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Protein TOC75-3, chloroplastic (75 kDa translocon at the outer-envelope-membrane of chloroplasts 3) (AtTOC75-III)

 TC753_ARATH             Reviewed;         818 AA.
Q9STE8;
22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
25-OCT-2017, entry version 108.
RecName: Full=Protein TOC75-3, chloroplastic;
AltName: Full=75 kDa translocon at the outer-envelope-membrane of chloroplasts 3;
Short=AtTOC75-III;
Flags: Precursor;
Name=TOC75-3; Synonyms=TOC75; OrderedLocusNames=At3g46740;
ORFNames=T6H20.230;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130713; DOI=10.1038/35048706;
Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M.,
Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B.,
Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P.,
De Simone V., Choisne N., Artiguenave F., Robert C., Brottier P.,
Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F.,
Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V.,
Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S.,
Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G.,
Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B.,
Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G.,
Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J.,
Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D.,
Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
Monfort A., Argiriou A., Flores M., Liguori R., Vitale D.,
Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W.,
Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J.,
Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P.,
Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S.,
Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V.,
Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C.,
Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E.,
Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y.,
Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A.,
Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
Watanabe A., Yamada M., Yasuda M., Tabata S.;
"Sequence and analysis of chromosome 3 of the plant Arabidopsis
thaliana.";
Nature 408:820-822(2000).
[2]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[4]
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).
[5]
INDUCTION.
PubMed=11549763; DOI=10.1105/tpc.13.9.2053;
Sun C.-W., Chen L.-J., Lin L.-C., Li H.-M.;
"Leaf-specific upregulation of chloroplast translocon genes by a CCT
motif-containing protein, CIA2.";
Plant Cell 13:2053-2061(2001).
[6]
TOC CORE COMPLEX COMPOSITION AND ARCHITECTURE.
PubMed=12591914; DOI=10.1083/jcb.200210060;
Schleiff E., Soll J., Kuechler M., Kuehlbrandt W., Harrer R.;
"Characterization of the translocon of the outer envelope of
chloroplasts.";
J. Cell Biol. 160:541-551(2003).
[7]
IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE
SCALE ANALYSIS].
STRAIN=cv. Wassilewskija;
PubMed=12766230; DOI=10.1074/mcp.M300030-MCP200;
Ferro M., Salvi D., Brugiere S., Miras S., Kowalski S., Louwagie M.,
Garin J., Joyard J., Rolland N.;
"Proteomics of the chloroplast envelope membranes from Arabidopsis
thaliana.";
Mol. Cell. Proteomics 2:325-345(2003).
[8]
PROTEOLYTIC PROCESSING.
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).
[9]
SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND INTERACTION WITH
TOC132; TOC120 AND TOC159.
PubMed=15090618; DOI=10.1091/mbc.E03-12-0923;
Ivanova Y., Smith M.D., Chen K., Schnell D.J.;
"Members of the Toc159 import receptor family represent distinct
pathways for protein targeting to plastids.";
Mol. Biol. Cell 15:3379-3392(2004).
[10]
FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
STRAIN=cv. Columbia; TISSUE=Seedling;
PubMed=15908591; DOI=10.1104/pp.105.063289;
Baldwin A., Wardle A., Patel R., Dudley P., Park S.K., Twell D.,
Inoue K., Jarvis P.;
"A molecular-genetic study of the Arabidopsis toc75 gene family.";
Plant Physiol. 138:715-733(2005).
[11]
INTERACTION WITH SP1.
PubMed=23118188; DOI=10.1126/science.1225053;
Ling Q., Huang W., Baldwin A., Jarvis P.;
"Chloroplast biogenesis is regulated by direct action of the
ubiquitin-proteasome system.";
Science 338:655-659(2012).
-!- FUNCTION: Essential protein. Mediates the insertion of proteins
targeted to the outer membrane of chloroplasts (By similarity).
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. {ECO:0000250, ECO:0000269|PubMed:15908591}.
