TC754_ARATH
ID TC754_ARATH Reviewed; 396 AA.
AC Q5IZC8; Q9M0R9;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Protein TOC75-4, chloroplastic;
DE AltName: Full=75 kDa translocon at the outer-envelope-membrane of chloroplasts 4;
DE Short=AtTOC75-IV;
GN Name=TOC75-4; OrderedLocusNames=At4g09080; ORFNames=F23J3.110;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=cv. Columbia; TISSUE=Seedling;
RX PubMed=15908591; DOI=10.1104/pp.105.063289;
RA Baldwin A., Wardle A., Patel R., Dudley P., Park S.K., Twell D., Inoue K.,
RA Jarvis P.;
RT "A molecular-genetic study of the Arabidopsis toc75 gene family.";
RL Plant Physiol. 138:715-733(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
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).
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 (By similarity). Required for etioplast
CC formation and/or etioplast-chloroplast transition during deetiolation.
CC {ECO:0000250, ECO:0000269|PubMed:15908591}.
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 also interacts with these complexes
CC (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast outer membrane
CC {ECO:0000269|PubMed:15908591}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:15908591}.
CC -!- TISSUE SPECIFICITY: Expressed ubiquitously at low levels.
CC {ECO:0000269|PubMed:15908591}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB78032.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY585655; AAT08975.1; -; mRNA.
DR EMBL; AL161514; CAB78032.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE82720.1; -; Genomic_DNA.
DR PIR; H85091; H85091.
DR RefSeq; NP_001329162.1; NM_001340610.1.
DR RefSeq; NP_192647.2; NM_116977.3.
DR AlphaFoldDB; Q5IZC8; -.
DR IntAct; Q5IZC8; 2.
DR STRING; 3702.AT4G09080.1; -.
DR PaxDb; Q5IZC8; -.
DR PRIDE; Q5IZC8; -.
DR EnsemblPlants; AT4G09080.1; AT4G09080.1; AT4G09080.
DR GeneID; 826486; -.
DR Gramene; AT4G09080.1; AT4G09080.1; AT4G09080.
DR KEGG; ath:AT4G09080; -.
DR Araport; AT4G09080; -.
DR TAIR; locus:2122328; AT4G09080.
DR eggNOG; ENOG502QTZ3; Eukaryota.
DR HOGENOM; CLU_000837_26_1_1; -.
DR InParanoid; Q5IZC8; -.
DR OMA; RWYHGEG; -.
DR OrthoDB; 455003at2759; -.
DR PhylomeDB; Q5IZC8; -.
DR PRO; PR:Q5IZC8; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q5IZC8; baseline and differential.
DR Genevisible; Q5IZC8; AT.
DR GO; GO:0009707; C:chloroplast outer membrane; IBA:GO_Central.
DR GO; GO:0031359; C:integral component of chloroplast outer membrane; IDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0001401; C:SAM complex; IBA:GO_Central.
DR GO; GO:0009658; P:chloroplast organization; IBA:GO_Central.
DR GO; GO:0009662; P:etioplast organization; IMP:TAIR.
DR GO; GO:0045037; P:protein import into chloroplast stroma; IBA:GO_Central.
DR GO; GO:0045040; P:protein insertion into mitochondrial outer membrane; IBA:GO_Central.
DR GO; GO:0045036; P:protein targeting to chloroplast; IDA:TAIR.
DR InterPro; IPR000184; Bac_surfAg_D15.
DR InterPro; IPR039910; D15-like.
DR PANTHER; PTHR12815; PTHR12815; 1.
DR Pfam; PF01103; Omp85; 1.
PE 2: Evidence at transcript level;
KW Chloroplast; Membrane; Plastid; Plastid outer membrane; Protein transport;
KW Reference proteome; Transmembrane; Transmembrane beta strand; Transport.
FT CHAIN 1..396
FT /note="Protein TOC75-4, chloroplastic"
FT /id="PRO_0000144794"
FT TOPO_DOM 1..23
FT /note="Chloroplast intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 24..32
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 33..87
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 88..96
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 97..140
FT /note="Chloroplast intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 141..148
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 149..156
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 157..164
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 165..271
FT /note="Chloroplast intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 272..280
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 281..292
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 293..301
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 302..363
FT /note="Chloroplast intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 364..370
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 371..384
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 385..392
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 393..396
FT /note="Chloroplast intermembrane"
FT /evidence="ECO:0000255"
SQ SEQUENCE 396 AA; 43632 MW; F6606F1A031E9A6E CRC64;
MEAVKEAVRK IKSLVIPHAD EKDNGIVFEI KLNETDQRVE KWGLDPSLDF FEVTGNCNLG
RPNSEGSNQS LMGSVTIRNI FNPKLDDLLS KIEYVRFLEA VKKPRNRTFK TSFFNSRKLS
PVFTGGPGYE DLVPPMFVGR DCLKATITEN LTRQRELTYG VMFEEIITRD ENRRISENGL
LLSPDGGISI NGPPTTLSGT GIDHIATLQA NITRDNTKLV NGAVVGEKNI FQVDQGLGIG
NNFPLFNRHQ LSLTSFIQLK QVEEGSDKPQ PPVLVLHGRY GGCIGDLPSY DVFALGGPNS
VRGYSMGELG AAKNILELGA EIRIPVKNTH VYAFAEHGND LGSSKDVKGN PTGLYRKMGH
GSSYGLGVKL GMVRAEYTVR HNRGTGALFL RFGERY
