SRF8_ARATH
ID SRF8_ARATH Reviewed; 703 AA.
AC Q6R2J8; O65461;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Protein STRUBBELIG-RECEPTOR FAMILY 8;
DE AltName: Full=Leucine-rich repeat receptor kinase-like protein SRF8;
DE Flags: Precursor;
GN Name=SRF8; OrderedLocusNames=At4g22130; ORFNames=F1N20.230;
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;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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] OF 366-703.
RC STRAIN=cv. Columbia;
RA Bautista V.R., Kim C.J., Chen H., Quinitio C., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- INTERACTION:
CC Q6R2J8; Q0WVM4: At2g23950; NbExp=2; IntAct=EBI-16941202, EBI-20655099;
CC Q6R2J8; Q8VYT3: At4g30520; NbExp=2; IntAct=EBI-16941202, EBI-16902452;
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=Q6R2J8-1; 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 SRF8 may lead to seedling lethality
CC in both cv. Landsberg and cv. Columbia.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA18116.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB79168.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY518293; AAR99876.1; -; mRNA.
DR EMBL; AL022140; CAA18116.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161556; CAB79168.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE84560.1; -; Genomic_DNA.
DR EMBL; BT029473; ABL66730.1; -; mRNA.
DR RefSeq; NP_193944.2; NM_118334.5. [Q6R2J8-1]
DR AlphaFoldDB; Q6R2J8; -.
DR SMR; Q6R2J8; -.
DR BioGRID; 13591; 60.
DR IntAct; Q6R2J8; 61.
DR STRING; 3702.AT4G22130.1; -.
DR iPTMnet; Q6R2J8; -.
DR PaxDb; Q6R2J8; -.
DR PRIDE; Q6R2J8; -.
DR ProteomicsDB; 226869; -. [Q6R2J8-1]
DR EnsemblPlants; AT4G22130.1; AT4G22130.1; AT4G22130. [Q6R2J8-1]
DR GeneID; 828302; -.
DR Gramene; AT4G22130.1; AT4G22130.1; AT4G22130. [Q6R2J8-1]
DR KEGG; ath:AT4G22130; -.
DR Araport; AT4G22130; -.
DR TAIR; locus:2120683; AT4G22130.
DR eggNOG; KOG1187; Eukaryota.
DR InParanoid; Q6R2J8; -.
DR OMA; PEREGDM; -.
DR PhylomeDB; Q6R2J8; -.
DR PRO; PR:Q6R2J8; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q6R2J8; baseline and differential.
DR Genevisible; Q6R2J8; 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; 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; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Glycoprotein; Leucine-rich repeat;
KW Membrane; Nucleotide-binding; Receptor; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..703
FT /note="Protein STRUBBELIG-RECEPTOR FAMILY 8"
FT /id="PRO_0000311848"
FT TOPO_DOM 28..291
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 292..312
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 313..703
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 96..120
FT /note="LRR 1"
FT REPEAT 122..142
FT /note="LRR 2"
FT REPEAT 143..165
FT /note="LRR 3"
FT REPEAT 166..190
FT /note="LRR 4"
FT REPEAT 192..212
FT /note="LRR 5"
FT REPEAT 213..233
FT /note="LRR 6"
FT REPEAT 234..256
FT /note="LRR 7"
FT DOMAIN 395..672
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 247..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..278
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 401..409
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 423
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 120
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 130
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 149
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 178
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 226
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 703 AA; 76086 MW; C880E346DDDD7712 CRC64;
MAIGDRAMFT VLLLFIASIS GFSVVRCVTD PSDVQALQVL YTSLNSPSQL TNWKNGGGDP
CGESWKGITC EGSAVVTIDI SDLGVSGTLG YLLSDLKSLR KLDVSGNSIH DTLPYQLPPN
LTSLNLARNN LSGNLPYSIS AMGSLSYMNV SGNSLTMSIG DIFADHKSLA TLDLSHNNFS
GDLPSSLSTV STLSVLYVQN NQLTGSIDVL SGLPLKTLNV ANNHFNGSIP KELSSIQTLI
YDGNSFDNVP ASPQPERPGK KETPSGSKKP KIGSEEKSSD SGKGLSGGVV TGIVFGSLFV
AGIIALVLYL CLHKKKRKVR GSTRASQRSL PLSGTPEVQE QRVKSVASVA DLKSSPAEKV
TVDRVMKNGS ISRIRSPITA SQYTVSSLQV ATNSFSQENI IGEGSLGRVY RAEFPNGKIM
AIKKIDNAAL SLQEEDNFLE AVSNMSRLRH PNIVPLAGYC TEHGQRLLVY EYVGNGNLDD
TLHTNDDRSM NLTWNARVKV ALGTAKALEY LHEVCLPSIV HRNFKSANIL LDEELNPHLS
DSGLAALTPN TERQVSTQVV GSFGYSAPEF ALSGIYTVKS DVYTFGVVML ELLTGRKPLD
SSRTRAEQSL VRWATPQLHD IDALSKMVDP SLNGMYPAKS LSRFADIIAL CIQPEPEFRP
PMSEVVQQLV RLVQRASVVK RRSSDDTGFS YRTPEHEHVD ISF