-!- 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. The TOC complex contains a specific subset of polar
lipids such as digalactosyldiacylglyceride (DGDG),
phosphatidylcholine (PC) and phosphatidylglycerol (PG). TOC75-3
interacts with TOC34/OEP34, TOC159/TOC86, TOC132 and TOC120
(PubMed:15090618). Interacts with SP1 (PubMed:23118188).
{ECO:0000269|PubMed:15090618, ECO:0000269|PubMed:23118188}.
-!- INTERACTION:
Q8L7N4:SP1; NbExp=2; IntAct=EBI-639078, EBI-6559199;
-!- SUBCELLULAR LOCATION: Plastid, chloroplast outer membrane
{ECO:0000269|PubMed:12766230, ECO:0000269|PubMed:15090618}; Multi-
pass membrane protein {ECO:0000269|PubMed:12766230,
ECO:0000269|PubMed:15090618}.
-!- TISSUE SPECIFICITY: Mostly expressed in young and actively
dividing photosynthetic tissues and, to a lower extent, in old
leaves and roots. Particularly low levels in leaves after
etiolation. {ECO:0000269|PubMed:15908591}.
-!- DEVELOPMENTAL STAGE: Expressed predominantly during the early
stages of plant growth, peaking at three weeks after germination
(at protein level). {ECO:0000269|PubMed:15090618}.
-!- INDUCTION: Up-regulated by CIA2 in leaves.
{ECO:0000269|PubMed:11549763}.
-!- DOMAIN: Transmembrane regions consist mainly of membrane-spanning
sided beta-sheets, which are not predicted by sequence analysis
tools.
-!- DISRUPTION PHENOTYPE: Plants have an embryo development arrested
at the two cells stage. {ECO:0000269|PubMed:15908591}.
-!- SIMILARITY: Belongs to the TOC75 family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AL096859; CAB51191.1; -; Genomic_DNA.
EMBL; CP002686; AEE78199.1; -; Genomic_DNA.
EMBL; AY127014; AAM83239.1; -; mRNA.
EMBL; BT006358; AAP21166.1; -; mRNA.
PIR; T12975; T12975.
RefSeq; NP_190258.1; NM_114541.3.
UniGene; At.3633; -.
UniGene; At.67270; -.
PDB; 5UAY; X-ray; 2.50 A; A=141-449.
PDB; 5UBC; X-ray; 2.86 A; A/B=141-449.
PDBsum; 5UAY; -.
PDBsum; 5UBC; -.
ProteinModelPortal; Q9STE8; -.
SMR; Q9STE8; -.
BioGrid; 9147; 5.
IntAct; Q9STE8; 3.
STRING; 3702.AT3G46740.1; -.
PaxDb; Q9STE8; -.
PRIDE; Q9STE8; -.
EnsemblPlants; AT3G46740.1; AT3G46740.1; AT3G46740.
GeneID; 823827; -.
Gramene; AT3G46740.1; AT3G46740.1; AT3G46740.
KEGG; ath:AT3G46740; -.
Araport; AT3G46740; -.
TAIR; locus:2102767; AT3G46740.
eggNOG; ENOG410IISX; Eukaryota.
eggNOG; COG4775; LUCA.
HOGENOM; HOG000029694; -.
InParanoid; Q9STE8; -.
OMA; FLESTWQ; -.
OrthoDB; EOG093602P2; -.
PhylomeDB; Q9STE8; -.
PRO; PR:Q9STE8; -.
Proteomes; UP000006548; Chromosome 3.
Genevisible; Q9STE8; AT.
GO; GO:0009507; C:chloroplast; IDA:TAIR.
GO; GO:0009941; C:chloroplast envelope; IDA:TAIR.
GO; GO:0031359; C:integral component of chloroplast outer membrane; IDA:TAIR.
GO; GO:0016020; C:membrane; IDA:TAIR.
GO; GO:0009536; C:plastid; IDA:TAIR.
GO; GO:0010006; C:Toc complex; ISS:TAIR.
GO; GO:0005774; C:vacuolar membrane; IDA:TAIR.
GO; GO:0015450; F:P-P-bond-hydrolysis-driven protein transmembrane transporter activity; IEA:InterPro.
