RETIC_ARATH
ID RETIC_ARATH Reviewed; 432 AA.
AC B9DFK5; C0Z2Z2; Q8RXC6;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Protein RETICULATA, chloroplastic {ECO:0000303|PubMed:16873448};
DE AltName: Full=Protein LOWER CELL DENSITY 1 {ECO:0000303|PubMed:12848826};
DE Flags: Precursor;
GN Name=RE {ECO:0000303|PubMed:16873448};
GN Synonyms=LCD1 {ECO:0000303|PubMed:12848826};
GN OrderedLocusNames=At2g37860 {ECO:0000312|Araport:AT2G37860};
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=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 [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] (ISOFORM 2).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12848826; DOI=10.1046/j.1365-313x.2003.01795.x;
RA Barth C., Conklin P.L.;
RT "The lower cell density of leaf parenchyma in the Arabidopsis thaliana
RT mutant lcd1-1 is associated with increased sensitivity to ozone and
RT virulent Pseudomonas syringae.";
RL Plant J. 35:206-218(2003).
RN [6]
RP FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP PRO-295 AND GLY-328.
RX PubMed=16873448; DOI=10.1093/jxb/erl063;
RA Gonzalez-Bayon R., Kinsman E.A., Quesada V., Vera A., Robles P.,
RA Ponce M.R., Pyke K.A., Micol J.L.;
RT "Mutations in the RETICULATA gene dramatically alter internal architecture
RT but have little effect on overall organ shape in Arabidopsis leaves.";
RL J. Exp. Bot. 57:3019-3031(2006).
RN [7]
RP FUNCTION, DEVELOPMENTAL STAGE, GENE FAMILY, NOMENCLATURE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=23596191; DOI=10.1104/pp.113.217323;
RA Perez-Perez J.M., Esteve-Bruna D., Gonzalez-Bayon R., Kangasjarvi S.,
RA Caldana C., Hannah M.A., Willmitzer L., Ponce M.R., Micol J.L.;
RT "Functional redundancy and divergence within the Arabidopsis RETICULATA-
RT RELATED gene family.";
RL Plant Physiol. 162:589-603(2013).
CC -!- FUNCTION: May play a role in leaf development. Required for leaf
CC mesophyll cell division in the early stages of leaf organogenesis
CC (PubMed:12848826, PubMed:16873448). Acts in a developmental pathway
CC that involves PPT1/CUE1 but does not include ASE2/DOV1
CC (PubMed:16873448). {ECO:0000269|PubMed:12848826,
CC ECO:0000269|PubMed:16873448}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast membrane
CC {ECO:0000250|UniProtKB:Q9C9Z2}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=B9DFK5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=B9DFK5-2; Sequence=VSP_057777;
CC -!- TISSUE SPECIFICITY: Highly expressed in the vasculature of developing
CC leaf primordia, margins of fully expanded leaves, hydathodes of rosette
CC of cauline leaves, basal region of the lamina, stipules, root tips,
CC stamens and in the abscission zone of the funiculus.
CC {ECO:0000269|PubMed:16873448}.
CC -!- DEVELOPMENTAL STAGE: During embryo development, expressed from torpedo
CC stage onwards. {ECO:0000269|PubMed:23596191}.
CC -!- DISRUPTION PHENOTYPE: Pale interveinal phenotype due to marked
CC reduction in the density of mesophyll cells in interveinal regions of
CC leaves (PubMed:12848826, PubMed:16873448). Increased sensitivity to
CC ozone and a virulent strain of the bacterial pathogen Pseudomonas
CC syringae pv. maculicola (PubMed:12848826).
CC {ECO:0000269|PubMed:12848826, ECO:0000269|PubMed:16873448}.
CC -!- SIMILARITY: Belongs to the RETICULATA family. {ECO:0000305}.
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DR EMBL; CP002685; AEC09457.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09458.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09459.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM61867.1; -; Genomic_DNA.
DR EMBL; AY081345; AAL91234.1; -; mRNA.
DR EMBL; BT002153; AAN72164.1; -; mRNA.
DR EMBL; AK316808; BAH19522.1; -; mRNA.
DR EMBL; AK318956; BAH57071.1; -; mRNA.
DR RefSeq; NP_001031506.1; NM_001036429.2. [B9DFK5-1]
DR RefSeq; NP_001324059.1; NM_001336677.1. [B9DFK5-1]
DR RefSeq; NP_850287.1; NM_179956.2. [B9DFK5-2]
DR RefSeq; NP_850288.2; NM_179957.3. [B9DFK5-2]
DR AlphaFoldDB; B9DFK5; -.
