SD17_ARATH
ID SD17_ARATH Reviewed; 843 AA.
AC Q39086; Q9SHX7;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Receptor-like serine/threonine-protein kinase SD1-7;
DE EC=2.7.11.1;
DE AltName: Full=Arabidopsis thaliana receptor kinase 1;
DE AltName: Full=S-domain-1 (SD1) receptor kinase 7;
DE Short=SD1-7;
DE Flags: Precursor;
GN Name=SD17; Synonyms=ARK1; OrderedLocusNames=At1g65790; ORFNames=F1E22.15;
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], TISSUE SPECIFICITY, AND ALTERNATIVE
RP SPLICING.
RC STRAIN=cv. C24;
RX PubMed=16668863; DOI=10.1104/pp.99.1.284;
RA Tobias C.M., Howlett B., Nasrallah J.B.;
RT "An Arabidopsis thaliana gene with sequence similarity to the S-Locus
RT receptor kinase of Brassica oleracea: sequence and expression.";
RL Plant Physiol. 99:284-290(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, ALTERNATIVE SPLICING,
RP PHOSPHORYLATION, AND CATALYTIC ACTIVITY.
RC STRAIN=cv. C24;
RX PubMed=8811866; DOI=10.1046/j.1365-313x.1996.10030523.x;
RA Tobias C.M., Nasrallah J.B.;
RT "An S-locus-related gene in Arabidopsis encodes a functional kinase and
RT produces two classes of transcripts.";
RL Plant J. 10:523-531(1996).
RN [3]
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 [4]
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 [5]
RP INDUCTION BY WOUNDING AND XANTHOMONAS CAMPESTRIS.
RX PubMed=11814694; DOI=10.1016/s0378-1119(01)00821-6;
RA Pastuglia M., Swarup R., Rocher A., Saindrenan P., Roby D., Dumas C.,
RA Cock J.M.;
RT "Comparison of the expression patterns of two small gene families of S gene
RT family receptor kinase genes during the defence response in Brassica
RT oleracea and Arabidopsis thaliana.";
RL Gene 282:215-225(2002).
RN [6]
RP GENE FAMILY, NOMENCLATURE, INTERACTION WITH PUB9; PUB13; PUB14 AND PUB38,
RP CATALYTIC ACTIVITY, MUTAGENESIS OF LYS-547, FUNCTION, AND DISRUPTION
RP PHENOTYPE.
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. Mediates subcellular relocalization of PUB9 from
CC nucleus to plasma membrane in a protein-phosphorylation-dependent
CC manner. May be involved in the abscisic acid-mediated signaling
CC pathway, at least during germination. {ECO:0000269|PubMed:18552232,
CC ECO:0000269|PubMed:8811866}.
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, ECO:0000269|PubMed:8811866};
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 ECO:0000269|PubMed:8811866};
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q39086-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q39086-2; Sequence=Not described;
CC -!- TISSUE SPECIFICITY: Mostly expressed in leaves, and, to a lower extent,
CC in stems and flower buds. {ECO:0000269|PubMed:16668863}.
CC -!- INDUCTION: By wounding and Xanthomonas campestris pv. campestris.
CC {ECO:0000269|PubMed:11814694}.
CC -!- PTM: Autophosphorylated on serine and threonine residues.
CC {ECO:0000269|PubMed:8811866}.
CC -!- DISRUPTION PHENOTYPE: Reduced abscisic acid (ABA) sensitivity during
CC seed germination. {ECO:0000269|PubMed:18552232}.
CC -!- MISCELLANEOUS: [Isoform 2]: Receptor domain alone. {ECO:0000305}.
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};
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DR EMBL; M80238; AAA32786.1; -; Genomic_DNA.
DR EMBL; AC007234; AAF23832.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE34423.1; -; Genomic_DNA.
DR PIR; S70769; S70769.
DR RefSeq; NP_176755.1; NM_105252.2. [Q39086-1]
DR AlphaFoldDB; Q39086; -.
DR SMR; Q39086; -.
DR BioGRID; 28111; 5.
DR IntAct; Q39086; 1.
DR STRING; 3702.AT1G65790.1; -.
DR iPTMnet; Q39086; -.
DR PaxDb; Q39086; -.
DR PRIDE; Q39086; -.
DR ProteomicsDB; 232753; -. [Q39086-1]
DR EnsemblPlants; AT1G65790.1; AT1G65790.1; AT1G65790. [Q39086-1]
DR GeneID; 842890; -.
