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TIC40_ARATH
ID   TIC40_ARATH             Reviewed;         447 AA.
AC   Q9FMD5;
DT   19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   25-MAY-2022, entry version 130.
DE   RecName: Full=Protein TIC 40, chloroplastic;
DE   AltName: Full=Protein PIGMENT DEFECTIVE EMBRYO 120;
DE   AltName: Full=Translocon at the inner envelope membrane of chloroplasts 40;
DE            Short=AtTIC40;
DE   Flags: Precursor;
GN   Name=TIC40; Synonyms=PDE120; OrderedLocusNames=At5g16620; ORFNames=MTG13.6;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=9501997; DOI=10.1093/dnares/4.6.401;
RA   Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. III. Sequence
RT   features of the regions of 1,191,918 bp covered by seventeen physically
RT   assigned P1 clones.";
RL   DNA Res. 4:401-414(1997).
RN   [2]
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [4]
RP   FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, AND DISRUPTION PHENOTYPE.
RX   PubMed=12805212; DOI=10.1093/emboj/cdg281;
RA   Chou M.L., Fitzpatrick L.M., Tu S.L., Budziszewski G., Potter-Lewis S.,
RA   Akita M., Levin J.Z., Keegstra K., Li H.M.;
RT   "Tic40, a membrane-anchored co-chaperone homolog in the chloroplast protein
RT   translocon.";
RL   EMBO J. 22:2970-2980(2003).
RN   [5]
RP   TISSUE SPECIFICITY.
RX   PubMed=15033972; DOI=10.1074/jbc.m401968200;
RA   Vojta A., Alavi M., Becker T., Hoermann F., Kuechler M., Soll J.,
RA   Thomson R., Schleiff E.;
RT   "The protein translocon of the plastid envelopes.";
RL   J. Biol. Chem. 279:21401-21405(2004).
RN   [6]
RP   FUNCTION, AND INTERACTION WITH TIC110.
RX   PubMed=15829604; DOI=10.1105/tpc.105.030700;
RA   Inaba T., Alvarez-Huerta M., Li M., Bauer J., Ewers C., Kessler F.,
RA   Schnell D.J.;
RT   "Arabidopsis tic110 is essential for the assembly and function of the
RT   protein import machinery of plastids.";
RL   Plant Cell 17:1482-1496(2005).
RN   [7]
RP   FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=15659100; DOI=10.1111/j.1365-313x.2004.02307.x;
RA   Kovacheva S., Bedard J., Patel R., Dudley P., Twell D., Rios G., Koncz C.,
RA   Jarvis P.;
RT   "In vivo studies on the roles of Tic110, Tic40 and Hsp93 during chloroplast
RT   protein import.";
RL   Plant J. 41:412-428(2005).
RN   [8]
RP   SUBCELLULAR LOCATION, PROTEOLYTIC PROCESSING, AND TOPOLOGY.
RX   PubMed=17060496; DOI=10.1083/jcb.200605162;
RA   Li M., Schnell D.J.;
RT   "Reconstitution of protein targeting to the inner envelope membrane of
RT   chloroplasts.";
RL   J. Cell Biol. 175:249-259(2006).
RN   [9]
RP   FUNCTION, INTERACTION WITH TIC110 AND HSP93, AND MUTAGENESIS OF ASN-396;
RP   ASN-405 AND ASN-418.
RX   PubMed=17158958; DOI=10.1083/jcb.200609172;
RA   Chou M.L., Chu C.C., Chen L.J., Akita M., Li H.M.;
RT   "Stimulation of transit-peptide release and ATP hydrolysis by a cochaperone
RT   during protein import into chloroplasts.";
RL   J. Cell Biol. 175:893-900(2006).
RN   [10]
RP   FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH TIC110, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=17535810; DOI=10.1074/jbc.m611545200;
RA   Bedard J., Kubis S., Bimanadham S., Jarvis P.;
RT   "Functional similarity between the chloroplast translocon component, Tic40,
RT   and the human co-chaperone, Hsp70-interacting protein (Hip).";
RL   J. Biol. Chem. 282:21404-21414(2007).
RN   [11]
RP   SUBCELLULAR LOCATION, AND PROTEOLYTIC PROCESSING.
RX   PubMed=17883373; DOI=10.1111/j.1365-313x.2007.03279.x;
RA   Tripp J., Inoue K., Keegstra K., Froehlich J.E.;
RT   "A novel serine/proline-rich domain in combination with a transmembrane
RT   domain is required for the insertion of AtTic40 into the inner envelope
RT   membrane of chloroplasts.";
RL   Plant J. 52:824-838(2007).
RN   [12]
RP   FUNCTION.
RX   PubMed=18657235; DOI=10.1111/j.1365-313x.2008.03638.x;
RA   Chiu C.C., Li H.M.;
RT   "Tic40 is important for reinsertion of proteins from the chloroplast stroma
RT   into the inner membrane.";
RL   Plant J. 56:793-801(2008).
RN   [13]
RP   INTERACTION WITH LTD.
