SRF3_ARATH
ID SRF3_ARATH Reviewed; 776 AA.
AC Q6R2K3; Q0WS32; Q9ZQZ2;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Protein STRUBBELIG-RECEPTOR FAMILY 3;
DE AltName: Full=Leucine-rich repeat receptor kinase-like protein SRF3;
DE Flags: Precursor;
GN Name=SRF3; OrderedLocusNames=At4g03390; ORFNames=F4C21.35;
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] (ISOFORM 1), FUNCTION, AND TISSUE 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=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] (ISOFORM 2).
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 FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17027738; DOI=10.1016/j.ydbio.2006.09.009;
RA Kwak S.-H., Schiefelbein J.;
RT "The role of the SCRAMBLED receptor-like kinase in patterning the
RT Arabidopsis root epidermis.";
RL Dev. Biol. 302:118-131(2007).
CC -!- FUNCTION: Not essential for epidermal patterning and not redundant with
CC STRUBBELIG. {ECO:0000269|PubMed:17027738, ECO:0000269|PubMed:17397538}.
CC -!- INTERACTION:
CC Q6R2K3; O04567: At1g27190; NbExp=2; IntAct=EBI-20651925, EBI-1238687;
CC Q6R2K3; Q94F62: BAK1; NbExp=2; IntAct=EBI-20651925, EBI-617138;
CC Q6R2K3; Q42371: ERECTA; NbExp=2; IntAct=EBI-20651925, EBI-16940407;
CC Q6R2K3; Q6XAT2: ERL2; NbExp=2; IntAct=EBI-20651925, EBI-16895926;
CC Q6R2K3; C0LGQ5: GSO1; NbExp=2; IntAct=EBI-20651925, EBI-16905069;
CC Q6R2K3; Q9ZVD4: LRR-RLK; NbExp=2; IntAct=EBI-20651925, EBI-20651739;
CC Q6R2K3; C0LGU0: PRK1; NbExp=2; IntAct=EBI-20651925, EBI-20665360;
CC Q6R2K3; Q8RWZ1: SUB; NbExp=2; IntAct=EBI-20651925, EBI-17072125;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6R2K3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6R2K3-2; Sequence=VSP_029610, VSP_029611;
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: Plants do not show root phenotype alteration.
CC {ECO:0000269|PubMed:17027738}.
CC -!- MISCELLANEOUS: Over-expression of SRF3 led to male-sterility in both
CC 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 -!- CAUTION: An alternative isoform might be encoded by the 3'part of the
CC transcript derived from AK228109. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD14467.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAF00067.1; Type=Erroneous translation; Note=Wrong choice of CDS.; Evidence={ECO:0000305};
CC Sequence=CAB77824.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY518288; AAR99871.1; -; mRNA.
DR EMBL; AC005275; AAD14467.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161496; CAB77824.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE82313.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM67568.1; -; Genomic_DNA.
DR EMBL; AK228109; BAF00067.1; ALT_SEQ; mRNA.
DR PIR; A85043; A85043.
DR RefSeq; NP_001329389.1; NM_001340445.1. [Q6R2K3-1]
DR RefSeq; NP_192248.2; NM_116577.5. [Q6R2K3-1]
DR AlphaFoldDB; Q6R2K3; -.
DR SMR; Q6R2K3; -.
DR BioGRID; 13232; 37.
DR IntAct; Q6R2K3; 45.
DR STRING; 3702.AT4G03390.1; -.
DR iPTMnet; Q6R2K3; -.
DR SwissPalm; Q6R2K3; -.
DR PaxDb; Q6R2K3; -.
DR PRIDE; Q6R2K3; -.
DR ProteomicsDB; 226725; -. [Q6R2K3-1]
DR EnsemblPlants; AT4G03390.1; AT4G03390.1; AT4G03390. [Q6R2K3-1]
DR EnsemblPlants; AT4G03390.2; AT4G03390.2; AT4G03390. [Q6R2K3-1]
DR GeneID; 827941; -.
