ID C3W2M9_PINPS Unreviewed; 1823 AA.
AC C3W2M9;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 2.
DT 27-MAR-2024, entry version 34.
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:ACP52560.2};
GN Synonyms=TIC214 {ECO:0000256|RuleBase:RU364085};
GN ORFNames=PLC-5287 {ECO:0000313|EMBL:ACP52560.2};
OS Pinus pinaster (Maritime pine).
OG Plastid; Chloroplast {ECO:0000313|EMBL:ACP52560.2}.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae; Pinus;
OC Pinus subgen. Pinus.
OX NCBI_TaxID=71647 {ECO:0000313|EMBL:ACP52560.2};
RN [1] {ECO:0000313|EMBL:ACP52560.2}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PINA04 {ECO:0000313|EMBL:ACP52560.2};
RX PubMed=19954512; DOI=10.1186/1741-7007-7-84;
RA Parks M., Cronn R., Liston A.;
RT "Increasing phylogenetic resolution at low taxonomic levels using massively
RT parallel sequencing of chloroplast genomes.";
RL BMC Biol. 7:84-84(2009).
RN [2] {ECO:0000313|EMBL:ACP52560.2}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PINA04 {ECO:0000313|EMBL:ACP52560.2};
RA Parks M.B., Liston A., Cronn R.C.;
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00002515, ECO:0000256|RuleBase:RU364085}.
CC -!- SUBUNIT: Part of the Tic complex. {ECO:0000256|ARBA:ARBA00011510,
CC 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; FJ899583; ACP52560.2; -; 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:SF49; 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:ACP52560.2};
KW Membrane {ECO:0000256|RuleBase:RU364085};
KW Plastid {ECO:0000256|RuleBase:RU364085, ECO:0000313|EMBL:ACP52560.2};
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 12..35
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU364085"
FT TRANSMEM 55..75
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU364085"
FT TRANSMEM 87..105
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU364085"
FT TRANSMEM 125..143
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU364085"
FT TRANSMEM 163..184
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU364085"
FT TRANSMEM 205..223
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU364085"
FT REGION 1510..1568
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1512..1530
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1823 AA; 212965 MW; ECBD6F6BF1AFB736 CRC64;
MIKVLGLLLG PLSSWVEVSG PIIIFGLYYG FLATLPFGPS KIYSTRSFLL GKPGYGIIAI
SGSITGQLIG FLSMYYSPIY AALWKPYAIT LLVVPYMLFR FFQIMDKPSS SESPHLMNSI
NNPKALSLFM DGLILQLLNP ILLANPVLTR LVNLFLFRYS PNISFMISGL CGWLGGHILL
TIFIKWVSFR IDRNSLIDNT SLRRYINQTF SLLILCYCSF YLGRAPLPFS KGKNYEDNNG
RSVTMARDDR SVARDDRSVA RDDRSVARDD RSVARDDRSV ARDYRSVARD PQKLQELIKE
ELLFFYKFFQ QQPWPIICFD HNRVYQPIRY IGNSPFTRLG PVRTEVSQYF FGAYSSDGKK
RISFTFLPSV SVLMEMIYEY RDYIYNPRAA FLKTSSLSED PYYTWNHTMK RKRDSLGNEF
SDRVKALSNG SPAENVIERR VKFSNSKGDS FTEMYDPFLN GAFRGTINQF ESPQMLNDSI
ISNLSDFIEI SMKDRTEISL EDQKGFPNDP LGYGYHISYL WEELEHESFP LPWEPLPTDT
VRSLLPVFIS SDIGTQPQYA SNRFKLQIFS NLHRIPEINP SYWLWIALRS SNVNVARQIA
LGNGPIYTTY LIYAYTRFDH LTKPSLSGLI KMELILCLFK KEHLFVYENM CLLFECLAQY
EWTVLRSSRG LIPLDKHDSI ENKDFIALYR EILLNEPLQI REIRKHVPRW SSGLTIGEYD
DVDPVLLSSN RILSRKVQDT MTFDIGQRRI GVVQNRYSAE ADYRRNLIQG SIRAKRRKIM
IWKRIQPNVH SIFFLKRKEI PAYPKDYYDT SDSGRVDKEQ IEEEVEVREK IQRVEDPLSQ
QTIAESLCLT WPELHYFRGS LLMAQSNIRK NIILPSLIIA KNMGRILLFQ VPEFYKDWEE
MRREMHVICA SDGTELSETT FPEKWETQGM QIKLLFPFRL KPWHRSKPQS AKRVRWSYLT
TFGLETDIPF GDPNSKLGIF SKFLKPIFKK VKRRLMGSTG IRRVPRVGYI DKSELNDRIQ
NKLLSEITPM GSANDSSEVN DQFGYEPQTI NVKDQDDWTT TMKERIESIA IINSSPLTGM
SLVDSEIHTG SKGSFNILGS TLKKRLVQIR RIPGLFRNKS VQLIRKRFYS MKFFIKRMGR
RMDRDLLPSV INFIASNFKF WIQSAWIRYT RNITTIYGRI FNINKDISRI NRGKITNYYS
INEKIQDFEI RPDRNMFSMS QAYIFHKIWQ IRALDIQRIL DHEKPQDLKE NDWKQWLRCF
DRYNLSPQIW SRINPNKCRN IVNKQCTCYE ERFVPYEQQE DSIFATVMEP FLGLLRKMNK
RYRYDLLSYS YLNSTKDLDI LNLTDIPGPP VQPAIPDERD ITDREGILKE KLINDIIEED
WKGTDFNIVN GSRSTVDIYD AIRSCYYDHT TSIDRQNKKT DLITNQQGID ETRRENVGIM
DSPKIEKRIS QLDLNFWLFP ELSGIKNIYY ETKSKFIPGN SILREERERK KIEEEERKET
TNVLEQIIDI RSNVKNKQDK DGQDKKGSSR RSKGSSRRSR XXXXXXXXXX XXXXXXXGQN
QDGQVEDQQT DGKKKGIFHC KVVDVLGKKR FFYLADICRV MSGMEDPGTY LRVQKGNIDL
SLMAFCIAIQ KNSSAKKISK ELALQSNVRV KVRNDNEIRK DKKIMVFQPY RLSSIVDDQF
LMYKIVSISL KLKKRAGEWI DGDFYDGSVQ RGKILGDEKK IFSSLNLEDI LLPKRRREFR
ILNRFDLEND HVGFSNGKDI QNDEELMGRD QHLSVDTTQI IKRFLWPSYR LEDIICMNRY
WFNTNDGSRS AMLRIRMYPL TVN
//
