ID TOC34_PEA STANDARD; PRT; 310 AA. AC Q41009; Q41029; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 24-JAN-2006 (Rel. 49, Last annotation update) DE Translocase of chloroplast 34 (EC 3.6.5.-) (34 kDa chloroplast outer DE envelope protein) (GTP-binding protein OEP34) (GTP-binding protein DE IAP34). GN Name=TOC34; Synonyms=IAP34, OEP34; OS Pisum sativum (Garden pea). OG Plastid; Chloroplast. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids I; Fabales; Fabaceae; Papilionoideae; Vicieae; Pisum. OX NCBI_TaxID=3888; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE. RC STRAIN=cv. Miranda; TISSUE=Leaf; RX MEDLINE=95276777; PubMed=7757113; RA Seedorf M., Waegemann K., Soll J.; RT "A constituent of the chloroplast import complex represents a new type RT of GTP-binding protein."; RL Plant J. 7:401-411(1995). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 119-139 AND RP 157-180. RX MEDLINE=95063938; PubMed=7973656; RA Kessler F., Blobel G., Patel H.V., Schnell D.J.; RT "Identification of two GTP-binding proteins in the chloroplast protein RT import machinery."; RL Science 266:1035-1039(1994). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-258 IN COMPLEX WITH GTP, RP HOMODIMERIZATION, AND MUTAGENESIS OF ARG-128. RX MEDLINE=21671739; PubMed=11753431; DOI=10.1038/nsb744; RA Sun Y.-J., Forouhar F., Li Hm H.-M., Tu S.-L., Yeh Y.-H., Kao S., RA Shr H.-L., Chou C.-C., Chen C., Hsiao C.-D.; RT "Crystal structure of pea Toc34, a novel GTPase of the chloroplast RT protein translocon."; RL Nat. Struct. Biol. 9:95-100(2002). CC -!- FUNCTION: GTPase involved in protein precursor import into CC chloroplasts. Seems to recognize chloroplast-destined precursor CC proteins and regulate their presentation to the translocation CC channel through GTP hydrolysis. CC -!- SUBUNIT: Homodimer and monomer. Part of the TOC core complex that CC includes one protein for the specific recognition of transit CC peptides surrounded by a ring composed of four proteins forming CC translocation channels, and four to five GTP-binding proteins CC providing energy. This core complex can interact with components CC of the TIC complex to form a larger import complex. Chloroplastic CC protein precursor such as prSS (precursor of the RuBisCO small CC subunit) interacts with these complexes. The TOC complex contains CC a specific subset of polar lipids such as CC digalactosyldiacylglyceride (DGDG), phosphatidylcholine (PC) and CC phosphatidylglycerol (PG). TOC34 interacts at least with TOC75. CC -!- SUBCELLULAR LOCATION: Chloroplast; outer membrane. CC -!- SIMILARITY: Belongs to the TOC34 family. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; Z28341; CAA82196.1; -; mRNA. DR EMBL; L36856; AAC25785.1; -; mRNA. DR PIR; B55171; B55171. DR PDB; 1H65; X-ray; A/B/C=1-258. DR InterPro; IPR006703; AIG1. DR InterPro; IPR005688; Toc34. DR Pfam; PF04548; AIG1; 1. DR TIGRFAMs; TIGR00991; 3a0901s02IAP34; 1. KW 3D-structure; Chloroplast; Direct protein sequencing; GTP-binding; KW Hydrolase; Membrane; Nucleotide-binding; Outer membrane; Plastid; KW Protein transport; Transmembrane; Transport. FT TOPO_DOM 1 268 Cytoplasmic (Potential). FT TRANSMEM 269 289 Potential. FT TOPO_DOM 290 310 Chloroplast intermembrane (Potential). FT NP_BIND 49 54 GTP; phosphate group. FT BINDING 73 73 GTP; phosphate group. FT NP_BIND 210 211 GTP; guanine group. FT REGION 68 71 Homodimerization. FT REGION 128 133 Homodimerization. FT MUTAGEN 128 128 R->A: No dimerization and reduced GTPase FT activity. SQ SEQUENCE 310 AA; 34157 MW; 00D5E79735BF041F CRC64; MASQQQTVRE WSGINTFAPA TQTKLLELLG NLKQEDVNSL TILVMGKGGV GKSSTVNSII GERVVSISPF QSEGPRPVMV SRSRAGFTLN IIDTPGLIEG GYINDMALNI IKSFLLDKTI DVLLYVDRLD AYRVDNLDKL VAKAITDSFG KGIWNKAIVA LTHAQFSPPD GLPYDEFFSK RSEALLQVVR SGASLKKDAQ ASDIPVVLIE NSGRCNKNDS DEKVLPNGIA WIPHLVQTIT EVALNKSESI FVDKNLIDGP NPNQRGKLWI PLIFALQYLF LAKPIEALIR RDIATETKPA WETRDVGDRK //