THF1_ARATH
ID THF1_ARATH Reviewed; 300 AA.
AC Q9SKT0; Q8LB69;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 114.
DE RecName: Full=Protein THYLAKOID FORMATION 1, chloroplastic;
DE Flags: Precursor;
GN Name=THF1; OrderedLocusNames=At2g20890; ORFNames=F5H14.14;
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 [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=15516501; DOI=10.1104/pp.104.049841;
RA Wang Q., Sullivan R.W., Kight A., Henry R.L., Huang J., Jones A.M.,
RA Korth K.L.;
RT "Deletion of the chloroplast-localized thylakoid formation1 gene product in
RT Arabidopsis leads to deficient thylakoid formation and variegated leaves.";
RL Plant Physiol. 136:3594-3604(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 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 [6]
RP FUNCTION, SUBCELLULAR LOCATION, POSSIBLE TOPOLOGY, TISSUE SPECIFICITY, AND
RP INTERACTION WITH GPA1.
RX PubMed=16582010; DOI=10.1105/tpc.105.037259;
RA Huang J., Taylor J.P., Chen J.-G., Uhrig J.F., Schnell D.J., Nakagawa T.,
RA Korth K.L., Jones A.M.;
RT "The plastid protein THYLAKOID FORMATION1 and the plasma membrane G-protein
RT GPA1 interact in a novel sugar-signaling mechanism in Arabidopsis.";
RL Plant Cell 18:1226-1238(2006).
CC -!- FUNCTION: Involved in a dynamic process of vesicle-mediated thylakoid
CC membrane biogenesis. Required for the normal organization of vesicles
CC into mature thylakoid stacks and ultimately for leaf development. Also
CC involved in a sugar-signaling mechanism in roots by mediating signaling
CC between the plasma membrane and the plastid. Probably acts downstream
CC of the plasma membrane-delimited heterotrimeric G-protein GPA1 in a D-
CC glucose signaling pathway. {ECO:0000269|PubMed:15516501,
CC ECO:0000269|PubMed:16582010}.
CC -!- SUBUNIT: Interacts with GPA1. {ECO:0000269|PubMed:16582010}.
CC -!- INTERACTION:
CC Q9SKT0; P18064: GPA1; NbExp=4; IntAct=EBI-972220, EBI-443890;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast outer membrane; Single-pass
CC membrane protein. Plastid, chloroplast stroma.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Present at higher level in hypocotyls
CC (at protein level). Ubiquitously expressed in all organs, in roots of
CC both light-grown and dark-grown seedlings. Highly expressed in the root
CC apical meristems. {ECO:0000269|PubMed:15516501,
CC ECO:0000269|PubMed:16582010}.
CC -!- DEVELOPMENTAL STAGE: Rapidly degraded upon D-glucose but not L-glucose
CC treatment (at protein level). Accumulates in leaves of plants grown
CC under normal long daylight (16 hours)/dark (8 hours) conditions. Levels
CC are greatly reduced in leaves from plants placed in complete darkness
CC for 24 hours. Transcript levels return to normal within 6 hours after
CC plants are returned to normal light levels.
CC -!- SIMILARITY: Belongs to the THF1 family. {ECO:0000305}.
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DR EMBL; AY899908; AAW82331.1; -; mRNA.
DR EMBL; AC006234; AAD20906.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07092.1; -; Genomic_DNA.
DR EMBL; AY062799; AAL32877.1; -; mRNA.
DR EMBL; AY081596; AAM10158.1; -; mRNA.
DR EMBL; AY087394; AAM64943.1; -; mRNA.
DR PIR; F84594; F84594.
DR RefSeq; NP_565491.1; NM_127659.4.
DR AlphaFoldDB; Q9SKT0; -.
DR SMR; Q9SKT0; -.
DR BioGRID; 1976; 5.
DR IntAct; Q9SKT0; 3.
DR STRING; 3702.AT2G20890.1; -.
DR iPTMnet; Q9SKT0; -.
DR PaxDb; Q9SKT0; -.
