OCTC_MOUSE
ID OCTC_MOUSE Reviewed; 612 AA.
AC Q9DC50; Q921I4;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Peroxisomal carnitine O-octanoyltransferase;
DE Short=COT;
DE EC=2.3.1.137 {ECO:0000269|PubMed:15492013};
GN Name=Crot; Synonyms=Cot;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Lung;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Liver, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-40; LYS-57 AND LYS-406, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-406, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEXES WITH CARNITINE AND
RP OCTANOYLCARNITINE, ACTIVE SITE, CATALYTIC ACTIVITY, FUNCTION, AND
RP MUTAGENESIS OF CYS-323; MET-335 AND GLY-553.
RX PubMed=15492013; DOI=10.1074/jbc.m409894200;
RA Jogl G., Hsiao Y.S., Tong L.;
RT "Crystal structure of mouse carnitine octanoyltransferase and molecular
RT determinants of substrate selectivity.";
RL J. Biol. Chem. 280:738-744(2005).
CC -!- FUNCTION: Beta-oxidation of fatty acids. The highest activity concerns
CC the C6 to C10 chain length substrate. {ECO:0000269|PubMed:15492013}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-carnitine + octanoyl-CoA = CoA + O-octanoyl-(R)-carnitine;
CC Xref=Rhea:RHEA:17177, ChEBI:CHEBI:16347, ChEBI:CHEBI:18102,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57386; EC=2.3.1.137;
CC Evidence={ECO:0000269|PubMed:15492013};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-carnitine + 4,8-dimethylnonanoyl-CoA = CoA + O-4,8-
CC dimethylnonanoyl-(R)-carnitine; Xref=Rhea:RHEA:44860,
CC ChEBI:CHEBI:16347, ChEBI:CHEBI:57287, ChEBI:CHEBI:77061,
CC ChEBI:CHEBI:84654; Evidence={ECO:0000250|UniProtKB:Q9UKG9};
CC -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the carnitine/choline acetyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AK004567; BAB23378.1; -; mRNA.
DR EMBL; BC006593; AAH06593.1; -; mRNA.
DR EMBL; BC012308; AAH12308.1; -; mRNA.
DR CCDS; CCDS19087.1; -.
DR RefSeq; NP_076222.1; NM_023733.3.
DR PDB; 1XL7; X-ray; 2.00 A; A/B=1-612.
DR PDB; 1XL8; X-ray; 2.20 A; A/B=1-612.
DR PDB; 1XMC; X-ray; 2.00 A; A/B=1-612.
DR PDB; 1XMD; X-ray; 2.10 A; A/B=1-612.
DR PDBsum; 1XL7; -.
DR PDBsum; 1XL8; -.
DR PDBsum; 1XMC; -.
DR PDBsum; 1XMD; -.
DR AlphaFoldDB; Q9DC50; -.
DR SMR; Q9DC50; -.
DR STRING; 10090.ENSMUSP00000003720; -.
DR iPTMnet; Q9DC50; -.
DR PhosphoSitePlus; Q9DC50; -.
DR SwissPalm; Q9DC50; -.
DR EPD; Q9DC50; -.
DR jPOST; Q9DC50; -.
DR MaxQB; Q9DC50; -.
DR PaxDb; Q9DC50; -.
DR PeptideAtlas; Q9DC50; -.
DR PRIDE; Q9DC50; -.
DR ProteomicsDB; 293830; -.
DR Antibodypedia; 15286; 347 antibodies from 34 providers.
DR DNASU; 74114; -.
DR Ensembl; ENSMUST00000003720; ENSMUSP00000003720; ENSMUSG00000003623.
DR GeneID; 74114; -.
DR KEGG; mmu:74114; -.
DR UCSC; uc008wkt.1; mouse.
DR CTD; 54677; -.
DR MGI; MGI:1921364; Crot.
DR VEuPathDB; HostDB:ENSMUSG00000003623; -.
DR eggNOG; KOG3718; Eukaryota.
DR GeneTree; ENSGT01050000244969; -.
DR HOGENOM; CLU_013513_5_3_1; -.
DR InParanoid; Q9DC50; -.
DR OMA; DVWAKDY; -.
DR OrthoDB; 559299at2759; -.
DR PhylomeDB; Q9DC50; -.
DR TreeFam; TF313836; -.
DR BRENDA; 2.3.1.137; 3474.
DR Reactome; R-MMU-389887; Beta-oxidation of pristanoyl-CoA.
DR Reactome; R-MMU-9033241; Peroxisomal protein import.
DR UniPathway; UPA00659; -.
DR BioGRID-ORCS; 74114; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Crot; mouse.
DR EvolutionaryTrace; Q9DC50; -.
DR PRO; PR:Q9DC50; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q9DC50; protein.
