ID   TI110_PEA               Reviewed;         996 AA.
AC   O24303; O24293;
DT   19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   16-APR-2014, entry version 46.
DE   RecName: Full=Protein TIC110, chloroplastic;
DE   AltName: Full=Chloroplast inner envelope protein, 110 kDa;
DE            Short=psIEP110;
DE   AltName: Full=IAP100;
DE   AltName: Full=Translocon at the inner envelope membrane of chloroplasts 110;
DE   Flags: Precursor;
GN   Name=TIC110; Synonyms=IEP110;
OS   Pisum sativum (Garden pea).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; fabids; Fabales; Fabaceae; Papilionoideae;
OC   Fabeae; Pisum.
OX   NCBI_TaxID=3888;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 38-46, SUBCELLULAR
RP   LOCATION, AND TOPOLOGY.
RX   PubMed=8861951;
RA   Luebeck J., Soll J., Akita M., Nielsen E., Keegstra K.;
RT   "Topology of IEP110, a component of the chloroplastic protein import
RT   machinery present in the inner envelope membrane.";
RL   EMBO J. 15:4230-4238(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8755536; DOI=10.1073/pnas.93.15.7684;
RA   Kessler F., Blobel G.;
RT   "Interaction of the protein import and folding machineries of the
RT   chloroplast.";
RL   Proc. Natl. Acad. Sci. U.S.A. 93:7684-7689(1996).
RN   [3]
RP   DOMAIN.
RX   PubMed=9182662; DOI=10.1083/jcb.137.6.1279;
RA   Luebeck J., Heins L., Soll J.;
RT   "A nuclear-coded chloroplastic inner envelope membrane protein uses a
RT   soluble sorting intermediate upon import into the organelle.";
RL   J. Cell Biol. 137:1279-1286(1997).
RN   [4]
RP   TOPOLOGY.
RX   PubMed=9632730; DOI=10.1074/jbc.273.26.16583;
RA   Jackson D.T., Froehlich J.E., Keegstra K.;
RT   "The hydrophilic domain of Tic110, an inner envelope membrane
RT   component of the chloroplastic protein translocation apparatus, faces
RT   the stromal compartment.";
RL   J. Biol. Chem. 273:16583-16588(1998).
RN   [5]
RP   FUNCTION, AND INTERACTION WITH HHSP93; CPN60; TOC75 AND TOC159.
RX   PubMed=12874276; DOI=10.1074/jbc.M306367200;
RA   Inaba T., Li M., Alvarez-Huerta M., Kessler F., Schnell D.J.;
RT   "atTic110 functions as a scaffold for coordinating the stromal events
RT   of protein import into chloroplasts.";
RL   J. Biol. Chem. 278:38617-38627(2003).
RN   [6]
RP   INTERACTION WITH TIC32.
RX   PubMed=15180984; DOI=10.1074/jbc.M402817200;
RA   Hoermann F., Kuechler M., Sveshnikov D., Oppermann U., Li Y., Soll J.;
RT   "Tic32, an essential component in chloroplast biogenesis.";
RL   J. Biol. Chem. 279:34756-34762(2004).
RN   [7]
RP   FUNCTION, AND TOPOLOGY.
RX   PubMed=18986981; DOI=10.1074/jbc.M807134200;
RA   Balsera M., Goetze T.A., Kovacs-Bogdan E., Schuermann P., Wagner R.,
RA   Buchanan B.B., Soll J., Boelter B.;
RT   "Characterization of Tic110, a channel-forming protein at the inner
RT   envelope membrane of chloroplasts, unveils a response to Ca(2+) and a
RT   stromal regulatory disulfide bridge.";
RL   J. Biol. Chem. 284:2603-2616(2009).
RN   [8]
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
RT   import in pea.";
RL   Plant Physiol. 150:1050-1061(2009).
RN   [9]
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
RT   regulation.";
RL   Biochim. Biophys. Acta 1803:740-747(2010).
CC   -!- FUNCTION: Involved in protein precursor import into chloroplasts.
CC       Forms a voltage-dependent cation-selective channel at the inner
CC       envelope of chloroplasts, which specifically responds to a transit
CC       peptide. Calcium acts as an effector of gating and selectivity.
CC   -!- SUBUNIT: Part of the Tic complex. Interacts with TIC32, HSP93 and
CC       CPN60. Interacts with the Toc complex components TOC75 and TOC159.
CC       Binds specifically chloroplast pre-proteins.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast inner membrane; Multi-
CC       pass membrane protein (Probable).
CC   -!- INDUCTION: Down-regulated by cold stress.
CC   -!- DOMAIN: The N1 region (38-149) is sufficient for re-targeting to
CC       the inner membrane and proper insertion. The N2 region (150-269)
CC       may act as a start transfer signal, but it cannot direct proteins
CC       to the inner envelope.
CC   -!- PTM: Contains at least one interchain redox-active disulfide bond.
CC   -!- MISCELLANEOUS: PubMed:9632730 shows that the region 121-996 is
CC       located in the stroma while PubMed:18986981 indicates that it
CC       contains probably 4 trans-membrane domains resulting in 2 regions
CC       in the intermembrane space localized to form supercomplexes with
CC       the TOC machinery and to receive the transit peptide of pre-
CC       proteins.
CC   -!- MISCELLANEOUS: Inserts into the inner envelope membrane from the
CC       stroma after import from the cytoplasm.
