Entry euk:AKRP_ARATH

ID   AKRP_ARATH              Reviewed;         435 AA.
AC   Q05753; Q3E852; Q8GYN6; Q940Y0;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   13-DEC-2002, sequence version 2.
DT   12-APR-2017, entry version 130.
DE   RecName: Full=Ankyrin repeat domain-containing protein, chloroplastic;
DE            Short=AKRP;
DE   AltName: Full=Protein EMBRYO DEFECTIVE 2036;
DE   Flags: Precursor;
GN   Name=AKRP; Synonyms=AKR, EMB2036; OrderedLocusNames=At5g66055;
GN   ORFNames=K2A18.13;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION BY LIGHT.
RC   STRAIN=cv. Landsberg erecta; TISSUE=Leaf;
RX   PubMed=1281700; DOI=10.1105/tpc.4.12.1575;
RA   Zhang H., Scheirer D.C., Fowle W.H., Goodman H.M.;
RT   "Expression of antisense or sense RNA of an ankyrin repeat-containing
RT   gene blocks chloroplast differentiation in Arabidopsis.";
RL   Plant Cell 4:1575-1588(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), INTERACTION WITH
RP   EMB506, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND DISRUPTION
RP   PHENOTYPE.
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).
RN   [3]
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
RT   physically assigned P1 and TAC clones.";
RL   DNA Res. 5:131-145(1998).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RG   The Arabidopsis Information Portal (Araport);
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=cv. Columbia;
RX   PubMed=11910074; DOI=10.1126/science.1071006;
RA   Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA   Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M.,
RA   Hayashizaki Y., Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T.,
RA   Shibata K., Shinagawa A., Shinozaki K.;
RT   "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL   Science 296:141-145(2002).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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.,
RA   Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA   Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA   Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA   Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA   Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA   Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA   Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA   Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA   Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA   Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA   Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [7]
RP   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC   STRAIN=cv. C24;
RX   PubMed=12232406; DOI=10.1104/pp.106.4.1261;
RA   Zhang H., Wang J., Goodman H.M.;
RT   "Expression of the Arabidopsis gene Akr coincides with chloroplast
RT   development.";
RL   Plant Physiol. 106:1261-1267(1994).
CC   -!- FUNCTION: Involved in the initial differentiation of the
CC       proplastid during the embryo development and in plastid
CC       differentiation linked to cell differentiation, morphogenesis and
CC       organogenesis during the plant life cycle.
CC   -!- SUBUNIT: Interacts with EMB506. No homodimerization observed.
CC       {ECO:0000269|PubMed:17092312}.
CC   -!- INTERACTION:
CC       Q9SQK3:EMB506; NbExp=3; IntAct=EBI-2114020, EBI-2114010;
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC       {ECO:0000269|PubMed:17092312}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q05753-1; Sequence=Displayed;
CC         Note=Found predominantly in leaves and inflorescence stems.;
CC       Name=2;
CC         IsoId=Q05753-2; Sequence=VSP_030158, VSP_030159;
CC         Note=Found predominantly in flower buds and siliques. Seems to
CC         be unable to interact with EMB506.;
CC   -!- TISSUE SPECIFICITY: Expressed mainly in chloroplast-containing
CC       tissues. Also detected in roots, stems, flower buds, developing
CC       siliques and dry seeds. {ECO:0000269|PubMed:12232406,
CC       ECO:0000269|PubMed:17092312}.
CC   -!- DEVELOPMENTAL STAGE: Highest expression occurs in four-day-old
CC       plants and declines as plants develop further.
CC       {ECO:0000269|PubMed:12232406}.
CC   -!- INDUCTION: By light. {ECO:0000269|PubMed:1281700}.
CC   -!- DISRUPTION PHENOTYPE: Plants show a developmental arrest of the
CC       embryos at the globular stage. {ECO:0000269|PubMed:17092312}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA32812.1; Type=Frameshift; Positions=397; Evidence={ECO:0000305};
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DR   EMBL; M82883; AAA32812.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; AB011474; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CP002688; AED98151.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED98152.1; -; Genomic_DNA.
DR   EMBL; AK117484; BAC42148.1; -; mRNA.
DR   EMBL; AY052363; AAK96554.1; -; mRNA.
DR   EMBL; BT001055; AAN46809.1; -; mRNA.
DR   PIR; JQ1729; JQ1729.
DR   RefSeq; NP_569027.2; NM_126003.3. [Q05753-1]
DR   RefSeq; NP_975000.1; NM_203271.2. [Q05753-2]
DR   UniGene; At.68506; -.
DR   ProteinModelPortal; Q05753; -.
DR   SMR; Q05753; -.
DR   BioGrid; 21979; 1.
DR   IntAct; Q05753; 1.
DR   STRING; 3702.AT5G66055.1; -.
DR   iPTMnet; Q05753; -.
DR   PaxDb; Q05753; -.
DR   EnsemblPlants; AT5G66055.1; AT5G66055.1; AT5G66055. [Q05753-1]
DR   GeneID; 836737; -.
DR   Gramene; AT5G66055.1; AT5G66055.1; AT5G66055.
DR   KEGG; ath:AT5G66055; -.
DR   Araport; AT5G66055; -.
DR   TAIR; locus:505006718; AT5G66055.
DR   eggNOG; KOG0504; Eukaryota.
