MCATL_MOUSE
ID MCATL_MOUSE Reviewed; 306 AA.
AC Q8BL03; Q922X4;
DT 30-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Mitochondrial basic amino acids transporter;
DE AltName: Full=Carnitine/acylcarnitine translocase-like;
DE Short=CACT-like;
DE AltName: Full=Mitochondrial carnitine/acylcarnitine carrier protein CACL;
DE AltName: Full=Mitochondrial ornithine transporter 3;
DE AltName: Full=Solute carrier family 25 member 29;
GN Name=Slc25a29; Synonyms=Ornt3 {ECO:0000303|PubMed:19287344};
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], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND INDUCTION.
RX PubMed=12882971; DOI=10.1074/jbc.m306372200;
RA Sekoguchi E., Sato N., Yasui A., Fukada S., Nimura Y., Aburatani H.,
RA Ikeda K., Matsuura A.;
RT "A novel mitochondrial carnitine-acylcarnitine translocase induced by
RT partial hepatectomy and fasting.";
RL J. Biol. Chem. 278:38796-38802(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Corpus striatum;
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 TISSUE=Mammary tumor;
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 FUNCTION, SUBCELLULAR LOCATION, AND 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=Heart, and Kidney;
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).
CC -!- FUNCTION: Transports arginine, lysine, homoarginine, methylarginine
CC and, to a much lesser extent, ornithine and histidine. Does not
CC transport carnitine nor acylcarnitines. Functions by both counter-
CC exchange and uniport mechanisms (By similarity). Can restore ornithine
CC transport in cells lacking the primary mitochondrial ornithine
CC transporter SLC25A15 (PubMed:19287344). {ECO:0000250|UniProtKB:Q8N8R3,
CC ECO:0000269|PubMed:19287344}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:12882971, ECO:0000269|PubMed:19287344}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:12882971,
CC ECO:0000269|PubMed:19287344}.
CC -!- TISSUE SPECIFICITY: Widely expressed, with highest levels in the brain,
CC including cortex, cerebellum, hippocampus and hypothalamus, and
CC moderate levels in liver, kidney, heart and testis.
CC {ECO:0000269|PubMed:12882971, ECO:0000269|PubMed:19287344}.
CC -!- INDUCTION: By partial hepactectomy and fasting.
CC {ECO:0000269|PubMed:12882971}.
CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC {ECO:0000305}.
CC -!- CAUTION: Was initially proposed to transport palmitoylcarnitine, based
CC on complementation experiments in yeast mutants lacking CRC1 and CIT2
CC and release of radiolabeled carnitine from mitochondria incubated with
CC radiolabeled palmitoylcarnithine (PubMed:12882971). Later experiments
CC done primarily with human indicate the protein functions instead as
CC transporter of basic amino acids. {ECO:0000269|PubMed:12882971,
CC ECO:0000305}.
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DR EMBL; AK047628; BAC33105.1; -; mRNA.
DR EMBL; BC006711; AAH06711.1; -; mRNA.
DR CCDS; CCDS26164.1; -.
DR RefSeq; NP_851845.1; NM_181328.3.
DR AlphaFoldDB; Q8BL03; -.
DR SMR; Q8BL03; -.
DR BioGRID; 229553; 1.
DR STRING; 10090.ENSMUSP00000021693; -.
DR TCDB; 2.A.29.8.5; the mitochondrial carrier (mc) family.
DR PhosphoSitePlus; Q8BL03; -.
DR SwissPalm; Q8BL03; -.
DR EPD; Q8BL03; -.
DR MaxQB; Q8BL03; -.
DR PaxDb; Q8BL03; -.
DR PeptideAtlas; Q8BL03; -.
DR PRIDE; Q8BL03; -.
DR ProteomicsDB; 295839; -.
DR Antibodypedia; 14405; 36 antibodies from 16 providers.
DR DNASU; 214663; -.
