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SRF2_ARATH
ID   SRF2_ARATH              Reviewed;         735 AA.
AC   Q9FG24;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 150.
DE   RecName: Full=Protein STRUBBELIG-RECEPTOR FAMILY 2;
DE   AltName: Full=Leucine-rich repeat receptor kinase-like protein SRF2;
DE   Flags: Precursor;
GN   Name=SRF2; OrderedLocusNames=At5g06820; ORFNames=MPH15.19;
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 [MRNA], FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION
RP   PHENOTYPE.
RC   STRAIN=cv. Columbia;
RX   PubMed=17397538; DOI=10.1186/1471-2229-7-16;
RA   Eyueboglu B., Pfister K., Haberer G., Chevalier D., Fuchs A., Mayer K.F.X.,
RA   Schneitz K.;
RT   "Molecular characterisation of the STRUBBELIG-RECEPTOR FAMILY of genes
RT   encoding putative leucine-rich repeat receptor-like kinases in Arabidopsis
RT   thaliana.";
RL   BMC Plant Biol. 7:16-16(2007).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RA   Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL   Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
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).
CC   -!- INTERACTION:
CC       Q9FG24; Q8VYT3: At4g30520; NbExp=2; IntAct=EBI-16955365, EBI-16902452;
CC       Q9FG24; Q6XAT2: ERL2; NbExp=2; IntAct=EBI-16955365, EBI-16895926;
CC       Q9FG24; Q9FG24: SRF2; NbExp=2; IntAct=EBI-16955365, EBI-16955365;
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed in seedlings, roots, stems, leaves,
CC       flowers and siliques. {ECO:0000269|PubMed:17397538}.
CC   -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC       inactive.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC       {ECO:0000269|PubMed:17397538}.
CC   -!- MISCELLANEOUS: Cannot functionally replace STRUBBELIG.
CC   -!- MISCELLANEOUS: Over-expression of SRF2 led to male-sterility in cv.
CC       Columbia but not in cv. Landsberg.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR   EMBL; AY518287; AAR99870.1; -; mRNA.
DR   EMBL; AP002032; BAB09817.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED91070.1; -; Genomic_DNA.
DR   RefSeq; NP_196300.1; NM_120765.3.
DR   AlphaFoldDB; Q9FG24; -.
DR   SMR; Q9FG24; -.
DR   BioGRID; 15852; 54.
DR   IntAct; Q9FG24; 53.
DR   STRING; 3702.AT5G06820.1; -.
DR   PaxDb; Q9FG24; -.
DR   PRIDE; Q9FG24; -.
DR   EnsemblPlants; AT5G06820.1; AT5G06820.1; AT5G06820.
DR   GeneID; 830573; -.
DR   Gramene; AT5G06820.1; AT5G06820.1; AT5G06820.
DR   KEGG; ath:AT5G06820; -.
DR   Araport; AT5G06820; -.
DR   TAIR; locus:2170219; AT5G06820.
DR   eggNOG; ENOG502QR3N; Eukaryota.
DR   HOGENOM; CLU_000288_92_2_1; -.
DR   InParanoid; Q9FG24; -.
DR   OMA; RPPMTVI; -.
DR   OrthoDB; 684563at2759; -.
DR   PhylomeDB; Q9FG24; -.
DR   PRO; PR:Q9FG24; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9FG24; baseline and differential.
DR   Genevisible; Q9FG24; 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:InterPro.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR   GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR   Gene3D; 3.80.10.10; -; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   InterPro; IPR013210; LRR_N_plant-typ.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   Pfam; PF00560; LRR_1; 2.
DR   Pfam; PF08263; LRRNT_2; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS51450; LRR; 5.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   Glycoprotein; Leucine-rich repeat; Membrane; Receptor; Reference proteome;
KW   Repeat; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..735
FT                   /note="Protein STRUBBELIG-RECEPTOR FAMILY 2"
FT                   /id="PRO_0000311842"
FT   TOPO_DOM        24..297
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        298..318
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        319..735
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REPEAT          78..94
FT                   /note="LRR 1"
FT   REPEAT          96..119
FT                   /note="LRR 2"
FT   REPEAT          120..140
FT                   /note="LRR 3"
FT   REPEAT          142..163
FT                   /note="LRR 4"
FT   REPEAT          165..187
FT                   /note="LRR 5"
FT   REPEAT          189..211
FT                   /note="LRR 7"
FT   REPEAT          212..232
FT                   /note="LRR 7"
FT   REPEAT          233..253
FT                   /note="LRR 8"
FT   DOMAIN          415..695
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          358..378
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        118
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        128
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        147
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        175
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        189
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        264
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   735 AA;  81299 MW;  1330848327280703 CRC64;
     MKTKQQLRFL ATILLTTILF VLAKTDTDPL EVLALQDLYK SLRNPEQLRG WRLEGGDPCG
     EAWLGISCSG SSIVDLQLRE LKLLGSLGNQ LQHLHNLKIL DVSFNNLEGE IPFGLPPNAT
     HINMAYNNLT QSIPFSLPLM TSLQSLNLSH NSLSGPLGNV FSGLQIKEMD LSFNNLTGDL
     PSSFGTLMNL TSLYLQNNRL TGSVIYLADL PLADLNIEDN QFSGIIPSHF QSIPHLWIWG
     NKFHVEPNYK PWKFPLDVRP LIQNDTGYPT TESSAIMNFP RPETQKVKKK KKGIGAGSTF
     LLVGGLALLG TFFALFAVRM NHRRAQNLAA IHRSNNSIAY SLPVSTGREY PVATEDNPQI
     KRFQPPPAPQ LRHLPSPPVR IDKSARRKSF SATCQYPSFA KLFSAAELQL ATNCFSEENL
     LGEGPLGSVY RAKLPDGQFA VVRNIPMSSL SLHEEEQFTE VLQTASKLRH PNIVTLLGFC
     IENGEHLLVY EYVGHLSLYN AMHDEVYKPL SWGLRLRIAI GVARALDYLH SSFCPPIAHS
     DLKATNILLD EELTPRIADC GLASLRPLTS NSVKLRASEI AIQNTGYIAP EHGQPGSSGT
     KSDTYALGVL LLELLTGRKA FDSSRPRGEQ LLVKWASTRL HDRRSLEQMI DGGIAGTFSS
     RVASQYADII SLCTQAEKEF RPPVSEIVEA LTALIQKQNK EASSSVADKT DPFSKSFCST
     RTRFISSPTF SYLSS
 
 
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