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Q9FMD5

- TIC40_ARATH

UniProt

Q9FMD5 - TIC40_ARATH

Protein

Protein TIC 40, chloroplastic

Gene

TIC40

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 93 (01 Oct 2014)
      Sequence version 1 (01 Mar 2001)
      Previous versions | rss
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    Functioni

    Involved in protein precursor import into chloroplasts. Part of the motor complex consisting of a co-chaperone (TIC40) and a chaperone (HSP93) associated with the import channel (TIC110). Causes the release of bound transit peptides from TIC110 and stimulates ATP hydrolysis by HSP93. Involved in reinsertion of proteins from the chloroplast stroma into the inner membrane.6 Publications

    GO - Molecular functioni

    1. protein binding Source: UniProtKB

    GO - Biological processi

    1. chloroplast organization Source: TAIR
    2. protein import into chloroplast stroma Source: TAIR

    Keywords - Biological processi

    Protein transport, Transport

    Protein family/group databases

    TCDBi3.A.9.1.2. the chloroplast envelope protein translocase (cept or tic-toc) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein TIC 40, chloroplastic
    Alternative name(s):
    Protein PIGMENT DEFECTIVE EMBRYO 120
    Translocon at the inner envelope membrane of chloroplasts 40
    Short name:
    AtTIC40
    Gene namesi
    Name:TIC40
    Synonyms:PDE120
    Ordered Locus Names:At5g16620
    ORF Names:MTG13.6
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 5

    Organism-specific databases

    TAIRiAT5G16620.

    Subcellular locationi

    Plastidchloroplast inner membrane 4 Publications; Single-pass membrane protein 4 Publications

    GO - Cellular componenti

    1. chloroplast Source: TAIR
    2. chloroplast envelope Source: TAIR
    3. chloroplast inner membrane Source: TAIR
    4. chloroplast thylakoid membrane Source: TAIR
    5. integral component of membrane Source: UniProtKB-KW
    6. membrane Source: TAIR
    7. Tic complex Source: TAIR

    Keywords - Cellular componenti

    Chloroplast, Membrane, Plastid, Plastid inner membrane

    Pathology & Biotechi

    Disruption phenotypei

    Small and chlorotic, but not seedling lethal. Defective in chloroplast protein import.3 Publications

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi396 – 3961N → A: Loss of stimulation of HSP93 ATP hydrolysis. 1 Publication
    Mutagenesisi405 – 4051N → A: Loss of stimulation of HSP93 ATP hydrolysis. 1 Publication
    Mutagenesisi418 – 4181N → A: No effect on stimulation of HSP93 ATP hydrolysis. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 4343ChloroplastSequence AnalysisAdd
    BLAST
    Transit peptidei44 – 7633Chloroplast; inner membraneSequence AnalysisAdd
    BLAST
    Chaini77 – 447371Protein TIC 40, chloroplasticPRO_0000413673Add
    BLAST

    Proteomic databases

    PaxDbiQ9FMD5.
    PRIDEiQ9FMD5.

    Expressioni

    Tissue specificityi

    Expressed in seedlings, flowers, leaves, stems and roots.2 Publications

    Developmental stagei

    Expressed throughout development.1 Publication

    Gene expression databases

    GenevestigatoriQ9FMD5.

    Interactioni

    Subunit structurei

    Part of the Tic complex. Interacts with HSP93, TIC110 and LTD.4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    TIC110Q8LPR93EBI-639157,EBI-639092

    Protein-protein interaction databases

    BioGridi16800. 5 interactions.
    IntActiQ9FMD5. 2 interactions.
    STRINGi3702.AT5G16620.1-P.

    Structurei

    Secondary structure

    1
    447
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi387 – 3937
    Helixi397 – 4026
    Helixi406 – 41510
    Helixi419 – 4213
    Helixi422 – 4254
    Helixi429 – 44113
    Beta strandi442 – 4443

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2LNMNMR-A386-447[»]
    ProteinModelPortaliQ9FMD5.
    SMRiQ9FMD5. Positions 386-447.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini77 – 10428Chloroplast intermembraneSequence AnalysisAdd
    BLAST
    Topological domaini126 – 447322StromalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei105 – 12521HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini310 – 34435STI1 1Add
    BLAST
    Domaini386 – 42540STI1 2Add
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi44 – 10764Ser-richAdd
    BLAST

    Domaini

    The C-terminal half (89-105) of the Ser/Pro-rich region and the transmembrane domain are necessary and sufficient for membrane integration.
    The TPR region (238-373) interacts with TIC110.
    The STI1 2 domain (386-425) has a stimulatory effect on HSP93 ATP hydrolysis.

