EM506_ARATH
ID EM506_ARATH Reviewed; 315 AA.
AC Q9SQK3;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Ankyrin repeat domain-containing protein EMB506, chloroplastic;
DE AltName: Full=Protein EMBRYO DEFECTIVE 506;
DE Flags: Precursor;
GN Name=EMB506; OrderedLocusNames=At5g40160; ORFNames=MSN9.60;
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].
RX PubMed=10074714; DOI=10.1046/j.1365-313x.1999.00361.x;
RA Albert S., Despres B., Guilleminot J., Bechtold N., Pelletier G.,
RA Delseny M., Devic M.;
RT "The EMB 506 gene encodes a novel ankyrin repeat containing protein that is
RT essential for the normal development of Arabidopsis embryos.";
RL Plant J. 17:169-179(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9679202; DOI=10.1093/dnares/5.2.131;
RA Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence
RT features of the regions of 1,381,565 bp covered by twenty one physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:131-145(1998).
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 FUNCTION, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, AND SUBCELLULAR
RP LOCATION.
RX PubMed=11489192; DOI=10.1046/j.1365-313x.2001.01078.x;
RA Despres B., Delseny M., Devic M.;
RT "Partial complementation of embryo defective mutations: a general strategy
RT to elucidate gene function.";
RL Plant J. 27:149-159(2001).
RN [6]
RP FUNCTION.
RX PubMed=16786300; DOI=10.1007/s11103-006-6268-6;
RA Latvala-Kilby S.M.H., Kilby N.J.;
RT "Uncovering the post-embryonic role of embryo essential genes in
RT Arabidopsis using the controlled induction of visibly marked genetic
RT mosaics: EMB506, an illustration.";
RL Plant Mol. Biol. 61:179-194(2006).
RN [7]
RP INTERACTION WITH AKR, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=17092312; DOI=10.1111/j.1365-313x.2006.02922.x;
RA Garcion C., Guilleminot J., Kroj T., Parcy F., Giraudat J., Devic M.;
RT "AKRP and EMB506 are two ankyrin repeat proteins essential for plastid
RT differentiation and plant development in Arabidopsis.";
RL Plant J. 48:895-906(2006).
CC -!- FUNCTION: Involved in the initial differentiation of the proplastid
CC during the embryo development. Also required for correct cotyledon,
CC true leaf and cauline leaf margin development.
CC {ECO:0000269|PubMed:11489192, ECO:0000269|PubMed:16786300}.
CC -!- SUBUNIT: Interacts with AKR. No homodimerization observed.
CC {ECO:0000269|PubMed:17092312}.
CC -!- INTERACTION:
CC Q9SQK3; Q05753: AKRP; NbExp=3; IntAct=EBI-2114010, EBI-2114020;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:11489192, ECO:0000269|PubMed:17092312}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, inflorescence stems, flowers,
CC siliques, dry seeds and mature cauline leaves.
CC {ECO:0000269|PubMed:11489192, ECO:0000269|PubMed:17092312}.
CC -!- DEVELOPMENTAL STAGE: Expressed during embryo development and after the
CC bolting stage, in mature culine leaves and in flowers. Not detected at
CC the protein level at the rosette stage of development.
CC {ECO:0000269|PubMed:11489192}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF026167; AAD55746.1; -; mRNA.
DR EMBL; AB010699; BAB10897.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94515.1; -; Genomic_DNA.
DR EMBL; AY063792; AAL36099.1; -; mRNA.
DR EMBL; AY117280; AAM51355.1; -; mRNA.
DR RefSeq; NP_198832.1; NM_123380.3.
DR PDB; 6JD6; X-ray; 2.20 A; A=41-315.
DR PDBsum; 6JD6; -.
DR AlphaFoldDB; Q9SQK3; -.
DR SMR; Q9SQK3; -.
DR BioGRID; 19265; 5.
DR IntAct; Q9SQK3; 4.
