ID   DIT2_SPIOL              Reviewed;         564 AA.
AC   Q8L7Z9;
DT   03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   25-MAY-2022, entry version 45.
DE   RecName: Full=Dicarboxylate transporter 2, chloroplastic;
DE   AltName: Full=Glutamate/malate translocator;
DE   Flags: Precursor;
GN   Name=DIT2;
OS   Spinacia oleracea (Spinach).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   Caryophyllales; Chenopodiaceae; Chenopodioideae; Anserineae; Spinacia.
OX   NCBI_TaxID=3562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND
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).
CC   -!- FUNCTION: Glutamate/malate translocator involved with DIT1 in primary
CC       ammonia assimilation and in the re-assimilation of ammonia generated by
CC       the photorespiratory pathway. Exports the end product of ammonia
CC       assimilation, glutamate, from plastids to the cytosol. The precursor
CC       for ammonia assimilation, 2-oxoglutarate, is imported from the cytosol
CC       by DIT1. {ECO:0000269|PubMed:12887583}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.30 mM for malate {ECO:0000269|PubMed:12887583};
CC         KM=1.59 mM for glutamate {ECO:0000269|PubMed:12887583};
CC         KM=2.46 mM for 2-oxoglutarate {ECO:0000269|PubMed:12887583};
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast inner membrane
CC       {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed in leaves. {ECO:0000269|PubMed:12887583}.
CC   -!- SIMILARITY: Belongs to the SLC13A/DASS transporter (TC 2.A.47) family.
CC       DIT1 subfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AY123846; AAM89396.1; -; mRNA.
DR   AlphaFoldDB; Q8L7Z9; -.
DR   SMR; Q8L7Z9; -.
DR   OrthoDB; 842017at2759; -.
DR   SABIO-RK; Q8L7Z9; -.
DR   GO; GO:0009706; C:chloroplast inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005313; F:L-glutamate transmembrane transporter activity; IDA:UniProtKB.
DR   GO; GO:0015140; F:malate transmembrane transporter activity; IDA:UniProtKB.
DR   GO; GO:0015813; P:L-glutamate transmembrane transport; IDA:UniProtKB.
DR   GO; GO:0071423; P:malate transmembrane transport; IDA:UniProtKB.
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   Chloroplast; Membrane; Plastid; Plastid inner membrane; Transit peptide;
KW   Transmembrane; Transmembrane helix; Transport.
FT   TRANSIT         1..22
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..564
FT                   /note="Dicarboxylate transporter 2, chloroplastic"
FT                   /id="PRO_0000419186"
FT   TRANSMEM        94..114
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        127..147
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        166..186
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        235..255
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        262..282
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        307..327
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        356..376
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        380..400
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        415..435
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        451..471
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        484..504
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        538..558
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          35..58
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   564 AA;  59874 MW;  6DC64D3E7925F209 CRC64;
     MESLALLPTL SLSTTTTTSK ATAFLRSSTT SLHHRRPHLS LSLSSTPKPT LTFSSHSHSH
     SLSSKPLLAL KPLNATASSS SSPATTSPPP TKSGAKLIPL ILSVSVGLLL RFAVPKPAEL
     TPQAWQLLAI FLSTVAGLVL SPLPVGAWAF LGVTASVVTK TLPFPTAFCA FTNEVIWLIV
     ISFFFARGFV KTGLGDRIAT YFVKWLGKST LGLSYGLTIS EALVAPAMPS TTARAGGIFL
     PIIKSLSISS GSLPGGESRK KLGTYLIMTQ FQSAGNSSAL FLTAAAQNLL CLKLAEELGV
     KIASPWVFWL KAASLPAFVA LLLTPLILYK LYPPELKDTP EAPALAAEKL KNMGPVTKNE
     WVMVGTMLLA VSLWVFGEKI GVSSVVAAML GLSVLLLLGV LDWNDCLNEK SAWDTLAWFA
     VLVGMASQLT NLGIVSWMSG CVARSLKTMN LSWPAAFGIL QAAYFFVHYL FASQTGHVGA
     LYSAFLAMNI ASGVPGVLAA LALAYNTNLF GALTHYSSGQ AAVYYGAGYV DLPDVFKMGF
     IMAVINATIW TVVGGVWWKI LGIY