SD22_ARATH
ID SD22_ARATH Reviewed; 797 AA.
AC Q39203; F4JH44; O23068;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=G-type lectin S-receptor-like serine/threonine-protein kinase SD2-2;
DE EC=2.7.11.1;
DE AltName: Full=Receptor-like kinase 4;
DE AltName: Full=S-domain-2 (SD2) receptor kinase 2;
DE Short=SD2-2;
DE Flags: Precursor;
GN Name=SD22; Synonyms=RLK4; OrderedLocusNames=At4g00340;
GN ORFNames=A_IG005I10.19, F5I10.19;
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].
RC STRAIN=cv. Columbia;
RX PubMed=8220453; DOI=10.1111/j.1365-313x.1993.tb00164.x;
RA Walker J.C.;
RT "Receptor-like protein kinase genes of Arabidopsis thaliana.";
RL Plant J. 3:451-456(1993).
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 FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AUTOPHOSPHORYLATION, AND
RP MUTAGENESIS OF LYS-490.
RX DOI=10.1016/S0168-9452(98)00247-7;
RA Coelloa P., Sassena A., Haywoodb V., Davisb K.R., Walker J.C.;
RT "Biochemical characterization and expression of RLK4, a receptor-like
RT kinase from Arabidopsis thaliana.";
RL Plant Sci. 142:83-91(1999).
RN [5]
RP SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC STRAIN=cv. La-0;
RX PubMed=14506206; DOI=10.1074/mcp.t300006-mcp200;
RA Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
RT "Large-scale analysis of in vivo phosphorylated membrane proteins by
RT immobilized metal ion affinity chromatography and mass spectrometry.";
RL Mol. Cell. Proteomics 2:1234-1243(2003).
RN [6]
RP SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [7]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=18552232; DOI=10.1104/pp.108.123380;
RA Samuel M.A., Mudgil Y., Salt J.N., Delmas F., Ramachandran S., Chilelli A.,
RA Goring D.R.;
RT "Interactions between the S-domain receptor kinases and AtPUB-ARM E3
RT ubiquitin ligases suggest a conserved signaling pathway in Arabidopsis.";
RL Plant Physiol. 147:2084-2095(2008).
CC -!- FUNCTION: Serine/threonine-protein kinase. {ECO:0000269|Ref.4}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000269|Ref.4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000269|Ref.4};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14506206,
CC ECO:0000269|PubMed:15308754}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:14506206, ECO:0000269|PubMed:15308754}.
CC -!- TISSUE SPECIFICITY: Expressed in the shoot apex and roots, specifically
CC in lateral roots and at the root-hypocotyl transition zone.
CC {ECO:0000269|Ref.4}.
CC -!- PTM: Autophosphorylated.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB62838.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAF02796.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AEE81862.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB80792.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; M84659; AAA32858.1; -; mRNA.
DR EMBL; AF013293; AAB62838.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AF195115; AAF02796.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161471; CAB80792.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE81862.1; ALT_SEQ; Genomic_DNA.
DR PIR; T01537; T01537.
DR RefSeq; NP_567172.4; NM_116257.5.
DR AlphaFoldDB; Q39203; -.
DR SMR; Q39203; -.
DR BioGRID; 13370; 7.
DR IntAct; Q39203; 7.
DR STRING; 3702.AT4G00340.1; -.
DR PaxDb; Q39203; -.
DR PRIDE; Q39203; -.
DR ProteomicsDB; 232720; -.
DR GeneID; 828079; -.
DR KEGG; ath:AT4G00340; -.
DR Araport; AT4G00340; -.
DR eggNOG; ENOG502QRRX; Eukaryota.
DR HOGENOM; CLU_000288_116_2_1; -.
DR InParanoid; Q39203; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; Q39203; -.
DR PRO; PR:Q39203; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q39203; baseline and differential.
DR Genevisible; Q39203; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005516; F:calmodulin binding; ISS:UniProtKB.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:UniProt.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0048544; P:recognition of pollen; IEA:InterPro.
DR CDD; cd00028; B_lectin; 1.
