TOC75_PEA
ID TOC75_PEA Reviewed; 809 AA.
AC Q43715;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Protein TOC75, chloroplastic;
DE AltName: Full=75 kDa chloroplast outer envelope protein;
DE AltName: Full=75 kDa translocon at the outer-envelope membrane of chloroplasts;
DE AltName: Full=Import intermediate-associated protein of 75 kDa;
DE Flags: Precursor;
GN Name=TOC75; Synonyms=IAP75, OEP75;
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], PROTEIN SEQUENCE OF 179-189; 304-318; 369-387;
RP 507-517 AND 742-758, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=7973649; DOI=10.1126/science.7973649;
RA Schnell D.J., Kessler F., Blobel G.;
RT "Isolation of components of the chloroplast protein import machinery.";
RL Science 266:1007-1012(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 136-150; 185-196; 360-367;
RP 532-545 AND 642-660, FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=cv. Little Marvel; TISSUE=Leaf;
RX PubMed=7781598; DOI=10.1002/j.1460-2075.1995.tb07241.x;
RA Tranel P.J., Froehlich J., Goyal A., Keegstra K.;
RT "A component of the chloroplastic protein import apparatus is targeted to
RT the outer envelope membrane via a novel pathway.";
RL EMBO J. 14:2436-2446(1995).
RN [3]
RP PROTEIN SEQUENCE OF 132-135; 387-389 AND 411-414, AND TOPOLOGY.
RX PubMed=11030426; DOI=10.1515/bc.2000.089;
RA Sveshnikova N., Grimm R., Soll J., Schleiff E.;
RT "Topology studies of the chloroplast protein import channel Toc75.";
RL Biol. Chem. 381:687-693(2000).
RN [4]
RP TOC CORE COMPLEX COMPOSITION.
RX PubMed=7601278; DOI=10.1016/0014-5793(95)00529-i;
RA Seedorf M., Soll J.;
RT "Copper chloride, an inhibitor of protein import into chloroplasts.";
RL FEBS Lett. 367:19-22(1995).
RN [5]
RP PROTEOLYTIC PROCESSING, AND SUBCELLULAR LOCATION.
RX PubMed=8953773; DOI=10.2307/3870415;
RA Tranel P.J., Keegstra K.;
RT "A novel, bipartite transit peptide targets OEP75 to the outer membrane of
RT the chloroplastic envelope.";
RL Plant Cell 8:2093-2104(1996).
RN [6]
RP FUNCTION, AND INTERACTION BETWEEN TOC COMPLEXES AND PRSS.
RX PubMed=9118955; DOI=10.1093/emboj/16.5.935;
RA Nielsen E., Akita M., Davila-Aponte J., Keegstra K.;
RT "Stable association of chloroplastic precursors with protein translocation
RT complexes that contain proteins from both envelope membranes and a stromal
RT Hsp100 molecular chaperone.";
RL EMBO J. 16:935-946(1997).
RN [7]
RP IMPORT COMPLEX COMPOSITION.
RX PubMed=9405363; DOI=10.1093/emboj/16.24.7342;
RA Caliebe A., Grimm R., Kaiser G., Luebeck J., Soll J., Heins L.;
RT "The chloroplastic protein import machinery contains a Rieske-type iron-
RT sulfur cluster and a mononuclear iron-binding protein.";
RL EMBO J. 16:7342-7350(1997).
RN [8]
RP FUNCTION, AND TOPOLOGY.
RX PubMed=9405364; DOI=10.1093/emboj/16.24.7351;
RA Hinnah S.C., Hill K., Wagner R., Schlicher T., Soll J.;
RT "Reconstitution of a chloroplast protein import channel.";
RL EMBO J. 16:7351-7360(1997).
RN [9]
RP TOC CORE COMPLEX AND IMPORT COMPLEX COMPOSITIONS.
RX PubMed=9060464; DOI=10.1083/jcb.136.5.983;
RA Akita M., Nielsen E., Keegstra K.;
RT "Identification of protein transport complexes in the chloroplastic
RT envelope membranes via chemical cross-linking.";
RL J. Cell Biol. 136:983-994(1997).
RN [10]
RP NOMENCLATURE.
RX DOI=10.1016/S0962-8924(97)01111-2;
RA Schnell D.J., Blobel G., Keegstra K., Kessler F., Ko K., Soll J.;
RT "A consensus nomenclature for the protein-import components of the
RT chloroplast envelope.";
RL Trends Cell Biol. 7:303-304(1997).
