TI214_SELUN
ID TI214_SELUN Reviewed; 1601 AA.
AC Q2WGD3;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 1.
DT 25-MAY-2022, entry version 31.
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 Selaginella uncinata (Blue spike-moss) (Lycopodium uncinatum).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Lycopodiopsida; Selaginellales; Selaginellaceae; Selaginella.
OX NCBI_TaxID=307165;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=17297557; DOI=10.1007/s10265-006-0055-y;
RA Tsuji S., Ueda K., Nishiyama T., Hasebe M., Yoshikawa S., Konagaya A.,
RA Nishiuchi T., Yamaguchi K.;
RT "The chloroplast genome from a lycophyte (microphyllophyte), Selaginella
RT uncinata, has a unique inversion, transpositions and many gene losses.";
RL J. Plant Res. 120:281-290(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}.
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DR EMBL; AB197035; BAE00243.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2WGD3; -.
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..1601
FT /note="Protein TIC 214"
FT /id="PRO_0000262628"
FT TRANSMEM 25..45
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 68..88
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 147..167
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TRANSMEM 181..201
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT REGION 209..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 351..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 411..470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 535..558
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 787..806
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 879..916
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1216..1244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1521..1574
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..379
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 790..806
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1227..1241
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1525..1546
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1601 AA; 176986 MW; 492A852AE0FBC74C CRC64;
MQKWASHLCA PQVPLSLWIR SSGPPILLGL YCGFAATLPT GPFHVPSVRA SVSGREGVSG
RSVASSSVTG QPVIIPSAYS PHFHVVSVKP HAVTSSAPPC ISLYWYRHRV GIEAPRTAEP
RAVTAIGWAY AAVASRDTEV WVRRSTLLDI IILPLPHHVP VLSPALARLV RLFVLRHSNQ
FLLVISSLRG WSGGSIPLEY LATPLVVPKI DPTDDGPSEP PVEPPAEAST THRVPGTIVT
ALRLLCLGRA PLPVLFRETR HEPQRSSGGG DQEDFSWLNA WPASAFDYQK GVRPFRYVTD
GYNPGSSVKK ELSQYHFCTV VGPRKQTLSL SSPPGLSIPD DNSDKSVNLS LLPTTHKEPP
PCREWIRTGG RKESDSNNDS MNRTEAPREG YSLVKVVDSN NGLYDHGESV PAEIHDPSIS
NGSRGRIVGF RSTRLSTRRK SGRRTASNSF RNSPGAPVEE GRNTGNHHRE HPLLFVDATR
RNSYSSLVTR VLRTHDMIRL LCIIIEHKQT FRWILNVVND LLSVGSSDNS DDAYAADGAN
DAATGGGDDT DDDADDDANA AGYIRSMKVR NVEYAVNERT GNLRVLKRPV LQPDYRRNLI
AGLMRARRRK TLVWESLQSR THSPLFLRMI GNSAPPQFSP GINAKAILTP HRSAAEEEDN
KAKPVFRRSA KMATAKRIAA AKRWDFTTAH LTRGCSPIAQ LYLRRNVILP TLTIFRNICY
LIMFQKGEWG EDWNELNKEV YVGRSYDGNA AEVAKGLPRR WYRNGLQIKI VNPFYLKHRR
HFVYGQSEPD DGTGINSTGT RNGMSKSISS YETNSYGNSS SAGGGMGFGH STVLGCLAES
PLGDRIKRPS FWKPLLMELG RVWWGNVPWI RKTHIENLPS RPAGKDPSPV GKADGLDAGT
GKSIGDRVAG TRPGECGAHS AKVGGGISDL SIEFMPERDC PLAVSDQSEY RARMSTGELG
CLVARGNDGA SRVTGEFAGA GKAIAPFGPT GQDRGYTGGS GTAAPILIHR IVVRARGRCL
RLLRVSTCFV QIPFSGFHGA AAPICRFLPV WFNIRLITRS TRRYVSKVRR ARDLLAGRGG
GDSIGVYSSR RDVRVISQAY VLSRAWRLSA VNKFRPADPE YGRGNPGARK STAHLGVGGQ
GILGKRPLRA LGGRYEWARD PRRYNVPSGI WCRIAPRGRK MKDEYPRMKD RELNKKQSMT
LDEAICLRGI DPEPAAGVER SRKIDRQYGS NPPSKSSPDV VPDSSEIRGF AKPWRMGRGI
IPNDRTRKHR ERIVSGGGWD RPENRMNERK NLPFGSNIHS WLYIDIPERF HILEMPEFVA
TRYLGLACEL NVSTASGYVC AGRGSARARV ETEFREDRIE GRWDLGSKQV TVRARKMRDA
TNVPHAVFIG SNIEYPREGS VESTCESMSR DMAPPPYHAA PPDSTNGMLD GNRGHRATGV
DKRFLKHKML SVLPNFQNRF RGILDFIAYY EKSVPPRTGI LEDGGDKTIC PHSSHIGDVP
LPKRRAGSRI LESFYLAEGR SRGARSEGGT VEGHERRDEE PPVQNRNAEE NETQTINSIL
RPGHRPEDPS RMNRPRFCTN NGSQFAAARV RIYPSAGIFM T
