REC2_ARATH
ID REC2_ARATH Reviewed; 1819 AA.
AC F4JKH6; Q9SUD1;
DT 22-JUL-2015, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 25-MAY-2022, entry version 68.
DE RecName: Full=Protein REDUCED CHLOROPLAST COVERAGE 2 {ECO:0000303|PubMed:26862170};
DE AltName: Full=Protein TPR-domain suppressor of STIMPY {ECO:0000303|PubMed:21185286};
GN Name=REC2 {ECO:0000303|PubMed:26862170};
GN Synonyms=TSS {ECO:0000303|PubMed:21185286};
GN OrderedLocusNames=At4g28080 {ECO:0000312|Araport:AT4G28080};
GN ORFNames=T13J8.190 {ECO:0000312|EMBL:CAB36777.1};
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1244 AND SER-1320, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [5]
RP FUNCTION, INDUCTION BY SUCROSE, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=21185286; DOI=10.1016/j.ydbio.2010.12.019;
RA Skylar A., Sung F., Hong F., Chory J., Wu X.;
RT "Metabolic sugar signal promotes Arabidopsis meristematic proliferation via
RT G2.";
RL Dev. Biol. 351:82-89(2011).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=26862170; DOI=10.1073/pnas.1515741113;
RA Larkin R.M., Stefano G., Ruckle M.E., Stavoe A.K., Sinkler C.A.,
RA Brandizzi F., Malmstrom C.M., Osteryoung K.W.;
RT "REDUCED CHLOROPLAST COVERAGE genes from Arabidopsis thaliana help to
RT establish the size of the chloroplast compartment.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:E1116-E1125(2016).
CC -!- FUNCTION: Negatively regulates meristematic tissue proliferation by
CC integrating developmental signals with carbon source availability
CC (PubMed:21185286). May act as the scaffold of a protein complex, which
CC sequesters key factors that are required for the G2 to M transition in
CC meristematic tissues (PubMed:21185286). Together with REC2, REC3 and
CC FMT/CLU, contributes to the establishment of the cellular volume
CC devoted to the chloroplast compartment (PubMed:26862170).
CC {ECO:0000269|PubMed:21185286, ECO:0000269|PubMed:26862170}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:F4HS99}.
CC Cytoplasm, cytosol {ECO:0000250|UniProtKB:F4HS99}.
CC -!- TISSUE SPECIFICITY: Expressed in the non-epidermal tissues of the true
CC leaves (PubMed:21185286). Not detected in the vegetative shoot meristem
CC and leaf primordia (PubMed:21185286). {ECO:0000269|PubMed:21185286}.
CC -!- INDUCTION: Down-regulated by sucrose. {ECO:0000269|PubMed:21185286}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype (PubMed:21185286). Reduced
CC proportion of the cellular volume devoted to chloroplasts leading to an
CC abnormal chloroplasts distributions (PubMed:26862170). Lower levels of
CC chlorophyll, especially in plants lacking REC1, REC2, REC3 and FMT/CLU
CC (PubMed:26862170). {ECO:0000269|PubMed:21185286,
CC ECO:0000269|PubMed:26862170}.
CC -!- MISCELLANEOUS: The sucrose repression of TSS is a response specific to
CC the rescue of stip mutants, and the presence of STIP in the wild-type
CC may be sufficient to repress TSS expression even under sugar
CC deprivation. {ECO:0000303|PubMed:21185286}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB36777.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB79610.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL035524; CAB36777.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161572; CAB79610.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE85436.1; -; Genomic_DNA.
DR PIR; T02909; T02909.
DR RefSeq; NP_194537.7; NM_118947.8.
DR AlphaFoldDB; F4JKH6; -.
DR SMR; F4JKH6; -.
DR STRING; 3702.AT4G28080.1; -.
DR iPTMnet; F4JKH6; -.
DR PaxDb; F4JKH6; -.
DR PRIDE; F4JKH6; -.
DR ProteomicsDB; 234652; -.
DR EnsemblPlants; AT4G28080.1; AT4G28080.1; AT4G28080.
DR GeneID; 828923; -.
DR Gramene; AT4G28080.1; AT4G28080.1; AT4G28080.
DR KEGG; ath:AT4G28080; -.
DR Araport; AT4G28080; -.
DR TAIR; locus:2133012; AT4G28080.
DR eggNOG; KOG1839; Eukaryota.
DR HOGENOM; CLU_001902_0_0_1; -.
DR InParanoid; F4JKH6; -.
DR OMA; CTEQINK; -.
DR OrthoDB; 60958at2759; -.
DR PRO; PR:F4JKH6; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; F4JKH6; baseline and differential.
DR Genevisible; F4JKH6; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0019750; P:chloroplast localization; IMP:UniProtKB.
DR GO; GO:0006996; P:organelle organization; IEA:InterPro.
DR CDD; cd15466; CLU-central; 1.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR033646; CLU-central.
DR InterPro; IPR025697; CLU_dom.
DR InterPro; IPR028275; CLU_N.
DR InterPro; IPR027523; CLU_prot.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR12601; PTHR12601; 1.
DR Pfam; PF15044; CLU_N; 1.
DR Pfam; PF12807; eIF3_p135; 1.
DR SMART; SM00028; TPR; 3.
DR SUPFAM; SSF48452; SSF48452; 2.
DR PROSITE; PS51823; CLU; 1.
DR PROSITE; PS50005; TPR; 3.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Coiled coil; Cytoplasm; Developmental protein; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; TPR repeat.