CC   -!- SIMILARITY: Belongs to the chloroplast envelope anion channel-
CC       forming Tic110 (TC 1.A.18) family.
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DR   EMBL; Z68506; CAA92823.1; -; mRNA.
DR   EMBL; U56419; AAC49399.1; -; mRNA.
DR   PIR; S71750; S71750.
DR   IntAct; O24303; 4.
DR   TCDB; 1.A.18.1.1; the chloroplast envelope anion channel-forming tic110 (tic110) family.
DR   TCDB; 1.A.9.1.1; the neurotransmitter receptor, cys loop, ligand-gated ion channel (lic) family.
DR   TCDB; 3.A.9.1.1; the chloroplast envelope protein translocase (cept or tic-toc) family.
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.
PE   1: Evidence at protein level;
KW   Chloroplast; Direct protein sequencing; Disulfide bond; Membrane;
KW   Plastid; Plastid inner membrane; Protein transport; Transit peptide;
KW   Transmembrane; Transmembrane helix; Transport.
FT   TRANSIT       1     37       Chloroplast.
FT   CHAIN        38    996       Protein TIC110, chloroplastic.
FT                                /FTId=PRO_0000413669.
FT   TOPO_DOM     38     73       Stromal (Probable).
FT   TRANSMEM     74     92       Helical; (Probable).
FT   TOPO_DOM     93    100       Chloroplast intermembrane (Probable).
FT   TRANSMEM    101    120       Helical; (Probable).
FT   TOPO_DOM    121    244       Stromal (Probable).
FT   TRANSMEM    245    262       Helical; (Probable).
FT   TOPO_DOM    263    349       Chloroplast intermembrane (Probable).
FT   TRANSMEM    350    367       Helical; (Probable).
FT   TOPO_DOM    368    613       Stromal (Probable).
FT   TRANSMEM    614    631       Helical; (Probable).
FT   TOPO_DOM    632    702       Chloroplast intermembrane (Probable).
FT   TRANSMEM    703    719       Helical; (Probable).
FT   TOPO_DOM    720    996       Stromal (Probable).
FT   COMPBIAS     46     49       Poly-Ser.
FT   COMPBIAS     72    129       Ala-rich.
FT   COMPBIAS    726    729       Poly-Lys.
FT   CONFLICT    313    313       C -> R (in Ref. 1; CAA92823).
FT   CONFLICT    359    359       I -> L (in Ref. 1; CAA92823).
FT   CONFLICT    364    364       A -> S (in Ref. 1; CAA92823).
FT   CONFLICT    416    416       L -> P (in Ref. 1; CAA92823).
FT   CONFLICT    594    594       K -> R (in Ref. 1; CAA92823).
FT   CONFLICT    662    688       MRITSDTQENKTGQRACRKDGKAWSDR -> WESLQTLKKT
FT                                RPDKELVEKMGKPGQTE (in Ref. 1; CAA92823).
FT   CONFLICT    919    919       F -> S (in Ref. 1; CAA92823).
SQ   SEQUENCE   996 AA;  109982 MW;  E36649FF7A0C2680 CRC64;
     MNPSTLKPSH THPSLLLPAP SPLRTQRRRF RVSLPRCSSD TNNPASSSSP PQRPPKELNG
     IEILVDKLSS PARLATSAVI VAGAVAAGYG LGSRFGGSRN AALGGAVALG AAGGAAAYAL
     NAAAPQVAAV NLHNYVAGFD DPSILTREDI EVIANKYGVS KQDEAFKAEI CDIYSEFVSS
     VIPPGGEELK GDEVDKIVNF KSSLGLDDPD AAAVHMEIGR KLFRQRLEVG DREGGVEQRR
     AFQKLIYVSN IVFGDASSFL LPWKRVFKVT ESQVEVAIRD NAQRLYASKL KSVGRDFDLG
     KLVTLKETQS LCCLSDELAE NLFREHARKL VEENISVALG ILKSRTRAVP GVSQVVEEIE
     KVLAFNDLLI SFKNHSDIDR LARGVGPVSL VGGEYDADRK IEDLKLLYRA YVSDALSSGR
     MEDNKFAALN QLKNIFGLGK REAEAILLDI TRKVYRKRLG QTVSSGELEM ADSKAAFLQN
     LCDELHFDPQ KASELHEEIY RQKLQQCVAD GELTDENVAA LLKLRVMLCV PQQTVEAAHA
     EICGNLFEKI VKDAIASGVD GYDDETKKSV RKAAHGLRLT KETALSIASK AVRKMFITYV
     KRSRSAKGNG ESAKELKKLI AFNTLVVTKL VEDIKGESPD VKIEEPKIEE PEEIRESEEY
     EMRITSDTQE NKTGQRACRK DGKAWSDRIT LKDDLPEKDR ADLYKTFLTY CLTGDVVRIP
     FGVEIKKKKD DTEYIYLNQL GGILGLTGKV IMDVHRGLAE QAFRKQAEVL LADGQLTKAR
     VEQLGKMQKE IGLSQEYAQK IIKNITTTKM AAAIETAVTQ GKLNMKQIRE LKESNVDLDS
     MVSVSLRETI FKKTVGDIFS SGTGEFDEEE VYEKIPLDLN INKEKARGVV CELAQNRLSN
     SLIQAVALLR QRNHKGVVFS LNNLLACDKA VPSQTLSWEV SEELSDLYTI YLKSDPSPEK
     LSRLQYLLGI NDSTAAALRD SEDSLLETAE EEKFVF
//