DIT1_ARATH
ID DIT1_ARATH Reviewed; 557 AA.
AC Q9LXV3; Q93Y83;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 116.
DE RecName: Full=Dicarboxylate transporter 1, chloroplastic;
DE AltName: Full=2-oxoglutarate/malate translocator 1;
DE Short=AtpOMT1;
DE Flags: Precursor;
GN Name=DIT1; OrderedLocusNames=At5g12860; ORFNames=T24H18.30;
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] OF 17-557.
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 FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, INDUCTION, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=12154133; DOI=10.1093/pcp/pcf109;
RA Taniguchi M., Taniguchi Y., Kawasaki M., Takeda S., Kato T., Sato S.,
RA Tabata S., Miyake H., Sugiyama T.;
RT "Identifying and characterizing plastidic 2-oxoglutarate/malate and
RT dicarboxylate transporters in Arabidopsis thaliana.";
RL Plant Cell Physiol. 43:706-717(2002).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=12887583; DOI=10.1046/j.1365-313x.2003.01806.x;
RA Renne P., Dressen U., Hebbeker U., Hille D., Flugge U.I., Westhoff P.,
RA Weber A.P.;
RT "The Arabidopsis mutant dct is deficient in the plastidic glutamate/malate
RT translocator DiT2.";
RL Plant J. 35:316-331(2003).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21175886; DOI=10.1111/j.1365-313x.2010.04397.x;
RA Kinoshita H., Nagasaki J., Yoshikawa N., Yamamoto A., Takito S.,
RA Kawasaki M., Sugiyama T., Miyake H., Weber A.P., Taniguchi M.;
RT "The chloroplastic 2-oxoglutarate/malate transporter has dual function as
RT the malate valve and in carbon/nitrogen metabolism.";
RL Plant J. 65:15-26(2011).
CC -!- FUNCTION: 2-oxoglutarate/malate translocator involved with DIT2-1 in
CC primary ammonia assimilation and in the re-assimilation of ammonia
CC generated by the photorespiratory pathway. Imports 2-oxoglutarate into
CC plastids as precursor for ammonia assimilation. 2-oxoglutarate is
CC converted to glutamate, the end product of ammonia assimilation, which
CC is exported to the cytosol by DIT2-1. {ECO:0000269|PubMed:12154133,
CC ECO:0000269|PubMed:21175886}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.7 mM for malate {ECO:0000269|PubMed:12154133};
CC KM=0.042 mM for oxaloacetate {ECO:0000269|PubMed:12154133};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast inner membrane
CC {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9LXV3-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in roots, rosette and cauline leaves,
CC stems, flowers and siliques. {ECO:0000269|PubMed:12154133,
CC ECO:0000269|PubMed:12887583}.
CC -!- INDUCTION: By nitrate after two days of nitrogen deprivation and re-
CC illumination after three days of dark adaptation.
CC {ECO:0000269|PubMed:12154133}.
CC -!- DISRUPTION PHENOTYPE: Reduced growth and amino acid levels, but growth
CC inhibition is prevented when mutant plants are grown under non-
CC photorespiratory high CO(2) conditions. {ECO:0000269|PubMed:12154133,
CC ECO:0000269|PubMed:21175886}.
CC -!- SIMILARITY: Belongs to the SLC13A/DASS transporter (TC 2.A.47) family.
CC DIT1 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK43871.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL353013; CAB88250.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91822.1; -; Genomic_DNA.
DR EMBL; AF370494; AAK43871.1; ALT_INIT; mRNA.
DR PIR; T49900; T49900.
DR RefSeq; NP_568283.2; NM_121289.4. [Q9LXV3-1]
DR AlphaFoldDB; Q9LXV3; -.
DR SMR; Q9LXV3; -.
DR BioGRID; 16404; 36.
DR IntAct; Q9LXV3; 35.
DR STRING; 3702.AT5G12860.1; -.
DR SwissPalm; Q9LXV3; -.
