ID U3R6R2_9ASTE Unreviewed; 2036 AA.
AC U3R6R2;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Protein TIC 214 {ECO:0000256|ARBA:ARBA00016640, ECO:0000256|RuleBase:RU364085};
DE AltName: Full=Translocon at the inner envelope membrane of chloroplasts 214 {ECO:0000256|ARBA:ARBA00029978, ECO:0000256|RuleBase:RU364085};
GN Name=ycf1 {ECO:0000313|EMBL:AGW98931.1};
GN Synonyms=TIC214 {ECO:0000256|RuleBase:RU364085};
OS Ipomoea macalusoi.
OG Plastid; Chloroplast {ECO:0000313|EMBL:AGW98931.1}.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Convolvulaceae; Ipomoeeae; Ipomoea.
OX NCBI_TaxID=2607137 {ECO:0000313|EMBL:AGW98931.1};
RN [1] {ECO:0000313|EMBL:AGW98931.1}
RP NUCLEOTIDE SEQUENCE.
RA Eserman L.A., Tiley G.P., Jarret R.L., Leebens-Mack J.H., Miller R.E.;
RT "Phylogenetics and diversification of morning glories based on whole
RT plastome sequences.";
RL Am. J. Bot. 0:0-0(2013).
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|ARBA:ARBA00011510,
CC 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|ARBA:ARBA00009956, ECO:0000256|RuleBase:RU364085}.
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DR EMBL; KF242503; AGW98931.1; -; 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; 3.
PE 3: Inferred from homology;
KW Chloroplast {ECO:0000256|RuleBase:RU364085, ECO:0000313|EMBL:AGW98931.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU364085};
KW Plastid {ECO:0000256|RuleBase:RU364085, ECO:0000313|EMBL:AGW98931.1};
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 14..35
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU364085"
FT TRANSMEM 56..75
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU364085"
FT TRANSMEM 87..104
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU364085"
FT TRANSMEM 208..226
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU364085"
FT REGION 284..314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 622..800
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 882..901
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1585..1607
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1704..1796
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 624..800
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 882..896
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2036 AA; 240307 MW; A15FCFCB8B901600 CRC64;
MGNPFEFRSV YYKIINSVLA AGLYYGFLSA FSIKTSHLLL LRTLVFEEEE ETKKRIVAKT
GLIMGQILLF ISIYYKPFHI ALTRPRTITA LGFFYIFFQI FWKSQKRVFA NQNSMSNLSC
IFLNHLILQQ LLNTCILPSS AARRLVSIYT FRSNNKMLFV TSSFFAWFIG QILVCKFFEL
AGKHIRIELA GKHIGKNRSI RSIIRSDYFH FFFVILFFMM SLHSFGRIPS PILLPKMSDR
SQIETRELRL KGTDEEEEND QIDEEIEQEM EEIEQEIEEI EQQRKLANHR KKKKDREKKQ
GTGGHSDKEV HSNSNNWYSK SKIEILKSEM RVIKEKEKKN IMSPLLFDYR RWHRPFRYIQ
NNRLEQAIRN EMSQYFFDTQ QSDGKERISF TYPRSLSTFL KMIKRKINIL LEKTLSNELD
NAWVSRNKKK MNHLKKDFFN RINHLDKEKI DREIEQEKER EQKAVEILET RTRLCIQDDK
TKQEYYLPQM YDPFLNGPYR GRIKKELPPS IIKNTLIADS RETGEQNRLH DLLLPNSNNK
VLNSNYENFD QNTNTLDIGD ILEIDAFSSI VIHKISKKVP RWSYKLISEL DQLSFHYSPP
AEHEIRSRRA IGEYILFDPQ KAHSTTKATD KETKPNASKE TPTVDKETKT NASKETHTVD
KETKTNASKE THTVDKETKP DANKETPTVD KETKPDANKE TPTVDKETKT NASKETHTVD
KETKTNASKE THTVDKETKT NASKETHTID KETKPNASKE THTIDKETKP DANKETPTVD
KETKTKTPEE EAKEDEENGI VLMRYAHQPD FRHGLIKGSM RTQRRKIVIE KLFQANAHSP
LFFDRIKKKK LFSFAIPRPV QLNRIFRNWS AGKGFRILES TDEQTKREEK PKRESKKKSE
RVKAKKRLEI EEAWETFELT QMLRGCILIA QSSLRKNLIL PSLIIGKNLG RMLLLQSPEW
SEDFEEWNRE KHIKCTYTGN PFSETEFPEN WLIQGIQIKI LYPFHLKPWH TSKSLTSRDD
VCFLTIFGRE TELPFGSPRK TPSFFEPILK ELEKKIGKYE KVTAESVLKK IKLFKKVSKE
TRTTNQNLPF IKKIEKDLSK GKPIFLFRSR EEIGGMEKEK DSRISNQIIN ESFSQIQIPD
WTNSSLIETK MQDMTDRTST IKNQIEKITE EKKKVTLELD ISTYKKSCRL ELSKKIWQSV
KIKNIICKFH YFRKLLIQII YNDICLSGIH IRLKNTLLFL KFTKNLIEKY ISKNETNKKI
MNKKTKNAIH FISNIKTYNS CKKNSEIFCD LSNLSQAYVF YKISQTGVVN LSKLRSVLQH
HGTSFFLKTQ MKDSFRTQGI FQSEVIHKKL QRSITGQWKN WLRGNYQYDL SQIIWSSLMS
QKHKWRNRVN RYCRSQKKYL KKWNSCGKYQ LSHYKKKKGL NSYQKDNFQK CYRYDLLSYK
SINNENKGDS VFYRSIPQVT KRQAVSDNYN MSQNSLFAIT GNIPINIFIG RIERVYIPYI
EKNLNRKYFN WENIYFDLRK KVAIESWVAV NPGSNQKTRI GTNNFQLIDP IDKQEEVNPS
SNQKTPIGTN KDEIFYPIDK EEEEEINPEE EINPEEEINP SSNQKTRIGT NNFQLIDPID
KQEKDPFYIP INQNPEINQP NSANSFFDWM GMNEQILNRP ISNLELWFFP EFVRLFNVYK
MKPWIIPSKL LLLNSNLSET DNKKKNIAEN KNLEEEDSTK SDMKKGTKKS KTNSEKKSET
DSEKKSETDS EKKSETDSEN QSETDSEKKS ETDSENQSET NSEKKSETNS ENQSLSRREV
RELFMKKYFL LQLRWDQRNI GQNIRKNVRI LALPKSSINL ETMTISCIER RKLQLNVMWK
SKRNLSILKF FKNMRVVMDR LGLSVKNNGQ FLMYQTIGIS LVHKSKNKTN QQYRKQRIIR
ARENNHFDAL VLENILSSRR RRELRILICF NSNNWNDVDT NSVFFNENGV KNCSHFWEER
NPRDKDKNEL IQFKFFLWPN YRLEDLACMN RYWFDTNNGS RFSILRIHMY LPLKIR
//