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PID2_ARATH
ID   PID2_ARATH              Reviewed;         525 AA.
AC   Q64FQ2; O48785; Q0WP71;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 130.
DE   RecName: Full=Protein kinase PINOID 2;
DE            EC=2.7.11.1;
DE   AltName: Full=Protein kinase AGC1-10;
GN   Name=PID2; Synonyms=AGC1-10; OrderedLocusNames=At2g26700; ORFNames=F18A8.7;
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 / MRNA].
RA   Berendzen K.W., Okresz L., Anthony R., Henriques R., Bogre L., Koncz C.;
RT   "Characterization of an AGC family member kinase, AGC1-10.";
RL   Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2]
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   [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;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX   PubMed=19075219; DOI=10.1073/pnas.0809761106;
RA   Cheng Y., Qin G., Dai X., Zhao Y.;
RT   "NPY genes and AGC kinases define two key steps in auxin-mediated
RT   organogenesis in Arabidopsis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:21017-21022(2008).
CC   -!- FUNCTION: Serine/threonine-protein kinase involved in the regulation of
CC       auxin signaling. Plays a minor role in the regulation of cellular auxin
CC       efflux and cotyledon organogenesis. {ECO:0000269|PubMed:19075219}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.1;
CC   -!- INTERACTION:
CC       Q64FQ2; Q9XF67: PDPK1; NbExp=2; IntAct=EBI-1103769, EBI-1103587;
CC   -!- DEVELOPMENTAL STAGE: Expressed throughout the embryogenesis in the
CC       provascular tissues. {ECO:0000269|PubMed:19075219}.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC       conditions. {ECO:0000269|PubMed:19075219}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB95304.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=BAF01078.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AY705432; AAU14162.1; -; Genomic_DNA.
DR   EMBL; AY705433; AAU14163.1; -; mRNA.
DR   EMBL; AC003105; AAB95304.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002685; AEC07877.1; -; Genomic_DNA.
DR   EMBL; AK229209; BAF01078.1; ALT_INIT; mRNA.
DR   PIR; G84663; G84663.
DR   RefSeq; NP_180238.2; NM_128227.5.
DR   AlphaFoldDB; Q64FQ2; -.
DR   SMR; Q64FQ2; -.
DR   BioGRID; 2563; 1.
DR   IntAct; Q64FQ2; 1.
DR   STRING; 3702.AT2G26700.1; -.
DR   PaxDb; Q64FQ2; -.
DR   PRIDE; Q64FQ2; -.
DR   EnsemblPlants; AT2G26700.1; AT2G26700.1; AT2G26700.
DR   GeneID; 817211; -.
DR   Gramene; AT2G26700.1; AT2G26700.1; AT2G26700.
DR   KEGG; ath:AT2G26700; -.
DR   Araport; AT2G26700; -.
DR   TAIR; locus:2043813; AT2G26700.
DR   eggNOG; KOG0610; Eukaryota.
DR   eggNOG; KOG4198; Eukaryota.
DR   HOGENOM; CLU_000288_63_30_1; -.
DR   InParanoid; Q64FQ2; -.
DR   OMA; PWVPKEE; -.
DR   OrthoDB; 799520at2759; -.
DR   PhylomeDB; Q64FQ2; -.
DR   PRO; PR:Q64FQ2; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q64FQ2; baseline and differential.
DR   Genevisible; Q64FQ2; AT.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016301; F:kinase activity; ISS:TAIR.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR   GO; GO:0009734; P:auxin-activated signaling pathway; IEA:UniProtKB-KW.
DR   GO; GO:0048825; P:cotyledon development; IGI:TAIR.
DR   GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR   InterPro; IPR000961; AGC-kinase_C.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   Pfam; PF00069; Pkinase; 2.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Auxin signaling pathway; Developmental protein; Kinase;
KW   Nucleotide-binding; Phosphoprotein; Reference proteome;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..525
FT                   /note="Protein kinase PINOID 2"
FT                   /id="PRO_0000411971"
FT   DOMAIN          87..465
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   DOMAIN          466..525
FT                   /note="AGC-kinase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        214
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         93..101
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         118
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   CONFLICT        214
FT                   /note="D -> G (in Ref. 4; BAF01078)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   525 AA;  59294 MW;  75D92040920BB88F CRC64;
     MANSSIFYKD NESDYESSTV GPDSSRRTSW LSSSFTASPS CSSISHLSNH GLNSYNQSKP
     HKANQVAWEA MARLRRCCGR AVGLEHFRLL KRLGSGDIGS VYLCQIRGSP ETAFYAMKVV
     DKEAVAVKKK LGRAEMEKKI LGMLDHPFCP TLYAAFEASH YSFLVMEYCP GGDLYAVRLR
     QPSKRFTISS TRFYAAETLV ALEYLHMMGI VYRDLKPENV LIREDGHVML SDFDLSFKCD
     VVPQFLSDND RDRGHQEDDD DISIRRKCST PSCTTTPLNP VISCFSPTSS RRRKKNVVTT
     TIHENAAGTS DSVKSNDVSR TFSRSPSSCS RVSNGLRDIS GGCPSIFAEP INARSKSFVG
     THEYLAPEVI SGQGHGSAVD WWTYGIFLYE MIFGRTPFKG DNNEKTLVNI LKAPLTFPKV
     IVNSPKEYED MVNAQDLIIK LLVKNPKKRL GSLKGSIEIK RHEFFEGVNW ALIRSIKPPW
     VPKEETSHKT KGDNRSVNYY LPPRFMMSRK ERNEPYHVSN YFDYF
 
 
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