TI110_PEA
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 25-MAY-2022, entry version 65.
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; 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 38-46, SUBCELLULAR
RP LOCATION, AND TOPOLOGY.
RX PubMed=8861951; DOI=10.1002/j.1460-2075.1996.tb00797.x;
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 component of
RT the chloroplastic protein translocation apparatus, faces the stromal
RT 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 of
RT 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 import in
RT 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 regulation.";
RL Biochim. Biophys. Acta 1803:740-747(2010).
CC -!- FUNCTION: Involved in protein precursor import into chloroplasts. Forms
CC a voltage-dependent cation-selective channel at the inner envelope of
CC chloroplasts, which specifically responds to a transit peptide. Calcium
CC acts as an effector of gating and selectivity.
CC {ECO:0000269|PubMed:12874276, ECO:0000269|PubMed:18986981}.
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 {ECO:0000269|PubMed:12874276, ECO:0000269|PubMed:15180984}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast inner membrane
CC {ECO:0000305|PubMed:8861951}; Multi-pass membrane protein
CC {ECO:0000305|PubMed:8861951}.
CC -!- INDUCTION: Down-regulated by cold stress.
CC {ECO:0000269|PubMed:19403728}.
CC -!- DOMAIN: The N1 region (38-149) is sufficient for re-targeting to the
CC inner membrane and proper insertion. The N2 region (150-269) may act as
CC a start transfer signal, but it cannot direct proteins to the inner
CC envelope. {ECO:0000269|PubMed:9182662}.
CC -!- PTM: Contains at least one interchain redox-active disulfide bond.
CC -!- MISCELLANEOUS: PubMed:9632730 shows that the region 121-996 is located
CC in the stroma while PubMed:18986981 indicates that it contains probably
CC 4 trans-membrane domains resulting in 2 regions in the intermembrane
CC space localized to form supercomplexes with the TOC machinery and to
CC receive the transit peptide of pre-proteins.
CC -!- MISCELLANEOUS: Inserts into the inner envelope membrane from the stroma
CC after import from the cytoplasm.
CC -!- SIMILARITY: Belongs to the chloroplast envelope anion channel-forming
CC Tic110 (TC 1.A.18) family. {ECO:0000305}.
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DR EMBL; Z68506; CAA92823.1; -; mRNA.
DR EMBL; U56419; AAC49399.1; -; mRNA.
DR PIR; S71750; S71750.
DR AlphaFoldDB; O24303; -.
DR DIP; DIP-33729N; -.
DR IntAct; O24303; 6.
DR TCDB; 1.A.18.1.1; the chloroplast envelope anion channel-forming tic110 (tic110) family.
DR TCDB; 3.A.9.1.1; the chloroplast envelope protein translocase (cept or tic-toc) family.
DR PRIDE; O24303; -.
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; IPR031610; TIC110.
DR PANTHER; PTHR34935; PTHR34935; 1.
DR Pfam; PF16940; Tic110; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Direct protein sequencing; Disulfide bond; Membrane; Plastid;
KW Plastid inner membrane; Protein transport; Transit peptide; Transmembrane;
KW Transmembrane helix; Transport.
FT TRANSIT 1..37
FT /note="Chloroplast"
FT /evidence="ECO:0000269|PubMed:8861951"
FT CHAIN 38..996
FT /note="Protein TIC110, chloroplastic"
FT /id="PRO_0000413669"
FT TOPO_DOM 38..73
FT /note="Stromal"
FT /evidence="ECO:0000305"
FT TRANSMEM 74..92
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 93..100
FT /note="Chloroplast intermembrane"
FT /evidence="ECO:0000305"
FT TRANSMEM 101..120
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 121..244
FT /note="Stromal"
FT /evidence="ECO:0000305"
FT TRANSMEM 245..262
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 263..349
FT /note="Chloroplast intermembrane"
FT /evidence="ECO:0000305"
FT TRANSMEM 350..367
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 368..613
FT /note="Stromal"
FT /evidence="ECO:0000305"
FT TRANSMEM 614..631
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 632..702
FT /note="Chloroplast intermembrane"
FT /evidence="ECO:0000305"
FT TRANSMEM 703..719
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 720..996
FT /note="Stromal"
FT /evidence="ECO:0000305"
FT REGION 1..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 313
FT /note="C -> R (in Ref. 1; CAA92823)"
FT /evidence="ECO:0000305"
FT CONFLICT 359
FT /note="I -> L (in Ref. 1; CAA92823)"
FT /evidence="ECO:0000305"
FT CONFLICT 364
FT /note="A -> S (in Ref. 1; CAA92823)"
FT /evidence="ECO:0000305"
FT CONFLICT 416
FT /note="L -> P (in Ref. 1; CAA92823)"
FT /evidence="ECO:0000305"
FT CONFLICT 594
FT /note="K -> R (in Ref. 1; CAA92823)"
FT /evidence="ECO:0000305"
FT CONFLICT 662..688
FT /note="MRITSDTQENKTGQRACRKDGKAWSDR -> WESLQTLKKTRPDKELVEKMG
FT KPGQTE (in Ref. 1; CAA92823)"
FT /evidence="ECO:0000305"
FT CONFLICT 919
FT /note="F -> S (in Ref. 1; CAA92823)"
FT /evidence="ECO:0000305"
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
