ID MCAT_MOUSE Reviewed; 301 AA.
AC Q9Z2Z6; Q3U801;
DT 11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 27-MAR-2024, entry version 164.
DE RecName: Full=Mitochondrial carnitine/acylcarnitine carrier protein {ECO:0000305};
DE AltName: Full=Carnitine/acylcarnitine translocase;
DE Short=CAC;
DE Short=CACT;
DE Short=mCAC;
DE AltName: Full=Solute carrier family 25 member 20;
GN Name=Slc25a20 {ECO:0000312|EMBL:BAA74768.1}; Synonyms=Cac, Cact;
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 [MRNA].
RA Lu K., Kuwajima M., Shima K., Nakamura Y., Nishimori H.;
RT "Cloning, genomic structure and chromosomal localization of murine
RT mitochondrial carnitine-acylcarnitine translocase gene and mutation
RT analysis in the juvenile visceral steatosis (JVS) mouse.";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary gland;
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 [4]
RP TISSUE SPECIFICITY.
RX PubMed=19287344; DOI=10.1203/pdr.0b013e3181a283c1;
RA Camacho J.A., Rioseco-Camacho N.;
RT "The human and mouse SLC25A29 mitochondrial transporters rescue the
RT deficient ornithine metabolism in fibroblasts of patients with the
RT hyperornithinemia-hyperammonemia-homocitrullinuria (HHH) syndrome.";
RL Pediatr. Res. 66:35-41(2009).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen, and
RC 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 [6]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-170, AND IDENTIFICATION BY MASS
RP 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 [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-148; LYS-157 AND LYS-170, AND
RP IDENTIFICATION BY MASS 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).
CC -!- FUNCTION: Mediates the electroneutral exchange of acylcarnitines (O-
CC acyl-(R)-carnitine or L-acylcarnitine) of different acyl chain lengths
CC (ranging from O-acetyl-(R)-carnitine to long-chain O-acyl-(R)-
CC carnitines) with free carnitine ((R)-carnitine or L-carnitine) across
CC the mitochondrial inner membrane, via a ping-pong mechanism. Key player
CC in the mitochondrial oxidation pathway, it translocates the fatty acids
CC in the form of acylcarnitines into the mitochondrial matrix, where the
CC carnitine palmitoyltransferase 2 (CPT-2) activates them to undergo
CC fatty acid beta-oxidation. Catalyzes the unidirectional transport
CC (uniport) of carnitine at lower rates than the antiport (exchange).
CC {ECO:0000250|UniProtKB:O43772}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-carnitine(out) + O-acetyl-(R)-carnitine(in) = (R)-
CC carnitine(in) + O-acetyl-(R)-carnitine(out); Xref=Rhea:RHEA:49908,
CC ChEBI:CHEBI:16347, ChEBI:CHEBI:57589;
CC Evidence={ECO:0000250|UniProtKB:P97521};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-carnitine(out) + O-acyl-(R)-carnitine(in) = (R)-
CC carnitine(in) + O-acyl-(R)-carnitine(out); Xref=Rhea:RHEA:49924,
CC ChEBI:CHEBI:16347, ChEBI:CHEBI:75659;
CC Evidence={ECO:0000250|UniProtKB:O43772};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-carnitine(out) + O-propanoyl-(R)-carnitine(in) = (R)-
CC carnitine(in) + O-propanoyl-(R)-carnitine(out); Xref=Rhea:RHEA:49912,
CC ChEBI:CHEBI:16347, ChEBI:CHEBI:53210;
CC Evidence={ECO:0000250|UniProtKB:P97521};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-carnitine(out) + O-hexadecanoyl-(R)-carnitine(in) = (R)-
CC carnitine(in) + O-hexadecanoyl-(R)-carnitine(out);
CC Xref=Rhea:RHEA:49916, ChEBI:CHEBI:16347, ChEBI:CHEBI:17490;
CC Evidence={ECO:0000250|UniProtKB:P97521};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-carnitine(out) + O-octanoyl-(R)-carnitine(in) = (R)-
CC carnitine(in) + O-octanoyl-(R)-carnitine(out); Xref=Rhea:RHEA:49920,
CC ChEBI:CHEBI:16347, ChEBI:CHEBI:18102;
CC Evidence={ECO:0000250|UniProtKB:P97521};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-carnitine(in) = (R)-carnitine(out); Xref=Rhea:RHEA:34959,
CC ChEBI:CHEBI:16347; Evidence={ECO:0000250|UniProtKB:O43772};
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Widely expressed, with highest levels in the liver,
CC intermediate levels in heart, testis and kidney and low levels in
CC brain, including cortex, cerebellum, hippocampus and hypothalamus.
CC {ECO:0000269|PubMed:19287344}.
CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC {ECO:0000305}.
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DR EMBL; AB017112; BAA74768.1; -; mRNA.
DR EMBL; AK075624; BAC35865.1; -; mRNA.
DR EMBL; AK152436; BAE31218.1; -; mRNA.
