SD16_ARATH
ID SD16_ARATH Reviewed; 847 AA.
AC Q9S972; Q0WL12; Q9SHX7;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Receptor-like serine/threonine-protein kinase SD1-6;
DE EC=2.7.11.1;
DE AltName: Full=Arabidopsis thaliana receptor kinase 2;
DE AltName: Full=S-domain-1 (SD1) receptor kinase 6;
DE Short=SD1-6;
DE Flags: Precursor;
GN Name=SD16; Synonyms=ARK2; OrderedLocusNames=At1g65800; ORFNames=F1E22.21;
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 [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC STRAIN=cv. C24;
RX PubMed=7866027; DOI=10.2307/3869911;
RA Dwyer K.G., Kandasamy M.K., Mahosky D.I., Acciai J., Kudish B.I.,
RA Miller J.E., Nasrallah M.E., Nasrallah J.B.;
RT "A superfamily of S locus-related sequences in Arabidopsis: diverse
RT structures and expression patterns.";
RL Plant Cell 6:1829-1843(1994).
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;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 354-847.
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 [6]
RP GENE FAMILY, NOMENCLATURE, INTERACTION WITH PUB9; PUB13; PUB14 AND PUB38,
RP AND CATALYTIC ACTIVITY.
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: Involved in the regulation of cellular expansion and
CC differentiation. {ECO:0000250}.
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|PubMed:18552232};
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|PubMed:18552232};
CC -!- SUBUNIT: Interacts with PUB9, PUB13, PUB14 and PUB38.
CC {ECO:0000269|PubMed:18552232}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in cotyledons, leaves and sepals.
CC {ECO:0000269|PubMed:7866027}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF23832.1; Type=Erroneous gene model prediction; Note=The predicted gene At1g65790 has been split into 2 genes: At1g65790 and At1g65800.; Evidence={ECO:0000305};
CC Sequence=AY045777; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AC007234; AAF23832.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE34424.1; -; Genomic_DNA.
DR EMBL; AY045777; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK230397; BAF02195.1; -; mRNA.
DR RefSeq; NP_176756.1; NM_105253.2.
DR AlphaFoldDB; Q9S972; -.
DR SMR; Q9S972; -.
DR BioGRID; 28112; 4.
DR STRING; 3702.AT1G65800.1; -.
DR PaxDb; Q9S972; -.
DR PRIDE; Q9S972; -.
DR ProteomicsDB; 232871; -.
DR EnsemblPlants; AT1G65800.1; AT1G65800.1; AT1G65800.
DR GeneID; 842891; -.
DR Gramene; AT1G65800.1; AT1G65800.1; AT1G65800.
DR KEGG; ath:AT1G65800; -.
DR Araport; AT1G65800; -.
DR TAIR; locus:2018506; AT1G65800.
DR eggNOG; ENOG502QS2H; Eukaryota.
DR HOGENOM; CLU_000288_116_5_1; -.
DR InParanoid; Q9S972; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; Q9S972; -.
DR PRO; PR:Q9S972; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9S972; baseline and differential.
DR Genevisible; Q9S972; AT.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
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:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IDA:TAIR.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0004675; F:transmembrane receptor protein serine/threonine kinase activity; ISS:TAIR.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:TAIR.
DR GO; GO:0006468; P:protein phosphorylation; IDA:TAIR.
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; IPR022126; S-locus_recpt_kinase.
DR InterPro; IPR021820; S-locus_recpt_kinase_C.
DR InterPro; IPR000858; S_locus_glycoprot_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR024171; SRK-like_kinase.
DR Pfam; PF01453; B_lectin; 1.
DR Pfam; PF11883; DUF3403; 1.
DR Pfam; PF12398; DUF3660; 1.
DR Pfam; PF08276; PAN_2; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF00954; S_locus_glycop; 1.
DR PIRSF; PIRSF000641; SRK; 1.
DR SMART; SM00108; B_lectin; 1.
DR SMART; SM00473; PAN_AP; 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;
KW Reference proteome; Serine/threonine-protein kinase; Signal; Transferase;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..31
FT /evidence="ECO:0000255"
FT CHAIN 32..847
FT /note="Receptor-like serine/threonine-protein kinase SD1-6"
FT /id="PRO_0000401294"
FT TOPO_DOM 32..439
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 440..460
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 461..847
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 32..151
FT /note="Bulb-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00038"
FT DOMAIN 291..327
FT /note="EGF-like; atypical"
FT DOMAIN 345..426
FT /note="PAN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00315"
FT DOMAIN 523..813
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 612..629
FT /note="CaM-binding"
FT /evidence="ECO:0000250"
FT ACT_SITE 648
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 529..537
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 551
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 557
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT MOD_RES 652
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT MOD_RES 665
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT MOD_RES 682
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT MOD_RES 824
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT CARBOHYD 29
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 41
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 92
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 116
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 171
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 256
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 385
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 295..307
FT /evidence="ECO:0000250"
FT DISULFID 301..315
FT /evidence="ECO:0000250"
FT DISULFID 376..401
FT /evidence="ECO:0000250"
FT DISULFID 380..386
FT /evidence="ECO:0000250"
FT CONFLICT 11
FT /note="Y -> YF (in Ref. 1; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 328
FT /note="A -> AW (in Ref. 1; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 445
FT /note="I -> L (in Ref. 1; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 478
FT /note="L -> LQ (in Ref. 1; no nucleotide entry)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 847 AA; 95980 MW; EC721042AE9A5182 CRC64;
MRNVPNYHHS YFILFIIILF LAFSVYASNF SATESLTISS NKTIISPSQI FELGFFNPDS
SSRWYLGIWY KIIPIRTYVW VANRDNPLSS SNGTLKISDN NLVIFDQSDR PVWSTNITGG
DVRSPVAAEL LDYGNFVLRD SKNNKPSGFL WQSFDFPTDT LLSDMKMGWD NKSGGFNRIL
RSWKTTDDPS SGDFSTKLRT SGFPEFYIYN KESITYRSGP WLGNRFSSVP GMKPVDYIDN
SFTENNQQVV YSYRVNKTNI YSILSLSSTG LLQRLTWMEA AQSWKQLWYS PKDLCDNYKE
CGNYGYCDAN TSPICNCIKG FEPMNEQAAL RDDSVGCVRK TKLSCDGRDG FVRLKKMRLP
DTTETSVDKG IGLKECEERC LKGCNCTAFA NTDIRNGGSG CVIWSGGLFD IRNYAKGGQD
LYVRVAAGDL EDKRIKSKKI IGSSIGVSIL LLLSFIIFHF WKRKQKRSIT IQTPIVDLVR
SQDSLMNELV KASRSYTSKE NKTDYLELPL MEWKALAMAT NNFSTDNKLG QGGFGIVYKG
MLLDGKEIAV KRLSKMSSQG TDEFMNEVRL IAKLQHINLV RLLGCCVDKG EKMLIYEYLE
NLSLDSHLFD QTRSSNLNWQ KRFDIINGIA RGLLYLHQDS RCRIIHRDLK ASNVLLDKNM
TPKISDFGMA RIFGREETEA NTRRVVGTYG YMSPEYAMDG IFSMKSDVFS FGVLLLEIIS
GKRNKGFYNS NRDLNLLGFV WRHWKEGKEL EIVDPINIDA LSSEFPTHEI LRCIQIGLLC
VQERAEDRPV MSSVMVMLGS ETTAIPQPKR PGFCVGRSSL EVDSSSSTQR DDECTVNQVT
LSVIDAR
