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IRE4_ARATH
ID   IRE4_ARATH              Reviewed;        1042 AA.
AC   F4HPN2; Q0WLU7; Q9MAJ4;
DT   26-NOV-2014, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=Probable serine/threonine protein kinase IRE4 {ECO:0000305};
DE            Short=AtIRE4 {ECO:0000303|PubMed:17237187};
DE            EC=2.7.11.1 {ECO:0000305};
GN   Name=IRE4 {ECO:0000303|PubMed:17237187};
GN   OrderedLocusNames=At1g45160 {ECO:0000312|Araport:AT1G45160};
GN   ORFNames=F27F5.23 {ECO:0000312|EMBL:AAF69167.1};
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=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(2000).
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].
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   [4]
RP   GENE FAMILY.
RX   PubMed=17237187; DOI=10.1104/pp.106.092494;
RA   Pislariu C.I., Dickstein R.;
RT   "An IRE-like AGC kinase gene, MtIRE, has unique expression in the invasion
RT   zone of developing root nodules in Medicago truncatula.";
RL   Plant Physiol. 144:682-694(2007).
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         Evidence={ECO:0000305};
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; Evidence={ECO:0000305};
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms are produced. According to EST
CC         sequences.;
CC       Name=1;
CC         IsoId=F4HPN2-1; Sequence=Displayed;
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC       protein kinase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF69167.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AC007915; AAF69167.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002684; AEE32085.1; -; Genomic_DNA.
DR   EMBL; AK230091; BAF01910.1; -; mRNA.
DR   PIR; H96509; H96509.
DR   RefSeq; NP_175130.2; NM_103590.3. [F4HPN2-1]
DR   AlphaFoldDB; F4HPN2; -.
DR   SMR; F4HPN2; -.
DR   STRING; 3702.AT1G45160.2; -.
DR   iPTMnet; F4HPN2; -.
DR   PaxDb; F4HPN2; -.
DR   PRIDE; F4HPN2; -.
DR   EnsemblPlants; AT1G45160.1; AT1G45160.1; AT1G45160. [F4HPN2-1]
DR   GeneID; 841084; -.
DR   Gramene; AT1G45160.1; AT1G45160.1; AT1G45160. [F4HPN2-1]
DR   KEGG; ath:AT1G45160; -.
DR   Araport; AT1G45160; -.
DR   eggNOG; KOG0606; Eukaryota.
DR   PRO; PR:F4HPN2; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; F4HPN2; baseline and differential.
DR   Genevisible; F4HPN2; AT.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR   GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; ATP-binding; Kinase; Metal-binding;
KW   Nucleotide-binding; Phosphoprotein; Reference proteome;
KW   Serine/threonine-protein kinase; Transferase; Zinc; Zinc-finger.
FT   CHAIN           1..1042
FT                   /note="Probable serine/threonine protein kinase IRE4"
FT                   /id="PRO_0000431356"
FT   DOMAIN          670..955
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   DOMAIN          956..1042
FT                   /note="AGC-kinase C-terminal"
FT                   /evidence="ECO:0000255"
FT   ZN_FING         402..421
FT                   /note="C2H2-type; atypical"
FT                   /evidence="ECO:0000250|UniProtKB:Q9LE81"
FT   REGION          1..75
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          90..115
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          297..327
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          830..850
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        15..48
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        834..850
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        793
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         676..684
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         699
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         854
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P42818"
FT   CONFLICT        313
FT                   /note="Y -> C (in Ref. 3; BAF01910)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1042 AA;  117997 MW;  2D7FA2E06004E77B CRC64;
     MAEENRKDRG VSSTVAIPSG LNRIKTRLAS SGPRPEDSSD TVLKPPFNRN QKTIVPRGHG
     RTTGSSKQER KGTKLSRWLA SYKPKYSCHP PKYACSSTTS SEEIKLRGKN SGKDEEKMIK
     ISETNPPCSK SMGIKSFSHE LGPRGGVQTP YPRPHSYNDL KELLGSLHSR FDVAKETVDK
     KLDVFVRDVK EAMEKMDPSC PEDREMAEQL LDVARACMEM TSAQLRATCE SIVQDLTRKR
     KQCQAGLVKW LFSQLLFILT HCTRVVMFQK ETEPIDESSF RKFKECLERI PALETDWGST
     PRVDDSGSGY PEYQRNEAGQ KFKRRDKESL ESETALDYVV PNDHGNNAAR EGYAAAKQEF
     PSHEPQFDSK VVEQRFYLSD EYEDKMSNEP GKELGGSDYV ICRICEEEVP LFHLEPHSYI
     CAYADKCEIN CVDVDERLLK LEEILEQIID SRSLNSFTQA GGLENSVLRK SGVASEGCSP
     KINEWRNKGL EGMFEDLHEM DTAFIDESYT YPIHLKSHVG AKFCHHATSS STGSITSVSS
     TNTPRTSHFD SYWLERHCPE QEDLRLMMDL SDIARCGAST DFSKEGSCDY IMACMQDIQA
     VLKQGKLKAL VIDTFGGRIE KLLCEKYLHA RELTADKSSV GNIKESEDVL EHASATPQLL
     LKDRISIDDF EIIKPISRGA FGKVFLARKR TTGDFFAIKV LKKLDMIRKN DIERILQERN
     ILITVRYPFL VRFFYSFTCR DNLYLVMEYL NGGDLYSLLQ KVGCLDEEIA RIYIAELVLA
     LEYLHSLKIV HRDLKPDNLL IAYNGHIKLT DFGLSKIGLI NNTIDLSGHE SDVSPRTNSH
     HFQKNQEEER IRHSAVGTPD YLAPEILLGT EHGYAADWWS AGIVLFELLT GIPPFTASRP
     EKIFDNILNG KMPWPDVPGE MSYEAQDLIN RLLVHEPEKR LGANGAAEVK SHPFFQGVDW
     ENLALQKAAF VPQPESINDT SYFVSRFSES SCSDTETGNN SGSNPDSGDE VGIWKLHPFL
     SRYSICNHRI YRKLFFLLLC VF
 
 
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