ID M0R2H6_HUMAN Unreviewed; 336 AA.
AC M0R2H6;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE SubName: Full=Carnitine palmitoyltransferase 1C {ECO:0000313|Ensembl:ENSP00000472579.1};
DE Flags: Fragment;
GN Name=CPT1C {ECO:0000313|Ensembl:ENSP00000472579.1};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000472579.1, ECO:0000313|Proteomes:UP000005640};
RN [1] {ECO:0000313|Ensembl:ENSP00000472579.1, ECO:0000313|Proteomes:UP000005640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [2] {ECO:0000313|Ensembl:ENSP00000472579.1}
RP IDENTIFICATION.
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; AC011495; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KF456599; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; M0R2H6; -.
DR SMR; M0R2H6; -.
DR MassIVE; M0R2H6; -.
DR PeptideAtlas; M0R2H6; -.
DR Antibodypedia; 3052; 285 antibodies from 33 providers.
DR Ensembl; ENST00000595031.1; ENSP00000472579.1; ENSG00000169169.15.
DR UCSC; uc061bit.1; human.
DR HGNC; HGNC:18540; CPT1C.
DR VEuPathDB; HostDB:ENSG00000169169; -.
DR GeneTree; ENSGT01060000248595; -.
DR HOGENOM; CLU_826265_0_0_1; -.
DR ChiTaRS; CPT1C; human.
DR Proteomes; UP000005640; Chromosome 19.
DR Bgee; ENSG00000169169; Expressed in right hemisphere of cerebellum and 124 other cell types or tissues.
DR ExpressionAtlas; M0R2H6; baseline and differential.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 2.
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; CARNITINE O-ACYLTRANSFERASE; 1.
DR PANTHER; PTHR22589:SF55; CARNITINE O-PALMITOYLTRANSFERASE 1, BRAIN ISOFORM; 1.
DR Pfam; PF00755; Carn_acyltransf; 1.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
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|EPD:M0R2H6,
KW ECO:0007829|MaxQB:M0R2H6};
KW Reference proteome {ECO:0000313|Proteomes:UP000005640};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003801}.
FT DOMAIN 2..246
FT /note="Choline/carnitine acyltransferase"
FT /evidence="ECO:0000259|Pfam:PF00755"
FT REGION 306..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 318..336
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 92
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600542-1"
FT NON_TER 1
FT /evidence="ECO:0000313|Ensembl:ENSP00000472579.1"
SQ SEQUENCE 336 AA; 37242 MW; D8F0589CD5AA314B CRC64;
LAALTAAPRG TWAQVRTSLK TQAAEALEAV EGAAFFVSLD AEPAGLTRED PAASLDAYAH
ALLAGRGHDR WFDKSFTLIV FSNGKLGLSV EHSWADCPIS GHMWEFTLAT ECFQLGYSTD
GHCKGHPDPT LPQPQRLQWD LPDQIHSSIS LALRGAKILS ENVDCHVVPF SLFGKSFIRR
CHLSSDSFIQ IALQLAHFRD RGQFCLTYES AMTRLFLEGR TETVRSCTRE ACNFVRAMED
KEKTADDHGY GVSYIFMGDG MITFHISSKK SSTKTDSHRL GQHIEDALLD VASLFQAGQH
FKRRFRGSGK ENSRHRCGFL SRQTGASKAS MTSTDF
//
