RA   Baysgalan B., Li Q., Jia Z., Turigenbayila, Subudenggerile, Narenmanduhu,
RA   Wang Z., Wang J., Pan L., Chen Y., Ganerdene Y., Dabxilt, Erdemt, Altansha,
RA   Altansukh, Liu T., Cao M., Aruuntsever, Bayart, Hosblig, He F., Zha-ti A.,
RA   Zheng G., Qiu F., Sun Z., Zhao L., Zhao W., Liu B., Li C., Chen Y.,
RA   Tang X., Guo C., Liu W., Ming L., Temuulen, Cui A., Li Y., Gao J., Li J.,
RA   Wurentaodi, Niu S., Sun T., Zhai Z., Zhang M., Chen C., Baldan T.,
RA   Bayaer T., Li Y., Meng H.;
RT   "Genome sequences of wild and domestic bactrian camels.";
RL   Nat. Commun. 3:1202-1202(2012).
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   EMBL; KB016378; EPY89739.1; -; Genomic_DNA.
DR   RefSeq; XP_006173105.1; XM_006173043.2.
DR   AlphaFoldDB; S9XQ06; -.
DR   UniPathway; UPA00659; -.
DR   Proteomes; UP000030684; 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: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:UP000030684};
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   772 AA;  87943 MW;  3E1D9F13D55D57B7 CRC64;
     MAEAHQAVAF QFTVTPEGVD FRLSREALKQ IYLSGINSWK KRLIRIKNGI LRGVYPGSPT
     SWLVVVITTV GSSYCNVDIS RGLVCYIQRC LPERCGPYRT PQTRALLSMA VFSTGVWMMG
     IFFFRQTLKL LLSYHGWMFE MHGKTSCFTK VWAICVRLLS SRRPMLYSFQ ASLPKLPVPS
     VPATVHRYLE SVQHLLDDEE YCRMEVLAKE FQEKTAPRLQ KYLVLKSWWA TNYVSDWWEE
     YVYLRGRTPL MVNSNYYVMD LVLVKNTDVQ AARLGNAVHA MIMYRRKLDR EEIKPVMALG
     IVPMCSYQME RMFNTTRIPG KDADVLQHLT DSRHVAVYHK GRFFKVWLYE GSHLLKPRDL
     EMQFQRILDD PSPPQPGEER LAALTAGGRV EWAQARQAFF SSGKNKAALD AIERAAFFVA
     LDEESHGYDP EDEASLSLYG KALLHGNCCN RWFDKSFTLI AFKNGQLGLN TEHAWADAPI
     IGHLWEFVVG TDAFHLGYAE TGHCLGKPNP VLAPPQRLQW DIPEQCQAVI ESSYQVAKAL
     ADDVELYCFQ FLPFGKGLIK KCRTSPDAFV QIALQLAHFR DRGKFCLTYE ASMTRMFREG
     RTETVRSCTR ESTAFVQAVV EGRHMKADLQ DLFRKAAEKH QNMYRLAMTG AGIDRHLFCL
     YVVSKYLGVS SPFLAEVLSE PWRLSTSQIA QFQIRMFDPN KYPNHLAAGG GFGPVADDGY
     GVSYMIAGEN TIFFHVSSKF SSSETNAQRF GNHIRQALLD IADLFQVPKA DR
//

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