TI214_IPOPU
ID TI214_IPOPU Reviewed; 2057 AA.
AC A7Y3K2;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 25-MAY-2022, entry version 31.
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 Ipomoea purpurea (Common morning glory) (Pharbitis purpurea).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Convolvulaceae; Ipomoeeae; Ipomoea.
OX NCBI_TaxID=4121;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=17956636; DOI=10.1186/1471-2229-7-57;
RA McNeal J.R., Kuehl J.V., Boore J.L., dePamphilis C.W.;
RT "Complete plastid genome sequences suggest strong selection for retention
RT of photosynthetic genes in the parasitic plant genus Cuscuta.";
RL BMC Plant Biol. 7:57-57(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; EU118126; ABV02395.1; -; Genomic_DNA.
DR EMBL; EU118126; ABV02409.1; -; Genomic_DNA.
DR RefSeq; YP_001468355.1; NC_009808.1.
DR RefSeq; YP_001468369.1; NC_009808.1.
DR AlphaFoldDB; A7Y3K2; -.
DR PRIDE; A7Y3K2; -.
DR GeneID; 5601217; -.
DR GeneID; 5601314; -.
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; 3.
DR Pfam; PF05758; Ycf1; 3.
PE 3: Inferred from homology;
KW Chloroplast; Coiled coil; Membrane; Plastid; Plastid inner membrane;
KW Protein transport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..2057
FT /note="Protein TIC 214"
FT /id="PRO_0000326577"
FT TRANSMEM 13..33
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 62..82
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 158..178
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 206..226
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 288..316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 614..807
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 890..910
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1597..1634
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1724..1817
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 248..340
FT /evidence="ECO:0000255"
FT COMPBIAS 617..705
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 718..807
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1597..1617
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1618..1634
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2057 AA; 242083 MW; 497F69CDF234F126 CRC64;
MRNQFPFRSV YYKIINSVLA AGLYYGFLSA FSIKTSHLLL LRTLVFEEEE ETKKRIVAKT
GLIMGQILLF ISIYYKPFHI ALTRPRTITA LGFFYLFFQI FWKSQKRVFA NQNSMSNLSC
IFLNHLILQQ LLNTCILPSS AARRLVSIYT FRSNNKMLFV TSSFFAWFIG QILVCEFFEL
AGKHIRIELA GKHIGKNRSI RSIIRSDYFH FFFVILFFMM SLHSFGRIPS PILLPKMSNL
SQIEKRALIL KGTDEEEEND KIDEEIEQEM EKLEQEIEEI EQQRKLANHL KKKKDRQKKQ
GTRGHSDKEF HSNSNTSYSK RKIEVLKSEI RVIQEKERKS LISPLLFDYR RWYRPFRYIQ
NNRLEQAIRN EMSQYFFDTQ QSDGKERISF TYPRSLSTFF KVIKRKINIL LEKTLSNQLD
NAWVSRNKKK MNHLKNDFFN RINHLDKEKI DGEIEQEKER EQKAVEILET RTRLCIEDDT
TKQEYYLPQM YDPFLNGPYR GKIKKELPPS IIKNTLIADS RETGEQNRLH DLLLPNSNYE
NFDQNTNTLE IGDILEIDAF SSIVIHKISK KVPRWSYKLI SELEQLSFHY SPPAEHEIRS
RRAVGEYLLF DPTETHTTTK ATDKETKPNA SKETDTVNKE TKPNASKETD TIDKETKTNA
SKETNTVDKE TKTNASKETD TVDKETKPNA SKETDTIDKE TKTNASKETN TVNKETKPNA
SKETDTVDKE TKTNASKETD TVNKETKTNA SKETDTVDKE TKPNASKETD TVNKETKTNA
SKETDTVNKE TKTKTPEEEA KEDEEKGLVL MRYAHQPDFK HGLIKGSMRT QRRKIVIEKL
FQANAHSPLF FDRIKKKKLF SFAIPRPVQL NRIFRNWSAG KGFRILESTD EQTKREEKPK
RESKKKNDRV KEKKRLEIGE TWDTFEITQM LRGCILIAQS SLRKNLILPS LIIGKNLGRM
LLLQIPEWSE DFEEWNREKH IKCTYTGNPV SETEFPENWL TQGIQIKIVY PFHLKPWHTS
KPLTSRDDVC FLTIFGRETE LPFGSPRKTP SFFEPILKEL EKKIGKYEKV TAESVLKKII
IKLFKKVSKE TRTTNQNLPF IEKDLSKGKP ILLFRSREIG GMEKEKDSRI SNQIIDESFS
QIQKIQIPDW TNSSLIETKM QDMTDRTSTI KNQIERITEE KKKVTLELDI STYKKSCRLE
LSKKIWQIVK LKNIICKFHY FRKFFIQRIY NDICLSTIHI CQTNTQLFVE STKNLIEKYI
SKNETNKKII NKKTKNTIHF ISNIKTYTYN SCKKNSEIFC DLSNLSQAYV FYKISQTGVV
NLSKLRSVLQ HHGTSFFLKT QMKDSFRTQG IFQSEVIHKK LQRSITSQWK NWLRGNYQYD
LSQIIWSSLM SQKQKWRNRV NRYCRSQKKD LKKWNSCGKY QLSHYKKKKG PNSLSNQKDN
FQKCYRYDLL SYKSINNENK GDSVFYRSIP QVTKRQAVSD NYNMSQNSLF AITGSIPINI
FIGRIERVYI PYIEKNLNRK YFNWENIYFD LRKKVAIESW VAVNPSSNQK TRIGTNNFQL
IDPIDKEEEE EINPSSNQKT PIGTNKDEIF YAIDKEEEEE INPEEEINPE EEINPEEEIN
PSSNQKTPIG TNNDQLIDPI EKQEKDPFYI PINQNPEINQ PNSPNSFFDW MGMNEQILNR
PISNLELWFF PEFVRLFNVY KTKPWIIPSK LLLLNSNLSE TDNKKKNIAE NQNLEEEDSA
KSDMKKGTKK SKTNSEKKSK TNSEKKSETD SEKKSETDSE KKSETDSEKK SETDSEKKSE
TDSEKKSETD SEKKSLSTRE LRELFMKKYF LLQLRWDQRN IGQNIRKNVR ILALPKSSIN
LETMTLSCIE RRKLQLNVMW KSKSNLSILK FFKSIGMVVD RLGLSVKNNG QFLMYQTIGI
SLVHKSKNKT NQQYRKQRII RARENNHFDA LVLENILSSR RRRELRILIC FNSNNWNDVD
TNSVFFNENG VKNCSHFWEE RNLRDKEKNE LIQFKFFLWP NYRLEDLACM NRYWFDTNNG
SRFSILRIHM YLPLKIR