DR Bgee; ENSMUSG00000003623; Expressed in left lobe of liver and 252 other tissues.
DR Genevisible; Q9DC50; MM.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005777; C:peroxisome; IDA:MGI.
DR GO; GO:0008458; F:carnitine O-octanoyltransferase activity; IDA:UniProtKB.
DR GO; GO:0009437; P:carnitine metabolic process; IDA:UniProtKB.
DR GO; GO:0015936; P:coenzyme A metabolic process; IDA:UniProtKB.
DR GO; GO:0006635; P:fatty acid beta-oxidation; ISO:MGI.
DR GO; GO:0006631; P:fatty acid metabolic process; IDA:UniProtKB.
DR GO; GO:0015908; P:fatty acid transport; IDA:MGI.
DR GO; GO:0006091; P:generation of precursor metabolites and energy; ISO:MGI.
DR GO; GO:0051791; P:medium-chain fatty acid metabolic process; ISO:MGI.
DR GO; GO:0009410; P:response to xenobiotic stimulus; ISO:MGI.
DR Gene3D; 1.10.275.20; -; 1.
DR Gene3D; 3.30.559.10; -; 1.
DR Gene3D; 3.30.559.70; -; 1.
DR InterPro; IPR000542; Carn_acyl_trans.
DR InterPro; IPR042572; Carn_acyl_trans_N.
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; PTHR22589; 1.
DR Pfam; PF00755; Carn_acyltransf; 1.
DR PROSITE; PS00439; ACYLTRANSF_C_1; 1.
DR PROSITE; PS00440; ACYLTRANSF_C_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Acyltransferase; Fatty acid metabolism;
KW Lipid metabolism; Peroxisome; Reference proteome; Transferase; Transport.
FT CHAIN 1..612
FT /note="Peroxisomal carnitine O-octanoyltransferase"
FT /id="PRO_0000210170"
FT MOTIF 610..612
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT ACT_SITE 327
FT /note="Proton acceptor"
FT /evidence="ECO:0000269|PubMed:15492013"
FT BINDING 406
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 410..417
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 439
FT /ligand="(R)-carnitine"
FT /ligand_id="ChEBI:CHEBI:16347"
FT BINDING 441
FT /ligand="(R)-carnitine"
FT /ligand_id="ChEBI:CHEBI:16347"
FT BINDING 452
FT /ligand="(R)-carnitine"
FT /ligand_id="ChEBI:CHEBI:16347"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9UKG9"
FT MOD_RES 40
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 57
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 406
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 406
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MUTAGEN 323
FT /note="C->M: Increases activity with octanoyl-CoA."
FT /evidence="ECO:0000269|PubMed:15492013"
FT MUTAGEN 335
FT /note="M->A: Slightly decreases activity with octanoyl-
FT CoA."
FT /evidence="ECO:0000269|PubMed:15492013"
FT MUTAGEN 335
FT /note="M->A: Strongly decreases activity with octanoyl-
FT CoA."
FT /evidence="ECO:0000269|PubMed:15492013"
FT MUTAGEN 553
FT /note="G->M: Loss of activity with octanoyl-CoA and
FT myristoyl-CoA."
FT /evidence="ECO:0000269|PubMed:15492013"
FT CONFLICT 459
FT /note="T -> A (in Ref. 2; AAH12308)"
FT /evidence="ECO:0000305"
FT TURN 13..16
FT /evidence="ECO:0007829|PDB:1XL7"
FT HELIX 17..19
FT /evidence="ECO:0007829|PDB:1XL7"
FT HELIX 28..39
FT /evidence="ECO:0007829|PDB:1XL7"
FT HELIX 40..42
FT /evidence="ECO:0007829|PDB:1XL7"
FT HELIX 45..60
FT /evidence="ECO:0007829|PDB:1XL7"
FT HELIX 62..76
FT /evidence="ECO:0007829|PDB:1XL7"