DR EMBL; BC029733; AAH29733.1; -; mRNA.
DR CCDS; CCDS23535.1; -.
DR RefSeq; NP_065266.1; NM_020520.4.
DR AlphaFoldDB; Q9Z2Z6; -.
DR SMR; Q9Z2Z6; -.
DR BioGRID; 208247; 5.
DR IntAct; Q9Z2Z6; 3.
DR STRING; 10090.ENSMUSP00000035222; -.
DR iPTMnet; Q9Z2Z6; -.
DR PhosphoSitePlus; Q9Z2Z6; -.
DR SwissPalm; Q9Z2Z6; -.
DR EPD; Q9Z2Z6; -.
DR jPOST; Q9Z2Z6; -.
DR MaxQB; Q9Z2Z6; -.
DR PaxDb; 10090-ENSMUSP00000035222; -.
DR ProteomicsDB; 252741; -.
DR Pumba; Q9Z2Z6; -.
DR Antibodypedia; 3111; 257 antibodies from 27 providers.
DR DNASU; 57279; -.
DR Ensembl; ENSMUST00000035222.6; ENSMUSP00000035222.6; ENSMUSG00000032602.7.
DR GeneID; 57279; -.
DR KEGG; mmu:57279; -.
DR UCSC; uc009rqs.1; mouse.
DR AGR; MGI:1928738; -.
DR CTD; 788; -.
DR MGI; MGI:1928738; Slc25a20.
DR VEuPathDB; HostDB:ENSMUSG00000032602; -.
DR eggNOG; KOG0758; Eukaryota.
DR GeneTree; ENSGT00940000157863; -.
DR HOGENOM; CLU_015166_16_0_1; -.
DR InParanoid; Q9Z2Z6; -.
DR OMA; QQKCPED; -.
DR OrthoDB; 4064096at2759; -.
DR PhylomeDB; Q9Z2Z6; -.
DR TreeFam; TF300894; -.
DR Reactome; R-MMU-200425; Carnitine metabolism.
DR BioGRID-ORCS; 57279; 3 hits in 80 CRISPR screens.
DR ChiTaRS; Slc25a20; mouse.
DR PRO; PR:Q9Z2Z6; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q9Z2Z6; Protein.
DR Bgee; ENSMUSG00000032602; Expressed in brown adipose tissue and 259 other cell types or tissues.
DR Genevisible; Q9Z2Z6; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005740; C:mitochondrial envelope; IBA:GO_Central.
DR GO; GO:0005743; C:mitochondrial inner membrane; HDA:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0015227; F:acyl carnitine transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:1902603; P:carnitine transmembrane transport; ISS:UniProtKB.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR GO; GO:0006839; P:mitochondrial transport; IBA:GO_Central.
DR Gene3D; 1.50.40.10; Mitochondrial carrier domain; 2.
DR InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR InterPro; IPR023395; Mt_carrier_dom_sf.
DR PANTHER; PTHR45624; MITOCHONDRIAL BASIC AMINO ACIDS TRANSPORTER-RELATED; 1.
DR PANTHER; PTHR45624:SF56; MITOCHONDRIAL CARNITINE_ACYLCARNITINE CARRIER PROTEIN; 1.
DR Pfam; PF00153; Mito_carr; 3.
DR SUPFAM; SSF103506; Mitochondrial carrier; 1.
DR PROSITE; PS50920; SOLCAR; 3.
PE 1: Evidence at protein level;
KW Acetylation; Lipid transport; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O43772"
FT CHAIN 2..301
FT /note="Mitochondrial carnitine/acylcarnitine carrier
FT protein"
FT /id="PRO_0000090630"
FT TOPO_DOM 2..12
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 13..31
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 32..73
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 74..93
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 94..112
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 113..131
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 132..170
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 171..190
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 191..211
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 212..230
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 231..267
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 268..287
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 288..301
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 8..99
FT /note="Solcar 1"
FT REPEAT 108..196
FT /note="Solcar 2"
FT REPEAT 207..293
FT /note="Solcar 3"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:O43772"
FT MOD_RES 148
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 157
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 170
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 170
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
SQ SEQUENCE 301 AA; 33027 MW; 0E332BF4D7584490 CRC64;
MADEPKPISP FKNLLAGGFG GMCLVFVGHP LDTVKVRLQT QPPSLSGQPP MYSGTLDCFR
KTLMREGITG LYRGMAAPII GVTPMFAVCF FGFGLGKKLQ QKSPEDELSY PQLFTAGMLS
GVFTTGIMTP GERIKCLLQI QASSGENKYS GTLDCAKKLY QEFGIRGFYK GTVLTLMRDV
PASGMYFMTY EWLKNLFTPE GKSVSDLSVP RILVAGGFAG IFNWAVAIPP DVLKSRFQTA
PPGKYPNGFR DVLRELIREE GVTSLYKGFN AVMIRAFPAN AACFLGFEIA MKFLNWIAPN
L
//
