TI214_PINKO
ID TI214_PINKO Reviewed; 2046 AA.
AC Q85WU2; A4QMC6;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 2.
DT 25-MAY-2022, entry version 43.
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 Pinus koraiensis (Korean pine).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae; Pinus;
OC Pinus subgen. Strobus.
OX NCBI_TaxID=88728;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KangWon16;
RA Noh E.W., Lee J.S., Choi Y.I., Han M.S., Yi Y.S., Han S.U.;
RT "Complete nucleotide sequence of Pinus koraiensis.";
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP SEQUENCE REVISION.
RA Noh E.W., Lee J.S., Choi Y.I., Han M.S., Yi Y.S., Han S.U.;
RL Submitted (APR-2007) 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: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 ---------------------------------------------------------------------------
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; AY228468; ABP35463.1; -; Genomic_DNA.
DR RefSeq; YP_001152223.1; NC_004677.2.
DR AlphaFoldDB; Q85WU2; -.
DR PRIDE; Q85WU2; -.
DR GeneID; 5048614; -.
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; 3.
DR Pfam; PF05758; Ycf1; 3.
PE 3: Inferred from homology;
KW Chloroplast; Membrane; Plastid; Plastid inner membrane; Protein transport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..2046
FT /note="Protein TIC 214"
FT /id="PRO_0000262623"
FT TRANSMEM 18..38
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 54..74
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 79..99
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TRANSMEM 125..145
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 163..183
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TRANSMEM 214..234
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT REGION 278..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 320..472
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1833..1898
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 320..453
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1833..1884
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2046 AA; 238002 MW; 12A1202774B30A3F CRC64;
MIRVLGLLWD PLSSWVEVSG PIILFGLYYG FIATLPFGPS KIYSMRSFFL GETLYGIIAI
SGSITGQLIV FLSMYYSPIY AALWKPHAIT LLVIPYTFCR VFRSLEKPSS PESTHPMNSI
KNPKILSLFM GGLILQLLNP ILLANPVLTR LVNLFLFRYS DNISFMISSF CGWLGGHILF
INLTKLVSLR LVSFRIERNS PIDHTSLRRY IHQTFSVLLI SYFSFYLGRS PLIFHRKKKD
NKKKDRSAAM AKKDRSVAMA KKNCSVAMVK KDRSVAEDED RSVAMAKKGR SVAEDEDRSE
PLAMVMVQEA RSVSFIAKKA RSVAEDKDPE DEHRSVAMAK KARSVAEDKD PEDEHRSVAM
AKKDRSVAED EDRSVAMAKK DRSVAEDEDR SVAEDEDRSV AEDEDRSVAE DEDRSVAEDE
DRSVAEDEDR FVAEDEDRSV AEDEDRSVAE DEDRSVAEDE DPEDEDRSVP REQKKLKGLP
ISWFKQPCPI KFFDPDRIYQ PIRYIGNSPF HCLKPVMRTE VSQYFFGAYS SDGKKRISFT
LLPSVLALGE KLGKYRDLLD TSCLSEDPYH RWNHTMKRRR DSLENEFSDR VKALSHGSPA
ENVIERRVKF SNSQGDSFTE MYDPLLNGAL RGTIDQFESP KMLNDLIISI ISNLSDFIEI
PIKDCKEGFP NDQFGYGYHI SEHWQELEHK SFRLPWEPLP TDTFRSLVPS TKSSRRGKVE
PISKRLYPLA ERIIPNKAKK IFEEYLSNID SSFGKLIYPK DLLEMQIQEI YTKDDDSLIH
FLWLEIAFRV AYMDLAPEIA SCNERIYTNS LVNIYNRIDG RNVAPTGTVK WELILSLFTT
KQIFLFESLA QHEWTILRNC RGNVSTDDST QTKDFIDLYG KILLNEPLQF REIKKHLPRW
PSDLMRAERD GDGDDRGPIQ ISTSRIRTRK VKSKLTLDFG KERIVLKRYH AESDYRRSLI
RGSMRAKRRK IMIWKRVQPN VHSLFFLRRM EIPTYPKDYY DTFDSGRVNQ EQIQKEVREK
IHRGKYLDPV LHNTTLAEQV CLAWPEVHYF RGLILVAQSN IRKNIILPSL IIAKNIGRIL
LFKAPEFAQD WEEMKEELHI KCGSDGTEFS KKGFPDKWYK YGMQIKLIFP FRLKPWHSQS
KKRLRLRWSY LTTLGFETDI PFGDPKPKLG IFSEFFQPIF KKVKKGLKKG LKKGLKKGLK
RELILFKKVK RRLMGSTGIR RVSRVRYIDK SELNDRIQNK LLSETETTPM GSANDSSEVN
DQFGYETQTI NVKDPDDWTT TMKERIESIA IINSSPITGM SLMDSEIHTG SKGSFNILGS
TLKKRLVQIR RIPGRFRNKS VQLIRKRFYS MKLMKLFLKR MDRYLLLSVI HFIGSNIKFW
IRSAWIRSTG NIATIYGRIF IINNDISKIN RGKITNYYSI NEKRKDFEIR PDRNMLSMSQ
AYVFHKIWQI GAIDRSYSKY FLKYRAQTSY PLIKKKIKEL LDIQRILDHE KPQDLKENDW
KQWLRCFDRY KLSPQIWSRI NPQKWRNRVN KQCTCYEERF IPYEKKKDYI FATVIEPSLG
LLRKMNKRYR YDLLSYSYLN STKELDILNL TKDSDILNLT KDSDILNLTK DSDILNLTKD
SDILNLTKDS DTLKIEKRRS GLDLKFWLFP ELSGKENIYD NSKFIPGYSI LSEAQERKKI
EEKEREERIK VIEERIGIIR SDVQNKKVEE KQTGTGEVEE KQTGKVKQKQ FGLKVEDQKT
DGKKKTNQVL VQHKILKDIG EEDISDLAGM CRILIEIEDP TKFMQIYEEN INLNLMFLII
YEDLKGYEKY INARDSNAND INANDINAND INAKDSNAND INAKDSNAND INANDSNAKD
SNANDINAKD INAKDSNAND INAKDSNADV PKKKEDEIPK TVVSSEPYRL SSIVNDNLLI
YKIVSMWLKS EKIKRAGLGD DKNILSSFNL EDILLPKRRR EFRILNRFDL ENDHVGFFNG
KSIQNDEELM GRDQHLSVDT TQRIKRFLWP SYRLEDLLCM NRYWFNTNDG SRSAMLRIRM
YPLNVN
