TI214_ATRBE
ID TI214_ATRBE Reviewed; 1880 AA.
AC Q8S8U2; Q8S8V1;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 25-MAY-2022, entry version 46.
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 Atropa belladonna (Belladonna) (Deadly nightshade).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Hyoscyameae; Atropa.
OX NCBI_TaxID=33113;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Ab5p(kan);
RX PubMed=12200487; DOI=10.1093/oxfordjournals.molbev.a004222;
RA Schmitz-Linneweber C., Regel R., Du T.G., Hupfer H., Herrmann R.G.,
RA Maier R.M.;
RT "The plastid chromosome of Atropa belladonna and its comparison with that
RT of Nicotiana tabacum: the role of RNA editing in generating divergence in
RT the process of plant speciation.";
RL Mol. Biol. Evol. 19:1602-1612(2002).
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 -!- MISCELLANEOUS: There is a partial copy of the N-terminus (positions 1-
CC 489) of ycf1 in the inverted repeat (CAC88092).
CC -!- SIMILARITY: Belongs to the TIC214 family. {ECO:0000305}.
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DR EMBL; AJ316582; CAC88104.1; -; Genomic_DNA.
DR EMBL; AJ316582; CAC88092.1; -; Genomic_DNA.
DR RefSeq; NP_783278.1; NC_004561.1.
DR RefSeq; NP_783290.1; NC_004561.1.
DR AlphaFoldDB; Q8S8U2; -.
DR PRIDE; Q8S8U2; -.
DR GeneID; 1497116; -.
DR GeneID; 806466; -.
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; 1.
DR Pfam; PF05758; Ycf1; 1.
PE 3: Inferred from homology;
KW Chloroplast; Membrane; Plastid; Plastid inner membrane; Protein transport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1880
FT /note="Protein TIC 214"
FT /id="PRO_0000262601"
FT TRANSMEM 18..38
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 64..84
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 87..107
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 124..144
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 172..192
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 221..241
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 248..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1572..1622
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 266..283
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1572..1589
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1601..1622
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 480..489
FT /note="NRLEVLDKES -> IFNVNKKKI (in Ref. 1; CAC88092)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1880 AA; 223869 MW; 4CD46A1497C8B6D8 CRC64;
MIFQSFLLGN LVSLCMKIIN SVVVVGLYYG FLTTFSIGPS YLFLLRALVM EEGTEKKVSA
TAGFITGQLM MFISIYYAPL HLALGRPHTI TVLALPYLLF HFFWNNHKHF FDYGSTTRNS
MRNLSIQCVF LNNLIFQLFN HFILPSSMLA RLVNIYLFRC NNKILFVTSG FVGWLIGHIL
FMKWLGLVLV WIRQNHSIRP NKYIRSNKYL VLELRNSMAR IFSILLFITC VYYLGRIPSP
ILTKKLKEAS KTEERVESEE ERDVEIETAS EMKGTKQEQE GSTEEDPYPS PSLFSEEGWD
PDKIYETEEI RVNGKDKIKD KFHSQLTETG YNNINTSNSP IYYYEDSYLN NNNTGNPENF
KLQLLDKKNE NKDLFWFQKP LVSLLFNYNR WNRPFRYIKN NRFEQAVRTE MSQYFFDTCK
SDGKQRISFT YPPSLSTFWK MIKGRLPLLS LQKTLPNELD NQWVSTNKEK SNNLNKEFLN
RLEVLDKESL SLDILETRTR LSNDDTKKEY VPKMYDPLLN GPYRGTIKKG FSPSIINNTS
IENLKERVIL NRIHTIFLPN TDYQEFEQKV DTVDKKPLST EIDEFLTLIN EFGNEPKSSL
KVNSEKKTKF VKFLFNAIDP NGTKSVKKSI GIKEISKKIP RWSHKLITEL EQQLGEFKEG
VSLDHQIRSR KARRVVIFTT NMDSDDPEVK EEVALISYSQ QSDFRRGIIK GSMRAQRRKT
VIWKLFQANV HSPFFLDRIT PPRLFSFDIS ELIKPIFRNW AGKEGEFEII EFREEQPKRE
EKKETDKKGE TKSKKEKARI AIAEAWDSIL FAQIIRGSML ITQSILRKYI LLPSLIIAKN
LGRMLFLQLP EWSEDLEEWN REMHIKCTYN GVQLSETEFP KNWLRDGIQI KILFPFCLKP
WHISKLYPSH EELMKKKKQK DDFCFLTVWG MEAELPFGSP RSRPSFFEPI FKELEKKNGK
LKKKYFITLK VLKGKTKLFR RISKETKKWL IKSILFLKKI RKELSKIKLI VLFRFKEISE
SNETKKEKDS LISNQIINES FSQIESVNWP NSSLIETKMK DLTDRTSTIK NQIERITKEK
KKVTPEIDIS RNKTNNIKKF ESTKNIFQIL QRRNTRLIWK FHYFIKLFIQ RLYINLFLSI
INIPRINTQL FLESTNKLID KYISNNEINQ EKINNKKKIH FISTLKKSLY NISNKNSHIF
FDLSYLSQAY VFYKLSQTQV INLSKFRSVL QYNRTSFFLK TKIKDYFRTL GIFHSELKHK
KLQSYRINQW KNWLRRHYQY DLSQIRWSRL MPQKWRNRVN QSCMAQNKNI NLNKWNSYEN
DQLIHYKKEN DSELYSLSNQ EDNFQKCYRY DLLSYKSINY KNKSDSFISR LPFQVNKNLE
ISYNSNTSKH NFFDMPGNLY INNYLRKGNI LYIERNLDRK YFDWKIIHFS LRQKGDIEAW
VKIDTNSNPN TKFGINNYQI IEKIDKKGLF YLTIHQNPEN TQKNSKKVFF DWMGMNEKIF
NRPIFNLEFW FFPEFVLLYN VYKIKPWIIP SKLLLLNLNT NENVSQNKNI NKNQKQNFFL
PSNKKIKNRI QEAKEPANQG ERERGSDIEN KVNPGPVLSK HQNDLEKDYA ESDTKKSKKK
KQYKSNTEAE LDLFLKRYLL FQLKWNDDLN QRMIENIKVY CLLLRLINPT KISISSVQRG
EMSLDIMLIQ GNLTLTELMK KGILIIEPIR LSVKNNGQFI MYQTIGISLV HKSKHQTNQR
YRDQRYVDKK NFDESILQPQ TQRINTDKNH FDLLVPENIL WSRRRRELRI RSFFNSLNWN
GVDRNSVFCN ETNVKNWSQF LDERKPLYKE KNELIKLKFF LWPNYRLEDL ACMNRYWFDN
NNGSRFSILR IHMYPRLKIN
