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 14-DEC-2022, entry version 67. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 GO; GO:0009706; C:chloroplast inner membrane; IEA:UniProtKB-SubCell. DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW. DR InterPro; IPR031610; TIC110. DR PANTHER; PTHR34935; PROTEIN TIC110, CHLOROPLASTIC; 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 //