ID E3W0G5_THECC Unreviewed; 1887 AA.
AC E3W0G5;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 2.
DT 22-FEB-2023, entry version 32.
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:ADO64947.2};
GN Synonyms=TIC214 {ECO:0000256|RuleBase:RU364085};
OS Theobroma cacao (Cacao) (Cocoa).
OG Plastid; Chloroplast {ECO:0000313|EMBL:ADO64947.2}.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Byttnerioideae; Theobroma.
OX NCBI_TaxID=3641 {ECO:0000313|EMBL:ADO64947.2};
RN [1] {ECO:0000313|EMBL:ADO64947.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20935065; DOI=10.1093/molbev/msq261;
RA Jansen R.K., Saski C., Lee S.B., Hansen A.K., Daniell H.;
RT "Complete plastid genome sequences of three Rosids (Castanea, Prunus,
RT Theobroma): evidence for at least two independent transfers of rpl22 to the
RT nucleus.";
RL Mol. Biol. Evol. 28:835-847(2011).
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: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Plastid,
CC chloroplast inner membrane {ECO:0000256|RuleBase:RU364085}.
CC -!- SIMILARITY: Belongs to the TIC214 family.
CC {ECO:0000256|RuleBase:RU364085}.
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DR EMBL; HQ336404; ADO64947.2; -; 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; 1.
PE 3: Inferred from homology;
KW Chloroplast {ECO:0000256|RuleBase:RU364085, ECO:0000313|EMBL:ADO64947.2};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU364085};
KW Plastid {ECO:0000256|RuleBase:RU364085, ECO:0000313|EMBL:ADO64947.2};
KW Plastid inner membrane {ECO:0000256|RuleBase:RU364085};
KW Protein transport {ECO:0000256|RuleBase:RU364085};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU364085};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU364085}; Transport {ECO:0000256|RuleBase:RU364085}.
FT TRANSMEM 21..43
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU364085"
FT TRANSMEM 63..83
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU364085"
FT TRANSMEM 90..107
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU364085"
FT TRANSMEM 127..147
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU364085"
FT TRANSMEM 168..195
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU364085"
FT TRANSMEM 220..238
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU364085"
FT REGION 251..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1579..1601
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1611..1630
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..272
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1887 AA; 224672 MW; E311036F91234B6E CRC64;
MIFKSFIPGN LISLCMKIIN SVVVVGLYYG FLTTFSIGPS YLFLLRARVM EEGEEGTEKK
VSATTGFIAG QLMMFISIYY APLHLALGRP HTITVLALPY LLFHFFWNNH KDFFDYGSTT
RNSMRNLSIQ CVFLNNLIFQ LFNHFILPSS MLARLVNIYM FRCNNKMLFV TSSFVGWLIG
HFLFMKWVGL VLVWIQQNNF IRSNVLIRSN KYLVSEFRNS MTRIFSILLF ITCVYYLGRI
PSPILTKKLK GTSETEEKRE SEEERDIETI SEGGGYKQEQ EVSTEEDPSS SLFSEEGWDP
NKIDETEEIR VNGKKKKKTK GDPRFRFKET YYKNSPVYET SYLDGHQENS KLEILKKKED
KYLLWFEKPL VTLLFDYKRW NRPFRYIKND RFENAIKKEM SQYFFYTCQS DGKEKISFTY
PPSLATFGEM IQKKISFLTP ENLFSDELYT DWSFTNELKR RNLSKEFINR VESLDKESFD
LGILEKRTRF SNNESKKEYL PKIYDPFLNG PYRGRIQKLF SPSSINQTSK KKNTDPFWIN
KIHALLLTTD YHEFEQTIDT LNIKSLSTEK DLSLLPEDEQ GNIDSEDRVK ILKFLFNIVI
TNPNNQTIRK KSIGIKEISK KVPRRSYKLI DDLEQQEGET EENVTAEHEI RSRKSKRVVI
FTNNQSNTDT YTNTKDANDP DQTNEVALIR YSQQSDFRRD IIKGSMRAQR RKTVTWELFQ
ANVHSPLFLD RIDKPLFFSF DISGPMKLIS RNWIGKNKES QISNYTEKKT KKIEKKDEDK
REKYKREEKM RIEIAEAWDS ILLAQVIRGS VLITQSILRK YIILPSLIIA KNIARMLLFQ
FPEWSEDLKD WNREMHVKCT YNGVQLSETE FPKNWLTDGI QIKILFPFCL KPWHRFKLQP
SHKDPMKKKK GQKNDFCFLT VWGMETELPF GSPRKGRSFF EPIFKELKKK IKKFKTKSLT
ILKERTKLFR KVSKETKKWI TKSILFLKGI IKGLSKRNPI PFFGLREIYE LGETKKDSII
SNKIIHESSL QIQSMEWTNY SLTEKKIKDL TKRTNTIKNQ LEKIIKDKKN EFLTQEINIS
SNKISYQDKI LESSKKKLQI LKRRNIRLIR KLDFFIKFFI EKIYIDIFLY IINIPRTNTQ
LFLESTKKII DKFIYNNEAN QERINKTNKN TIHFISTIKN SLSNIRNKNA KAFCDLSSLS
QAYVFYKLSQ TQVISFYKFN PILQYHGTSL FLKNEIKDYF EEQGKSHSRL RHHYGLRQKS
FWHSGMNEWK NWLRGHYQYD LSQSRWLRLV PGQWRNRVNQ HYMAQNKDLT KWDSYEKERL
IHYEKKNDFQ ANSLSNQEYK LNQEKKYKKY NFKKDYGYDF LSYKSINYQD KRDSYTYGSP
FQVNKKEEIS YNYNMDKRKF FDTLGDIPIH NYLGEDDIMD AMGKFSHRKY FDWRIINFCL
RNKAEIESWV STSTKSNKNI KTVVNNYQII DKINKRGLFY FTIYQDQESN PSNKKRSPFD
WMGMNEEILS RPISNLELWF FPEFVLLYNA YKVKSWIIPI KLLLLNFNGN GNINKKIIEN
KKRDSLIASN EKKFIGLENR NQEEKEPIGQ GNPVSDAQKQ GNLRSILSNQ EKDGEEDYGK
SDIKKRKKKK QYKSNTEAEL DFFLKRYLRF QLRWDDSLNQ RIINNIKVYC LLLRLINPNE
IVISSIQRGE MNLDILMIQK DLTLRELMKK GILIIEPVRL SVKNDGQFIL YQTISISLVH
KNKHQINQRY QEKNYIDKKN FNESITRHQK MTENKDKNHY DLFVPENILS PNHRRELRIL
ISFNSRDKNG MQRNAVFLNT VKNCGQVLNK NKHLDSDKKK LIKLKFFLWP NYRLEDLACM
NRYWFNTNNG SRFSMVRIHM YPRLKIR
//