DIT1_SPIOL
ID DIT1_SPIOL Reviewed; 569 AA.
AC Q41364;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 75.
DE RecName: Full=Dicarboxylate transporter 1, chloroplastic;
DE Short=SODIT1;
DE AltName: Full=2-oxoglutarate/malate translocator;
DE Flags: Precursor;
GN Name=DIT1;
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], PROTEIN SEQUENCE OF 439-449, FUNCTION, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=cv. Polka; TISSUE=Leaf;
RX PubMed=7873543; DOI=10.1021/bi00008a028;
RA Weber A., Menzlaff E., Arbinger B., Gutensohn M., Eckerskorn C.,
RA Fluegge U.-I.;
RT "The 2-oxoglutarate/malate translocator of chloroplast envelope membranes:
RT molecular cloning of a transporter containing a 12-helix motif and
RT expression of the functional protein in yeast cells.";
RL Biochemistry 34:2621-2627(1995).
RN [2]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, AND INDUCTION.
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: 2-oxoglutarate/malate translocator that transports carbon
CC skeletons into chloroplasts for net glutamate synthesis. This
CC translocator exchanges malate for internal succinate, fumarate and 2-
CC oxoglutarate but not for aspartate and glutamate. Involved with DIT2 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. {ECO:0000269|PubMed:12887583,
CC ECO:0000269|PubMed:7873543}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.35 mM for malate {ECO:0000269|PubMed:12887583};
CC KM=0.17 mM for 2-oxoglutarate {ECO:0000269|PubMed:12887583};
CC KM=0.04 mM for oxaloacetate {ECO:0000269|PubMed:12887583};
CC -!- SUBUNIT: Monomer. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast inner membrane
CC {ECO:0000305|PubMed:7873543}; Multi-pass membrane protein
CC {ECO:0000305|PubMed:7873543}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves. {ECO:0000269|PubMed:12887583}.
CC -!- INDUCTION: Circadian regulation with a peak in the middle of the light
CC period. {ECO:0000269|PubMed:12887583}.
CC -!- PTM: The N-terminus is blocked.
CC -!- SIMILARITY: Belongs to the SLC13A/DASS transporter (TC 2.A.47) family.
CC DIT1 subfamily. {ECO:0000305}.
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DR EMBL; U13238; AAA68148.1; -; mRNA.
DR AlphaFoldDB; Q41364; -.
DR SMR; Q41364; -.
DR TCDB; 2.A.47.3.1; the divalent anion:na(+) symporter (dass) family.
DR SABIO-RK; Q41364; -.
DR GO; GO:0009706; C:chloroplast inner membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0015742; P:alpha-ketoglutarate transport; IDA:UniProtKB.
DR GO; GO:0015743; P:malate 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; Direct protein sequencing; Membrane; Plastid;
KW Plastid inner membrane; Transit peptide; Transmembrane;
KW Transmembrane helix; Transport.
FT TRANSIT 1..93
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 94..569
FT /note="Dicarboxylate transporter 1, chloroplastic"
FT /id="PRO_0000032663"
FT TRANSMEM 106..126
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 134..154
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 172..192
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 241..261
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 268..288
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 317..337
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 367..387
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 388..408
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 423..443
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 450..470
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 490..510
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 543..563
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 23..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..53
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..92
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 569 AA; 60288 MW; 5BF756490B1F7AA4 CRC64;
MASMALSLTS SPTYSLSFRS LPSLKPLSKS QPSISLPSLR SNASKSPSLS HKHFLSPPSL
LLPHKLKPIS ASSPTNPPPP PAPVPSPAPV SAPAQVQPWQ GASIKPLLAS ILTGVIIWFI
PTPEGVSRNA WQLLAIFLST IVGIITQPLP LGAVALMGLG ASVLTKTLTF SAAFSAFGDP
IPWLIALAFF FARGFIKTGL GNRIAYQFVK LFGSSSLGLG YSLVFSEALL APAIPSVSAR
AGGIFLPLVK SLCIACGSNV GDGTERKLGA WLMLTCFQTS VISSSMFLTA MAANPLSATL
TFNTIGKAIG WMDWAKAAFV PGLVSLIVVP LLLYVVYPPE IKSSPDAPRL AKEKLDKMGP
MTKNESIMAV TLLLTVGLWV FGGKLGVDAV TAAILGLSVL LITGVVTWKE CLAESVAWDT
LTWFAALIAM AGYLNKYGLI TWFSENVVKV VGGLGLSWQM SFGVLVLLYF YSHYFFASGA
AHIGAMFTAF LSVASALGTP PFLAAIVLSF LSNLMGGLTH YGIGSAPVFY GANYVPLPQW
WGYGFLISIV NLIIWLGVGG LWWKAIGLW
