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Y1148_ARATH
ID   Y1148_ARATH             Reviewed;         809 AA.
AC   O64771;
DT   30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2010, sequence version 2.
DT   03-AUG-2022, entry version 162.
DE   RecName: Full=G-type lectin S-receptor-like serine/threonine-protein kinase At1g61480;
DE            EC=2.7.11.1;
DE   Flags: Precursor;
GN   OrderedLocusNames=At1g61480; ORFNames=T1F9.2;
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;
RX   PubMed=14993207; DOI=10.1101/gr.1515604;
RA   Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA   Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA   Weissenbach J., Salanoubat M.;
RT   "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT   combined approach to evaluate and improve Arabidopsis genome annotation.";
RL   Genome Res. 14:406-413(2004).
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   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC       membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC13892.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=BX816606; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AC004255; AAC13892.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002684; AEE33843.1; -; Genomic_DNA.
DR   EMBL; BX816606; -; NOT_ANNOTATED_CDS; mRNA.
DR   PIR; A96640; A96640.
DR   RefSeq; NP_176343.2; NM_104829.3.
DR   AlphaFoldDB; O64771; -.
DR   SMR; O64771; -.
DR   STRING; 3702.AT1G61480.1; -.
DR   PaxDb; O64771; -.
DR   PRIDE; O64771; -.
DR   EnsemblPlants; AT1G61480.1; AT1G61480.1; AT1G61480.
DR   GeneID; 842442; -.
DR   Gramene; AT1G61480.1; AT1G61480.1; AT1G61480.
DR   KEGG; ath:AT1G61480; -.
DR   Araport; AT1G61480; -.
DR   TAIR; locus:2197709; AT1G61480.
DR   eggNOG; ENOG502QSUU; Eukaryota.
DR   HOGENOM; CLU_000288_116_1_1; -.
DR   InParanoid; O64771; -.
DR   OMA; NENIFHP; -.
DR   OrthoDB; 407794at2759; -.
DR   PhylomeDB; O64771; -.
DR   PRO; PR:O64771; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; O64771; baseline and differential.
DR   Genevisible; O64771; AT.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005516; F:calmodulin binding; ISS:UniProtKB.
DR   GO; GO:0030246; F:carbohydrate 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; ISS:UniProtKB.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:UniProt.
DR   GO; GO:0045087; P:innate immune response; IBA:GO_Central.
DR   GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR   GO; GO:0048544; P:recognition of pollen; IEA:InterPro.
DR   CDD; cd00028; B_lectin; 1.
DR   Gene3D; 2.90.10.10; -; 1.
DR   InterPro; IPR001480; Bulb-type_lectin_dom.
DR   InterPro; IPR036426; Bulb-type_lectin_dom_sf.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR003609; Pan_app.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR021820; S-locus_recpt_kinase_C.
DR   InterPro; IPR000858; S_locus_glycoprot_dom.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR024171; SRK-like_kinase.
DR   Pfam; PF01453; B_lectin; 1.
DR   Pfam; PF11883; DUF3403; 1.
DR   Pfam; PF08276; PAN_2; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   Pfam; PF00954; S_locus_glycop; 1.
DR   PIRSF; PIRSF000641; SRK; 1.
DR   SMART; SM00108; B_lectin; 1.
DR   SMART; SM00473; PAN_AP; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF51110; SSF51110; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS50927; BULB_LECTIN; 1.
DR   PROSITE; PS50948; PAN; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Cell membrane; Disulfide bond; EGF-like domain; Glycoprotein;
KW   Kinase; Lectin; Membrane; Nucleotide-binding; Phosphoprotein; Receptor;
KW   Reference proteome; Serine/threonine-protein kinase; Signal; Transferase;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..809
FT                   /note="G-type lectin S-receptor-like serine/threonine-
FT                   protein kinase At1g61480"
FT                   /id="PRO_0000401322"
FT   TOPO_DOM        25..425
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        426..446
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        447..809
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          25..144
FT                   /note="Bulb-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00038"
FT   DOMAIN          278..314
FT                   /note="EGF-like"
FT   DOMAIN          333..415
FT                   /note="PAN"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00315"
FT   DOMAIN          496..781
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          585..602
FT                   /note="CaM-binding"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        621
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         502..510
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         524
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         530
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT   MOD_RES         545
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT   MOD_RES         625
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT   MOD_RES         638
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT   MOD_RES         655
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT   MOD_RES         698
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT   MOD_RES         792
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT   CARBOHYD        53
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        88
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        94
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        103
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        117
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        134
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        236
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        320
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        375
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        282..294
FT                   /evidence="ECO:0000250"
FT   DISULFID        288..302
FT                   /evidence="ECO:0000250"
FT   DISULFID        368..389
FT                   /evidence="ECO:0000250"
FT   DISULFID        372..378
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   809 AA;  90741 MW;  4BD5AF08635185D0 CRC64;
     MGKKRIMFFA SLLLITIFLS FSYAGITRES PLSIGKTLSS SNGVYELGFF SFNNSQNQYV
     GIWFKGIIPR VVVWVANREK PVTDSAANLT ISSNGSLLLF NENHSVVWSI GETFASNGSR
     AELTDNGNLV VIDNNSGRTL WESFEHFGDT MLPFSNLMYN LATGEKRVLT SWKSHTDPSP
     GDFTVQITPQ VPSQACTMRG SKTYWRSGPW AKTRFTGIPV MDDTYTSPFS LQQDTNGSGS
     FTYFERNFKL SYIMITSEGS LKIFQHNGMD WELNFEAPEN SCDIYGFCGP FGICVMSVPP
     KCKCFKGFVP KSIEEWKRGN WTDGCVRHTE LHCQGNTNGK TVNGFYHVAN IKPPDFYEFA
     SFVDAEGCYQ ICLHNCSCLA FAYINGIGCL MWNQDLMDAV QFSAGGEILS IRLASSELGG
     NKRNKIIVAS IVSLSLFVIL AFAAFCFLRY KVKHTVSAKI SKIASKEAWN NDLEPQDVSG
     LKFFEMNTIQ TATDNFSLSN KLGQGGFGSV YKGKLQDGKE IAVKRLSSSS GQGKEEFMNE
     IVLISKLQHK NLVRILGCCI EGEERLLVYE FLLNKSLDTF LFDSRKRLEI DWPKRFNIIE
     GIARGLHYLH RDSCLRVIHR DLKVSNILLD EKMNPKISDF GLARMYQGTE YQDNTRRVAG
     TLGYMAPEYA WTGMFSEKSD IYSFGVILLE IITGEKISRF SYGRQGKTLL AYAWESWCES
     GGIDLLDKDV ADSCHPLEVE RCVQIGLLCV QHQPADRPNT MELLSMLTTT SDLTSPKQPT
     FVVHTRDEES LSQGLITVNE MTQSVILGR
 
 
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