TI214_JASNU
ID TI214_JASNU Reviewed; 1933 AA.
AC Q06R72;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 25-MAY-2022, entry version 35.
DE RecName: Full=Protein TIC 214 {ECO:0000250|UniProtKB:P56785};
DE AltName: Full=Translocon at the inner envelope membrane of chloroplasts 214 {ECO:0000250|UniProtKB:P56785};
DE Short=AtTIC214 {ECO:0000250|UniProtKB:P56785};
GN Name=TIC214 {ECO:0000250|UniProtKB:P56785}; Synonyms=ycf1-A;
GN and
GN Name=TIC214 {ECO:0000250|UniProtKB:P56785}; Synonyms=ycf1-B;
OS Jasminum nudiflorum (Winter jasmine).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Oleaceae; Jasmineae; Jasminum.
OX NCBI_TaxID=126431;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=17329229; DOI=10.1093/molbev/msm036;
RA Lee H.-L., Jansen R.K., Chumley T.W., Kim K.-J.;
RT "Gene relocations within chloroplast genomes of Jasminum and Menodora
RT (Oleaceae) are due to multiple, overlapping inversions.";
RL Mol. Biol. Evol. 24:1161-1180(2007).
CC -!- FUNCTION: Involved in protein precursor import into chloroplasts. May
CC be part of an intermediate translocation complex acting as a protein-
CC conducting channel at the inner envelope.
CC {ECO:0000250|UniProtKB:P56785}.
CC -!- SUBUNIT: Part of the Tic complex. {ECO:0000250|UniProtKB:P56785}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast inner membrane
CC {ECO:0000250|UniProtKB:P56785}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the TIC214 family. {ECO:0000305}.
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DR EMBL; DQ673255; ABG74675.1; -; Genomic_DNA.
DR EMBL; DQ673255; ABG74687.1; -; Genomic_DNA.
DR RefSeq; YP_778537.1; NC_008407.1.
DR RefSeq; YP_778549.1; NC_008407.1.
DR AlphaFoldDB; Q06R72; -.
DR PRIDE; Q06R72; -.
DR GeneID; 4319827; -.
DR GeneID; 4319840; -.
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; IPR008896; TIC214.
DR PANTHER; PTHR33163; PTHR33163; 2.
DR Pfam; PF05758; Ycf1; 3.
PE 3: Inferred from homology;
KW Chloroplast; Membrane; Plastid; Plastid inner membrane; Protein transport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1933
FT /note="Protein TIC 214"
FT /id="PRO_0000262612"
FT TRANSMEM 18..38
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 60..80
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 87..107
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 128..148
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 176..196
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 230..250
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1135..1155
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 266..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 473..514
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 808..832
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1066..1121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1562..1642
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..291
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1066..1080
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1081..1103
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1104..1121
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1933 AA; 230211 MW; A67E3894B3524076 CRC64;
MLFHFFLRCN LASLCIKIVN SVVVVGLYYG LLTTFSIGPS YFFLLRAQVM EEGTEKKVSA
TTGFITGQLI MFISIYYAPL HRALARPHTI TVLALPYLFV YFIFYTDKRF MHPRKNAMLN
TTTSMRNFSI QCVFLNNLIF QLFNHFILPS SMVARLVNIY MFRCNNKMLF VTSSFVGWLI
GHILFWKWLG LVLVWIRQNR SIRIRPNKYI PFYKLIRLDK YLVSKWGDRI FYILVILIWF
YLGGKIPAPL LSMKFDESTI QLEKGAKGKK KKRGKGEEEG DVEKEDEVGV GEKKGEIDES
EEIRVNGELF KSLVAHFFVF DPNHFATLLF DPNRWNRPFR YIKNDRFDNA FRTEMSQYFF
DTCPSAGKER ISFTYPPSLS TFWEMIERRI SLPTLDKFSS NELSNHWVYT NEQKSNNLKN
EFVNRIEALD KESVSLNRLE TTSRLCNDNT TKEYLPEPYD PFLNGPYRRT IKKTKSLSPE
KTSGDNLETS RDNLETSRDN LETSRDNLET SRDNLETSRD NLIDKIGINR IHSILLPDIP
DTDYQKLEDQ FDKKQLSIEI VDLFTFAFIS EFGKKKGPKS ESNLISRDLL ISRDLSVFSD
EKEVRIEDGK GVIIDDEKGK KYFEYLENRI GTNTDDENID KDSIAKIRKK VSRWIYNATS
ELDQAYGEDE RKDPMDNEIR SRDAKRVIVV PKEKLERDDD DDEEEPTDID KIIFPEHGDF
RRDVIWGSIR AQRRKIVIWR TLQRYTHSPL FLDSLKDFRH YFVDFLLDIL NIFEPIWRII
RNLRIFLIKL IRKRFALKIL EHREEQQTHR EEKKKRKKDE KNEKNAKNAE DPEREPRLWV
SEFWTIIEYA QEVRGCVLLT HSFIRRNIVI PLLIIVKNIG RMLLFQRPEL YEDFEDWQRE
SHVKCTYEGI PLSETDFPED WLVEGIQIKI LYPFRLKPWH VPGSDSDQNR KKAEEKGDFC
FLTVYGTETN LPFGYSRLPP PTFESFFKPI FQELKKQMRN SKKNIWKLGK MLFQKVKGTK
FLRKVAKKWV RKSIILGKKI IEGLKKIKEL VKKERDPITS NQMIPESFTQ ISSPSSTNSE
KKRNKMQDLT NRANKARNEI ERIRKEKKKK KRSLKKTSSN AKRLQRIKDR LIRKLPVYLK
LFIQRIYTGI FFSIINIRRM SQKFRNKFIP DQERKDILPF IYTINKIKES LYTNNSEENS
HIFYDLSYLS QAYVFYKLSE IQLSNLDKFK SVLQYQGIPF FLRSEIKDSF KTQGIVHSKR
LPSSEMNQWK NWLRGHSQYD LSKTRWSILI PQRWRNRVHR MVKRKNFNKR NLYEKYEKDQ
FIDSKKENIC EVSNRNQKDD NFQKCCKYDL LSYKSIHSEN KKDSRSLFDK LSFNSNTAFF
DLLVDRARGM PIDINNLTGT GDIPYTEKTP DRKYLDWKMI HFDFIRNQLD IENWITIDVN
RKDNRNQKTP IYTNNYLTND HDTNFEIIYK IDKKTKKPIL DLDFLRIPEK NPSNSSKGFL
DWMGLNETQT HPVVLNKFNR LKMEANLFPE IVLFYNAYKT QPWLLSSKLL LLNLNNNENE
INADNEKNEK KEAKKEAKKE AKKEAKKEEK QNIKKELTTK GDLENKGDLE SVPSKEKNPS
KDSKEKKDIQ KDSAESTTKK VTSKELQKEL DAFLQRYSGY LVKWNRRVDP DIVPKSEINW
EVYSYLYRLF DDENPRNRKE IDPTHLVLSS AKRGELAFEI LATRPIQSWK KLLLKRKELV
FFEPIRLFGK NNGQFIMYQT IGISLVHNNK HEIQPRFRKK KKRYGSKTNF DESIPPHERI
TRNDERIPTN DEDEKRNKRL RINYERNADK NHLDLLVPEN IFSFRRRRKL RILNCLNSKN
RNDVDRNPVF CNEKNSSQDL DREKNLLMKL KFFLWPNYRL EDLACMNRYW FDTNNGSRFS
MLRIRLYPRL KIR