ID U3R0W9_9ASTE Unreviewed; 1971 AA.
AC U3R0W9;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 27-MAR-2024, entry version 26.
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:AGW96906.1};
GN Synonyms=TIC214 {ECO:0000256|RuleBase:RU364085};
OS Ipomoea argillicola.
OG Plastid; Chloroplast {ECO:0000313|EMBL:AGW96906.1}.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Convolvulaceae; Ipomoeeae; Ipomoea.
OX NCBI_TaxID=89638 {ECO:0000313|EMBL:AGW96906.1};
RN [1] {ECO:0000313|EMBL:AGW96906.1}
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; KF242479; AGW96906.1; -; 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:AGW96906.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU364085};
KW Plastid {ECO:0000256|RuleBase:RU364085, ECO:0000313|EMBL:AGW96906.1};
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 12..33
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU364085"
FT TRANSMEM 87..105
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..319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 610..729
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 810..830
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1517..1547
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1638..1725
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 617..729
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1517..1531
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1532..1547
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1971 AA; 232492 MW; 9485A29D774ACDB5 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 EKIEQEIEEI EQQRKLANHL KKKKDRQKKQ
GTGGHSDKEF HSNSNTSYSK SKIEGLKSEI RVIQEKERKS LISPLLFDYR RWYRPFRYIQ
NNRLEQAIRN EMSQYFFDTQ QSDGKERISF TYPRSLSTFF KVIKRKINIL LEKTLSNQLD
NAWVSRNKKK MNHLKNDFFN RINHLDKEKI DGEIEQEKER EQKAVEILET RTRLCIEDDE
TKQEYYLPQM YDPFLNGPYR GKIKKELPPS IIKNTLIADS RETGEQNRLH DLLLPNSNYE
NFDQNTNTLE IGDILEIDAF SSIVIHKISK KVPRWSYKLI SELEQLSFHY SPPAEHEIRS
RRAVGEYLLF DPPETHTTTK ATDKETKTNA SKETDTVNKE TKPNASKETD TIDKETKTNA
SKETNTVDKE TKTNASKETD TVDKETXSKE TDTVDKETKT NASKETDTVN KETKTKTPEE
EAKEDEEKGL VLMRYAHQPD FKHGLIKGSM RTQRRKIVIE KLFQANAHSP LFFDRIKKKK
LFSFTIPRPV QLNRIFRNWS AGKGFRILES TDEQTKREEK PKRESKKKND RVKEKKRLEI
GEAWDTFEIT QMLRGCILIA QSSLRKNLIL PSLIIGKNLG RMLLLQIPEW SEDFEEWNRE
KHIKCTYTGN PLSETEFPEN WLTQGIQIKI VYPFHLKPWH TSKPLTSRDD VCFLTIFGRE
TELPFGSPRK TPSFFEPILK ELEKKIGKYE KVTAESVLKK IIRKLFKKVS KETRTTNQNL
PFIEKDLSKG KPILLFRSRE IGGMEKEKDS RISNQIINES FSQIQKIQIP DWTNSSLIET
KMQDMTDRTS TIKNQIERIT EEKKKVTLEL DISTYKKSCR LELSKKIWQI VKLKNIICKF
HYFRKFFIQR IYNDICLSTI HICQTNTQLF VESTKNLIEK YISKNETNKK IINKKTKNTI
HFISNIKTYN 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 EEINPSSNQK TPIGTNNEQL IDPIDKQEKD
PFYIPINQNP EINQPNSPNS FFDWMGMNEQ ILNRPISNLE LWFFPEFVRL FNVYKTKPWI
IPSKLLLLNS NLSETDNKKK NIAENQNLEE EDSAKSDMKK GTKKSKTNSE KKSKTNSEKK
SETDSEKKSE TDSEKKSETD SEKKSETDSE KKSETDSEKK SETDSEKKSL STRELRELFM
KKYFLLQLRW DQRNIGQNIR KNVRILALPK SSINLETMTL SCIERRKLQL NVMWKSKSNW
SILKLFKNMG VAMDRLGLSV KNNGQFLMYQ TIGISLVHKS KNKTNQQYRK QRIIRARENN
HFDALVLENI LSSRRRRELR ILICFNSNNW NDVDTNSVFF NENGVKNCSH FWEERNLRDK
EKNELIQFKF FLWPNYRLED LACMNRYWFD TNNGSRFSIL RIHMYLPLKI R
//
