REC1_ARATH
ID REC1_ARATH Reviewed; 1797 AA.
AC F4HS99; Q8H2C0; Q9LNJ1;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 25-MAY-2022, entry version 69.
DE RecName: Full=Protein REDUCED CHLOROPLAST COVERAGE 1 {ECO:0000303|PubMed:26862170};
GN Name=REC1 {ECO:0000303|PubMed:26862170};
GN OrderedLocusNames=At1g01320 {ECO:0000312|Araport:AT1G01320};
GN ORFNames=F6F3.12 {ECO:0000312|EMBL:AEE27271.1};
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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] OF 1279-1797.
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 [4]
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, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
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: 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 (By similarity). 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:0000250|UniProtKB:F4JKH6, ECO:0000269|PubMed:26862170}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768,
CC ECO:0000269|PubMed:26862170}. Cytoplasm, cytosol
CC {ECO:0000269|PubMed:26862170}. Note=Excluded from the nucleus upon
CC treatment with amitrole, which inhibits cell expansion and chloroplast
CC function. {ECO:0000269|PubMed:26862170}.
CC -!- DISRUPTION PHENOTYPE: Reduced proportion of the cellular volume devoted
CC to chloroplasts leading to an abnormal chloroplasts distributions
CC (PubMed:26862170). Inhibited far-red block of seedlings greening
CC associated with reduced levels of chlorophyll and chlorophyll a/b-
CC binding proteins of photosystem II (e.g. Lhcb1.2) (PubMed:26862170).
CC Lower levels of chlorophyll, especially in plants lacking REC1, REC2,
CC REC3 and FMT/CLU (PubMed:26862170). {ECO:0000269|PubMed:26862170}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF97330.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC023628; AAF97330.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE27271.1; -; Genomic_DNA.
DR EMBL; AY080760; AAN16486.1; -; mRNA.
DR PIR; E86143; E86143.
DR RefSeq; NP_171639.3; NM_100014.8.
DR AlphaFoldDB; F4HS99; -.
DR SMR; F4HS99; -.
DR STRING; 3702.AT1G01320.1; -.
DR PaxDb; F4HS99; -.
DR PRIDE; F4HS99; -.
DR ProteomicsDB; 202182; -.
DR EnsemblPlants; AT1G01320.1; AT1G01320.1; AT1G01320.
DR EnsemblPlants; AT1G01320.3; AT1G01320.3; AT1G01320.
DR GeneID; 839293; -.
DR Gramene; AT1G01320.1; AT1G01320.1; AT1G01320.
DR Gramene; AT1G01320.3; AT1G01320.3; AT1G01320.
DR Araport; AT1G01320; -.
DR TAIR; locus:2035327; AT1G01320.
DR eggNOG; KOG1839; Eukaryota.
DR InParanoid; F4HS99; -.
DR OMA; VPTIAPW; -.
DR OrthoDB; 60958at2759; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; F4HS99; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0005576; C:extracellular region; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0019750; P:chloroplast localization; IMP:UniProtKB.
DR GO; GO:0006996; P:organelle organization; IEA:InterPro.
DR GO; GO:0010906; P:regulation of glucose metabolic process; IMP:TAIR.
DR CDD; cd15466; CLU-central; 1.
DR Gene3D; 1.25.40.10; -; 2.
DR InterPro; IPR033646; CLU-central.
DR InterPro; IPR025697; CLU_dom.
DR InterPro; IPR028275; CLU_N.
DR InterPro; IPR027523; CLU_prot.
DR InterPro; IPR023231; GSKIP_dom_sf.
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; SSF103107; SSF103107; 1.
DR SUPFAM; SSF48452; SSF48452; 1.
DR PROSITE; PS51823; CLU; 1.
DR PROSITE; PS50005; TPR; 3.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Nucleus; Reference proteome; Repeat; TPR repeat.
