SRF6_ARATH
ID SRF6_ARATH Reviewed; 719 AA.
AC Q9C8M9; Q9C8M8;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Protein STRUBBELIG-RECEPTOR FAMILY 6;
DE AltName: Full=Leucine-rich repeat receptor kinase-like protein SRF6;
DE Flags: Precursor;
GN Name=SRF6; OrderedLocusNames=At1g53730; ORFNames=F22G10.3, F22G10.31;
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=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 [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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Cheuk R.F., Chen H., Kim C.J., Shinn P., Carninci P., Hayashizaki Y.,
RA Ishida J., Kamiya A., Kawai J., Narusaka M., Sakurai T., Satou M., Seki M.,
RA Shinozaki K., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-377, 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-377, 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-377, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
CC -!- INTERACTION:
CC Q9C8M9; O04567: At1g27190; NbExp=2; IntAct=EBI-16954301, EBI-1238687;
CC Q9C8M9; C0LGI5: At1g69990; NbExp=3; IntAct=EBI-16954301, EBI-20651225;
CC Q9C8M9; Q8VYT3: At4g30520; NbExp=2; IntAct=EBI-16954301, EBI-16902452;
CC Q9C8M9; C0LGU5: At5g45780; NbExp=3; IntAct=EBI-16954301, EBI-16964970;
CC Q9C8M9; Q9ASS4: At5g48380; NbExp=2; IntAct=EBI-16954301, EBI-6298290;
CC Q9C8M9; Q94F62: BAK1; NbExp=4; IntAct=EBI-16954301, EBI-617138;
CC Q9C8M9; Q9ZWC8: BRL1; NbExp=2; IntAct=EBI-16954301, EBI-590903;
CC Q9C8M9; C0LGW6: ERL1; NbExp=2; IntAct=EBI-16954301, EBI-16914248;
CC Q9C8M9; Q6XAT2: ERL2; NbExp=3; IntAct=EBI-16954301, EBI-16895926;
CC Q9C8M9; Q9ZVD4: LRR-RLK; NbExp=2; IntAct=EBI-16954301, EBI-20651739;
CC Q9C8M9; Q9ZRF9: RPK1; NbExp=2; IntAct=EBI-16954301, EBI-1238953;
CC Q9C8M9; Q94AG2: SERK1; NbExp=3; IntAct=EBI-16954301, EBI-1555537;
CC Q9C8M9; Q8RWZ1: SUB; NbExp=2; IntAct=EBI-16954301, EBI-17072125;
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=Q9C8M9-1; 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 SRF6 induces no obvious phenotypes.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG51973.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY518291; AAR99874.1; -; mRNA.
DR EMBL; AC024260; AAG51973.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC024260; AAG51974.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32990.1; -; Genomic_DNA.
DR EMBL; AK227057; BAE99117.1; -; mRNA.
DR EMBL; BT010600; AAQ89622.1; -; mRNA.
DR PIR; F96577; F96577.
DR RefSeq; NP_175777.1; NM_104251.4. [Q9C8M9-1]
DR AlphaFoldDB; Q9C8M9; -.
DR SMR; Q9C8M9; -.
DR BioGRID; 27036; 34.
DR IntAct; Q9C8M9; 47.
DR STRING; 3702.AT1G53730.2; -.
DR iPTMnet; Q9C8M9; -.
DR PaxDb; Q9C8M9; -.
DR PRIDE; Q9C8M9; -.
DR ProteomicsDB; 226868; -. [Q9C8M9-1]
DR EnsemblPlants; AT1G53730.1; AT1G53730.1; AT1G53730. [Q9C8M9-1]
DR GeneID; 841811; -.
DR Gramene; AT1G53730.1; AT1G53730.1; AT1G53730. [Q9C8M9-1]
DR KEGG; ath:AT1G53730; -.
DR Araport; AT1G53730; -.
DR eggNOG; ENOG502QRHD; Eukaryota.
DR InParanoid; Q9C8M9; -.
DR PhylomeDB; Q9C8M9; -.
DR PRO; PR:Q9C8M9; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C8M9; baseline and differential.
DR Genevisible; Q9C8M9; 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: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; IPR003591; Leu-rich_rpt_typical-subtyp.
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; PF13516; LRR_6; 1.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SMART; SM00369; LRR_TYP; 4.
DR SUPFAM; SSF56112; SSF56112; 1.
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; Leucine-rich repeat; Membrane;
KW Nucleotide-binding; Phosphoprotein; Receptor; Reference proteome; Repeat;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..719
FT /note="Protein STRUBBELIG-RECEPTOR FAMILY 6"
FT /id="PRO_0000311846"
FT TOPO_DOM 30..293
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 294..314
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 315..719
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 97..118
FT /note="LRR 1"
FT REPEAT 119..140
FT /note="LRR 2"
FT REPEAT 143..164
FT /note="LRR 3"
FT REPEAT 167..190
FT /note="LRR 4"
FT REPEAT 191..213
FT /note="LRR 5"
FT REPEAT 214..234
FT /note="LRR 6"
FT DOMAIN 416..690
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 242..287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 322..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 364..383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 700..719
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 246..260
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 266..283
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 328..355
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 422..430
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 444
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 377
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17586839,
FT ECO:0007744|PubMed:17869214, ECO:0007744|PubMed:19376835"
SQ SEQUENCE 719 AA; 78085 MW; 88189A8C71B64412 CRC64;
MRENWAVVAL FTLCIVGFEL RFIHGATDAS DTSALNTLFS GMHSPAQLTQ WTAAAGDPCG
QNWRGVTCSG SRVTQIKLSG LELSGTLGGY MLDKLTSLTE LDLSSNNLGG DLPYQFPPNL
QRLNLANNQF TGAASYSLSQ ITPLKYLNLG HNQFKGQIAI DFSKLDSLTT LDFSFNSFTN
SLPATFSSLT SLKSLYLQNN QFSGTVDVLA GLPLETLNIA NNDFTGWIPS SLKGITLIKD
GNSFNTGPAP PPPPGTPPIR GSPSRKSGGR ESRSSDESTR NGDSKKSGIG AGAIAGIIIS
LLVVTALLVA FFLFRRKKSK RSSPMDIEKT DNQPFTLASN DFHENNSIQS SSSVETKKLD
TSLSINLRPP PIDRNKSFDD EDSTRKPIAV KKSTVVVPSN VRLYSVADLQ IATGSFSVDN
LLGEGTFGRV YRAEFDDGKV LAVKKIDSSA LPHGMTDDFI EMVSKIANLD HPNVTKLVGY
CAEHGQHLVV YEFHKNGSLH DFLHLSEEES KALVWNSRVK IALGTARALE YLHEVCSPSI
VDKNIKSANI LLDSELNPHL SDSGLASFLP TANELLNQTD EGYSAPEVSM SGQYSLKSDI
YSFGVVMLEL LTGRKPFDST RSRSEQSLVR WATPQLHDID ALAKMVDPAL KGLYPVKSLS
RFADVIALCV QPEPEFRPPM SEVVQALVVL VQRANMSKRT VGVDPSQRAG SADTTSDYM