DR Gene3D; 2.90.10.10; -; 1.
DR InterPro; IPR001480; Bulb-type_lectin_dom.
DR InterPro; IPR036426; Bulb-type_lectin_dom_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR003609; Pan_app.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR000858; S_locus_glycoprot_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR024171; SRK-like_kinase.
DR Pfam; PF01453; B_lectin; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00954; S_locus_glycop; 1.
DR PIRSF; PIRSF000641; SRK; 1.
DR SMART; SM00108; B_lectin; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF51110; SSF51110; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50927; BULB_LECTIN; 1.
DR PROSITE; PS50948; PAN; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Disulfide bond; EGF-like domain; Glycoprotein;
KW Kinase; Lectin; Membrane; Nucleotide-binding; Phosphoprotein; Receptor;
KW Reference proteome; Serine/threonine-protein kinase; Signal; Transferase;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..797
FT /note="G-type lectin S-receptor-like serine/threonine-
FT protein kinase SD2-2"
FT /id="PRO_5000143618"
FT TOPO_DOM 24..401
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 402..422
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 423..797
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 24..139
FT /note="Bulb-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00038"
FT DOMAIN 274..310
FT /note="EGF-like; atypical"
FT DOMAIN 321..407
FT /note="PAN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00315"
FT DOMAIN 461..742
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 550..566
FT /note="CaM-binding"
FT /evidence="ECO:0000250"
FT REGION 767..797
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 585
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 467..475
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 490
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 30
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 49
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 150
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 197
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 366
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 397
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 278..290
FT /evidence="ECO:0000250"
FT DISULFID 284..298
FT /evidence="ECO:0000250"
FT DISULFID 359..381
FT /evidence="ECO:0000250"
FT DISULFID 363..369
FT /evidence="ECO:0000250"
FT MUTAGEN 490
FT /note="K->E: Impaired serine/threonine-protein kinase
FT activity."
FT /evidence="ECO:0000269|Ref.4"
SQ SEQUENCE 797 AA; 88493 MW; CEF73CEB5EEADBFF CRC64;
MPCTTYLPLL LLLFLLPPPS VQSKVIIKGN QTILSFKAIF RLGFFSTTNG SSNWYLGISY
ASMPTPTHVW VANRIRPVSD PDSSTLELTS TGYLIVSNLR DGVVWQTDNK QPGTDFRFSE
TGNLILINDD GSPVWQSFDN PTDTWLPGMN VTGLTAMTSW RSLFDPSPGF YSLRLSPSFN
EFQLVYKGTT PYWSTGNWTG EAFVGVPEMT IPYIYRFHFV NPYTPTASFW YIVPPLDSVS
EPRLTRFMVG ANGQLKQYTW DPQTQSWNMF WLQPEDPCRV YNLCGQLGFC SSELLKPCAC
IRGFRPRNDA AWRSDDYSDG CRRENGDSGE KSDTFEAVGD LRYDGDVKMS RLQVSKSSCA
KTCLGNSSCV GFYHKEKSNL CKILLESPNN LKNSKGNISK SIIILCSVVG SISVLGFTLL
VPLILLKRSR KRKKTRKQDE DGFAVLNLKV FSFKELQSAT NGFSDKVGHG GFGAVFKGTL
PGSSTFVAVK RLERPGSGES EFRAEVCTIG NIQHVNLVRL RGFCSENLHR LLVYDYMPQG
SLSSYLSRTS PKLLSWETRF RIALGTAKGI AYLHEGCRDC IIHCDIKPEN ILLDSDYNAK
VSDFGLAKLL GRDFSRVLAT MRGTWGYVAP EWISGLPITT KADVYSFGMT LLELIGGRRN
VIVNSDTLGE KETEPEKWFF PPWAAREIIQ GNVDSVVDSR LNGEYNTEEV TRMATVAIWC
IQDNEEIRPA MGTVVKMLEG VVEVTVPPPP KLIQALVSGD SYRGVSGTSC SEGHGCSDLN
TGLSSPGSRS SFGRPSP