FT CHAIN 1..1797
FT /note="Protein REDUCED CHLOROPLAST COVERAGE 1"
FT /id="PRO_0000453545"
FT DOMAIN 304..573
FT /note="Clu"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01167"
FT REPEAT 880..913
FT /note="TPR 1"
FT /evidence="ECO:0000255"
FT REPEAT 922..955
FT /note="TPR 2"
FT /evidence="ECO:0000255"
FT REPEAT 964..997
FT /note="TPR 3"
FT /evidence="ECO:0000255"
FT REPEAT 1006..1039
FT /note="TPR 4"
FT /evidence="ECO:0000255"
FT REPEAT 1048..1081
FT /note="TPR 5"
FT /evidence="ECO:0000255"
FT REGION 124..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 565..634
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1166..1273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1341..1384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1423..1442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 805..812
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT COMPBIAS 124..155
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 565..587
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 598..634
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1166..1186
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1221..1239
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1341..1356
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1370..1384
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1797 AA; 198774 MW; 98712B124C391850 CRC64;
MAPKNNRGKT KGDKKKKEEK VLPVIVDVIV NLPDETEAIL KGISTDRIID VRRLLSVNFD
TCHVTNYSLS HEIRGSRLKD TVDVSALKPC VLTLTEEDYN EGTAVAHVRR LLDIVACTTC
FGPSPEKSDS VKSAQVKGGG KNSKQSDTSP PPSPASKDTV VDEAGETSHS FPKLGSFYEF
FSLAHLTPPL QYIRLATKRE TEDIAKEDHL LSIDVKLCNG KLVHIEGCRK GFYSIGKQRI
ICHNLVDLLR QISRAFDNAY SDLLKAFSER NKFGNLPYGF RANTWLIPPT AAQSPAAFPP
LPVEDERWGG DGGGQGRDGS YDLVPWSNEF AFIASMPCKT AEERQVRDRK VFLLHNLFVD
VATFRAIKAV QKVMAEPVLA EEDSEVLYSE TVRDLTVTVT RDTSNASSKV DTKIDGIQAT
GLDKKKLMER NLLKGLTADE NTAAHDVATL GTISLKYCGY IAVVKLEKES EELSPPSQIV
DLLEQPEGGA NALNINSLRF LLHKSSPEQN KKTPQQHDDE LTSSREFVSK MLEESIAKLE
GEEIDRDSIM RWELGACWIQ HLQDQKNTEK DKKQTGEKSK NELKVEGLGK PLKSLNSSKK
KTDVSSPKTP QTALSSQVDA VSSEADTAAS LQSDAEKNAQ ENVLILKNLL SDAAFTRLKE
SDTGLHHKSL QELVDLAQNY YTEVAIPKLV ADFGSLELSP VDGRTLTDFM HTRGLRMRSL
GYVVKLSDKL SHVQSLCVHE MIVRALKHIL QAVISAVATD TDKIAIKVAA ALNMMLGIPE
NVAATPHNPW NVHPLIFRWL EKFLKKRYDY DLNAFSYKDL RKFAILRGLC HKVGIELIPR
DFDMDSPAPF RKTDVVSLVP VHKTFYFKSM QQAACSSADG RQLLESSKTA LDKGKLEDAV
TYGTKALAKL VAVCGPYHRM TAGAYSLLAV VLYHTGDFNQ ATIYQQKALD INERELGLDH
PDTMKSYGDL AVFYYRLQHT ELALKYVKRA LYLLHLTCGP SHPNTAATYI NVAMMEEGLG
NVHVALRYLH KALKCNQRLL GPDHIQTAAS YHAIAIALSL MEAYHLSVQH EQTTLRILRA
KLGPDDLRTQ DAAAWLEYFE SKAFEQQEAA RNGTPKPDAS IASKGHLSVS DLLDYINPSH
NAKGKESVAA KRKNYILKLK EKSKQSNVSE HLVEIPREKQ KEMSEEDTEE TGSEEGKSSE
ENHETILAPV EEPPSPPVIE DATMDNSNPI TSSDVSTEPQ HPDGSEDGWQ PVQRPRSAGS
YGRRMKQRRA SIGKVYTYQK KNVEADIDNP LFQNATQQND KYYILKKRTA SYSSYADHHS
PGLTTQGTKF GRKIVKTLAY RVKSTQPSSG NAKTAGETSE EDGLKTDASS VEPPTLSSTV
QSEAYHTKNS VVSLGKSPSY KEVALAPPGS IAKYQVWVPQ AEVSDKQEDD EMEKKTEQGT
SMELTRDEQM ITGLEEEVKK EISADPESNI TQGEEEIKVE LQPSEGVLGG SHINENDESG
GGIQVEEQVE VELINDGVTD MIHSTREQQV IDQLAADSED LKAKLSISTT DSGDASRGLL
PNKKLSASAA PFNPSSPPSI IRPTPIGMNI GPSWPVNMTL HHGPPPPYPS PPTTPNLMQP
MSFVYPPPYS QSVPTSTYPV TSGPFHPNQF PWQLNVSDFV PRTVWPGCHP VEFPPPHMIT
EPIAATVLEP TVILPTDIDT SGVEETKEGT QDVAVADEVM DSVNHVNNAV ARSETENGNR
KSEEGEKTFS ILLRGRRNRK QTLRMPISLL NRPYDSQPFK LGYSRVIRDS EAPKSVA