FT CHAIN 1..1819
FT /note="Protein REDUCED CHLOROPLAST COVERAGE 2"
FT /id="PRO_0000433608"
FT DOMAIN 329..603
FT /note="Clu"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01167"
FT REPEAT 892..925
FT /note="TPR 1"
FT /evidence="ECO:0000255"
FT REPEAT 934..967
FT /note="TPR 2"
FT /evidence="ECO:0000255"
FT REPEAT 976..1009
FT /note="TPR 3"
FT /evidence="ECO:0000255"
FT REPEAT 1018..1051
FT /note="TPR 4"
FT /evidence="ECO:0000255"
FT REPEAT 1060..1093
FT /note="TPR 5"
FT /evidence="ECO:0000255"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 128..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 595..619
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 634..664
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1152..1360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1413..1456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1468..1513
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1527..1573
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1616..1670
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1731..1809
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 649..680
FT /evidence="ECO:0000255"
FT COMPBIAS 134..155
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1198..1240
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1259..1335
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1342..1358
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1415..1436
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1479..1513
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1535..1549
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1643..1665
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1744..1763
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1769..1785
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1786..1800
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1244
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT MOD_RES 1320
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
SQ SEQUENCE 1819 AA; 199116 MW; 9408FDDF8B1DEF8B CRC64;
MAPKAGKTKP HKSKGEKKKK EEKVLPTVIE ISVETPDESQ VTLKGISTDR ILDVRKLLAV
HVQTCHFTNF SLSHQVRGTK LKDSVDIVSL KPCHLTIVEE DYTEEQATAH IRRLLDIVAC
TTAFGPSKPP VSRTLPKDSE KKESGSTDGD SPTEKDAGDS NSGLSPKPKE SEKKSVGACE
AQSAEGAAKS DIDMCPPTRL GQFYEFFSFS YLTPPIQYIR RSVRPSKEDK GLDDLFQIDI
KVSSGKPFTV VASRTGFYPP GKQQLLCHSL VELLQQISRP FDAAYDALMK AFIEHNKFGN
LPYGFRANTW VVPPVVADSP STFPSLPVED ETWGGDGGGV GRSGKYDKRK WAKEFAILAA
MPCKTPEERQ VRDRKAFLLH SLFVDVSVFK AVEIIKKIVE NNQCSLKDPA ALGFHEERIG
DLIVRVARDD PDASAKLDRK SDGTQVLEIS QEELAQRNLL KGITADESAT VHDTSTLGVV
VVRHCGCTAI VKVASEFKLN DGHILQDIDI EDQSEGGANA LNVNSLRTLL HKSSTPSSLA
QRSPNADSEQ IRVAKSLVRK VIEDSLKKLE IEPSRYSKPI RWELGACWVQ HLQNQASSKS
ESKKTEDPKP EPAVKGLGKQ GALLKEIKRK IDVKANKTEQ GKEAPANDTD NTSETEDQKE
LEKQNEEIEK MWKELVTETA YQRLKESETG FHLKSPKELI EMARKYYTDT ALPKLVADFG
SLELSPVDGR TLTDFMHTRG LQMHSLGRVV ELAEKLPHVQ SLCVHEMIVR AYKHILQAVV
AAVENTADVA TSIATCLNVL LGTPSDTESV YDEKIKWTWV ETFISKRFGW DWKHEGCQEL
RKFSILRGLS HKVGLELVPK DYEMDTSYPF KKFDIISMVP VYKHVACSSA DGRTLLESSK
TSLDKGKLED AVNYGTKALA KLVAVCGPYH RMTAGAYSLL AVVLYHTGDF NQATIYQQKA
LDINERELGL DHPDTMKSYG DLAVFYYRLQ HTELALKYVN RALYLLHLTC GPSHPNTAAT
YINVAMMEEG MKNAHVALRY LHEALKCNQR LLGADHIQTA ASYHAIAIAL SLMDAYSLSV
QHEQTTLQIL QAKLGPEDLR TQDAAAWLEY FESKALEQQE AARNGTPKPD ASISSKGHLS
VSDLLDYITP DSGIKARDAQ RKARPKVKGK PGQSPGPVSE ENQKDDEILS PAHLTGESSS
DKENKSETKS EEKKVENFDL EQSKPQDQLK LVKPEATVHE DDDSDEGWQE AVPKNRFSSG
RRTRPSLAKL NTNFMNVTQQ PSRSRGKSTN FTSPRTSSNE LSISVAGSTS SPASKMFVKS
PLNKKQNNSS VVGERPVNDK SALASSACTE QINKPTPMLS PVSVKAGKLF SYKEVALAPP
GTIVKIVAEQ LPEETKAPQN LDAAKIAVDG PEKVNAQDAE SENKHVATET EAENTDCNEQ
GRVVVGGSEL TSSPKEIKNV EVEKAAEKAF PIETAVSNAR PGKSKSAQMA EDSDTCLLNK
SPTANDSNGS ESVIGVKLQK DLCDAELKTV DGETENLPNG DSSPKSSVAA DGEKQDACEA
QKEMSKKLSA SAPPYTPTTI PIFGSIAVPG FKDHGGILPS PLNMPPMLPI NHVRRSTPHQ
SVTARVPYGP RLSGGGYNRS GNRVPRNKPS FPNSTESNGE ANQFNGPRIM NPHAAEFIPS
QPWVSNGYPV SPNGYLASPN GAEITQNGYP LSPVAGGYPC NMSVTQPQDG LVSEELPGAG
SSEEKSGSEE ESNNDKNAGE DDEAVGQETT DTPENGHSTV GEVETTSHET CDEKNGERQG
GKCWGDYSDN EIEQIEVTS
