SRF5_ARATH
ID SRF5_ARATH Reviewed; 699 AA.
AC Q6R2K1; O64550;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Protein STRUBBELIG-RECEPTOR FAMILY 5;
DE AltName: Full=Leucine-rich repeat receptor kinase-like protein SRF5;
DE Flags: Precursor;
GN Name=SRF5; OrderedLocusNames=At1g78980; ORFNames=YUP8H12R.40;
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=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).
CC -!- INTERACTION:
CC Q6R2K1; A0A178UFM8: AXX17_At5g50380; NbExp=3; IntAct=EBI-20651875, EBI-20653342;
CC Q6R2K1; Q94F62: BAK1; NbExp=4; IntAct=EBI-20651875, EBI-617138;
CC Q6R2K1; Q6XAT2: ERL2; NbExp=3; IntAct=EBI-20651875, EBI-16895926;
CC Q6R2K1; Q8RWZ1: SUB; NbExp=2; IntAct=EBI-20651875, EBI-17072125;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves and flowers.
CC {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 SRF5 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC17069.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY518290; AAR99873.1; -; mRNA.
DR EMBL; AC002986; AAC17069.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE36188.1; -; Genomic_DNA.
DR PIR; T01057; T01057.
DR RefSeq; NP_178019.2; NM_106547.3.
DR AlphaFoldDB; Q6R2K1; -.
DR SMR; Q6R2K1; -.
DR BioGRID; 29457; 18.
DR IntAct; Q6R2K1; 22.
DR STRING; 3702.AT1G78980.1; -.
DR iPTMnet; Q6R2K1; -.
DR PaxDb; Q6R2K1; -.
DR PRIDE; Q6R2K1; -.
DR ProteomicsDB; 226867; -.
DR EnsemblPlants; AT1G78980.1; AT1G78980.1; AT1G78980.
DR GeneID; 844238; -.
DR Gramene; AT1G78980.1; AT1G78980.1; AT1G78980.
DR KEGG; ath:AT1G78980; -.
DR Araport; AT1G78980; -.
DR TAIR; locus:2207280; AT1G78980.
DR eggNOG; ENOG502QSZ9; Eukaryota.
DR HOGENOM; CLU_000288_92_2_1; -.
DR InParanoid; Q6R2K1; -.
DR OMA; CSRPSAY; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; Q6R2K1; -.
DR PRO; PR:Q6R2K1; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q6R2K1; baseline and differential.
DR Genevisible; Q6R2K1; 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; IPR045271; SRF-like.
DR PANTHER; PTHR27001; PTHR27001; 1.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00369; LRR_TYP; 4.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Glycoprotein; Leucine-rich repeat; Membrane;
KW Nucleotide-binding; Phosphoprotein; Receptor; Reference proteome; Repeat;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..699
FT /note="Protein STRUBBELIG-RECEPTOR FAMILY 5"
FT /id="PRO_0000311845"
FT TOPO_DOM 23..273
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 274..294
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 295..699
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 93..115
FT /note="LRR 1"
FT REPEAT 116..136
FT /note="LRR 2"
FT REPEAT 139..161
FT /note="LRR 3"
FT REPEAT 163..186
FT /note="LRR 4"
FT REPEAT 187..209
FT /note="LRR 5"
FT DOMAIN 404..675
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 239..263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 410..418
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 432
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 368
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9C8M9"
FT CARBOHYD 184
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 699 AA; 76945 MW; 07D89E9FB15B8989 CRC64;
MTQKLVRLVI VSLAITVTLL QAKTDNQEVS ALNVMFTSLN SPSKLKGWKA NGGDPCEDSW
EGVKCKGSSV TELQLSGFEL GGSRGYLLSN LKSLTTFDLS KNNLKGNIPY QLPPNIANLD
FSENELDGNV PYSLSQMKNL QSINLGQNKL NGELPDMFQK LSKLETLDFS LNKLSGKLPQ
SFANLTSLKK LHLQDNRFTG DINVLRNLAI DDLNVEDNQF EGWIPNELKD IDSLLTGGND
WSTETAPPPP PGVKYGRKSS GSKDGGGITA GTGMVIAGAC LGVLVLIIVL IALVSKKKSS
LSPHFIDEDN SHHTPKFKSL TSHGSAQELR VDFGNDYKDG KSGDSGDENI HRIGSKGLKH
YVSSRVMSFT DTEFANKLNA KRTTSTRSAV EFELSDLQSA TANFSPGNLL GEGSIGRVYR
AKYSDGRTLA VKKIDSTLFD SGKSEGITPI VMSLSKIRHQ NIAELVGYCS EQGHNMLVYE
YFRNGSLHEF LHLSDCFSKP LTWNTRVRIA LGTARAVEYL HEACSPSVMH KNIKSSNILL
DADLNPRLSD YGLSKFYLRT SQNLGEGYNA PEARDPSAYT PKSDVYSFGV VMLELLTGRV
PFDGEKPRPE RSLVRWATPQ LHDIDALSNI ADPALHGLYP PKSLSRFADI IALCVQVEPE
FRPPMSEVVE ALVRMVQRSS MKLKDDLSSS YRAHDDYDY