RN [11]
RP PROTEOLYTIC PROCESSING, AND MUTAGENESIS OF 53-LEU--HIS-77; 92-GLY--GLY-100;
RP ALA-129; ALA-131; ASP-132 AND GLU-133.
RX PubMed=12787247; DOI=10.1046/j.1365-313x.2003.01755.x;
RA Inoue K., Keegstra K.;
RT "A polyglycine stretch is necessary for proper targeting of the protein
RT translocation channel precursor to the outer envelope membrane of
RT chloroplasts.";
RL Plant J. 34:661-669(2003).
RN [12]
RP FUNCTION, AND INTERACTION WITH OEP14.
RX PubMed=15258267; DOI=10.1105/tpc.104.023952;
RA Tu S.-L., Chen L.-J., Smith M.D., Su Y.-S., Schnell D.J., Li H.-M.;
RT "Import pathways of chloroplast interior proteins and the outer-membrane
RT protein OEP14 converge at Toc75.";
RL Plant Cell 16:2078-2088(2004).
CC -!- FUNCTION: Mediates the insertion of proteins targeted to the outer
CC membrane of chloroplasts. Required for the import of protein precursors
CC into chloroplasts. Forms the voltage-dependent preprotein translocation
CC channels (hydrophilic beta barrel) of the TOC complex in the
CC chloroplastic outer membrane. The narrowest inner diameter of this
CC channel is approximately 14 Angstroms. {ECO:0000269|PubMed:15258267,
CC ECO:0000269|PubMed:7781598, ECO:0000269|PubMed:7973649,
CC ECO:0000269|PubMed:9118955, ECO:0000269|PubMed:9405364}.
CC -!- SUBUNIT: Part of the TOC core complex that includes a protein for the
CC specific recognition of transit peptides surrounded by a ring composed
CC of four proteins forming translocation channels, and four to five GTP-
CC binding proteins providing energy. This core complex can interact with
CC components of the TIC complex to form a larger import complex.
CC Chloroplastic protein precursors such as prSS (precursor of the RuBisCO
CC small subunit) also interact with these complexes. TOC75 interacts with
CC OEP14, TOC34/OEP34, TOC86/OEP86, TIC55, TIC110/IEP110 and CLPC.
CC {ECO:0000269|PubMed:15258267, ECO:0000269|PubMed:9118955}.
CC -!- INTERACTION:
CC Q43715; Q9MUK5: TOC64; NbExp=2; IntAct=EBI-638469, EBI-638487;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast outer membrane
CC {ECO:0000269|PubMed:7781598, ECO:0000269|PubMed:7973649,
CC ECO:0000269|PubMed:8953773}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:7781598, ECO:0000269|PubMed:7973649,
CC ECO:0000269|PubMed:8953773}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in young leaves, also present in
CC old leaves, roots and stems (at protein level).
CC {ECO:0000269|PubMed:7781598}.
CC -!- DOMAIN: Transmembrane regions consist mainly of membrane-spanning sided
CC beta-sheets, which are not predicted by sequence analysis tools.
CC -!- SIMILARITY: Belongs to the TOC75 family. {ECO:0000305}.
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DR EMBL; L36858; AAA53275.1; -; mRNA.
DR EMBL; X83767; CAA58720.1; -; mRNA.
DR PIR; S55344; S55344.
DR AlphaFoldDB; Q43715; -.
DR SMR; Q43715; -.
DR DIP; DIP-904N; -.
DR IntAct; Q43715; 6.
DR MINT; Q43715; -.
DR TCDB; 1.B.33.2.1; the outer membrane protein insertion porin (bam complex) (ompip) family.
DR EnsemblPlants; Psat7g209800.1; Psat7g209800.1.cds; Psat7g209800.
DR Gramene; Psat7g209800.1; Psat7g209800.1.cds; Psat7g209800.
DR GO; GO:0009707; C:chloroplast outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0015450; F:protein-transporting ATPase activity; IEA:InterPro.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR InterPro; IPR000184; Bac_surfAg_D15.
DR InterPro; IPR039910; D15-like.
DR InterPro; IPR005689; IAP75.
DR PANTHER; PTHR12815; PTHR12815; 1.
DR Pfam; PF01103; Omp85; 1.
DR TIGRFAMs; TIGR00992; 3a0901s03IAP75; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Direct protein sequencing; Membrane; Plastid;
KW Plastid outer membrane; Protein transport; Transit peptide; Transmembrane;
KW Transmembrane beta strand; Transport.
