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Protein TOC75, chloroplastic (75 kDa chloroplast outer envelope protein) (75 kDa translocon at the outer-envelope membrane of chloroplasts) (Import intermediate-associated protein of 75 kDa)

 TOC75_PEA               Reviewed;         809 AA.
Q43715;
22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
25-OCT-2017, entry version 77.
RecName: Full=Protein TOC75, chloroplastic;
AltName: Full=75 kDa chloroplast outer envelope protein;
AltName: Full=75 kDa translocon at the outer-envelope membrane of chloroplasts;
AltName: Full=Import intermediate-associated protein of 75 kDa;
Flags: Precursor;
Name=TOC75; Synonyms=IAP75, OEP75;
Pisum sativum (Garden pea).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; fabids; Fabales; Fabaceae; Papilionoideae;
Fabeae; Pisum.
NCBI_TaxID=3888;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 179-189; 304-318;
369-387; 507-517 AND 742-758, FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=7973649; DOI=10.1126/science.7973649;
Schnell D.J., Kessler F., Blobel G.;
"Isolation of components of the chloroplast protein import
machinery.";
Science 266:1007-1012(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 136-150; 185-196;
360-367; 532-545 AND 642-660, FUNCTION, SUBCELLULAR LOCATION, AND
TISSUE SPECIFICITY.
STRAIN=cv. Little Marvel; TISSUE=Leaf;
PubMed=7781598;
Tranel P.J., Froehlich J., Goyal A., Keegstra K.;
"A component of the chloroplastic protein import apparatus is targeted
to the outer envelope membrane via a novel pathway.";
EMBO J. 14:2436-2446(1995).
[3]
PROTEIN SEQUENCE OF 132-135; 387-389 AND 411-414, AND TOPOLOGY.
PubMed=11030426; DOI=10.1515/BC.2000.089;
Sveshnikova N., Grimm R., Soll J., Schleiff E.;
"Topology studies of the chloroplast protein import channel Toc75.";
Biol. Chem. 381:687-693(2000).
[4]
TOC CORE COMPLEX COMPOSITION.
PubMed=7601278; DOI=10.1016/0014-5793(95)00529-I;
Seedorf M., Soll J.;
"Copper chloride, an inhibitor of protein import into chloroplasts.";
FEBS Lett. 367:19-22(1995).
[5]
PROTEOLYTIC PROCESSING, AND SUBCELLULAR LOCATION.
PubMed=8953773; DOI=10.1105/tpc.8.11.2093;
Tranel P.J., Keegstra K.;
"A novel, bipartite transit peptide targets OEP75 to the outer
membrane of the chloroplastic envelope.";
Plant Cell 8:2093-2104(1996).
[6]
FUNCTION, AND INTERACTION BETWEEN TOC COMPLEXES AND PRSS.
PubMed=9118955; DOI=10.1093/emboj/16.5.935;
Nielsen E., Akita M., Davila-Aponte J., Keegstra K.;
"Stable association of chloroplastic precursors with protein
translocation complexes that contain proteins from both envelope
membranes and a stromal Hsp100 molecular chaperone.";
EMBO J. 16:935-946(1997).
[7]
IMPORT COMPLEX COMPOSITION.
PubMed=9405363; DOI=10.1093/emboj/16.24.7342;
Caliebe A., Grimm R., Kaiser G., Luebeck J., Soll J., Heins L.;
"The chloroplastic protein import machinery contains a Rieske-type
iron-sulfur cluster and a mononuclear iron-binding protein.";
EMBO J. 16:7342-7350(1997).
[8]
FUNCTION, AND TOPOLOGY.
PubMed=9405364; DOI=10.1093/emboj/16.24.7351;
Hinnah S.C., Hill K., Wagner R., Schlicher T., Soll J.;
"Reconstitution of a chloroplast protein import channel.";
EMBO J. 16:7351-7360(1997).
[9]
TOC CORE COMPLEX AND IMPORT COMPLEX COMPOSITIONS.
PubMed=9060464; DOI=10.1083/jcb.136.5.983;
Akita M., Nielsen E., Keegstra K.;
"Identification of protein transport complexes in the chloroplastic
envelope membranes via chemical cross-linking.";
J. Cell Biol. 136:983-994(1997).
[10]
NOMENCLATURE.
