TIC40_PEA
ID TIC40_PEA Reviewed; 436 AA.
AC Q8GT66; Q9SC41;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 40.
DE RecName: Full=Protein TIC 40, chloroplastic;
DE AltName: Full=Translocon at the inner envelope membrane of chloroplasts 40;
DE Short=PsTIC40;
DE Flags: Precursor;
GN Name=TIC40;
OS Pisum sativum (Garden pea).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX NCBI_TaxID=3888;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 73-98, FUNCTION,
RP SUBCELLULAR LOCATION, AND INTERACTION WITH TIC110.
RC STRAIN=cv. Golf; TISSUE=Leaf;
RX PubMed=10601321; DOI=10.1074/jbc.274.52.37467;
RA Stahl T., Glockmann C., Soll J., Heins L.;
RT "Tic40, a new 'old' subunit of the chloroplast protein import translocon.";
RL J. Biol. Chem. 274:37467-37472(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TOPOLOGY, AND INTERACTION
RP WITH HSP93; TIC110 AND TOC75.
RC STRAIN=cv. Little Marvel;
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 [3]
RP INTERACTION WITH TIC62.
RX PubMed=12426385; DOI=10.1093/emboj/cdf621;
RA Kuechler M., Decker S., Hoermann F., Soll J., Heins L.;
RT "Protein import into chloroplasts involves redox-regulated proteins.";
RL EMBO J. 21:6136-6145(2002).
RN [4]
RP FUNCTION, AND INTERACTION WITH TIC110 AND HSP93.
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 [5]
RP INDUCTION BY COLD.
RX PubMed=19403728; DOI=10.1104/pp.109.137265;
RA Dutta S., Mohanty S., Tripathy B.C.;
RT "Role of temperature stress on chloroplast biogenesis and protein import in
RT pea.";
RL Plant Physiol. 150:1050-1061(2009).
RN [6]
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:10601321, ECO:0000269|PubMed:17158958}.
CC -!- SUBUNIT: Part of the Tic complex. Interacts with HSP93, TIC110, TIC62
CC and TOC75. {ECO:0000269|PubMed:10601321, ECO:0000269|PubMed:12426385,
CC ECO:0000269|PubMed:12805212, ECO:0000269|PubMed:17158958}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast inner membrane
CC {ECO:0000269|PubMed:10601321, ECO:0000269|PubMed:12805212}; Single-pass
CC membrane protein {ECO:0000269|PubMed:10601321,
CC ECO:0000269|PubMed:12805212}.
CC -!- INDUCTION: Down-regulated by cold stress.
CC {ECO:0000269|PubMed:19403728}.
CC -!- DOMAIN: The STI1 2 domain (373-412) has a stimulatory effect on HSP93
CC ATP hydrolysis.
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; AJ243758; CAB50925.1; -; mRNA.
DR EMBL; AY157668; AAN75219.1; -; mRNA.
DR AlphaFoldDB; Q8GT66; -.
DR SMR; Q8GT66; -.
DR IntAct; Q8GT66; 2.
DR TCDB; 3.A.9.1.1; the chloroplast envelope protein translocase (cept or tic-toc) family.
DR PRIDE; Q8GT66; -.
DR GO; GO:0009706; C:chloroplast inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
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 Chloroplast; Direct protein sequencing; Membrane; Plastid;
KW Plastid inner membrane; Protein transport; Repeat; Transit peptide;
KW Transmembrane; Transmembrane helix; Transport.
FT TRANSIT 1..39
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT TRANSIT 40..72
FT /note="Chloroplast; inner membrane"
FT /evidence="ECO:0000255"
FT CHAIN 73..436
FT /note="Protein TIC 40, chloroplastic"
FT /id="PRO_0000413674"
FT TOPO_DOM 73..98
FT /note="Chloroplast intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 99..119
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 120..436
FT /note="Stromal"
FT /evidence="ECO:0000255"
FT DOMAIN 297..331
FT /note="STI1 1"
FT DOMAIN 373..412
FT /note="STI1 2"
FT REGION 74..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 160..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 245..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..88
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..191
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..284
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 28
FT /note="G -> R (in Ref. 1; CAB50925)"
FT /evidence="ECO:0000305"
FT CONFLICT 70
FT /note="D -> S (in Ref. 1; CAB50925)"
FT /evidence="ECO:0000305"
FT CONFLICT 277
FT /note="S -> G (in Ref. 1; CAB50925)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 436 AA; 47172 MW; B9C18DE99BC93EC7 CRC64;
MENLNLALVS SPKPLLLGHS SSKNVFSGRK SFTFGTFRVS ANSSSSHVTR AASKSHQNLK
SVQGKVNAHD FASISSSNGQ ETTSVGVSPQ LSPPPPSTVG SPLFWIGIGV GFSALFSVVA
SRVKKYAMQQ AFKSMMGQMN TQNNPFDSGA FSSGPPFPFP MPSASGPATP AGFAGNQSQA
TSTRSASQST VTVDIPATKV EAAAPAPDIN VKEEVEVKNE PKKSAFVDVS PEETVQKNAF
ERFKDVDESS SFKEARAPAE ASQNGTPFKQ GFGDSPSSPS ERKSALSVDA LEKMMEDPTV
QQMVYPYLPE EMRNPSTFKW MMQNPEYRQQ LEAMLNNMGG GTEWDSRMMD TLKNFDLNSP
DVKQQFDQIG LSPQEVISKI MANPDVAMAF QNPRVQAAIM DCSQNPMSIV KYQNDKEVMD
VFNKISELFP GVSGPP
