ID H2F5R0_ANEAS Unreviewed; 1778 AA.
AC H2F5R0;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 26.
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:AEX93993.1};
GN Synonyms=TIC214 {ECO:0000256|RuleBase:RU364085};
OS Anemarrhena asphodeloides (Zhi mu).
OG Plastid; Chloroplast {ECO:0000313|EMBL:AEX93993.1}.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Asparagales; Asparagaceae;
OC Agavoideae; Anemarrhena.
OX NCBI_TaxID=59045 {ECO:0000313|EMBL:AEX93993.1};
RN [1] {ECO:0000313|EMBL:AEX93993.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=22291168; DOI=10.3732/ajb.1100491;
RA Steele P.R., Hertweck K.L., Mayfield D., McKain M.R., Leebens-Mack J.,
RA Pires J.C.;
RT "Quality and quantity of data recovered from massively parallel sequencing:
RT Examples in Asparagales and Poaceae.";
RL Am. J. Bot. 99:330-348(2012).
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|ARBA:ARBA00009956, ECO:0000256|RuleBase:RU364085}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JQ274085; AEX93993.1; -; 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; 2.
PE 3: Inferred from homology;
KW Chloroplast {ECO:0000256|RuleBase:RU364085, ECO:0000313|EMBL:AEX93993.1};
KW Membrane {ECO:0000256|RuleBase:RU364085};
KW Plastid {ECO:0000256|RuleBase:RU364085, ECO:0000313|EMBL:AEX93993.1};
KW Plastid inner membrane {ECO:0000256|RuleBase:RU364085};
KW Protein transport {ECO:0000256|RuleBase:RU364085};
KW Transmembrane {ECO:0000256|RuleBase:RU364085};
KW Transmembrane helix {ECO:0000256|RuleBase:RU364085};
KW Transport {ECO:0000256|RuleBase:RU364085}.
FT TRANSMEM 27..46
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU364085"
FT TRANSMEM 58..78
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU364085"
FT TRANSMEM 84..104
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU364085"
FT TRANSMEM 124..144
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU364085"
FT TRANSMEM 164..192
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU364085"
FT TRANSMEM 212..229
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU364085"
FT REGION 240..281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 591..645
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1480..1506
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 606..620
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 621..642
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1492..1506
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1778 AA; 211990 MW; D6340DF86D1D3D5E CRC64;
MILKSFLLGN LLSLCMKIIN SVVVVGLYYG FLTTFSIGPS YLFLLRARVM EEGTEKEVSA
TTGFITGQLM MFISIYYAPL HLALGRPHTI TVLVLPYLLF HFFWNNHKNF FYYGSTTRNS
MRNLSIQCVF LNNLIFQLFN HFILPSSTLA RLVNIYMFRC NNKMLFVTSS FVGWLIGHIL
FMKWVGLVLF WIRQNHSIRS NKYLVSELRN SMARIFSILL FITCVYYLGR MPSPIVTKKL
KETSETEERG ERKEESDVET TYETKKTKQE QEGSVEEDKD SPVYEDSYLD THQDNWELGK
LKEEKNEKTY FWFEKPIVTF LFDYKRWNRP LRYIKNDRFE NAVRNEMSQY FFYICPSDGK
QIISFTYPPS LSTFSEMVER KISLYTTEKL SHEDLYNYWV YTNEQKKYNL NNELISRIKI
LEKEKGSLAL DILEKRTRLC DDENEQEYLP QIYDPFLNGP YRGTIKKFDS RAIMNDLITS
TADSVEMFWI NKIHGLFHNE SREFEHQQKK KTFTFDGELL LNSIENSLTS SDELSFEHAR
RVDSESQAKS LKVVFDVITT DPNDLTTIRK KSIGMEEISK RVSRWSYKLT DDLEEEEEEN
EEESTEDPEI RSRKGKRVVI YTDNDQSTHS SATNNNTSTS DEEEEVALIR YSQQSDFRRG
IIKGSMRAQR RKTVIWEMFQ ANVHSPLFLD RIDKTFFFSF FDISDMINLI FRNWVGGNPE
LQISYFEEEE TKEKEKTNED KEEENERIAI SEAWDTFIFT QGIRGLMLVT QSFLRKYIIL
PLLIISKNIG RMLLLQLPEW HEDLKEWNRE MHVKCTYNGV QLSETEFPQN WLTDGIQIKI
LFPFCLKPWR RSKIRSHHRD QKMSKKEKKD NFCFLTVWGR EAELPFGSPR KRPSFFEPVL
KELEKKMIKT KKQIFKVIRV FKERRKLFLK VSKEKTRWVI KIVLVINLIM KELKKVNPTF
LLKLRKVKIY EPNENGKASN INNKIIREST IRIQSMNCVN ENYSIIETKM KDLANKTITI
RAQIEGITKD KKKIIVTCDD KNKRSESQKD IWQIFKRKNI RLIRKSYYFM KSFIEKIYMD
ILLCIIKIPR TNAQLFFEST KKIINKSIYN DETSQEGIEK TNQNTMNFIS TIKKSFSNTN
ISNKNSNIYC DLSSLSQAYV FYKLSQNQLL NKYHLRSVLQ YHGTYPFLRD IIKNYCMTRG
IFDSKPRHKK IHKSGMNKWK IWLRGHYQYN LSQTKWAHLV PKKWRNRVNQ CRTIQKKDSM
KLDLYKKEKD QLIHCMKQNY YAVDSLMSQK EKWKKHYGYD LLSYKYINYG GSKDSYIYGS
TLQVKDKKIP YNLNTPELES FYGLISIAIS DYLEKRSIID TDKNLDRKFF DCRILHFCLR
NNIDIETWIN THIDTKIHKN AKTETTNSQK KYFFDWMGMN QERLYRTISN LEPWFFPEFV
LLFDAYKKKP WIIPIKLLIF HFHFYENISQ SEKIDINQKK NEQQGQGDLV SDLRKQNKKK
DVEEDYTGAD IKKGRKKKQS KSKKEAELEF FLKKYFLFQL RWDDPLNQRI INNIQVYCLL
LRLTDPREIA ISSIQRGEMH LDAMLIQKDL TLTELIKRGI FIIEPIRLSM KRDGKYIIYQ
TVGISLADKN KHQTNEKFIT KNGYVDKKNF DGSVARHSNM LVNRNKNHYD FFVPENILSP
RRRRELRILI CFNSKSWNVV DRNPIFCNQN NIKNCGQFLN EEKHLNTEAN KFIKFKLFLW
PNYRLEDLAC MNRYWFDTNN GSHFSMSRIH MYSRFRIS
//