DR PaxDb; Q9LXV3; -.
DR ProteomicsDB; 222149; -. [Q9LXV3-1]
DR EnsemblPlants; AT5G12860.1; AT5G12860.1; AT5G12860. [Q9LXV3-1]
DR GeneID; 831126; -.
DR Gramene; AT5G12860.1; AT5G12860.1; AT5G12860. [Q9LXV3-1]
DR KEGG; ath:AT5G12860; -.
DR Araport; AT5G12860; -.
DR TAIR; locus:2182270; AT5G12860.
DR eggNOG; ENOG502QQ8W; Eukaryota.
DR HOGENOM; CLU_005170_7_3_1; -.
DR InParanoid; Q9LXV3; -.
DR OMA; GLNPNAW; -.
DR PhylomeDB; Q9LXV3; -.
DR SABIO-RK; Q9LXV3; -.
DR PRO; PR:Q9LXV3; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LXV3; baseline and differential.
DR Genevisible; Q9LXV3; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0009706; C:chloroplast inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009534; C:chloroplast thylakoid; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0015139; F:alpha-ketoglutarate transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0015140; F:malate transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0015131; F:oxaloacetate transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0015742; P:alpha-ketoglutarate transport; IDA:UniProtKB.
DR GO; GO:0019676; P:ammonia assimilation cycle; IMP:UniProtKB.
DR GO; GO:0071423; P:malate transmembrane transport; IDA:UniProtKB.
DR GO; GO:0015729; P:oxaloacetate transport; IDA:UniProtKB.
DR GO; GO:0009624; P:response to nematode; HEP:TAIR.
DR InterPro; IPR030676; CitT-rel.
DR InterPro; IPR001898; SLC13A/DASS.
DR PANTHER; PTHR42826; PTHR42826; 1.
DR Pfam; PF00939; Na_sulph_symp; 1.
DR TIGRFAMs; TIGR00785; dass; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chloroplast; Membrane; Plastid;
KW Plastid inner membrane; Reference proteome; Transit peptide; Transmembrane;
KW Transmembrane helix; Transport.
FT TRANSIT 1..69
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 70..557
FT /note="Dicarboxylate transporter 1, chloroplastic"
FT /id="PRO_0000419183"
FT TRANSMEM 90..110
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 122..142
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 158..178
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 229..249
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 256..276
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 305..325
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 355..375
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 376..396
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 411..431
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 438..458
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 477..497
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 531..551
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CONFLICT 496
FT /note="L -> H (in Ref. 3; AAK43871)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 557 AA; 59213 MW; 13AE5458E9C5337C CRC64;
MASLALSGSC SLAFPLKSRS LSLPRPPSSS LNLTKPLRSL DSRFSLLKSP LPVSLRRRSS
TLVKASSTVA SASSSPTPPL VPAPVPWQGA AIKPLLASIA TGLILWFVPV PEGVTRNAWQ
LLAIFLATIV GIITQPLPLG AVALMGLGAS VLTKTLTFAA AFSAFGDPIP WLIALAFFFA
RGFIKTGLGN RVAYQFVRLF GSSSLGLGYS LVFSEALLAP AIPSVSARAG GIFLPLVKSL
CVACGSNVGD GTEHRLGSWL MLTCFQTSVI SSSMFLTAMA ANPLSANLAF NTIKQTIGWT
DWAKAAIVPG LVSLIVVPFL LYLIYPPTVK SSPDAPKLAQ EKLDKMGPMS KNELIMAATL
FLTVGLWIFG AKLGVDAVTA AILGLSVLLV TGVVTWKECL AESVAWDTLT WFAALIAMAG
YLNKYGLIEW FSQTVVKFVG GLGLSWQLSF GILVLLYFYT HYFFASGAAH IGAMFTAFLS
VSTALGTPPY FAALVLAFLS NLMGGLTHYG IGSAPIFYGA NYVPLAKWWG YGFLISIVNI
LIWLGVGGAW WKFIGLW
