ID H2F5U0_9ASPA Unreviewed; 1903 AA.
AC H2F5U0;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Protein TIC 214 {ECO:0000256|RuleBase:RU364085};
DE AltName: Full=Translocon at the inner envelope membrane of chloroplasts 214 {ECO:0000256|RuleBase:RU364085};
GN Name=ycf1 {ECO:0000313|EMBL:AEX94023.1};
GN Synonyms=TIC214 {ECO:0000256|RuleBase:RU364085};
OS Cordyline australis.
OG Plastid; Chloroplast {ECO:0000313|EMBL:AEX94023.1}.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Asparagales; Asparagaceae;
OC Lomandroideae; Cordyline.
OX NCBI_TaxID=1016831 {ECO:0000313|EMBL:AEX94023.1};
RN [1] {ECO:0000313|EMBL:AEX94023.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=22291168; DOI=10.3732/ajb.1100491;
RA Steele P.R., Hertweck K.L., Mayfield D., McKain M.R., Leebens-Mack J.,
RA Pires J.C.;
RT "Quality and quantity of data recovered from massively parallel sequencing:
RT Examples in Asparagales and Poaceae.";
RL Am. J. Bot. 99:330-348(2012).
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:0000256|RuleBase:RU364085}.
CC -!- SUBUNIT: Part of the Tic complex. {ECO:0000256|RuleBase:RU364085}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast inner membrane
CC {ECO:0000256|RuleBase:RU364085}.
CC -!- SIMILARITY: Belongs to the TIC214 family.
CC {ECO:0000256|ARBA:ARBA00009956, ECO:0000256|RuleBase:RU364085}.
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DR EMBL; JQ274115; AEX94023.1; -; Genomic_DNA.
DR GO; GO:0009706; C:chloroplast inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR008896; TIC214.
DR PANTHER; PTHR33163:SF40; PROTEIN TIC 214; 1.
DR PANTHER; PTHR33163; PROTEIN TIC 214-RELATED; 1.
DR Pfam; PF05758; Ycf1; 2.
PE 3: Inferred from homology;
KW Chloroplast {ECO:0000256|RuleBase:RU364085, ECO:0000313|EMBL:AEX94023.1};
KW Membrane {ECO:0000256|RuleBase:RU364085};
KW Plastid {ECO:0000256|RuleBase:RU364085, ECO:0000313|EMBL:AEX94023.1};
KW Plastid inner membrane {ECO:0000256|RuleBase:RU364085};
KW Protein transport {ECO:0000256|RuleBase:RU364085};
KW Transmembrane {ECO:0000256|RuleBase:RU364085};
KW Transmembrane helix {ECO:0000256|RuleBase:RU364085};
KW Transport {ECO:0000256|RuleBase:RU364085}.