RX   PubMed=21505433; DOI=10.1038/ncomms1278;
RA   Ouyang M., Li X., Ma J., Chi W., Xiao J., Zou M., Chen F., Lu C., Zhang L.;
RT   "LTD is a protein required for sorting light-harvesting chlorophyll-binding
RT   proteins to the chloroplast SRP pathway.";
RL   Nat. Commun. 2:277-277(2011).
RN   [14]
RP   REVIEW.
RX   PubMed=20100520; DOI=10.1016/j.bbamcr.2010.01.015;
RA   Kovacs-Bogdan E., Soll J., Bolter B.;
RT   "Protein import into chloroplasts: the Tic complex and its regulation.";
RL   Biochim. Biophys. Acta 1803:740-747(2010).
CC   -!- FUNCTION: Involved in protein precursor import into chloroplasts. Part
CC       of the motor complex consisting of a co-chaperone (TIC40) and a
CC       chaperone (HSP93) associated with the import channel (TIC110). Causes
CC       the release of bound transit peptides from TIC110 and stimulates ATP
CC       hydrolysis by HSP93. Involved in reinsertion of proteins from the
CC       chloroplast stroma into the inner membrane.
CC       {ECO:0000269|PubMed:12805212, ECO:0000269|PubMed:15659100,
CC       ECO:0000269|PubMed:15829604, ECO:0000269|PubMed:17158958,
CC       ECO:0000269|PubMed:17535810, ECO:0000269|PubMed:18657235}.
CC   -!- SUBUNIT: Part of the Tic complex. Interacts with HSP93, TIC110 and LTD.
CC       {ECO:0000269|PubMed:15829604, ECO:0000269|PubMed:17158958,
CC       ECO:0000269|PubMed:17535810, ECO:0000269|PubMed:21505433}.
CC   -!- INTERACTION:
CC       Q9FMD5; Q9FI56: CLPC1; NbExp=3; IntAct=EBI-639157, EBI-2297694;
CC       Q9FMD5; Q8LPR9: TIC110; NbExp=3; IntAct=EBI-639157, EBI-639092;
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast inner membrane
CC       {ECO:0000269|PubMed:12805212, ECO:0000269|PubMed:17060496,
CC       ECO:0000269|PubMed:17535810, ECO:0000269|PubMed:17883373}; Single-pass
CC       membrane protein {ECO:0000269|PubMed:12805212,
CC       ECO:0000269|PubMed:17060496, ECO:0000269|PubMed:17535810,
CC       ECO:0000269|PubMed:17883373}.
CC   -!- TISSUE SPECIFICITY: Expressed in seedlings, flowers, leaves, stems and
CC       roots. {ECO:0000269|PubMed:15033972, ECO:0000269|PubMed:15659100}.
CC   -!- DEVELOPMENTAL STAGE: Expressed throughout development.
CC       {ECO:0000269|PubMed:15659100}.
CC   -!- DOMAIN: The C-terminal half (89-105) of the Ser/Pro-rich region and the
CC       transmembrane domain are necessary and sufficient for membrane
CC       integration.
CC   -!- DOMAIN: The TPR region (238-373) interacts with TIC110.
CC   -!- DOMAIN: The STI1 2 domain (386-425) has a stimulatory effect on HSP93
CC       ATP hydrolysis.
CC   -!- DISRUPTION PHENOTYPE: Small and chlorotic, but not seedling lethal.
CC       Defective in chloroplast protein import. {ECO:0000269|PubMed:12805212,
CC       ECO:0000269|PubMed:15659100, ECO:0000269|PubMed:17535810}.
CC   -!- MISCELLANEOUS: Inserts into the inner envelope membrane from the stroma
CC       after import from the cytoplasm. The transit peptide undergoes a two-
CC       step processing. The initial cleavage to generate the intermediate
CC       found in the stroma is mediated by the stromal processing peptidase
CC       (SPP) while the final processing step by a signal peptidase I-type
CC       (SPase I), possibly PLSP1, requires association with the inner
CC       membrane.
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DR   EMBL; AB008270; BAB10189.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED92318.1; -; Genomic_DNA.
DR   EMBL; AF428299; AAL16131.1; -; mRNA.
DR   EMBL; AY093010; AAM13009.1; -; mRNA.
DR   EMBL; BT006595; AAP31939.1; -; mRNA.
DR   RefSeq; NP_197165.1; NM_121668.4.
DR   PDB; 2LNM; NMR; -; A=386-447.
DR   PDBsum; 2LNM; -.
DR   AlphaFoldDB; Q9FMD5; -.
DR   BMRB; Q9FMD5; -.
DR   SMR; Q9FMD5; -.
DR   BioGRID; 16800; 7.
DR   IntAct; Q9FMD5; 3.
DR   STRING; 3702.AT5G16620.1; -.
DR   TCDB; 3.A.9.1.2; the chloroplast envelope protein translocase (cept or tic-toc) family.
DR   iPTMnet; Q9FMD5; -.
DR   MetOSite; Q9FMD5; -.
DR   PaxDb; Q9FMD5; -.