DR   eggNOG; COG0666; LUCA.
DR   HOGENOM; HOG000239703; -.
DR   InParanoid; Q05753; -.
DR   OMA; CLRLGHH; -.
DR   OrthoDB; EOG09360CBT; -.
DR   PhylomeDB; Q05753; -.
DR   Reactome; R-ATH-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
DR   Reactome; R-ATH-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR   Reactome; R-ATH-349425; Autodegradation of the E3 ubiquitin ligase COP1.
DR   Reactome; R-ATH-5632684; Hedgehog 'on' state.
DR   Reactome; R-ATH-5668541; TNFR2 non-canonical NF-kB pathway.
DR   Reactome; R-ATH-5687128; MAPK6/MAPK4 signaling.
DR   Reactome; R-ATH-5689603; UCH proteinases.
DR   Reactome; R-ATH-5689880; Ub-specific processing proteases.
DR   Reactome; R-ATH-68949; Orc1 removal from chromatin.
DR   Reactome; R-ATH-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR   Reactome; R-ATH-69229; Ubiquitin-dependent degradation of Cyclin D1.
DR   Reactome; R-ATH-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR   Reactome; R-ATH-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   PRO; PR:Q05753; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q05753; baseline and differential.
DR   Genevisible; Q05753; AT.
DR   GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR   Gene3D; 1.25.40.20; -; 2.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR020683; Ankyrin_rpt-contain_dom.
DR   Pfam; PF12796; Ank_2; 1.
DR   SMART; SM00248; ANK; 5.
DR   SUPFAM; SSF48403; SSF48403; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 2.
PE   1: Evidence at protein level;
KW   Alternative splicing; ANK repeat; Chloroplast; Complete proteome;
KW   Plastid; Reference proteome; Repeat; Transit peptide.
FT   TRANSIT       1     36       Chloroplast. {ECO:0000255}.
FT   CHAIN        37    435       Ankyrin repeat domain-containing protein,
FT                                chloroplastic.
FT                                /FTId=PRO_0000001621.
FT   REPEAT      259    288       ANK 1.
FT   REPEAT      292    321       ANK 2.
FT   REPEAT      325    354       ANK 3.
FT   REPEAT      358    387       ANK 4.
FT   REPEAT      391    424       ANK 5.
FT   VAR_SEQ     358    358       D -> V (in isoform 2).
FT                                {ECO:0000303|PubMed:17092312}.
FT                                /FTId=VSP_030158.
FT   VAR_SEQ     360    435       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:17092312}.
FT                                /FTId=VSP_030159.
FT   CONFLICT     16     16       R -> G (in Ref. 1; AAA32812).
FT                                {ECO:0000305}.
FT   CONFLICT     30     30       A -> V (in Ref. 1; AAA32812).
FT                                {ECO:0000305}.
FT   CONFLICT     73     73       D -> E (in Ref. 1; AAA32812).
FT                                {ECO:0000305}.
FT   CONFLICT    105    105       L -> P (in Ref. 5; BAC42148).
FT                                {ECO:0000305}.
FT   CONFLICT    146    146       P -> Q (in Ref. 5; BAC42148).
FT                                {ECO:0000305}.
FT   CONFLICT    181    181       S -> F (in Ref. 1; AAA32812).
FT                                {ECO:0000305}.
FT   CONFLICT    296    296       V -> A (in Ref. 1; AAA32812).
FT                                {ECO:0000305}.
FT   CONFLICT    406    406       I -> T (in Ref. 1; AAA32812).
FT                                {ECO:0000305}.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT       325    354       ismart:ANK [T]
FT   MYHIT       358    387       ismart:ANK [T]
FT   MYHIT       325    357       iprf:ANK_REPEAT [T]
FT   MYHIT       308    389       ipfam:Ank_2 [T]
FT   MYHIT       259    288       ismart:ANK [T]
FT   MYHIT       259    415       iprf:ANK_REP_REGION [T]
FT   MYHIT       292    321       ismart:ANK [T]
FT   MYHIT       358    390       iprf:ANK_REPEAT [T]
FT   MYHIT       391    424       ismart:ANK [T]
SQ   SEQUENCE   435 AA;  48878 MW;  DE306D487CC894EC CRC64;
     MQSLSTPHTI SLLLPRTSPS RLSPSLHSLA FPTRLRSLSY SSQTSILPDA GDDFIVGDCL
     VYEDGVFEDP YLDKEVTQVA KQERKKNRRG GAKRLDESEI EPENLVPEEW RDIQAEVNLT
     KKDKRKIAQE MEFGVRVEKK RQGLIPLRKV DLNDFLTYKE AKLAQLRPVI LDKPGNFSDD
     SGASSDGETA VSSPSERVAP KNPRWAVYGK GFDHVAKFFN SDKYDPSDKK SDGPRKLLSK
     EEKFMLNSRN PDLAVATSKK WLPLHTLAAC GEFYLVDSLL KHNLDINATD VGGLTVLHRA
     IIGKKQAITN YLLRESANPF VLDDEGATLM HYAVQTASAP TIKLLLLYNA DINAQDRDGW
     TPLHVAVQAR RSDIVKLLLI KGADIEVKNK DGLTPLGLCL YLGREIRTYE VMKLLKEFPL
     SRHKKRLVTT DEDIE
//