TERC_ARATH
ID TERC_ARATH Reviewed; 384 AA.
AC F4JZG9; Q8LCU5; Q8VY96; Q9FMP9;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 25-MAY-2022, entry version 59.
DE RecName: Full=Thylakoid membrane protein TERC, chloroplastic {ECO:0000305};
DE AltName: Full=Protein PIGMENT DEFECTIVE 149 {ECO:0000312|EMBL:AED91766.1};
DE AltName: Full=Protein TELLURITE RESISTANCE C {ECO:0000303|PubMed:18429937};
DE Short=AtTerC {ECO:0000303|PubMed:18429937};
DE Flags: Precursor;
GN Name=TERC {ECO:0000303|PubMed:18429937};
GN Synonyms=PDE149 {ECO:0000312|EMBL:AED91766.1};
GN OrderedLocusNames=At5g12130 {ECO:0000312|Araport:AT5G12130};
GN ORFNames=MXC9.9 {ECO:0000312|EMBL:BAB10031.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9501997; DOI=10.1093/dnares/4.6.401;
RA Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. III. Sequence
RT features of the regions of 1,191,918 bp covered by seventeen physically
RT assigned P1 clones.";
RL DNA Res. 4:401-414(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 176-384.
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=18429937; DOI=10.1111/j.1365-313x.2008.03523.x;
RA Kwon K.C., Cho M.H.;
RT "Deletion of the chloroplast-localized AtTerC gene product in Arabidopsis
RT thaliana leads to loss of the thylakoid membrane and to seedling
RT lethality.";
RL Plant J. 55:428-442(2008).
RN [6]
RP FUNCTION, INTERACTION WITH ALB3, SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=24612058; DOI=10.1111/tpj.12474;
RA Schneider A., Steinberger I., Strissel H., Kunz H.H., Manavski N.,
RA Meurer J., Burkhard G., Jarzombski S., Schunemann D., Geimer S.,
RA Flugge U.I., Leister D.;
RT "The Arabidopsis tellurite resistance C protein together with ALB3 is
RT involved in photosystem II protein synthesis.";
RL Plant J. 78:344-356(2014).
CC -!- FUNCTION: Integral thylakoid membrane protein that plays a crucial role
CC in thylakoid membrane biogenesis and thylakoid formation in early
CC chloroplast development (PubMed:18429937). Is essential for de novo
CC synthesis of photosystem II (PSII) core proteins and required for
CC efficient insertion of thylakoid membrane proteins, presumably via
CC interaction with ALB3. May assist synthesis of thylakoid membrane
CC proteins at the membrane insertion step (PubMed:24612058).
CC {ECO:0000269|PubMed:18429937, ECO:0000269|PubMed:24612058}.
CC -!- SUBUNIT: Interacts with ALB3. {ECO:0000269|PubMed:24612058}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000269|PubMed:18429937, ECO:0000269|PubMed:24612058}; Multi-pass
CC membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, rosette and cauline leaves,
CC stems and flowers. {ECO:0000269|PubMed:18429937}.
CC -!- DISRUPTION PHENOTYPE: Pigment deficiency and seedling lethality.
CC {ECO:0000269|PubMed:18429937}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB10031.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB007727; BAB10031.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED91766.1; -; Genomic_DNA.
DR EMBL; AY086401; AAM64468.1; -; mRNA.
DR EMBL; AY072336; AAL61943.1; -; mRNA.
DR EMBL; AY114608; AAM47927.1; -; mRNA.
DR RefSeq; NP_001331346.1; NM_001343228.1.
DR RefSeq; NP_568257.1; NM_121251.4.
DR AlphaFoldDB; F4JZG9; -.
DR STRING; 3702.AT5G12130.1; -.
DR iPTMnet; F4JZG9; -.
DR PaxDb; F4JZG9; -.
DR PRIDE; F4JZG9; -.
DR ProteomicsDB; 234169; -.
DR EnsemblPlants; AT5G12130.1; AT5G12130.1; AT5G12130.
