TPT_PEA
ID TPT_PEA Reviewed; 402 AA.
AC P21727;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1991, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Triose phosphate/phosphate translocator, chloroplastic;
DE Short=cTPT;
DE AltName: Full=E30;
DE AltName: Full=p36;
DE Flags: Precursor;
OS Pisum sativum (Garden pea).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX NCBI_TaxID=3888;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 73-98; 249-260; 269-289
RP AND 324-350.
RC STRAIN=cv. Progress No. 9; TISSUE=Seedling;
RX PubMed=2172258; DOI=10.1083/jcb.111.5.1825;
RA Schnell D.J., Blobel G., Pain D.;
RT "The chloroplast import receptor is an integral membrane protein of
RT chloroplast envelope contact sites.";
RL J. Cell Biol. 111:1825-1838(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 73-82.
RC TISSUE=Leaf;
RA Willey D.L., Fischer K., Wachter E., Link T.A., Fluegge U.-I.;
RT "Molecular cloning and structural analysis of the phosphate translocator
RT from pea chloroplasts and its comparison to the spinach phosphate
RT translocator.";
RL Planta 183:451-461(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Weber A.;
RL Submitted (SEP-1992) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Mediates the export of fixed carbons from the chloroplasts
CC into the cytosol in the form of triose phosphates.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast membrane; Multi-pass
CC membrane protein. Note=Located in zones of contact between the inner
CC and outer membrane of the chloroplast.
CC -!- SIMILARITY: Belongs to the TPT transporter family. TPT (TC 2.A.7.9)
CC subfamily. {ECO:0000305}.
CC -!- CAUTION: Was originally thought to function as a chloroplast protein
CC import receptor. {ECO:0000305}.
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DR EMBL; X54639; CAA38451.1; -; mRNA.
DR EMBL; X68077; CAA48210.1; -; mRNA.
DR PIR; S23774; S23774.
DR AlphaFoldDB; P21727; -.
DR SMR; P21727; -.
DR GO; GO:0031969; C:chloroplast membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0015605; F:organophosphate ester transmembrane transporter activity; IEA:UniProt.
DR GO; GO:0015120; F:phosphoglycerate transmembrane transporter activity; IEA:UniProt.
DR InterPro; IPR004853; Sugar_P_trans_dom.
DR InterPro; IPR004696; Tpt_PEP_transl.
DR Pfam; PF03151; TPT; 1.
DR TIGRFAMs; TIGR00817; tpt; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Direct protein sequencing; Membrane; Plastid; Transit peptide;
KW Transmembrane; Transmembrane helix; Transport.
FT TRANSIT 1..72
FT /note="Chloroplast"
FT /evidence="ECO:0000269|PubMed:2172258, ECO:0000269|Ref.2"
FT CHAIN 73..402
FT /note="Triose phosphate/phosphate translocator,
FT chloroplastic"
FT /id="PRO_0000035708"
FT TOPO_DOM 73..96
FT /note="Chloroplast intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 97..117
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 118..129
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 130..150
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 151..207
FT /note="Chloroplast intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 208..228
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 229..272
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 273..292
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 293..370
FT /note="Chloroplast intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 371..391
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 392..402
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT VARIANT 227
FT /note="I -> L"
SQ SEQUENCE 402 AA; 43649 MW; D6EF731F3CEF7600 CRC64;
MESRVLSRAT TLSSLPTLNK LHRLPLANAS LPSVKSFGSV SDGGNLVWGR QLRPELCSPV
LKKGASLLRP CPATAGGNDS AGEEKVAPVG FFSRYPALTT GFFFFTWYFL NVIFNILNKK
IYNYFPYPYF VSVIHLAVGV VYCLVSWTVG LPKRAPIDGN LLKLLIPVAV CHALGHVTSN
VSFAAVAVSF THTVKALEPF FNAAASQFIL GQSIPITLWL SLAPVVIGVS MASLTELSFN
WLGFISAMIS NISFTYRSIY SKKAMTDMDS TNIYAYISII ALIVCIPPAL IIEGPTLLKT
GFNDAIAKVG LVKFVSDLFW VGMFYHLYNQ VATNTLERVA PLTHAVGNVL KRVFVIGFSI
IIFGNKISTQ TGIGTGIAIA GVALYSFIKA QIEEEKRQAK AA