DOI=10.1016/S0962-8924(97)01111-2;
Schnell D.J., Blobel G., Keegstra K., Kessler F., Ko K., Soll J.;
"A consensus nomenclature for the protein-import components of the
chloroplast envelope.";
Trends Cell Biol. 7:303-304(1997).
[11]
PROTEOLYTIC PROCESSING, AND MUTAGENESIS OF 53-LEU--HIS-77;
92-GLY--GLY-100; ALA-129; ALA-131; ASP-132 AND GLU-133.
PubMed=12787247; DOI=10.1046/j.1365-313X.2003.01755.x;
Inoue K., Keegstra K.;
"A polyglycine stretch is necessary for proper targeting of the
protein translocation channel precursor to the outer envelope membrane
of chloroplasts.";
Plant J. 34:661-669(2003).
[12]
FUNCTION, AND INTERACTION WITH OEP14.
PubMed=15258267; DOI=10.1105/tpc.104.023952;
Tu S.-L., Chen L.-J., Smith M.D., Su Y.-S., Schnell D.J., Li H.-M.;
"Import pathways of chloroplast interior proteins and the outer-
membrane protein OEP14 converge at Toc75.";
Plant Cell 16:2078-2088(2004).
-!- FUNCTION: Mediates the insertion of proteins targeted to the outer
membrane of chloroplasts. Required for the import of protein
precursors into chloroplasts. Forms the voltage-dependent
preprotein translocation channels (hydrophilic beta barrel) of the
TOC complex in the chloroplastic outer membrane. The narrowest
inner diameter of this channel is approximately 14 Angstroms.
{ECO:0000269|PubMed:15258267, ECO:0000269|PubMed:7781598,
ECO:0000269|PubMed:7973649, ECO:0000269|PubMed:9118955,
ECO:0000269|PubMed:9405364}.
-!- SUBUNIT: Part of the TOC core complex that includes a protein for
the specific recognition of transit peptides surrounded by a ring
composed of four proteins forming translocation channels, and four
to five GTP-binding proteins providing energy. This core complex
can interact with components of the TIC complex to form a larger
import complex. Chloroplastic protein precursors such as prSS
(precursor of the RuBisCO small subunit) also interact with these
complexes. TOC75 interacts with OEP14, TOC34/OEP34, TOC86/OEP86,
TIC55, TIC110/IEP110 and CLPC. {ECO:0000269|PubMed:15258267,
ECO:0000269|PubMed:9118955}.
-!- INTERACTION:
Q9MUK5:TOC64; NbExp=2; IntAct=EBI-638469, EBI-638487;
-!- SUBCELLULAR LOCATION: Plastid, chloroplast outer membrane
{ECO:0000269|PubMed:7781598, ECO:0000269|PubMed:7973649,
ECO:0000269|PubMed:8953773}; Multi-pass membrane protein
{ECO:0000269|PubMed:7781598, ECO:0000269|PubMed:7973649,
ECO:0000269|PubMed:8953773}.
-!- TISSUE SPECIFICITY: Mostly expressed in young leaves, also present
in old leaves, roots and stems (at protein level).
{ECO:0000269|PubMed:7781598}.
-!- DOMAIN: Transmembrane regions consist mainly of membrane-spanning
sided beta-sheets, which are not predicted by sequence analysis
tools.
-!- SIMILARITY: Belongs to the TOC75 family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; L36858; AAA53275.1; -; mRNA.
EMBL; X83767; CAA58720.1; -; mRNA.
PIR; S55344; S55344.
ProteinModelPortal; Q43715; -.
SMR; Q43715; -.
DIP; DIP-904N; -.
IntAct; Q43715; 6.
MINT; MINT-2584838; -.
TCDB; 1.B.33.2.1; the outer membrane protein insertion porin (bam complex) (ompip) family.
PRIDE; Q43715; -.
GO; GO:0009707; C:chloroplast outer membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0015450; F:P-P-bond-hydrolysis-driven protein transmembrane transporter activity; IEA:InterPro.
GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
InterPro; IPR000184; Bac_surfAg_D15.
InterPro; IPR005689; IAP75.
Pfam; PF01103; Bac_surface_Ag; 1.
TIGRFAMs; TIGR00992; 3a0901s03IAP75; 1.
