TI214_CUSGR
ID TI214_CUSGR Reviewed; 1673 AA.
AC A7M944;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 33.
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 gronovii (Common dodder) (Epithymum gronovii).
OG Plastid.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Convolvulaceae; Cuscuteae; Cuscuta;
OC Cuscuta subgen. Grammica; Cuscuta sect. Oxycarpae.
OX NCBI_TaxID=35886;
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; AM711639; CAM98372.1; -; Genomic_DNA.
DR RefSeq; YP_001430085.1; NC_009765.1.
DR AlphaFoldDB; A7M944; -.
DR GeneID; 5536778; -.
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; 5.
DR Pfam; PF05758; Ycf1; 4.
PE 3: Inferred from homology;
KW Chloroplast; Membrane; Plastid; Plastid inner membrane; Protein transport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1673
FT /note="Protein TIC 214"
FT /id="PRO_0000326570"
FT TRANSMEM 32..52
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 70..90
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 93..113
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 130..150
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 170..190
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 218..238
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 264..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 547..611
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1120..1146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1370..1433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 264..301
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 558..587
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 588..611
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1122..1146
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1382..1425
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1673 AA; 197167 MW; 046413EFFBC1371D CRC64;
MNFQYLVKIV AGSYYNISSS ILSKIINSVI MAGLYYGFLT ALALKTSYIL LIHAMVRENP
NHKAAAITGL ILGQLGQLLS IYYAPLYIAF GRPYTLTVLT LIYFLVNLFG NNLDKNASSF
GAYGNTIRNL EILCIFLNNL ILQLLNTCIF PSSTLARVVN VYLFRCNNKM VFLISSFSAW
LIGQILVLMC CQLVLGRGQN KNSIRSLIQK YLVRNSMFFL VVNCLFGSSL FILTIQSLGR
IPLPIPTQKL SEISRIEKRE EERLKKSGVA KEGKSTEDEE DLSHEKDSLK KEPYSKLENE
DEEIEKDIEQ AIGTLLFDYK RWTRPFRYIK NNQFEQAVRN EMSQYFFATQ QSDGKSRICF
TYPVNLSMFW KGISFLSRDK NYSNKLNRHW VERNKKKLKS LKRDLVNRIK NLDKTLKIEF
GTTRTRLCTC IHDDETKQEY VPEEYDPLLA GGYRGRIKKE QAILQKQENE TLTHPLDTLI
DVLENNTNAQ LFKTNPIDNQ KINFEEELRK KVPRWSYKLI TELEQISYYR NPPDDHDIRT
RKAKSLVVFD PSKHPNMETM EDNGNIQNNS SDKTINPQNN LTNLKPRTSE NDPDDNTTEK
EPKDDKSYSI RYSHQSDFRH GLIKDSMRSL RRKIVIKDLF KGNVHSPLFF ERRKKKNLFS
FSGLVKLKKL FIPGSAQKEF GDLKDSNKKL TIKDKKQQET KERIEIAEAW DSFELTQVLR
GVLLVTQSSL RRDILLPSLI IIKNLGRILL FQSSELSDDF KELAKETHVP CTYNGVPLGE
KEFPRNWLTE GIQIKILSPF CLKPWNEEKK PLPASENFCF LTIWGQETDQ IFGRPRRRPS
FFKPFLTKLD TTLKKINLFQ FFKEKRTPES NMVKEQKVDD LSDNILNEFQ FSKREKLEAI
TNRTSIIKTK LETIAEEKKK VTRDLDRSLS KKSLKRIRFK LVSNLFPFQS FLKLFIQEIY
NLFLRNILLI SGLLKKILNR EKEKLINQSC SKNEKMKKVH KKFNFSLNRK SKPSTNFSNL
SQAYVFYKIS QQIASFSVCK LRSILNQQVK AIFVKPEIKE FFARHGLIQT QEMDKKSIQL
RTPQWKHWLR VNSQHHLSQI LWFSFGAKKE NWRKKINRCN KQSLQKRNSS GNSNLDDSKN
RNTDNLILNK NQKDNFEKCY RYDVLSSKFI KFEKKKISFI HRSPLSLTRQ HQISYHKNMS
QNFLFALPKN MSVKNLMGKS QRMHIPYIEK DFDRKYLSFE NIEFSLKKKI NIESWIPLTS
RGNKTKTYNY EFLDELELME FIDQIYKKEK ELLFPCIERN NKIRNAKSKY SFIDWMGLNE
ELLKHPVTNL ELWFFPEFVS LLNIYKLKPW VLQSQLLFSK LTFNKLLSKQ QNQTTTKMNT
ETKNKQKSKV ENEKNKKTEN QQNAETKNKQ KSKTENEGNK ETENQQNDES EDDPQLAYIR
SFMKKHLLFQ LRGESIFKKS GFKNIQILCL LLRLMNQNEM LFSSIQRQKL NLHIMPEIGI
KELTLEVLEE IGVPEFLKEK RVNFEPFPLY INKNGKFLMY QLLNMSLVHN IKYPTNNESR
NQGVITTQKN NNMASHIPEN ILSSRRRREL RILMCLNHNK KKCESTEATN KSFIYKKKCA
KIWEEQKSTI EFFIWPNSRF EDLTCMNRYW FYTNNGSRFS MLRIFMYLPL KNY