FT TRANSMEM 57..79
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU364085"
FT TRANSMEM 86..103
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU364085"
FT TRANSMEM 123..143
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU364085"
FT TRANSMEM 164..190
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU364085"
FT TRANSMEM 240..257
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU364085"
FT REGION 274..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 648..669
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 683..726
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1592..1627
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..303
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 316..338
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 684..716
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1903 AA; 226856 MW; 49D15DB405A5BEBD CRC64;
MILKSFLLGN LCMKIINSVV VVGLYYGFLT TSIFSKGFSY LFLFRAWVME EGTEKEVSAT
TGFITGQLMM FISIYYAPLH LALSRPYTIT FLFLPYLLFH FFWNNCKNDF DYGSTTRNSM
RNLSIQCVFL NNLIFQLFNY FILPSSTLVR LINIYMFRCN NKMLFVTSSF VGWLIGHILF
MKWVEFIFYW TREKRSTRSK KYFVLNLRNS WAGSVLLWIQ EKQKRSIRYP CLVLELRDSM
ARSFSILFFL ACVYYLGRMP SPIFTRKMKE KESDVDTIEE TTEETTEETR KEQEGSTEED
KDSSVYEDSY DVETTEETTE ETRKEQEGST EEDKDSSVYE DSYLDTHQEN WKLEKLNLNK
NKEEKNKKIY FRFEKPLVTF LFDPKRWNRP GRPIRNDDVE NPMAPPIRNP MSQYFFYICP
SDGKQKISFT YPPSLSTFSE MIERKISLYT TEKLSHKDLY NYWVYTNDQK KDNLNNELIS
RIKILEKGKL ALDMLEKRTR LCHDEDNQEY LPKRYDPFLN GPYRGTIKKF DNDLITSTAD
SVEMFWINRI HGLFHNDSRE LEHQKNTFGF GEELLLNSNS IGNSLTSTDE LSFERAGRSE
SQRKSLKFVS DVITTDPNDL TTIRKKSIGM KEIRKKIPRW SYKLVEDLDK DEKDDEVEEE
STEDFESDVR TRVGKRELIY TFSDEDKNTN SSASKNNTST SDEDKNTNSS ASKNNTSTSD
EEEHEEQVIL IRFPEQPDFD RDLIKGSMRA QRRKTGIGGL FQAYVHSPLF FGRADNRFFF
SFFFDTISDN ISEMINLFFR NRVEETLDLE EELKISYSKD EERRQKEKKE REKKEHFKEI
DKESYENERM EIAEMWETFM FTQTARSLML VTHSLLRKYV ILPLLIIAKN CARMLLFQSP
EWAEDWKEWN KEMHVKCTYN GVQLSETEFP QNWLLDGIQI KILFPFRLKP WRRSKSHDRN
PDIDEKPEQS FCFLTVFGME TEVPFGLPRK PPSFFEPIFE ELKKKMRKQK KLFSQVRRVF
KKKRKWFLKV SKEKTRWVIK KVLVINLIMK ELEKVNPIFL LKPRKVKKAN KKGKDSNIKN
KIIRESTIRI RSTNCVNENY SLIETKMKDL ANRTITIRTQ IERITKDKKK IVQTCDDKRS
ESQKDIWQIF KRKNIRLIRK SHYFMKSFIE KKYMDILLYI TKIPRIDAQL FFESTKKIIR
KFVYNDETNQ EGIEKINQNT MNFISTINKR VSDTRYFINK INLSIYCDLS SLSQAYVFYK
LSQDQLLNKY RLRSVLQHHG TYPFLRDIIK NYCTTRGIFD SKPRHKKIHK SGMNKWKSWL
RGYYQSNLSQ TKWSRLVPKK WRNRVNRCST IQKKGPKKLD LSKKEREQFV DYIKQNYYVG
NSLRNPKRKL QKQYLYDLLS YKYINYGNSK DSYIYGSTRI SDYLSDTDKN TDRKFFDCRI
LGFCLRNDID IETWINIETW INTHIYTKIH KNAKTEIINS PKFEEEEKDL FSFTIHHKIN
PSNQKRSFFD WMGMNQERLY HTIPKSKSNL ELWFFPELVL LFDAYKIKPW IIPIKLLIFD
FHFYKNISQS EKIDVNQKKN IPILANQKEH LELKNSNKKK NEQQGQGDLV SDLRKQKKKK
KGVKKDYTEA DIKKGRKKKQ SKTALEVELD FLLNSYPVCQ LKFSEYMSQG MLSNIRVCCL
ILRLIDPWEI ALSSIRRDEM HLDLIWEMEK NPTAVELIKT GVLTIEPIHL SMKKDGKSII
YQTIGISLVD KNKHQTNGKC IKKNRYVDKN HYDFLVPENI LSPRRRRELR ILICLNSQNW
NVVDRNPIFC NKNCGQFLNG EKHLNTDANK FIKFKSFLWP NYRLEDLACM NRYWFDTNNG
SNFSMSRIRM YPRLRISYSE LVTELVNNGF SISLLDDILD MDR
//