DR Ensembl; ENSMUST00000021693; ENSMUSP00000021693; ENSMUSG00000021265.
DR GeneID; 214663; -.
DR KEGG; mmu:214663; -.
DR UCSC; uc007pad.1; mouse.
DR CTD; 123096; -.
DR MGI; MGI:2444911; Slc25a29.
DR VEuPathDB; HostDB:ENSMUSG00000021265; -.
DR eggNOG; KOG0762; Eukaryota.
DR GeneTree; ENSGT00940000157766; -.
DR HOGENOM; CLU_015166_16_1_1; -.
DR InParanoid; Q8BL03; -.
DR OMA; IFWLTSY; -.
DR OrthoDB; 1072378at2759; -.
DR PhylomeDB; Q8BL03; -.
DR TreeFam; TF351739; -.
DR Reactome; R-MMU-352230; Amino acid transport across the plasma membrane.
DR BioGRID-ORCS; 214663; 0 hits in 77 CRISPR screens.
DR ChiTaRS; Slc25a29; mouse.
DR PRO; PR:Q8BL03; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q8BL03; protein.
DR Bgee; ENSMUSG00000021265; Expressed in gastrula and 231 other tissues.
DR Genevisible; Q8BL03; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0015227; F:acyl carnitine transmembrane transporter activity; IDA:MGI.
DR GO; GO:0015174; F:basic amino acid transmembrane transporter activity; IMP:UniProtKB.
DR GO; GO:0005289; F:high-affinity L-arginine transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0005292; F:high-affinity lysine transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0006844; P:acyl carnitine transport; IDA:MGI.
DR GO; GO:1903826; P:L-arginine transmembrane transport; ISS:UniProtKB.
DR GO; GO:0089709; P:L-histidine transmembrane transport; ISS:UniProtKB.
DR GO; GO:1903401; P:L-lysine transmembrane transport; ISS:UniProtKB.
DR GO; GO:1990575; P:mitochondrial L-ornithine transmembrane transport; IMP:UniProtKB.
DR GO; GO:0015822; P:ornithine transport; ISS:UniProtKB.
DR Gene3D; 1.50.40.10; -; 1.
DR InterPro; IPR002067; Mit_carrier.
DR InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR InterPro; IPR023395; Mt_carrier_dom_sf.
DR Pfam; PF00153; Mito_carr; 3.
DR PRINTS; PR00926; MITOCARRIER.
DR SUPFAM; SSF103506; SSF103506; 1.
DR PROSITE; PS50920; SOLCAR; 3.
PE 1: Evidence at protein level;
KW Amino-acid transport; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..306
FT /note="Mitochondrial basic amino acids transporter"
FT /id="PRO_0000090633"
FT TRANSMEM 2..22
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 61..81
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 96..116
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TRANSMEM 153..172
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 187..207
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TRANSMEM 255..275
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT REPEAT 2..86
FT /note="Solcar 1"
FT REPEAT 90..178
FT /note="Solcar 2"
FT REPEAT 190..275
FT /note="Solcar 3"
FT REGION 284..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..306
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 306 AA; 32672 MW; F62E9CA8066B4BC7 CRC64;
MALDFLAGCA GGVAGVIVGH PFDIVKVRLQ VQSTEKPQYR GTLHCFQSII KQESVLGLYK
GLGSPLMGLT FINALVFGVQ GNTLRALGQD SPLNQFLAGA AAGAIQCVIC CPMELAKTRL
QLQAVGPART YKGSLDCLVQ IYRHEGLRGI NRGMVSTLLR ETPSFGVYFL TYDVMTRAMG
CEPGDRLLVP KLLLAGGTSG ITSWLSTYPM DVVKSRLQAD GLQGTPRYRG IVDCMRQSYQ
AEGWQVFTRG LASTLLRAFP VNAATFATVT VVLTYTRGEE AQVDSEAALG TSPTPAGSAL
AQPSSL
