MCAT_ARATH
ID MCAT_ARATH Reviewed; 300 AA.
AC Q93XM7; Q9FIP5;
DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Mitochondrial carnitine/acylcarnitine carrier-like protein;
DE AltName: Full=Carnitine/acylcarnitine translocase-like protein;
DE Short=CAC-like protein;
DE AltName: Full=Protein A BOUT DE SOUFFLE;
GN Name=BOU; OrderedLocusNames=At5g46800; ORFNames=MZA15.23;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia; TISSUE=Seedling hypocotyl;
RX PubMed=12215513; DOI=10.1105/tpc.002485;
RA Lawand S., Dorne A.-J., Long D., Coupland G., Mache R., Carol P.;
RT "Arabidopsis A BOUT DE SOUFFLE, which is homologous with mammalian
RT carnitine acyl carrier, is required for postembryonic growth in the
RT light.";
RL Plant Cell 14:2161-2173(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10048488; DOI=10.1093/dnares/5.6.379;
RA Asamizu E., Sato S., Kaneko T., Nakamura Y., Kotani H., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VIII. Sequence
RT features of the regions of 1,081,958 bp covered by seventeen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:379-391(1998).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=14671022; DOI=10.1105/tpc.016055;
RA Heazlewood J.L., Tonti-Filippini J.S., Gout A.M., Day D.A., Whelan J.,
RA Millar A.H.;
RT "Experimental analysis of the Arabidopsis mitochondrial proteome highlights
RT signaling and regulatory components, provides assessment of targeting
RT prediction programs, and indicates plant-specific mitochondrial proteins.";
RL Plant Cell 16:241-256(2004).
RN [6]
RP GENE FAMILY.
RX PubMed=15003237; DOI=10.1016/j.tplants.2004.01.007;
RA Picault N., Hodges M., Palmieri L., Palmieri F.;
RT "The growing family of mitochondrial carriers in Arabidopsis.";
RL Trends Plant Sci. 9:138-146(2004).
RN [7]
RP FUNCTION, TISSUE SPECIFICITY, INDUCTION BY LIGHT; NORFLURAZON AND
RP LINCOMYCIN, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=23181524; DOI=10.1111/tpj.12082;
RA Eisenhut M., Planchais S., Cabassa C., Guivarc'h A., Justin A.M.,
RA Taconnat L., Renou J.P., Linka M., Gagneul D., Timm S., Bauwe H., Carol P.,
RA Weber A.P.;
RT "Arabidopsis A BOUT DE SOUFFLE is a putative mitochondrial transporter
RT involved in photorespiratory metabolism and is required for meristem growth
RT at ambient CO(2) levels.";
RL Plant J. 73:836-849(2013).
CC -!- FUNCTION: Involved in photorespiratory metabolism. Acts probably as a
CC carrier for a glycine decarboxylase (GDC) cofactor or, alternatively,
CC may act as a mitochondrial glycine shuttle. Involved in the transition
CC from the embryonic stage to the juvenile autotrophic stage.
CC {ECO:0000269|PubMed:12215513, ECO:0000269|PubMed:23181524}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:12215513, ECO:0000269|PubMed:14671022}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:12215513,
CC ECO:0000269|PubMed:14671022}.
CC -!- TISSUE SPECIFICITY: High expression in cotyledons, leaves, flowers and
CC developing siliques. Lower expression in roots and maturing siliques.
CC Not detected in meristematic tissues. {ECO:0000269|PubMed:23181524}.
CC -!- DEVELOPMENTAL STAGE: Detected two days after germination and reached a
CC maximum at three days of growth.
CC -!- INDUCTION: Up-regulated by light and down-regulated by norflurazon and
CC lincomycin. Low expression in the dark. {ECO:0000269|PubMed:23181524}.
CC -!- DISRUPTION PHENOTYPE: Chlorotic leaves and impaired growth when grown
CC under ambient air, but normal growth under CO(2)-enriched air.
CC {ECO:0000269|PubMed:23181524}.
CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB08924.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AJ277732; CAC38047.1; -; mRNA.
DR EMBL; AB016882; BAB08924.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED95428.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM70893.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM70894.1; -; Genomic_DNA.
DR EMBL; AY136374; AAM97040.1; -; mRNA.
DR EMBL; BT000165; AAN15484.1; -; mRNA.
DR RefSeq; NP_001332469.1; NM_001344699.1.
DR RefSeq; NP_001332470.1; NM_001344700.1.
DR RefSeq; NP_568670.1; NM_124051.5.
DR AlphaFoldDB; Q93XM7; -.
DR SMR; Q93XM7; -.
DR BioGRID; 19972; 19.
DR STRING; 3702.AT5G46800.1; -.
DR TCDB; 2.A.29.8.16; the mitochondrial carrier (mc) family.
DR PaxDb; Q93XM7; -.
DR PRIDE; Q93XM7; -.
DR ProteomicsDB; 250824; -.
DR DNASU; 834724; -.
DR EnsemblPlants; AT5G46800.1; AT5G46800.1; AT5G46800.
DR EnsemblPlants; AT5G46800.2; AT5G46800.2; AT5G46800.
DR EnsemblPlants; AT5G46800.3; AT5G46800.3; AT5G46800.
DR GeneID; 834724; -.
DR Gramene; AT5G46800.1; AT5G46800.1; AT5G46800.
DR Gramene; AT5G46800.2; AT5G46800.2; AT5G46800.
DR Gramene; AT5G46800.3; AT5G46800.3; AT5G46800.
DR KEGG; ath:AT5G46800; -.
DR Araport; AT5G46800; -.
DR TAIR; locus:2178590; AT5G46800.
DR eggNOG; KOG0758; Eukaryota.
DR HOGENOM; CLU_015166_16_3_1; -.
DR InParanoid; Q93XM7; -.
DR OMA; QYTIGQI; -.
DR OrthoDB; 1072378at2759; -.
DR PhylomeDB; Q93XM7; -.
DR PRO; PR:Q93XM7; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q93XM7; baseline and differential.
DR Genevisible; Q93XM7; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
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; HDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0000064; F:L-ornithine transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:1990575; P:mitochondrial L-ornithine transmembrane transport; IBA:GO_Central.
DR GO; GO:0006839; P:mitochondrial transport; IDA:TAIR.
DR Gene3D; 1.50.40.10; -; 1.
DR InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR InterPro; IPR023395; Mt_carrier_dom_sf.
DR Pfam; PF00153; Mito_carr; 3.
DR SUPFAM; SSF103506; SSF103506; 1.
DR PROSITE; PS50920; SOLCAR; 3.
PE 1: Evidence at protein level;
KW Membrane; Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..300
FT /note="Mitochondrial carnitine/acylcarnitine carrier-like
FT protein"
FT /id="PRO_0000090634"
FT TRANSMEM 8..28
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 64..84
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 108..128
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TRANSMEM 176..195
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 211..231
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TRANSMEM 273..292
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT REPEAT 2..93
FT /note="Solcar 1"
FT REPEAT 102..201
FT /note="Solcar 2"
FT REPEAT 211..298
FT /note="Solcar 3"
SQ SEQUENCE 300 AA; 31023 MW; 2148A7BF6EB388AB CRC64;
MADAWKDLAS GTVGGAAQLV VGHPFDTIKV KLQSQPTPAP GQLPRYTGAI DAVKQTVASE
GTKGLYKGMG APLATVAAFN AVLFTVRGQM EGLLRSEAGV PLTISQQFVA GAGAGFAVSF
LACPTELIKC RLQAQGALAG ASTTSSVVAA VKYGGPMDVA RHVLRSEGGA RGLFKGLFPT
FAREVPGNAT MFAAYEAFKR FLAGGSDTSS LGQGSLIMAG GVAGASFWGI VYPTDVVKSV
LQVDDYKNPR YTGSMDAFRK ILKSEGVKGL YKGFGPAMAR SVPANAACFL AYEMTRSSLG
