TI214_CUSOB
ID TI214_CUSOB Reviewed; 1676 AA.
AC A8W3M6;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 25-MAY-2022, entry version 35.
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 obtusiflora (Peruvian dodder).
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. Cleistogrammica.
OX NCBI_TaxID=437280;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=17956636; DOI=10.1186/1471-2229-7-57;
RA McNeal J.R., Kuehl J.V., Boore J.L., dePamphilis C.W.;
RT "Complete plastid genome sequences suggest strong selection for retention
RT of photosynthetic genes in the parasitic plant genus Cuscuta.";
RL BMC Plant Biol. 7:57-57(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: Only inflorescences, fruits, starved seedlings and stressed
CC stem tips are green in this organism. {ECO:0000305}.
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DR EMBL; EU189133; ABW20601.1; -; Genomic_DNA.
DR RefSeq; YP_001531256.1; NC_009949.1.
DR AlphaFoldDB; A8W3M6; -.
DR PRIDE; A8W3M6; -.
DR GeneID; 5714769; -.
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; 4.
DR Pfam; PF05758; Ycf1; 4.
PE 3: Inferred from homology;
KW Chloroplast; Coiled coil; Membrane; Plastid; Plastid inner membrane;
KW Protein transport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1676
FT /note="Protein TIC 214"
FT /id="PRO_0000326571"
FT TRANSMEM 24..44
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 546..610
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1123..1151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1372..1436
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1384..1436
FT /evidence="ECO:0000255"
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..610
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1123..1148
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1372..1386
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1387..1426
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1676 AA; 197706 MW; DE6C353481250E3E CRC64;
MNFQYLVKIV AGSYYNISSS ILSKIINSVI LAGLYYGFLT ALALKTSYIL LIRAMVSENQ
NHKAAATTGL ILGQLGQFLS IYYAPLYIAF GRPYTLTVLT LIYFLVNLFG NNLDKNASSF
GAYGNKIRTL EILCIFLNNL ILQLLNTCIF PSSTLARVVN VYLFRCNNKM VFLISSFSAW
LIGQILVLMC CKLVLGRGQN KNSIRALIKK YLVRNSMFFL VVNCLFGSSL FILTIQSLGR
IPLPIPTQNL SEISRIEKRE EERLKKSGVA KEGKSTEDEE DLSHEKDSFK KEPYSKLENE
DEEIEKDIEQ AIGTLLFDYK RWTRPFRYIK NNQFEQAVRN EMSQYFFGTQ QSDGKSRICF
THPVNLSMFW KGISFLLRDK NYSNKLTRRW VQRNKKKLKS IKSDLVNRIR NLDNTIKIEF
GTPRTRLCTC IHENETKQEY VPEEYDPLLA GCYRGRIKKE QAIFQKQENE TLTNPLDTLI
DVLENNTNTQ LFKANPIGKQ KISFEEELRK KVPRWSYKLI TELEQISYYR NPPDDHDIRT
RKAKSLVVFD PSKHPNMETM EDSGNIQNKS SDKTINPQNN LTNSKTRTSE NDPDDNTTEK
EPKDDKSYSI RYSHQSDFRH GLIKDSMRSL RRKIVITDLF KGNVHSPLFF ERRKKKNLFS
FSGLLKLKQL FITWSAQKEF WDLKDSKKKL KIKDKKQQET KERIEIAEAW DSFELTQVLR
GVLLVIQSSL RKDILLPSLI IIKNLGRILL FQTSEWSHDF EELEKETHVP CTYNGVPLGE
KEFPRNWLTE GIQIKILSPF CLKPWNDEKK PLPASENFCF LTIWGQETDH IFGRPRRKPS
FFKPILTKLD TSLKKINVVQ FFKEKRTPES NIVKEQKVDD LSDNILNEFQ FSKREKLEAI
TNRTNLIKTK LETIAKEKKT VTRDLDKNLS KKSLKQIKFK LVSNLSLFQY FLKLFIQKIY
TLFLRNILLI SGLLKKILNG EKEQLIDQYC SKNEKIKKVH KKFNFILNRK SKLSTNFSNL
SQAYVFYKIS QEMANFSVCK LRSILNQQVK AVFVKPEIKE SFARYGLIQI QKMDKKNLQL
RTRQWKHWLR VNSQHHLSHI LWSSFGAKKE NWRKKIKRCN KFNKQSLQKG NSKGNSNLDD
SKNRNKNNLI LNKNKKDNFE KCYRYDVLSS KFIKFEKKKT SLFHRSRISL TRQKQILYHK
NMSQNFLFAL PKNMLVKNLM GKSERIHIPY IEKDLDRKYL SFENIQFSLK KKVNIESWIP
LTSRGNRTKT YNYELLDELE LMKFIDQIYK KEKEFLFPCI ERNKQIRNSK SKYSFIDWMG
LNQKLLKHPV TNLELWFFPE FVSLLNIYKL KPWVLQSQLL LSKLTFNKLS SQQQNQTTTK
INTETKNQQK NRVENEENKE TENQQNAETK NKQKSKTENE ENKETENQQN DESEDDPQLA
YIRSFMKKHL LFQLRGESIF KKSGFKNIQI LCLLLRLMNQ NEMLFSSIQR EKLNLHIMPE
IGIKDLTLEV LEEIGVPEFL KEKRVNFEPF PLYINKNGKF LIYQLLNMSL VHKIKYPTNN
ESRNQGVITT QKNNNVASHI PENILSSRRR RELRILMCLN KKKKKCKGTE ATNKSFSYKK
KCAKIWEEQK STIEFFIWPN SRFEDLTCMN RYWFYTNNGS RFSMLRIVMY LPLKNY