GO; GO:0009658; P:chloroplast organization; IMP:TAIR.
GO; GO:0048598; P:embryonic morphogenesis; IMP:TAIR.
GO; GO:0045037; P:protein import into chloroplast stroma; IMP:TAIR.
GO; GO:0045036; P:protein targeting to chloroplast; IDA:TAIR.
GO; GO:0009735; P:response to cytokinin; IDA:TAIR.
InterPro; IPR000184; Bac_surfAg_D15.
InterPro; IPR005689; IAP75.
Pfam; PF01103; Bac_surface_Ag; 1.
TIGRFAMs; TIGR00992; 3a0901s03IAP75; 1.
1: Evidence at protein level;
3D-structure; Chloroplast; Complete proteome; Membrane; Plastid;
Plastid outer membrane; Protein transport; Reference proteome;
Transit peptide; Transmembrane; Transmembrane beta strand; Transport.
TRANSIT 1 79 Chloroplast. {ECO:0000255}.
TRANSIT 80 140 Chloroplast; outer membrane.
{ECO:0000255}.
CHAIN 141 818 Protein TOC75-3, chloroplastic.
/FTId=PRO_0000042821.
TOPO_DOM 141 152 Chloroplast intermembrane. {ECO:0000255}.
TRANSMEM 153 161 Beta stranded. {ECO:0000255}.
TOPO_DOM 162 169 Cytoplasmic. {ECO:0000255}.
TRANSMEM 170 178 Beta stranded. {ECO:0000255}.
TOPO_DOM 179 234 Chloroplast intermembrane. {ECO:0000255}.
TRANSMEM 235 243 Beta stranded. {ECO:0000255}.
TOPO_DOM 244 256 Cytoplasmic. {ECO:0000255}.
TRANSMEM 257 263 Beta stranded. {ECO:0000255}.
TOPO_DOM 264 366 Chloroplast intermembrane. {ECO:0000255}.
TRANSMEM 367 374 Beta stranded. {ECO:0000255}.
TOPO_DOM 375 419 Cytoplasmic. {ECO:0000255}.
TRANSMEM 420 427 Beta stranded. {ECO:0000255}.
TOPO_DOM 428 436 Chloroplast intermembrane. {ECO:0000255}.
TRANSMEM 437 445 Beta stranded. {ECO:0000255}.
TOPO_DOM 446 451 Cytoplasmic. {ECO:0000255}.
TRANSMEM 452 461 Beta stranded. {ECO:0000255}.
TOPO_DOM 462 473 Chloroplast intermembrane. {ECO:0000255}.
TRANSMEM 474 482 Beta stranded. {ECO:0000255}.
TOPO_DOM 483 509 Cytoplasmic. {ECO:0000255}.
TRANSMEM 510 518 Beta stranded. {ECO:0000255}.
TOPO_DOM 519 562 Chloroplast intermembrane. {ECO:0000255}.
TRANSMEM 563 570 Beta stranded. {ECO:0000255}.
TOPO_DOM 571 578 Cytoplasmic. {ECO:0000255}.
TRANSMEM 579 586 Beta stranded. {ECO:0000255}.
TOPO_DOM 587 693 Chloroplast intermembrane. {ECO:0000255}.
TRANSMEM 694 702 Beta stranded. {ECO:0000255}.
TOPO_DOM 703 714 Cytoplasmic. {ECO:0000255}.
TRANSMEM 715 723 Beta stranded. {ECO:0000255}.
TOPO_DOM 724 785 Chloroplast intermembrane. {ECO:0000255}.
TRANSMEM 786 792 Beta stranded. {ECO:0000255}.
TOPO_DOM 793 806 Cytoplasmic. {ECO:0000255}.
TRANSMEM 807 814 Beta stranded. {ECO:0000255}.
TOPO_DOM 815 818 Chloroplast intermembrane. {ECO:0000255}.
DOMAIN 381 447 POTRA. {ECO:0000255}.
COMPBIAS 102 130 Gly-rich.