FT STRAND 78..81
FT /evidence="ECO:0007829|PDB:1XMC"
FT HELIX 82..89
FT /evidence="ECO:0007829|PDB:1XL7"
FT HELIX 97..100
FT /evidence="ECO:0007829|PDB:1XL7"
FT STRAND 103..106
FT /evidence="ECO:0007829|PDB:1XL7"
FT HELIX 108..111
FT /evidence="ECO:0007829|PDB:1XL7"
FT HELIX 121..140
FT /evidence="ECO:0007829|PDB:1XL7"
FT HELIX 157..161
FT /evidence="ECO:0007829|PDB:1XL7"
FT STRAND 162..168
FT /evidence="ECO:0007829|PDB:1XL7"
FT STRAND 175..178
FT /evidence="ECO:0007829|PDB:1XL7"
FT TURN 183..185
FT /evidence="ECO:0007829|PDB:1XL7"
FT STRAND 191..196
FT /evidence="ECO:0007829|PDB:1XL7"
FT STRAND 199..207
FT /evidence="ECO:0007829|PDB:1XL7"
FT HELIX 214..229
FT /evidence="ECO:0007829|PDB:1XL7"
FT HELIX 237..242
FT /evidence="ECO:0007829|PDB:1XL7"
FT HELIX 245..258
FT /evidence="ECO:0007829|PDB:1XL7"
FT HELIX 260..271
FT /evidence="ECO:0007829|PDB:1XL7"
FT STRAND 275..278
FT /evidence="ECO:0007829|PDB:1XL7"
FT HELIX 291..298
FT /evidence="ECO:0007829|PDB:1XL7"
FT HELIX 302..304
FT /evidence="ECO:0007829|PDB:1XL7"
FT STRAND 312..315
FT /evidence="ECO:0007829|PDB:1XL7"
FT STRAND 321..325
FT /evidence="ECO:0007829|PDB:1XL7"
FT STRAND 327..329
FT /evidence="ECO:0007829|PDB:1XL7"
FT HELIX 333..348
FT /evidence="ECO:0007829|PDB:1XL7"
FT TURN 349..351
FT /evidence="ECO:0007829|PDB:1XL7"
FT STRAND 366..368
FT /evidence="ECO:0007829|PDB:1XMC"
FT HELIX 374..392
FT /evidence="ECO:0007829|PDB:1XL7"
FT STRAND 394..401
FT /evidence="ECO:0007829|PDB:1XL7"
FT HELIX 406..409
FT /evidence="ECO:0007829|PDB:1XL7"
FT HELIX 410..412
FT /evidence="ECO:0007829|PDB:1XL7"
FT HELIX 416..432
FT /evidence="ECO:0007829|PDB:1XL7"
FT STRAND 438..443
FT /evidence="ECO:0007829|PDB:1XL7"
FT STRAND 452..456
FT /evidence="ECO:0007829|PDB:1XL7"
FT HELIX 460..470
FT /evidence="ECO:0007829|PDB:1XL7"
FT HELIX 476..498
FT /evidence="ECO:0007829|PDB:1XL7"
FT TURN 499..501
FT /evidence="ECO:0007829|PDB:1XMD"
FT HELIX 504..516
FT /evidence="ECO:0007829|PDB:1XL7"
FT HELIX 523..525
FT /evidence="ECO:0007829|PDB:1XL7"
FT HELIX 528..532
FT /evidence="ECO:0007829|PDB:1XL7"
FT TURN 533..537
FT /evidence="ECO:0007829|PDB:1XL7"
FT STRAND 540..545
FT /evidence="ECO:0007829|PDB:1XL7"
FT STRAND 548..550
FT /evidence="ECO:0007829|PDB:1XL7"
FT STRAND 563..570
FT /evidence="ECO:0007829|PDB:1XL7"
FT STRAND 573..581
FT /evidence="ECO:0007829|PDB:1XL7"
FT HELIX 589..611
FT /evidence="ECO:0007829|PDB:1XL7"
SQ SEQUENCE 612 AA; 70264 MW; 1C045A419A75C8B6 CRC64;
MENQLTKSVE ERTFQYQDSL PSLPVPALEE SLKKYLESVK PFANEDEYKK TEEIVQKFQE
GAGKRLHQKL LERARGKRNW LEEWWLNVAY LDVRIPSQLN VNFVGPCPHF EHYWPAREGT
QLERGSMMLW HNLNYWQLLR REKLPVHKSG NTPLDMNQFR MLFSTCKVPG ITRDSIMNYF
KTESEGHCPT HIAVLCRGRA FVFDVLHEGC LITPPELLRQ LTYIHKKCSN EPVGPSIAAL
TSEERTRWAK AREYLISLDP ENLTLLEKIQ TSLFVYSIED SSPHATPEEY SQVFEMLLGG
DPSVRWGDKS YNLISFANGI FGCCCDHAPY DAMVMVNIAH YVDERVLETE GRWKGSEKVR
DIPLPEELVF TVDEKILNDV SQAKAQHLKA ASDLQIAAST FTSFGKKLTK EEALHPDTFI
QLALQLAYYR LHGRPGCCYE TAMTRYFYHG RTETVRSCTV EAVRWCQSMQ DPSASLLERQ
QKMLEAFAKH NKMMKDCSHG KGFDRHLLGL LLIAKEEGLP VPELFEDPLF SRSGGGGNFV
LSTSLVGYLR VQGVVVPMVH NGYGFFYHIR DDRFVVACSS WRSCPETDAE KLVQMIFHAF
HDMIQLMNTA HL