DR Gramene; AT1G65790.1; AT1G65790.1; AT1G65790. [Q39086-1]
DR KEGG; ath:AT1G65790; -.
DR Araport; AT1G65790; -.
DR TAIR; locus:2018546; AT1G65790.
DR eggNOG; ENOG502QS2H; Eukaryota.
DR HOGENOM; CLU_000288_116_5_1; -.
DR InParanoid; Q39086; -.
DR OrthoDB; 684563at2759; -.
DR PRO; PR:Q39086; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q39086; baseline and differential.
DR Genevisible; Q39086; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
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; IDA:UniProtKB.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0071215; P:cellular response to abscisic acid stimulus; IMP: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 Abscisic acid signaling pathway; Alternative splicing; ATP-binding;
KW Cell membrane; Disulfide bond; EGF-like domain; Glycoprotein; Kinase;
KW Lectin; Membrane; Nucleotide-binding; Phosphoprotein; Receptor;
KW Reference proteome; Serine/threonine-protein kinase; Signal; Transferase;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..31
FT /evidence="ECO:0000255"
FT CHAIN 32..843
FT /note="Receptor-like serine/threonine-protein kinase SD1-7"
FT /id="PRO_0000401295"
FT TOPO_DOM 32..435
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 436..456
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 457..843
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 286..322
FT /note="EGF-like; atypical"
FT DOMAIN 341..422
FT /note="PAN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00315"
FT DOMAIN 519..809
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 608..625
FT /note="CaM-binding"
FT /evidence="ECO:0000250"
FT ACT_SITE 644
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 525..533
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 547
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305"
FT MOD_RES 553
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT MOD_RES 648
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT MOD_RES 661
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT MOD_RES 678
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT MOD_RES 820
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
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 236
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 251
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 381
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 290..302
FT /evidence="ECO:0000250"
FT DISULFID 296..310
FT /evidence="ECO:0000250"
FT DISULFID 372..397
FT /evidence="ECO:0000250"
FT DISULFID 376..382
FT /evidence="ECO:0000250"
FT MUTAGEN 547
FT /note="K->A: Loss of kinase activity."
FT /evidence="ECO:0000269|PubMed:18552232"
SQ SEQUENCE 843 AA; 95946 MW; 1D55EF0DAFE75967 CRC64;
MRSVPNYHHS FFIFLILILF LAFSVSPNTL SATESLTISS NKTIISPSQI FELGFFNPAS
SSRWYLGIWY KIIPIRTYVW VANRDNPLSS SNGTLKISGN NLVIFDQSDR PVWSTNITGG
DVRSPVAAEL LDNGNFLLRD SNNRLLWQSF DFPTDTLLAE MKLGWDQKTG FNRILRSWKT
TDDPSSGEFS TKLETSEFPE FYICSKESIL YRSGPWNGMR FSSVPGTIQV DYMVYNFTAS
KEEVTYSYRI NKTNLYSRLY LNSAGLLQRL TWFETTQSWK QLWYSPKDLC DNYKVCGNFG
YCDSNSLPNC YCIKGFKPVN EQAWDLRDGS AGCMRKTRLS CDGRDGFTRL KRMKLPDTTA
TIVDREIGLK VCKERCLEDC NCTAFANADI RNGGSGCVIW TREILDMRNY AKGGQDLYVR
LAAAELEDKR IKNEKIIGSS IGVSILLLLS FVIFHFWKRK QKRSITIQTP NVDQVRSQDS
LINDVVVSRR GYTSKEKKSE YLELPLLELE ALATATNNFS NDNKLGQGGF GIVYKGRLLD
GKEIAVKRLS KMSSQGTDEF MNEVRLIAKL QHINLVRLLG CCVDKGEKML IYEYLENLSL
DSHLFDQTRS SNLNWQKRFD IINGIARGLL YLHQDSRCRI IHRDLKASNV LLDKNMTPKI
SDFGMARIFG REETEANTRR VVGTYGYMSP EYAMDGIFSM KSDVFSFGVL LLEIISGKRN
KGFYNSNRDL NLLGFVWRHW KEGNELEIVD PINIDSLSSK FPTHEILRCI QIGLLCVQER
AEDRPVMSSV MVMLGSETTA IPQPKRPGFC IGRSPLEADS SSSTQRDDEC TVNQITLSVI
DAR