DR STRING; 3702.AT5G40160.1; -.
DR PaxDb; Q9SQK3; -.
DR PRIDE; Q9SQK3; -.
DR ProteomicsDB; 222322; -.
DR EnsemblPlants; AT5G40160.1; AT5G40160.1; AT5G40160.
DR GeneID; 834014; -.
DR Gramene; AT5G40160.1; AT5G40160.1; AT5G40160.
DR KEGG; ath:AT5G40160; -.
DR Araport; AT5G40160; -.
DR TAIR; locus:2173767; AT5G40160.
DR eggNOG; KOG0504; Eukaryota.
DR HOGENOM; CLU_069938_1_0_1; -.
DR InParanoid; Q9SQK3; -.
DR OMA; ISLCYGK; -.
DR OrthoDB; 1514637at2759; -.
DR PhylomeDB; Q9SQK3; -.
DR PRO; PR:Q9SQK3; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9SQK3; baseline and differential.
DR Genevisible; Q9SQK3; AT.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR DisProt; DP02919; -.
DR Gene3D; 1.25.40.20; -; 2.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR Pfam; PF12796; Ank_2; 1.
DR SMART; SM00248; ANK; 4.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 3.
PE 1: Evidence at protein level;
KW 3D-structure; ANK repeat; Chloroplast; Plastid; Reference proteome; Repeat;
KW Transit peptide.
FT TRANSIT 1..39
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 40..315
FT /note="Ankyrin repeat domain-containing protein EMB506,
FT chloroplastic"
FT /id="PRO_0000313815"
FT REPEAT 151..180
FT /note="ANK 1"
FT REPEAT 184..213
FT /note="ANK 2"
FT REPEAT 217..246
FT /note="ANK 3"
FT REPEAT 250..279
FT /note="ANK 4"
FT REPEAT 283..307
FT /note="ANK 5"
FT REGION 44..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..61
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..102
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 116..126
FT /evidence="ECO:0007829|PDB:6JD6"
FT HELIX 131..139
FT /evidence="ECO:0007829|PDB:6JD6"
FT TURN 145..147
FT /evidence="ECO:0007829|PDB:6JD6"
FT HELIX 155..161
FT /evidence="ECO:0007829|PDB:6JD6"
FT HELIX 165..173
FT /evidence="ECO:0007829|PDB:6JD6"
FT HELIX 188..194
FT /evidence="ECO:0007829|PDB:6JD6"
FT HELIX 198..206
FT /evidence="ECO:0007829|PDB:6JD6"
FT HELIX 221..227
FT /evidence="ECO:0007829|PDB:6JD6"
FT HELIX 231..239
FT /evidence="ECO:0007829|PDB:6JD6"
FT HELIX 254..260
FT /evidence="ECO:0007829|PDB:6JD6"
FT HELIX 264..272
FT /evidence="ECO:0007829|PDB:6JD6"
FT HELIX 287..292
FT /evidence="ECO:0007829|PDB:6JD6"
FT HELIX 300..309
FT /evidence="ECO:0007829|PDB:6JD6"
SQ SEQUENCE 315 AA; 35461 MW; B13F9C8D1850E714 CRC64;
MVSSVLSIPP QTCLLPRLPI SDSVNCKSKI VYCLSTSVRG SSVKRQSTAR TRSFTETNRR
TPSVQSKHEF WEDPDDGSDS ENEYEGEEED GIGNDLDNES DWEDDSRVQK LTTTDNYEEE
LAKEVEQLLE PEERVILQQN EKPNLKMIST KSWKPLQTLA LSMQIQLMDN LIENGLDIDD
VDKDNQTALH KAIIGKKEAV ISHLLRKGAN PHLQDRDGAA PIHYAVQVGA LQTVKLLFKY
NVDVNVADNE GWTPLHIAVQ SRNRDITKIL LTNGADKTRR TKDGKLALDL ALCFGRDFKS
YDLVKLLKIM PTGDI