    Sequence similaritiesi

    Contains 2 STI1 domains.Curated

    Keywords - Domaini

    Repeat, Transit peptide, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG276582.
    HOGENOMiHOG000082622.
    InParanoidiQ9FMD5.
    OMAiQDMLNNM.
    PhylomeDBiQ9FMD5.

    Family and domain databases

    InterProiIPR006636. STI1_HS-bd.
    [Graphical view]
    SMARTiSM00727. STI1. 2 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q9FMD5-1 [UniParc]FASTAAdd to Basket

    « Hide

    MENLTLVSCS ASSPKLLIGC NFTSSLKNPT GFSRRTPNIV LRCSKISASA    50
    QSQSPSSRPE NTGEIVVVKQ RSKAFASIFS SSRDQQTTSV ASPSVPVPPP 100
    SSSTIGSPLF WIGVGVGLSA LFSYVTSNLK KYAMQTAMKT MMNQMNTQNS 150
    QFNNSGFPSG SPFPFPFPPQ TSPASSPFQS QSQSSGATVD VTATKVETPP 200
    STKPKPTPAK DIEVDKPSVV LEASKEKKEE KNYAFEDISP EETTKESPFS 250
    NYAEVSETNS PKETRLFEDV LQNGAGPANG ATASEVFQSL GGGKGGPGLS 300
    VEALEKMMED PTVQKMVYPY LPEEMRNPET FKWMLKNPQY RQQLQDMLNN 350
    MSGSGEWDKR MTDTLKNFDL NSPEVKQQFN QIGLTPEEVI SKIMENPDVA 400
    MAFQNPRVQA ALMECSENPM NIMKYQNDKE VMDVFNKISQ LFPGMTG 447
    Length:447
    Mass (Da):48,903
    Last modified:March 1, 2001 - v1
    Checksum:i52D3E7222AB461CE
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB008270 Genomic DNA. Translation: BAB10189.1.
    CP002688 Genomic DNA. Translation: AED92318.1.
    AF428299 mRNA. Translation: AAL16131.1.
    AY093010 mRNA. Translation: AAM13009.1.
    BT006595 mRNA. Translation: AAP31939.1.
    RefSeqiNP_197165.1. NM_121668.3.
    UniGeneiAt.25049.
    At.57178.

    Genome annotation databases

    EnsemblPlantsiAT5G16620.1; AT5G16620.1; AT5G16620.
    GeneIDi831524.
    KEGGiath:AT5G16620.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB008270 Genomic DNA. Translation: BAB10189.1 .
    CP002688 Genomic DNA. Translation: AED92318.1 .
    AF428299 mRNA. Translation: AAL16131.1 .
    AY093010 mRNA. Translation: AAM13009.1 .
    BT006595 mRNA. Translation: AAP31939.1 .
    RefSeqi NP_197165.1. NM_121668.3.
    UniGenei At.25049.
    At.57178.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2LNM NMR - A 386-447 [» ]
    ProteinModelPortali Q9FMD5.
    SMRi Q9FMD5. Positions 386-447.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 16800. 5 interactions.
    IntActi Q9FMD5. 2 interactions.
    STRINGi 3702.AT5G16620.1-P.

    Protein family/group databases

    TCDBi 3.A.9.1.2. the chloroplast envelope protein translocase (cept or tic-toc) family.

    Proteomic databases

    PaxDbi Q9FMD5.
    PRIDEi Q9FMD5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT5G16620.1 ; AT5G16620.1 ; AT5G16620 .
    GeneIDi 831524.
    KEGGi ath:AT5G16620.

    Organism-specific databases

    TAIRi AT5G16620.

    Phylogenomic databases

    eggNOGi NOG276582.
    HOGENOMi HOG000082622.
    InParanoidi Q9FMD5.
    OMAi QDMLNNM.
    PhylomeDBi Q9FMD5.

