TAAC_ARATH
ID TAAC_ARATH Reviewed; 415 AA.
AC Q9M024; Q8LCT8;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Thylakoid ADP,ATP carrier protein, chloroplastic;
DE AltName: Full=Thylakoid ADP/ATP translocase;
DE Flags: Precursor;
GN Name=TAAC; OrderedLocusNames=At5g01500; ORFNames=F7A7.20;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
RP IDENTIFICATION, FUNCTION, DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE, TISSUE
RP SPECIFICITY, SUBCELLULAR LOCATION, ACTIVITY REGULATION, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=17261580; DOI=10.1074/jbc.m609130200;
RA Thuswaldner S., Lagerstedt J.O., Rojas-Stuetz M., Bouhidel K., Der C.,
RA Leborgne-Castel N., Mishra A., Marty F., Schoefs B., Adamska I.,
RA Persson B.L., Spetea C.;
RT "Identification, expression, and functional analyses of a thylakoid ATP/ADP
RT carrier from Arabidopsis.";
RL J. Biol. Chem. 282:8848-8859(2007).
CC -!- FUNCTION: Specifically transports adenine nucleotides. Involved in the
CC uptake of ATP into thylakoids in exchange for lumenal ADP.
CC {ECO:0000269|PubMed:17261580}.
CC -!- ACTIVITY REGULATION: KM and Vmax values toward ATP only are increased
CC by m-chlorocarbonyl cyanide phenylhydrazone (CCCP). The corresponding
CC values for ADP are not affected. {ECO:0000269|PubMed:17261580}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=47 uM for ATP (for the recombinant protein)
CC {ECO:0000269|PubMed:17261580};
CC KM=0.5 uM for ATP (in vivo) {ECO:0000269|PubMed:17261580};
CC KM=45 uM for ADP (for the recombinant protein)
CC {ECO:0000269|PubMed:17261580};
CC Vmax=0.71 nmol/h/mg enzyme toward ATP (for the recombinant protein)
CC {ECO:0000269|PubMed:17261580};
CC Vmax=0.53 nmol/h/mg enzyme toward ADP (for the recombinant protein)
CC {ECO:0000269|PubMed:17261580};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000269|PubMed:17261580}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:17261580}. Plastid, chloroplast envelope
CC {ECO:0000269|PubMed:17261580}. Note=Detected only in low amounts in the
CC chloroplast envelope and in non-photosynthetic plastids.
CC -!- TISSUE SPECIFICITY: Highly expressed in developing photosynthetic
CC organs such as leaves, flower buds and green siliques. Also detected in
CC roots, flowers, mature leaves and stems. {ECO:0000269|PubMed:17261580}.
CC -!- DEVELOPMENTAL STAGE: Expressed in dark-grown seedlings and remains
CC stable throughout the greening process. Highest expression in
CC developing green tissues and in leaves undergoing senescence or abiotic
CC stress, with the exception of heat shock conditions that induced a
CC drastic reduction of expression. {ECO:0000269|PubMed:17261580}.
CC -!- DISRUPTION PHENOTYPE: Plants show a 30-40% reduction in the thylakoid
CC ATP transport and metabolism. {ECO:0000269|PubMed:17261580}.
CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC {ECO:0000305}.
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DR EMBL; AL161946; CAB82266.1; -; Genomic_DNA.
DR EMBL; CP002688; AED90353.1; -; Genomic_DNA.
DR EMBL; AY074566; AAL67106.1; -; mRNA.
DR EMBL; BT006336; AAP21144.1; -; mRNA.
DR EMBL; AY086408; AAM64475.1; -; mRNA.
DR PIR; T48171; T48171.
DR RefSeq; NP_195770.1; NM_120228.4.
DR AlphaFoldDB; Q9M024; -.
DR SMR; Q9M024; -.
DR STRING; 3702.AT5G01500.1; -.
DR TCDB; 2.A.29.23.3; the mitochondrial carrier (mc) family.
DR PaxDb; Q9M024; -.
DR PRIDE; Q9M024; -.
DR ProteomicsDB; 245278; -.
DR EnsemblPlants; AT5G01500.1; AT5G01500.1; AT5G01500.
DR GeneID; 831861; -.
DR Gramene; AT5G01500.1; AT5G01500.1; AT5G01500.
DR KEGG; ath:AT5G01500; -.
DR Araport; AT5G01500; -.
DR TAIR; locus:2149725; AT5G01500.
DR eggNOG; KOG0752; Eukaryota.
DR HOGENOM; CLU_015166_10_5_1; -.
DR InParanoid; Q9M024; -.
DR OMA; YPTDMVK; -.
DR OrthoDB; 1253450at2759; -.
DR PhylomeDB; Q9M024; -.
DR SABIO-RK; Q9M024; -.
DR PRO; PR:Q9M024; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9M024; baseline and differential.
DR Genevisible; Q9M024; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0009526; C:plastid envelope; IDA:TAIR.
DR GO; GO:0042651; C:thylakoid membrane; IDA:TAIR.
DR GO; GO:0005347; F:ATP transmembrane transporter activity; IDA:TAIR.
DR GO; GO:0010117; P:photoprotection; IMP:TAIR.
DR GO; GO:0010206; P:photosystem II repair; IMP:TAIR.
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 Chloroplast; Membrane; Plastid; Reference proteome; Repeat; Thylakoid;
KW Transit peptide; Transmembrane; Transmembrane helix; Transport.
FT TRANSIT 1..61
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 62..415
FT /note="Thylakoid ADP,ATP carrier protein, chloroplastic"
FT /id="PRO_0000313084"
FT TRANSMEM 106..126
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TRANSMEM 182..207
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TRANSMEM 219..239
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TRANSMEM 273..293
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TRANSMEM 309..329
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TRANSMEM 362..388
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT REPEAT 113..205
FT /note="Solcar 1"
FT REPEAT 213..296
FT /note="Solcar 2"
FT REPEAT 307..387
FT /note="Solcar 3"
FT BINDING 187
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:P02722"
FT BINDING 330
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:P02722"
FT CONFLICT 411
FT /note="I -> T (in Ref. 4; AAM64475)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 415 AA; 45090 MW; D32B575A04994C2B CRC64;
MGEEKSLLQF RSFPSLKTSD FALTEEPSWR LENNVSSNRR RGNKRSGGVF TNFASLSVAI
RRDRRESTFN GRNGGGGGAF ASVSVVIPKE EDEFAPTSAQ LLKNPIALLS IVPKDAALFF
AGAFAGAAAK SVTAPLDRIK LLMQTHGVRA GQQSAKKAIG FIEAITLIGK EEGIKGYWKG
NLPQVIRIVP YSAVQLFAYE TYKKLFRGKD GQLSVLGRLG AGACAGMTST LITYPLDVLR
LRLAVEPGYR TMSQVALNML REEGVASFYN GLGPSLLSIA PYIAINFCVF DLVKKSLPEK
YQQKTQSSLL TAVVAAAIAT GTCYPLDTIR RQMQLKGTPY KSVLDAFSGI IAREGVVGLY
RGFVPNALKS MPNSSIKLTT FDIVKKLIAA SEKEIQRIAD DNRKKASPNT IDEQT