DR PRIDE; Q9SKT0; -.
DR ProteomicsDB; 234411; -.
DR EnsemblPlants; AT2G20890.1; AT2G20890.1; AT2G20890.
DR GeneID; 816623; -.
DR Gramene; AT2G20890.1; AT2G20890.1; AT2G20890.
DR KEGG; ath:AT2G20890; -.
DR Araport; AT2G20890; -.
DR TAIR; locus:2051353; AT2G20890.
DR eggNOG; ENOG502QUQV; Eukaryota.
DR HOGENOM; CLU_079763_0_1_1; -.
DR InParanoid; Q9SKT0; -.
DR OMA; MVEMHLL; -.
DR OrthoDB; 1385923at2759; -.
DR PhylomeDB; Q9SKT0; -.
DR PRO; PR:Q9SKT0; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SKT0; baseline and differential.
DR Genevisible; Q9SKT0; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0009707; C:chloroplast outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0009534; C:chloroplast thylakoid; HDA:TAIR.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0009528; C:plastid inner membrane; IDA:TAIR.
DR GO; GO:0009527; C:plastid outer membrane; IDA:TAIR.
DR GO; GO:0009532; C:plastid stroma; IDA:TAIR.
DR GO; GO:0010319; C:stromule; IDA:TAIR.
DR GO; GO:0015996; P:chlorophyll catabolic process; IMP:CACAO.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IMP:TAIR.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IPI:TAIR.
DR GO; GO:0010207; P:photosystem II assembly; TAS:TAIR.
DR GO; GO:1902458; P:positive regulation of stomatal opening; IMP:TAIR.
DR GO; GO:0045037; P:protein import into chloroplast stroma; IDA:TAIR.
DR GO; GO:0045038; P:protein import into chloroplast thylakoid membrane; IDA:TAIR.
DR GO; GO:1903426; P:regulation of reactive oxygen species biosynthetic process; IMP:TAIR.
DR GO; GO:2000070; P:regulation of response to water deprivation; IMP:TAIR.
DR GO; GO:0010182; P:sugar mediated signaling pathway; IMP:TAIR.
DR GO; GO:0010027; P:thylakoid membrane organization; IMP:TAIR.
DR HAMAP; MF_01843; Thf1; 1.
DR InterPro; IPR017499; Thf1.
DR PANTHER; PTHR34793; PTHR34793; 1.
DR Pfam; PF11264; ThylakoidFormat; 1.
DR TIGRFAMs; TIGR03060; PS_II_psb29; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Coiled coil; Membrane; Plastid; Plastid outer membrane;
KW Reference proteome; Transit peptide; Transmembrane; Transmembrane helix.
FT TRANSIT 1..67
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 68..300
FT /note="Protein THYLAKOID FORMATION 1, chloroplastic"
FT /id="PRO_0000235207"
FT TOPO_DOM 68..196
FT /note="Chloroplast intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 197..219
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 220..300
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT COILED 239..268
FT /evidence="ECO:0000255"
FT CONFLICT 254
FT /note="K -> N (in Ref. 1; AAW82331 and 5; AAM64943)"
FT /evidence="ECO:0000305"
FT CONFLICT 269
FT /note="G -> E (in Ref. 1; AAW82331 and 5; AAM64943)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 300 AA; 33796 MW; 3CC275DC2011FE47 CRC64;
MAATAISSLS FPALGQSDKI SNFASSRPLA SAIRICTKFS RLSLNSRSTS KSLIHCMSNV
TADVPPVSET KSKFLKAYKR PIPSIYNTVL QELIVQQHLM RYKKTYRYDP VFALGFVTVY
DQLMEGYPSD QDRDAIFKAY IEALNEDPKQ YRIDAQKMEE WARSQTSASL VDFSSKEGDI
EAVLKDIAGR AGSKEGFSYS RFFAVGLFRL LELASATDPT VLDKLCASLN INKKSVDRDL
DVYRNLLSKL VQAKELLKEY VEREKKKQGE RAQSQKANET ISKCLGDTLY NPSFLVERKS