FT TRANSIT 1..35
FT /note="Chloroplast"
FT TRANSIT 36..131
FT /note="Chloroplast; outer membrane"
FT /evidence="ECO:0000269|PubMed:11030426"
FT CHAIN 132..809
FT /note="Protein TOC75, chloroplastic"
FT /id="PRO_0000042823"
FT TOPO_DOM 132..143
FT /note="Chloroplast intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 144..152
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 153..160
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 161..169
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 170..225
FT /note="Chloroplast intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 226..234
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 235..247
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 248..254
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 255..357
FT /note="Chloroplast intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 358..365
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 366..410
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 411..418
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 419..427
FT /note="Chloroplast intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 428..436
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 437..442
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 443..452
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 453..464
FT /note="Chloroplast intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 465..473
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 474..500
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 501..509
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 510..553
FT /note="Chloroplast intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 554..561
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 562..569
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 570..577
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 578..684
FT /note="Chloroplast intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 685..693
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 694..705
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 706..714
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 715..776
FT /note="Chloroplast intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 777..783
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 784..797
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 798..805
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 806..809
FT /note="Chloroplast intermembrane"
FT /evidence="ECO:0000255"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..44
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 53..77
FT /note="Missing: Reduction of processed protein."
FT /evidence="ECO:0000269|PubMed:12787247"
FT MUTAGEN 92..100
FT /note="Missing: Mistargeting to the stroma."
FT /evidence="ECO:0000269|PubMed:12787247"
FT MUTAGEN 92..99
FT /note="GGAGGGGG->SAAAAAAA: Mistargeting to the stroma."
FT MUTAGEN 129
FT /note="A->G: Reduction of processed protein by 90%; when
FT associated with P-131."
FT /evidence="ECO:0000269|PubMed:12787247"
FT MUTAGEN 131
FT /note="A->P: Reduction of processed protein by 90%; when
FT associated with G-129."
FT /evidence="ECO:0000269|PubMed:12787247"
FT MUTAGEN 132
FT /note="D->N: Reduction of processed protein by more than
FT 50%; when associated with Q-133."
FT /evidence="ECO:0000269|PubMed:12787247"
FT MUTAGEN 133
FT /note="E->Q: Reduction of processed protein by 50%.
FT Reduction of processed protein by more than 50%; when
FT associated with N-132."
FT /evidence="ECO:0000269|PubMed:12787247"
SQ SEQUENCE 809 AA; 88269 MW; AFE51AE75F0617C5 CRC64;
MRTSVIPNRL TPTLTTHPSR RRNDHITTRT SSLKCHLSPS SGDNNDSFNS SLLKTISTTV
AVSSAAASAF FLTGSLHSPF PNFSGLNAAA GGGAGGGGGG SSSSGGGGGG WFNGDEGSFW
SRILSPARAI ADEPKSEDWD SHELPADITV LLGRLSGFKK YKISDILFFD RNKKSKVETQ
DSFLDMVSLK PGGVYTKAQL QKELESLATC GMFEKVDMEG KTNADGSLGL TISFAESMWE
RADRFRCINV GLMGQSKPVE MDPDMSEKEK IEFFRRQERE YKRRISSARP CLLPTSVHEE
IKDMLAEQGR VSARLLQKIR DRVQSWYHEE GYACAQVVNF GNLNTREVVC EVVEGDITKL
SIQYLDKLGN VVEGNTEGPV VQRELPKQLL PGHTFNIEAG KQALRNINSL ALFSNIEVNP
RPDEMNEGSI IVEIKLKELE QKSAEVSTEW SIVPGRGGRP TLASLQPGGT ITFEHRNLQG
LNRSLTGSVT TSNFLNPQDD LAFKMEYAHP YLDGVDNPRN RTLRVSCFNS RKLSPVFTGG
PGVDEVPSIW VDRAGVKANI TENFSRQSKF TYGLVMEEII TRDESNHICS NGQRVLPNGA
ISADGPPTTL SGTGIDRMAF LQANITRDNT RFVNGTIVGS RNMFQVDQGL GVGSNFPFFN
RHQLTVTKFL QLMSVEEGAG KSPPPVLVLH GHYGGCVGDL PSYDAFTLGG PYSVRGYNMG
EIGAARNILE LAAEIRIPIK GTHVYAFAEH GTDLGSSKDV KGNPTVVYRR MGQGSSYGAG
MKLGLVRAEY AVDHNSGTGA VFFRFGERF