DR STRING; 3702.AT2G37860.3; -.
DR PaxDb; B9DFK5; -.
DR PRIDE; B9DFK5; -.
DR ProteomicsDB; 234673; -. [B9DFK5-1]
DR EnsemblPlants; AT2G37860.1; AT2G37860.1; AT2G37860. [B9DFK5-2]
DR EnsemblPlants; AT2G37860.2; AT2G37860.2; AT2G37860. [B9DFK5-2]
DR EnsemblPlants; AT2G37860.3; AT2G37860.3; AT2G37860. [B9DFK5-1]
DR EnsemblPlants; AT2G37860.4; AT2G37860.4; AT2G37860. [B9DFK5-1]
DR GeneID; 818362; -.
DR Gramene; AT2G37860.1; AT2G37860.1; AT2G37860. [B9DFK5-2]
DR Gramene; AT2G37860.2; AT2G37860.2; AT2G37860. [B9DFK5-2]
DR Gramene; AT2G37860.3; AT2G37860.3; AT2G37860. [B9DFK5-1]
DR Gramene; AT2G37860.4; AT2G37860.4; AT2G37860. [B9DFK5-1]
DR KEGG; ath:AT2G37860; -.
DR Araport; AT2G37860; -.
DR TAIR; locus:2065649; AT2G37860.
DR eggNOG; ENOG502QPQK; Eukaryota.
DR HOGENOM; CLU_036961_1_0_1; -.
DR InParanoid; B9DFK5; -.
DR OMA; RFQRAYG; -.
DR OrthoDB; 1460743at2759; -.
DR PhylomeDB; B9DFK5; -.
DR PRO; PR:B9DFK5; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; B9DFK5; baseline and differential.
DR Genevisible; B9DFK5; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0031969; C:chloroplast membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0009658; P:chloroplast organization; IMP:TAIR.
DR GO; GO:0048366; P:leaf development; IMP:TAIR.
DR GO; GO:0009648; P:photoperiodism; IMP:TAIR.
DR GO; GO:0099402; P:plant organ development; IBA:GO_Central.
DR GO; GO:0000302; P:response to reactive oxygen species; IMP:TAIR.
DR InterPro; IPR021825; RETICULATA-related.
DR Pfam; PF11891; RETICULATA-like; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chloroplast; Developmental protein; Membrane;
KW Plastid; Reference proteome; Transit peptide; Transmembrane;
KW Transmembrane helix.
FT TRANSIT 1..47
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 48..432
FT /note="Protein RETICULATA, chloroplastic"
FT /evidence="ECO:0000255"
FT /id="PRO_0000433439"
FT TRANSMEM 249..269
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 322..342
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 109..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 348..432
FT /note="Missing (in isoform 2)"
FT /id="VSP_057777"
FT MUTAGEN 295
FT /note="P->L: In re-4; pale interveinal phenotype."
FT /evidence="ECO:0000269|PubMed:16873448"
FT MUTAGEN 328
FT /note="G->R: In re-3; pale interveinal phenotype."
FT /evidence="ECO:0000269|PubMed:16873448"
FT CONFLICT 137
FT /note="G -> S (in Ref. 4; BAH57071)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 432 AA; 46629 MW; DFA39C6AEBBB56F6 CRC64;
MAGCAMNLQF SSVVKVRNEI SSFGICNRDF VFRDLAKAMK VPVLRIRGGS GRQRSRLFVV
NMSQSPIEPQ SGGFAATEQI KGEGDNSILG KDNVRNLGTD QLENLDIDGN VGDGFNGSDG
NGGGGGGGNG GEGDGEGEDY EEKEFGPILK FEEVMKETEA RGATLPSDML EAAKNYGIRK
VLLLRYLDLQ SSAGLLGFAI RSWAMLRNRM LADPSFLFKI GAEIVIDSCC ATVAEVQKRG
KDFWAEFELY VADLLVGTVV NIALVGMLAP YVRFGQPSAS PGFLGRMVFA YNALPSSVFE
AERPGCRFSA QQRLATYFYK GIMYGAVGFG CGIVGQGIAN LIMTAKRNIN KSEENIPVPP
LIKSAALWGV FLSVSSNTRY QIINGLERVV EASPFAKKFP PAAMAFTVGV RLANNIYGGM
QFVDWARLSG CQ