STRAND 155 158 {ECO:0000244|PDB:5UAY}.
STRAND 170 179 {ECO:0000244|PDB:5UAY}.
TURN 180 183 {ECO:0000244|PDB:5UAY}.
STRAND 184 186 {ECO:0000244|PDB:5UAY}.
HELIX 188 190 {ECO:0000244|PDB:5UAY}.
HELIX 193 195 {ECO:0000244|PDB:5UAY}.
STRAND 202 204 {ECO:0000244|PDB:5UAY}.
HELIX 206 218 {ECO:0000244|PDB:5UAY}.
STRAND 219 231 {ECO:0000244|PDB:5UAY}.
STRAND 233 235 {ECO:0000244|PDB:5UAY}.
STRAND 237 245 {ECO:0000244|PDB:5UAY}.
STRAND 252 258 {ECO:0000244|PDB:5UAY}.
HELIX 276 296 {ECO:0000244|PDB:5UAY}.
HELIX 304 317 {ECO:0000244|PDB:5UAY}.
HELIX 322 338 {ECO:0000244|PDB:5UAY}.
STRAND 345 350 {ECO:0000244|PDB:5UAY}.
STRAND 356 362 {ECO:0000244|PDB:5UAY}.
STRAND 365 374 {ECO:0000244|PDB:5UAY}.
TURN 376 378 {ECO:0000244|PDB:5UAY}.
HELIX 384 386 {ECO:0000244|PDB:5UBC}.
HELIX 387 393 {ECO:0000244|PDB:5UAY}.
HELIX 396 398 {ECO:0000244|PDB:5UAY}.
HELIX 406 417 {ECO:0000244|PDB:5UAY}.
TURN 418 420 {ECO:0000244|PDB:5UAY}.
STRAND 422 431 {ECO:0000244|PDB:5UAY}.
STRAND 436 447 {ECO:0000244|PDB:5UAY}.
SEQUENCE 818 AA; 89189 MW; 332E04D308F370F6 CRC64;
MAAFSVNGQL IPTATSSTAS TSLSSRRKFL SPSSSRLPRI STQSPRVPSI KCSKSLPNRD
TETSSKDSLL KNLAKPLAVA SVSSAASFFL FRISNLPSVL TGGGGGGDGN FGGFGGGGGG
GDGNDGGFWG KLFSPSPAVA DEEQSPDWDS HGLPANIVVQ LNKLSGFKKY KVSDIMFFDR
RRQTTIGTED SFFEMVSIRP GGVYTKAQLQ KELETLATCG MFEKVDLEGK TKPDGTLGVT
ISFAESTWQS ADRFRCINVG LMVQSKPIEM DSDMTDKEKL EYYRSLEKDY KRRIDRARPC
LLPAPVYGEV MQMLRDQGKV SARLLQRIRD RVQKWYHDEG YACAQVVNFG NLNTKEVVCE
VVEGDITQLV IQFQDKLGNV VEGNTQVPVV RRELPKQLRQ GYVFNIEAGK KALSNINSLG
LFSNIEVNPR PDEKNEGGII VEIKLKELEQ KSAEVSTEWS IVPGRGGAPT LASFQPGGSV
TFEHRNLQGL NRSLMGSVTT SNFLNPQDDL SFKLEYVHPY LDGVYNPRNR TFKTSCFNSR
KLSPVFTGGP GVEEVPPIWV DRAGVKANIT ENFTRQSKFT YGLVMEEITT RDESSHIAAN
GQRLLPSGGI SADGPPTTLS GTGVDRMAFL QANITRDNTK FVNGAVVGQR TVFQVDQGLG
IGSKFPFFNR HQLTMTKFIQ LREVEQGAGK SPPPVLVLHG HYGGCVGDLP SYDAFVLGGP
YSVRGYNMGE LGAARNIAEV GAEIRIPVKN THVYAFVEHG NDLGSSKDVK GNPTAVYRRT
GQGSSYGAGV KLGLVRAEYA VDHNNGTGAL FFRFGERY


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