SRF7_ARATH
ID SRF7_ARATH Reviewed; 717 AA.
AC Q9LUL4; Q3EB62; Q3EB63;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Protein STRUBBELIG-RECEPTOR FAMILY 7;
DE AltName: Full=Leucine-rich repeat receptor kinase-like protein SRF7;
DE Flags: Precursor;
GN Name=SRF7; OrderedLocusNames=At3g14350; ORFNames=MLN21.15;
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, DISRUPTION PHENOTYPE, AND TISSUE
RP SPECIFICITY.
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;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(2000).
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-379, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15308754; DOI=10.1105/tpc.104.023150;
RA Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
RT "Phosphoproteomics of the Arabidopsis plasma membrane and a new
RT phosphorylation site database.";
RL Plant Cell 16:2394-2405(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-379, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17869214; DOI=10.1016/j.bbrc.2007.08.177;
RA Hem S., Rofidal V., Sommerer N., Rossignol M.;
RT "Novel subsets of the Arabidopsis plasmalemma phosphoproteome identify
RT phosphorylation sites in secondary active transporters.";
RL Biochem. Biophys. Res. Commun. 363:375-380(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-379, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Seedling;
RX PubMed=17586839; DOI=10.1074/mcp.m700164-mcp200;
RA Niittylae T., Fuglsang A.T., Palmgren M.G., Frommer W.B., Schulze W.X.;
RT "Temporal analysis of sucrose-induced phosphorylation changes in plasma
RT membrane proteins of Arabidopsis.";
RL Mol. Cell. Proteomics 6:1711-1726(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-379, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Root;
RX PubMed=18433157; DOI=10.1021/pr8000173;
RA de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,
RA Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C., Lorkovic Z.J.,
RA Barta A., Lecourieux D., Verhounig A., Jonak C., Hirt H.;
RT "Site-specific phosphorylation profiling of Arabidopsis proteins by mass
RT spectrometry and peptide chip analysis.";
RL J. Proteome Res. 7:2458-2470(2008).
CC -!- INTERACTION:
CC Q9LUL4; F4I336: At1g29730; NbExp=2; IntAct=EBI-16964596, EBI-20654003;
CC Q9LUL4; Q94F62: BAK1; NbExp=2; IntAct=EBI-16964596, EBI-617138;
CC Q9LUL4; Q6XAT2: ERL2; NbExp=3; IntAct=EBI-16964596, EBI-16895926;
CC Q9LUL4; C0LGQ5: GSO1; NbExp=2; IntAct=EBI-16964596, EBI-16905069;
CC Q9LUL4; O49654: LRR-RLK; NbExp=2; IntAct=EBI-16964596, EBI-16955165;
CC Q9LUL4; Q9SKG5: SERK4; NbExp=4; IntAct=EBI-16964596, EBI-6290483;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {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=Q9LUL4-1; Sequence=Displayed;
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 SRF7 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; AY518292; AAR99875.1; -; mRNA.
DR EMBL; AB022220; BAB01040.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75505.1; -; Genomic_DNA.
DR RefSeq; NP_188052.2; NM_112293.5. [Q9LUL4-1]
DR AlphaFoldDB; Q9LUL4; -.
DR SMR; Q9LUL4; -.
DR BioGRID; 5989; 69.
DR IntAct; Q9LUL4; 74.
DR STRING; 3702.AT3G14350.1; -.
DR iPTMnet; Q9LUL4; -.
DR PaxDb; Q9LUL4; -.
DR PRIDE; Q9LUL4; -.
DR ProteomicsDB; 226727; -. [Q9LUL4-1]
DR EnsemblPlants; AT3G14350.1; AT3G14350.1; AT3G14350. [Q9LUL4-1]
DR GeneID; 820655; -.
DR Gramene; AT3G14350.1; AT3G14350.1; AT3G14350. [Q9LUL4-1]
DR KEGG; ath:AT3G14350; -.
DR Araport; AT3G14350; -.
DR TAIR; locus:2091015; AT3G14350.
DR eggNOG; ENOG502QRHD; Eukaryota.
DR InParanoid; Q9LUL4; -.
DR PhylomeDB; Q9LUL4; -.
DR PRO; PR:Q9LUL4; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LUL4; baseline and differential.
DR Genevisible; Q9LUL4; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine 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; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR045271; SRF-like.
DR PANTHER; PTHR27001; PTHR27001; 1.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51450; LRR; 4.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Glycoprotein; Leucine-rich repeat;
KW Membrane; Nucleotide-binding; Phosphoprotein; Receptor; Reference proteome;
KW Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..717
FT /note="Protein STRUBBELIG-RECEPTOR FAMILY 7"
FT /id="PRO_0000311847"
FT TOPO_DOM 26..291
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 292..312
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 313..717
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 96..117
FT /note="LRR 1"
FT REPEAT 118..139
FT /note="LRR 2"
FT REPEAT 142..164
FT /note="LRR 3"
FT REPEAT 165..187
FT /note="LRR 4"
FT REPEAT 189..210
FT /note="LRR 5"
FT REPEAT 211..232
FT /note="LRR 6"
FT DOMAIN 419..693
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 237..287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 365..385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..259
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 260..286
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 425..433
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 447
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 379
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15308754,
FT ECO:0007744|PubMed:17586839, ECO:0007744|PubMed:17869214,
FT ECO:0007744|PubMed:18433157"
FT CARBOHYD 271
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 717 AA; 77635 MW; 5CECAC43C1D81E37 CRC64;
MTENRVVLAL LILCIVGFEP SFIHGATDSS DTSALNIMFS SMNSPGQLSQ WTASGGDPCG
QNWKGITCSG SRVTQIKLPS LGLSGSLGFM LDKLTSVTEF DMSNNNLGGD LPYQLPPNLE
RLNLANNQFT GSAQYSISMM APLKYLNLAH NQLKQLAIDF TKLTSLSILD LSSNAFIGSL
PNTCSSLTSA KSIYLQNNQF SGTIDILATL PLENLNIANN RFTGWIPDSL KGINLQKDGN
LLNSGPAPPP PPGTPPISKS SPTPKSGNRG NRSNGDSSNS KDSSKSGLGA GGVAGIVISL
IVVTAVIAFF LIKRKRSKRS SSTDIEKTDN NINQPIILAS NDFHQENKSV QNPPLVETKK
LDTSLSMNLR PPPSERHKSF DDDDSTMRKP IVAKKAAVVV PSNVNTYTVS DLQVATNSFS
VDNLLGEGTF GRVYRAQFED GKVLAVKKID SSALPTDTAD DFTEIVSKIA HLDHENVTKL
DGYCSEHGQH LVVYEFHRNG SLHDFLHLAE EESKPLIWNP RVKIALGTAR ALEYLHEVCS
PSIVHKNIKS ANILLDSELN PHLSDSGLAS FLPTANELLN QNDEGYSAPE TSMSGQYSLK
SDVYSFGVVM LELLTGRKPF DSTRSRSEQS LVRWATPQLH DIDALGKMVD PALKGLYPVK
SLSRFADVIA LCVQPEPEFR PPMSEVVQAL VVLVQRANMS KRTVGVGSGS SGVNDYM