1: Evidence at protein level;
Chloroplast; Direct protein sequencing; Membrane; Plastid;
Plastid outer membrane; Protein transport; Transit peptide;
Transmembrane; Transmembrane beta strand; Transport.
TRANSIT 1 35 Chloroplast.
TRANSIT 36 131 Chloroplast; outer membrane.
{ECO:0000269|PubMed:11030426}.
CHAIN 132 809 Protein TOC75, chloroplastic.
/FTId=PRO_0000042823.
TOPO_DOM 132 143 Chloroplast intermembrane. {ECO:0000255}.
TRANSMEM 144 152 Beta stranded. {ECO:0000255}.
TOPO_DOM 153 160 Cytoplasmic. {ECO:0000255}.
TRANSMEM 161 169 Beta stranded. {ECO:0000255}.
TOPO_DOM 170 225 Chloroplast intermembrane. {ECO:0000255}.
TRANSMEM 226 234 Beta stranded. {ECO:0000255}.
TOPO_DOM 235 247 Cytoplasmic. {ECO:0000255}.
TRANSMEM 248 254 Beta stranded. {ECO:0000255}.
TOPO_DOM 255 357 Chloroplast intermembrane. {ECO:0000255}.
TRANSMEM 358 365 Beta stranded. {ECO:0000255}.
TOPO_DOM 366 410 Cytoplasmic. {ECO:0000255}.
TRANSMEM 411 418 Beta stranded. {ECO:0000255}.
TOPO_DOM 419 427 Chloroplast intermembrane. {ECO:0000255}.
TRANSMEM 428 436 Beta stranded. {ECO:0000255}.
TOPO_DOM 437 442 Cytoplasmic. {ECO:0000255}.
TRANSMEM 443 452 Beta stranded. {ECO:0000255}.
TOPO_DOM 453 464 Chloroplast intermembrane. {ECO:0000255}.
TRANSMEM 465 473 Beta stranded. {ECO:0000255}.
TOPO_DOM 474 500 Cytoplasmic. {ECO:0000255}.
TRANSMEM 501 509 Beta stranded. {ECO:0000255}.
TOPO_DOM 510 553 Chloroplast intermembrane. {ECO:0000255}.
TRANSMEM 554 561 Beta stranded. {ECO:0000255}.
TOPO_DOM 562 569 Cytoplasmic. {ECO:0000255}.
TRANSMEM 570 577 Beta stranded. {ECO:0000255}.
TOPO_DOM 578 684 Chloroplast intermembrane. {ECO:0000255}.
TRANSMEM 685 693 Beta stranded. {ECO:0000255}.
TOPO_DOM 694 705 Cytoplasmic. {ECO:0000255}.
TRANSMEM 706 714 Beta stranded. {ECO:0000255}.
TOPO_DOM 715 776 Chloroplast intermembrane. {ECO:0000255}.
TRANSMEM 777 783 Beta stranded. {ECO:0000255}.
TOPO_DOM 784 797 Cytoplasmic. {ECO:0000255}.
TRANSMEM 798 805 Beta stranded. {ECO:0000255}.
TOPO_DOM 806 809 Chloroplast intermembrane. {ECO:0000255}.
COMPBIAS 91 117 Gly-rich.
MUTAGEN 53 77 Missing: Reduction of processed protein.
{ECO:0000269|PubMed:12787247}.
MUTAGEN 92 100 Missing: Mistargeting to the stroma.
{ECO:0000269|PubMed:12787247}.
MUTAGEN 92 99 GGAGGGGG->SAAAAAAA: Mistargeting to the
stroma.
MUTAGEN 129 129 A->G: Reduction of processed protein by
90%; when associated with P-131.
{ECO:0000269|PubMed:12787247}.
MUTAGEN 131 131 A->P: Reduction of processed protein by
90%; when associated with G-129.
{ECO:0000269|PubMed:12787247}.
MUTAGEN 132 132 D->N: Reduction of processed protein by
more than 50%; when associated with Q-
133. {ECO:0000269|PubMed:12787247}.
MUTAGEN 133 133 E->Q: Reduction of processed protein by
50%. Reduction of processed protein by
more than 50%; when associated with N-
132. {ECO:0000269|PubMed:12787247}.
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


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