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Database: UniProt
Entry: L0BEE9_9ASPA
LinkDB: L0BEE9_9ASPA
Original site: L0BEE9_9ASPA 
ID   L0BEE9_9ASPA            Unreviewed;       712 AA.
AC   L0BEE9;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   22-FEB-2023, entry version 20.
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};
DE   Flags: Fragment;
GN   Name=ycf1 {ECO:0000313|EMBL:AFZ85963.1};
GN   Synonyms=TIC214 {ECO:0000256|RuleBase:RU364085};
OS   Zephyranthes montana.
OG   Plastid; Chloroplast {ECO:0000313|EMBL:AFZ85963.1}.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Asparagales; Amaryllidaceae;
OC   Amaryllidoideae; Hippeastreae; Zephyranthes;
OC   Zephyranthes subgen. Myostemma.
OX   NCBI_TaxID=666564 {ECO:0000313|EMBL:AFZ85963.1};
RN   [1] {ECO:0000313|EMBL:AFZ85963.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Garcia N., Meerow A.W., Soltis D.E., Soltis P.S.;
RT   "Testing Deep Reticulate Evolution in Amaryllidaceae Tribe Hippeastreae
RT   (Asparagales) with ITS and Chloroplast Sequence Data.";
RL   Syst. Bot. 39:75-89(2014).
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|RuleBase:RU364085}.
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DR   EMBL; KC207535; AFZ85963.1; -; Genomic_DNA.
DR   AlphaFoldDB; L0BEE9; -.
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:AFZ85963.1};
KW   Membrane {ECO:0000256|RuleBase:RU364085};
KW   Plastid {ECO:0000256|RuleBase:RU364085, ECO:0000313|EMBL:AFZ85963.1};
KW   Plastid inner membrane {ECO:0000256|RuleBase:RU364085};
KW   Protein transport {ECO:0000256|RuleBase:RU364085};
KW   Transport {ECO:0000256|RuleBase:RU364085}.
FT   REGION          13..39
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        13..37
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AFZ85963.1"
FT   NON_TER         712
FT                   /evidence="ECO:0000313|EMBL:AFZ85963.1"
SQ   SEQUENCE   712 AA;  85400 MW;  B14F66BE2F17BA20 CRC64;
     EIRSRKGKRV VIYTDNDQST NSRASNNTTN NTNTSDEEEE VALIRYSQQS DFRRGIIKGS
     MRAQRRKTVT WKIFQANVHS PLFLDRIDKI FFFSFFDISE TINLVFRNWV GEPPELQISY
     FDEEEETKEK EKTNEEKEGE SERIAISEAW DTFIFTQAIR GFMLVTQSFL RKYVTLPLLI
     IAKNIGRMLL LQFPEWYEDL NEWNREMHVK CTYNGVQLSE TEFPKNWLTD GIQIKILFPF
     CLKPWRRSKI RSHHRDQQMT KKEKKDNFCF LTVWGREAEL PFGSPRKRPS FFEPILKELE
     KKMIRLKKKN FQLIRVFKER KKRFLKVSKE KTRWVAKIVL VINLIMKELE KRNPFFLSKL
     RKVEVYKSNE NGKDSNINNK IIRESTIRST SCVNENYSLI EKKMKDIANK TTTIRTQIEG
     ITKDKKKIVL NKKSESQKDF WQKFKRKNIR LIRKSYYFMK SLIEKIYTDI LLCIIKIPRI
     NAQLFFELTK KIINKSIFNN ETNQEGIENT NQNTMNFIST IKKSFSNTNI NKNSYCDLSS
     LSQAYVFYKL SQNQLLNKYH LRSVLQHHGT YSFLKDIIKN YCTTRGIFYS KSRHKKIDKY
     GMNKWKIWLR GHYQYNFSQT KWSYLVAKKW RNRVNQCRMI QKKNSMKLDL YKKEKDQLIH
     YMKENYYAVD SLMSQKAKLK KHYGYDLLSY KYINYGDSKD SYIYGSALQV ED
//
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