DR Gramene; AT4G03390.1; AT4G03390.1; AT4G03390. [Q6R2K3-1]
DR Gramene; AT4G03390.2; AT4G03390.2; AT4G03390. [Q6R2K3-1]
DR KEGG; ath:AT4G03390; -.
DR Araport; AT4G03390; -.
DR TAIR; locus:2125566; AT4G03390.
DR eggNOG; ENOG502QR8F; Eukaryota.
DR HOGENOM; CLU_000288_92_2_1; -.
DR InParanoid; Q6R2K3; -.
DR OMA; AGGRCCF; -.
DR PhylomeDB; Q6R2K3; -.
DR PRO; PR:Q6R2K3; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q6R2K3; baseline and differential.
DR Genevisible; Q6R2K3; 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:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0007623; P:circadian rhythm; IEP:TAIR.
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; 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 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..29
FT /evidence="ECO:0000255"
FT CHAIN 30..776
FT /note="Protein STRUBBELIG-RECEPTOR FAMILY 3"
FT /id="PRO_0000311843"
FT TOPO_DOM 30..35
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 36..56
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 57..316
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 317..337
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 338..776
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 99..120
FT /note="LRR 1"
FT REPEAT 121..143
FT /note="LRR 2"
FT REPEAT 145..167
FT /note="LRR 3"
FT REPEAT 169..191
FT /note="LRR 4"
FT REPEAT 193..215
FT /note="LRR 5"
FT REPEAT 216..236
FT /note="LRR 6"
FT DOMAIN 485..763
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 251..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 355..440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 265..282
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 384..414
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..440
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 491..499
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 513
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 72
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 179
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 248
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 253
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 310
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 258..265
FT /note="APSLSPSL -> TTTTSSFG (in isoform 2)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_029610"
FT VAR_SEQ 266..776
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_029611"
SQ SEQUENCE 776 AA; 84720 MW; 566E9F703A9D3773 CRC64;
MAAKRSIYCL LLLPLLLSLL IWIPSISLAA TNPDDVAAIN GLFAALGAPV LPGWIASGGD
PCGEAWQGII CNVSDIISIT VNAANLQGEL GDNLAKFTSI RGIDFSNNRI GGSIPSTLPV
TLQHFFLSAN QFTGSIPESL GTLSFLNDMS LNDNLLSGEL PDVFQNLVGL INLDISSNNI
SGTLPPSMEN LLTLTTLRVQ NNQLSGTLDV LQGLPLQDLN IENNLFSGPI PDKLLSIPKF
LHEGNPFNAT MINSTSTAPS LSPSLSPTKP APTRPFSGVP PPPNERNRGK VADGPSDSEG
SSSENSKGKN SSHTKKIILI AFAGVLVFII LVLAILLLLP KCARRREHAN RVFKPHQVGA
DRGSRENALE NGTPVLPPPG RSEKVQREPF KKAGEEPKVL HDLERLRRPA PISRQESQDI
DFSMLMPPPP PPPPPPPPPP LDEKVTVMPI ISPERPVKKT SPKRLPLTSV KHYSIASLQQ
YTESFAQENL IGSGMLGSVY RARLPNGKLF AVKKLDKRAS EQQQDHEFIE LVNNIDMIRH
SNIVELVGYC AEHDQRLLVY EYCSNGTLQD GLHSDDEFKK KLSWNTRVSM ALGAARALEY
LHEVCEPPII HRNFKSANVL LDDDLSVLVS DCGLAPLISS GSVSQLSGQL LAAYGYGAPE
FDSGIYTWQS DVYSFGVVML ELLTGRMSYD RDRSRGEQFL VRWAIPQLHD IDALGKMVDP
SLNGQYPAKS LSHFADIISR CVQSEPEFRP LMSEVVQDLL DMIRRERHGS GDSTAD
