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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   03-AUG-2022, entry version 157.
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; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; 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=10.2307/3869500;
RA   Zhang H., Scheirer D.C., Fowle W.H., Goodman H.M.;
RT   "Expression of antisense or sense RNA of an ankyrin repeat-containing gene
RT   blocks chloroplast differentiation in Arabidopsis.";
RL   Plant Cell 4:1575-1588(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), INTERACTION WITH EMB506,
RP   TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND DISRUPTION 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 physically
RT   assigned P1 and TAC clones.";
RL   DNA Res. 5:131-145(1998).
RN   [4]
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   [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., Hayashizaki Y.,
RA   Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA   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., 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   [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 proplastid
CC       during the embryo development and in plastid differentiation linked to
CC       cell differentiation, morphogenesis and organogenesis during the plant
CC       life cycle.
CC   -!- SUBUNIT: Interacts with EMB506. No homodimerization observed.
CC       {ECO:0000269|PubMed:17092312}.
CC   -!- INTERACTION:
CC       Q05753; 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       Name=2;
CC         IsoId=Q05753-2; Sequence=VSP_030158, VSP_030159;
CC   -!- TISSUE SPECIFICITY: Expressed mainly in chloroplast-containing tissues.
CC       Also detected in roots, stems, flower buds, developing siliques and dry
CC       seeds. {ECO:0000269|PubMed:12232406, ECO:0000269|PubMed:17092312}.
CC   -!- DEVELOPMENTAL STAGE: Highest expression occurs in four-day-old plants
CC       and declines as plants develop further. {ECO:0000269|PubMed:12232406}.
CC   -!- INDUCTION: By light. {ECO:0000269|PubMed:1281700}.
CC   -!- DISRUPTION PHENOTYPE: Plants show a developmental arrest of the embryos
CC       at the globular stage. {ECO:0000269|PubMed:17092312}.
CC   -!- MISCELLANEOUS: [Isoform 1]: Found predominantly in leaves and
CC       inflorescence stems.
CC   -!- MISCELLANEOUS: [Isoform 2]: Found predominantly in flower buds and
CC       siliques. Seems to be unable to interact with EMB506. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA32812.1; Type=Frameshift; 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   PDB; 6JD6; X-ray; 2.20 A; B=37-435.
DR   PDBsum; 6JD6; -.
DR   AlphaFoldDB; Q05753; -.
DR   SMR; Q05753; -.
DR   BioGRID; 21979; 1.
DR   IntAct; Q05753; 1.
DR   STRING; 3702.AT5G66055.1; -.
DR   iPTMnet; Q05753; -.
DR   PaxDb; Q05753; -.
DR   PRIDE; Q05753; -.
DR   ProteomicsDB; 244891; -. [Q05753-1]
DR   EnsemblPlants; AT5G66055.1; AT5G66055.1; AT5G66055. [Q05753-1]
DR   EnsemblPlants; AT5G66055.2; AT5G66055.2; AT5G66055. [Q05753-2]
DR   GeneID; 836737; -.
DR   Gramene; AT5G66055.1; AT5G66055.1; AT5G66055. [Q05753-1]
DR   Gramene; AT5G66055.2; AT5G66055.2; AT5G66055. [Q05753-2]
DR   KEGG; ath:AT5G66055; -.
DR   Araport; AT5G66055; -.
DR   TAIR; locus:505006718; AT5G66055.
DR   eggNOG; KOG0504; Eukaryota.
DR   HOGENOM; CLU_048352_0_0_1; -.
DR   InParanoid; Q05753; -.
DR   OMA; EDHVIGD; -.
DR   PhylomeDB; Q05753; -.
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   DisProt; DP02920; -.
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; 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   3D-structure; Alternative splicing; ANK repeat; Chloroplast; Plastid;
KW   Reference proteome; Repeat; Transit peptide.
FT   TRANSIT         1..36
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           37..435
FT                   /note="Ankyrin repeat domain-containing protein,
FT                   chloroplastic"
FT                   /id="PRO_0000001621"
FT   REPEAT          259..288
FT                   /note="ANK 1"
FT   REPEAT          292..321
FT                   /note="ANK 2"
FT   REPEAT          325..354
FT                   /note="ANK 3"
FT   REPEAT          358..387
FT                   /note="ANK 4"
FT   REPEAT          391..424
FT                   /note="ANK 5"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          175..199
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        178..196
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         358
FT                   /note="D -> V (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:17092312"
FT                   /id="VSP_030158"
FT   VAR_SEQ         360..435
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:17092312"
FT                   /id="VSP_030159"
FT   CONFLICT        16
FT                   /note="R -> G (in Ref. 1; AAA32812)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        30
FT                   /note="A -> V (in Ref. 1; AAA32812)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        73
FT                   /note="D -> E (in Ref. 1; AAA32812)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        105
FT                   /note="L -> P (in Ref. 5; BAC42148)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        146
FT                   /note="P -> Q (in Ref. 5; BAC42148)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        181
FT                   /note="S -> F (in Ref. 1; AAA32812)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        296
FT                   /note="V -> A (in Ref. 1; AAA32812)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        406
FT                   /note="I -> T (in Ref. 1; AAA32812)"
FT                   /evidence="ECO:0000305"
FT   HELIX           234..237
FT                   /evidence="ECO:0007829|PDB:6JD6"
FT   HELIX           240..246
FT                   /evidence="ECO:0007829|PDB:6JD6"
FT   TURN            253..256
FT                   /evidence="ECO:0007829|PDB:6JD6"
FT   HELIX           263..269
FT                   /evidence="ECO:0007829|PDB:6JD6"
FT   HELIX           273..279
FT                   /evidence="ECO:0007829|PDB:6JD6"
FT   HELIX           296..302
FT                   /evidence="ECO:0007829|PDB:6JD6"
FT   HELIX           306..314
FT                   /evidence="ECO:0007829|PDB:6JD6"
FT   HELIX           329..335
FT                   /evidence="ECO:0007829|PDB:6JD6"
FT   HELIX           339..347
FT                   /evidence="ECO:0007829|PDB:6JD6"
FT   HELIX           362..369
FT                   /evidence="ECO:0007829|PDB:6JD6"
FT   HELIX           372..380
FT                   /evidence="ECO:0007829|PDB:6JD6"
FT   HELIX           395..399
FT                   /evidence="ECO:0007829|PDB:6JD6"
FT   HELIX           406..417
FT                   /evidence="ECO:0007829|PDB:6JD6"
FT   HELIX           418..421
FT                   /evidence="ECO:0007829|PDB:6JD6"
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
 
 
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