DR GeneID; 831086; -.
DR Gramene; AT5G12130.1; AT5G12130.1; AT5G12130.
DR KEGG; ath:AT5G12130; -.
DR Araport; AT5G12130; -.
DR TAIR; locus:2177053; AT5G12130.
DR eggNOG; ENOG502QQNF; Eukaryota.
DR HOGENOM; CLU_045644_1_0_1; -.
DR InParanoid; F4JZG9; -.
DR OrthoDB; 1366675at2759; -.
DR PRO; PR:F4JZG9; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; F4JZG9; baseline and differential.
DR Genevisible; F4JZG9; AT.
DR GO; GO:0009534; C:chloroplast thylakoid; IDA:TAIR.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0090351; P:seedling development; IMP:TAIR.
DR GO; GO:0010027; P:thylakoid membrane organization; IMP:TAIR.
DR InterPro; IPR005496; Integral_membrane_TerC.
DR InterPro; IPR022369; Integral_membrane_TerC_rswitch.
DR PANTHER; PTHR30238:SF0; PTHR30238:SF0; 1.
DR Pfam; PF03741; TerC; 1.
DR TIGRFAMs; TIGR03718; R_switched_Alx; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Membrane; Plastid; Reference proteome; Thylakoid;
KW Transit peptide; Transmembrane; Transmembrane helix.
FT TRANSIT 1..48
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 49..384
FT /note="Thylakoid membrane protein TERC, chloroplastic"
FT /evidence="ECO:0000255"
FT /id="PRO_0000434012"
FT TOPO_DOM 49..115
FT /note="Stromal"
FT /evidence="ECO:0000305|PubMed:24612058"
FT TRANSMEM 116..136
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 137..145
FT /note="Lumenal, thylakoid"
FT /evidence="ECO:0000305|PubMed:24612058"
FT TRANSMEM 146..166
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 167..180
FT /note="Stromal"
FT /evidence="ECO:0000305|PubMed:24612058"
FT TRANSMEM 181..201
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 202..206
FT /note="Lumenal, thylakoid"
FT /evidence="ECO:0000305|PubMed:24612058"
FT TRANSMEM 207..227
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 228..275
FT /note="Stromal"
FT /evidence="ECO:0000305|PubMed:24612058"
FT TRANSMEM 276..296
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 297..301
FT /note="Lumenal, thylakoid"
FT /evidence="ECO:0000305|PubMed:24612058"
FT TRANSMEM 302..322
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 323..335
FT /note="Stromal"
FT /evidence="ECO:0000305|PubMed:24612058"
FT TRANSMEM 336..356
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 357
FT /note="Lumenal, thylakoid"
FT /evidence="ECO:0000305|PubMed:24612058"
FT TRANSMEM 358..378
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 379..384
FT /note="Stromal"
FT /evidence="ECO:0000305|PubMed:24612058"
FT REGION 68..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..87
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..104
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 304
FT /note="V -> G (in Ref. 3; AAM64468)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 384 AA; 41900 MW; 46AC3FA836CE6EDC CRC64;
MSLASVIHHG ILPPAKSDRI FLTIPVFPPD FRARGWTKSP FSLLINPSLA SAANRRLSHL
PPIACSRGID QEDEEKESRE LLPHKNDENA TTSRSSSSVD SGGLKDYQQE ETYKTSFKTV
ALCVGTAVAF GIGIGLKEGV GKASEFFAGY ILEQSLSVDN LFVFVLVFKY FKVPLMYQNK
VLTYGIAGAI VFRFTLILLG TATLQKFEAV NLLLAAVLLY SSFKLFASEE DDTDLSDNFI
VKTCQRFIPV TSSYDGNRFF TKHDGILKAT PLLLTVAVIE LSDIAFAVDS IPAVFGVTRD
PFIVLTSNLF AILGLRSLYT LISEGMDELE YLQPSIAVVL GFIGVKMILD FFGFHISTEA
SLGVVALSLS TGVLLSLTNK SSDS
