TI214_CUSRE
ID TI214_CUSRE Reviewed; 1750 AA.
AC A7M9B2;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 25-MAY-2022, entry version 34.
DE RecName: Full=Protein TIC 214 {ECO:0000250|UniProtKB:P56785};
DE AltName: Full=Translocon at the inner envelope membrane of chloroplasts 214 {ECO:0000250|UniProtKB:P56785};
DE Short=AtTIC214 {ECO:0000250|UniProtKB:P56785};
GN Name=TIC214 {ECO:0000250|UniProtKB:P56785}; Synonyms=ycf1;
OS Cuscuta reflexa (Southern Asian dodder).
OG Plastid.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Convolvulaceae; Cuscuteae; Cuscuta;
OC Cuscuta subgen. Monogynella.
OX NCBI_TaxID=4129;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=17714582; DOI=10.1186/1471-2229-7-45;
RA Funk H.T., Berg S., Krupinska K., Maier U.-G., Krause K.;
RT "Complete DNA sequences of the plastid genomes of two parasitic flowering
RT plant species, Cuscuta reflexa and Cuscuta gronovii.";
RL BMC Plant Biol. 7:45-45(2007).
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:0000250|UniProtKB:P56785}.
CC -!- SUBUNIT: Part of the Tic complex. {ECO:0000250|UniProtKB:P56785}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast inner membrane
CC {ECO:0000250|UniProtKB:P56785}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the TIC214 family. {ECO:0000305}.
CC -!- CAUTION: Young tissue from this organism is photosynthetic and contains
CC some thylakoids, although the photosynthetic activity does not exceed
CC the light compensation point. {ECO:0000305}.
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DR EMBL; AM711640; CAM98440.1; -; Genomic_DNA.
DR RefSeq; YP_001430153.1; NC_009766.1.
DR AlphaFoldDB; A7M9B2; -.
DR GeneID; 5536648; -.
DR GO; GO:0009706; C:chloroplast inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR008896; TIC214.
DR PANTHER; PTHR33163; PTHR33163; 2.
DR Pfam; PF05758; Ycf1; 2.
PE 3: Inferred from homology;
KW Chloroplast; Membrane; Plastid; Plastid inner membrane; Protein transport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1750
FT /note="Protein TIC 214"
FT /id="PRO_0000326572"
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 69..89
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 97..117
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 129..149
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 177..197
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 216..236
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 260..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 617..638
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 718..738
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1205..1225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1419..1512
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1422..1512
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1750 AA; 207376 MW; C35D8D1465C1023A CRC64;
MIVNNMYNLC PKIINSVIVV GLYYGFMTAL SIKPSHIFLI RALLLEKETN KNKGVAEETK
KKVAATTGFI MGQFIRLISI YYGPLYVALG RPHTITILAL PYLLIHLFWN TDKSFFAYDS
NKLNSIRNLE IYCVFLNHFA LQLLNSCILP NSTLARLVSI YMFRCNNKIL FLTSSFFAWF
IGQLFILNCF ELVLVWIRKK NSIRSTFRNY LLRNSIFVIF LNCIFGSLLF LLSIQCLGRI
PSPIPTQKLS EVSKIEQRER ERLQKEEERG VEKKEQSTEE DPSLFLEEKA GWDKEKEPDY
KFPDSELEIL QKKKIKNQEF EKHLAALLFD YKRWTRPFRY IKNNHLEQAL RNEMSQYFFD
TYQSDGKNRL SFTHPISLSA FLKMIKPKIP LLLVEKNTFN SNSLDNGWVY RNKKQMNYLR
IDFLNRVKNL DKAKAVALPR IEFETTRTQL CIHNDENKQE YLPENFDPLL NGPYRGRIKK
GLLPINDTLS EHLRETVMLN RLHALVLLNT NSKNSNQKMS TFGKKPLEIC GFSTFNLNLM
DSELKTEVLV NPIETHDLNF LKKYSTIEEI SKKVPRWSYK LITELEQISY YKNPPDDHDI
RSRKGISVVI FDPNKEATTT NSKTNTTKDT NLETKKESES DEDKLVVIRY PQQSDFRQGL
IKDSMRNQRR KIIIWELFNA NVHSPLFFDR LTIVFSFPRL KQLFINLSAR HVFGISKSTD
KKRGKTKKEE KRENKQREQK ERLEIGEAWD VFPVAQIIRG FLLLNQTFIR KKIILPSLII
GKNIGRILLF QIPEWSEDLR ELNRETHIKC TYNGIPLSEK EFPENWLTEG IQIKILFPFC
LKPWHPYKPQ TSHYDFCFLT VWGRETEQPF GHPRKTPSFF EPVLQELDKK IVNINIKARI
FSKVKINLFK RFSKEKDFQI SNQIINESFQ QIEEIPGCTN SSLIEKMQNM AHRTSTIKKE
IERVTEEKKR VTLERYICFY KRSYRLALAK NIFKKVKVKV TKNRLICKFF FFKKLFNQRI
YNNIFLETIY ICRITTQLFL ESTKKLIYKY IFNYERNKKR IDINKETKNK FNLISKLKTY
NHCKKNSYLS CDLSNLSQAY VFYKIPQTGV LNVCKLISAL QQNGIPSFIK TQIKDSFHTQ
GICKYELIQK KLQWPKTNQW KNWLRVNSEY DLSHILWFSL ISQKQKWRNR VEQYHRSKEK
YLNKRNSRGN YRLSDSKKQN VPKPVSDNYK KCYQYDLLSY KSINYAKKSA SVISRSTPKG
QAISYNDNML QNIPGKIKRL YITYIPYIGK TLDRKYLIWK NIHFYLRKKV DIESWVAVNT
SSDKDSTIGT YNYQLIDQID KKEKELFSIP IRQNTEINRP NSTNSLVDWM GMNEQILNRP
ITNLELWFFP EFVWFFNVYK TKPWIIPSKI LILNSNLSET DSKQKSETDS KQKSETDSKQ
KSETDSKQKS ETDSKQKSET DSKQKSETDS KQKSETDSKQ KSETDSKQKN NAEIQKDLDE
DSTKSDKKNK KEKETELELF AKKYFLFQLR GDPTFKKSFF KNIQIYCLLL RLTNRKKMTL
SCIQRRKFNL RIMPTMTNLF NVPEFLKMTG LVMDPLPLLI KTNGKFLLYQ IVGISLVHKS
KHQTNQTYRK RIIIRAGMTN LENNHLDVLV LENILSSRCR REFRTLICLN YKNWNGVNTN
SIFCSKNCNQ FWEERKPQYN EKRELIQKFL WPNYRLEDLA CVNRYSFDIT NGSRFSLLRF
HMYLPWKIHG