DR   PRIDE; Q9FMD5; -.
DR   ProteomicsDB; 234429; -.
DR   EnsemblPlants; AT5G16620.1; AT5G16620.1; AT5G16620.
DR   GeneID; 831524; -.
DR   Gramene; AT5G16620.1; AT5G16620.1; AT5G16620.
DR   KEGG; ath:AT5G16620; -.
DR   Araport; AT5G16620; -.
DR   TAIR; locus:2174155; AT5G16620.
DR   eggNOG; KOG1308; Eukaryota.
DR   HOGENOM; CLU_038645_1_0_1; -.
DR   InParanoid; Q9FMD5; -.
DR   OMA; WATSNVK; -.
DR   OrthoDB; 950146at2759; -.
DR   PhylomeDB; Q9FMD5; -.
DR   PRO; PR:Q9FMD5; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9FMD5; baseline and differential.
DR   Genevisible; Q9FMD5; AT.
DR   GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR   GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR   GO; GO:0009706; C:chloroplast inner membrane; IDA:TAIR.
DR   GO; GO:0009535; C:chloroplast thylakoid membrane; HDA:TAIR.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0009536; C:plastid; HDA:TAIR.
DR   GO; GO:0031897; C:Tic complex; TAS:TAIR.
DR   GO; GO:0009658; P:chloroplast organization; IMP:TAIR.
DR   GO; GO:0045037; P:protein import into chloroplast stroma; IMP:TAIR.
DR   InterPro; IPR041243; STI1.
DR   InterPro; IPR006636; STI1_HS-bd.
DR   Pfam; PF17830; STI1; 1.
DR   SMART; SM00727; STI1; 2.
PE   1: Evidence at protein level;
KW   3D-structure; Chloroplast; Membrane; Plastid; Plastid inner membrane;
KW   Protein transport; Reference proteome; Repeat; Transit peptide;
KW   Transmembrane; Transmembrane helix; Transport.
FT   TRANSIT         1..43
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   TRANSIT         44..76
FT                   /note="Chloroplast; inner membrane"
FT                   /evidence="ECO:0000255"
FT   CHAIN           77..447
FT                   /note="Protein TIC 40, chloroplastic"
FT                   /id="PRO_0000413673"
FT   TOPO_DOM        77..104
FT                   /note="Chloroplast intermembrane"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        105..125
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        126..447
FT                   /note="Stromal"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          310..344
FT                   /note="STI1 1"
FT   DOMAIN          386..425
FT                   /note="STI1 2"
FT   REGION          148..214
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          231..261
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        174..200
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        244..260
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MUTAGEN         396
FT                   /note="N->A: Loss of stimulation of HSP93 ATP hydrolysis."
FT                   /evidence="ECO:0000269|PubMed:17158958"
FT   MUTAGEN         405
FT                   /note="N->A: Loss of stimulation of HSP93 ATP hydrolysis."
FT                   /evidence="ECO:0000269|PubMed:17158958"
FT   MUTAGEN         418
FT                   /note="N->A: No effect on stimulation of HSP93 ATP
FT                   hydrolysis."
FT                   /evidence="ECO:0000269|PubMed:17158958"
FT   HELIX           387..393
FT                   /evidence="ECO:0007829|PDB:2LNM"
FT   HELIX           397..402
FT                   /evidence="ECO:0007829|PDB:2LNM"
FT   HELIX           406..415
FT                   /evidence="ECO:0007829|PDB:2LNM"
FT   HELIX           419..421
FT                   /evidence="ECO:0007829|PDB:2LNM"
FT   HELIX           422..425
FT                   /evidence="ECO:0007829|PDB:2LNM"
FT   HELIX           429..441
FT                   /evidence="ECO:0007829|PDB:2LNM"
FT   STRAND          442..444
FT                   /evidence="ECO:0007829|PDB:2LNM"
SQ   SEQUENCE   447 AA;  48903 MW;  52D3E7222AB461CE CRC64;
     MENLTLVSCS ASSPKLLIGC NFTSSLKNPT GFSRRTPNIV LRCSKISASA QSQSPSSRPE
     NTGEIVVVKQ RSKAFASIFS SSRDQQTTSV ASPSVPVPPP SSSTIGSPLF WIGVGVGLSA
     LFSYVTSNLK KYAMQTAMKT MMNQMNTQNS QFNNSGFPSG SPFPFPFPPQ TSPASSPFQS
     QSQSSGATVD VTATKVETPP STKPKPTPAK DIEVDKPSVV LEASKEKKEE KNYAFEDISP
     EETTKESPFS NYAEVSETNS PKETRLFEDV LQNGAGPANG ATASEVFQSL GGGKGGPGLS
     VEALEKMMED PTVQKMVYPY LPEEMRNPET FKWMLKNPQY RQQLQDMLNN MSGSGEWDKR
     MTDTLKNFDL NSPEVKQQFN QIGLTPEEVI SKIMENPDVA MAFQNPRVQA ALMECSENPM
     NIMKYQNDKE VMDVFNKISQ LFPGMTG
 
 
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