    Gene expression databases

    Genevestigatori Q9FMD5.

    Family and domain databases

    InterProi IPR006636. STI1_HS-bd.
    [Graphical view ]
    SMARTi SM00727. STI1. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Structural analysis of Arabidopsis thaliana chromosome 5. III. Sequence features of the regions of 1,191,918 bp covered by seventeen physically assigned P1 clones."
      Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N., Tabata S.
      DNA Res. 4:401-414(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Columbia.
    2. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      Strain: cv. Columbia.
    3. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
      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.
      Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: cv. Columbia.
    4. "Tic40, a membrane-anchored co-chaperone homolog in the chloroplast protein translocon."
      Chou M.L., Fitzpatrick L.M., Tu S.L., Budziszewski G., Potter-Lewis S., Akita M., Levin J.Z., Keegstra K., Li H.M.
      EMBO J. 22:2970-2980(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, DISRUPTION PHENOTYPE.
    5. Cited for: TISSUE SPECIFICITY.
    6. "Arabidopsis tic110 is essential for the assembly and function of the protein import machinery of plastids."
      Inaba T., Alvarez-Huerta M., Li M., Bauer J., Ewers C., Kessler F., Schnell D.J.
      Plant Cell 17:1482-1496(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH TIC110.
    7. "In vivo studies on the roles of Tic110, Tic40 and Hsp93 during chloroplast protein import."
      Kovacheva S., Bedard J., Patel R., Dudley P., Twell D., Rios G., Koncz C., Jarvis P.
      Plant J. 41:412-428(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE.
    8. "Reconstitution of protein targeting to the inner envelope membrane of chloroplasts."
      Li M., Schnell D.J.
      J. Cell Biol. 175:249-259(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, PROTEOLYTIC PROCESSING, TOPOLOGY.
    9. "Stimulation of transit-peptide release and ATP hydrolysis by a cochaperone during protein import into chloroplasts."
      Chou M.L., Chu C.C., Chen L.J., Akita M., Li H.M.
      J. Cell Biol. 175:893-900(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH TIC110 AND HSP93, MUTAGENESIS OF ASN-396; ASN-405 AND ASN-418.
    10. "Functional similarity between the chloroplast translocon component, Tic40, and the human co-chaperone, Hsp70-interacting protein (Hip)."
      Bedard J., Kubis S., Bimanadham S., Jarvis P.
      J. Biol. Chem. 282:21404-21414(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH TIC110, DISRUPTION PHENOTYPE.
    11. "A novel serine/proline-rich domain in combination with a transmembrane domain is required for the insertion of AtTic40 into the inner envelope membrane of chloroplasts."
      Tripp J., Inoue K., Keegstra K., Froehlich J.E.
      Plant J. 52:824-838(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, PROTEOLYTIC PROCESSING.
    12. "Tic40 is important for reinsertion of proteins from the chloroplast stroma into the inner membrane."
      Chiu C.C., Li H.M.
      Plant J. 56:793-801(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    13. "LTD is a protein required for sorting light-harvesting chlorophyll-binding proteins to the chloroplast SRP pathway."
      Ouyang M., Li X., Ma J., Chi W., Xiao J., Zou M., Chen F., Lu C., Zhang L.
      Nat. Commun. 2:277-277(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH LTD.
    14. "Protein import into chloroplasts: the Tic complex and its regulation."
      Kovacs-Bogdan E., Soll J., Bolter B.
      Biochim. Biophys. Acta 1803:740-747(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.

    Entry informationi

    Entry nameiTIC40_ARATH
    AccessioniPrimary (citable) accession number: Q9FMD5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 19, 2011
    Last sequence update: March 1, 2001
    Last modified: October 1, 2014
    This is version 93 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Inserts into the inner envelope membrane from the stroma after import from the cytoplasm. The transit peptide undergoes a two-step processing. The initial cleavage to generate the intermediate found in the stroma is mediated by the stromal processing peptidase (SPP) while the final processing step by a signal peptidase I-type (SPase I), possibly PLSP1, requires association with the inner membrane.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Arabidopsis thaliana
      Arabidopsis thaliana: entries and gene names
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3