GenomeNet

Database: UniProt
Entry: Q9S972
LinkDB: Q9S972
Original site: Q9S972 
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   16-JAN-2019, entry version 139.
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;
GN   ORFNames=F1E22.21;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC   STRAIN=cv. C24;
RX   PubMed=7866027; DOI=10.1105/tpc.6.12.1829;
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.,
RA   White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
RA   Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
RA   Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
RA   Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
RA   Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
RA   Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
RA   Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
RA   Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
RA   Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
RA   Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
RA   Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
RA   Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
RA   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.,
RA   Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis
RT   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
RT   reference 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.,
RA   Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA   Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA   Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA   Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA   Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA   Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA   Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA   Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA   Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA   Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA   Yuan S., Shinozaki K., Davis R.W., Theologis A., 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.,
RA   Hayashizaki Y., 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
RP   PUB38, 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.,
RA   Chilelli A., Goring D.R.;
RT   "Interactions between the S-domain receptor kinases and AtPUB-ARM E3
RT   ubiquitin ligases suggest a conserved signaling pathway in
RT   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,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216;
CC         EC=2.7.11.1; 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
CC       type I 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
CC       protein 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; Positions=599; Evidence={ECO:0000305};
CC   -!- WEB RESOURCE: Name=PlantP kinase Classification PPC;
CC       URL="http://plantsp.genomics.purdue.edu/family/class.html";
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   UniGene; At.302; -.
DR   ProteinModelPortal; Q9S972; -.
DR   SMR; Q9S972; -.
DR   BioGrid; 28112; 4.
DR   STRING; 3702.AT1G65800.1; -.
DR   PaxDb; Q9S972; -.
DR   PRIDE; Q9S972; -.
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; ENOG410IVAT; Eukaryota.
DR   eggNOG; COG0515; LUCA.
DR   HOGENOM; HOG000116559; -.
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: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:0034613; P:cellular protein localization; IGI:TAIR.
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; Pkinase_Tyr; 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; Complete proteome; Disulfide bond;
KW   EGF-like domain; Glycoprotein; Kinase; Lectin; Membrane;
KW   Nucleotide-binding; Phosphoprotein; Reference proteome;
KW   Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     31       {ECO:0000255}.
FT   CHAIN        32    847       Receptor-like serine/threonine-protein
FT                                kinase SD1-6.
FT                                /FTId=PRO_0000401294.
FT   TOPO_DOM     32    439       Extracellular. {ECO:0000255}.
FT   TRANSMEM    440    460       Helical. {ECO:0000255}.
FT   TOPO_DOM    461    847       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN       32    151       Bulb-type lectin. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00038}.
FT   DOMAIN      291    327       EGF-like; atypical.
FT   DOMAIN      345    426       PAN. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00315}.
FT   DOMAIN      523    813       Protein kinase. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   NP_BIND     529    537       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   REGION      612    629       CaM-binding. {ECO:0000250}.
FT   COMPBIAS    824    827       Poly-Ser.
FT   ACT_SITE    648    648       Proton acceptor. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159, ECO:0000255|PROSITE-
FT                                ProRule:PRU10027}.
FT   BINDING     551    551       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   MOD_RES     557    557       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9LPZ9}.
FT   MOD_RES     652    652       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9LPZ9}.
FT   MOD_RES     665    665       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9LPZ9}.
FT   MOD_RES     682    682       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:Q9LPZ9}.
FT   MOD_RES     824    824       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9LPZ9}.
FT   CARBOHYD     29     29       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD     41     41       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD     92     92       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    116    116       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    171    171       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    256    256       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    385    385       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    295    307       {ECO:0000250}.
FT   DISULFID    301    315       {ECO:0000250}.
FT   DISULFID    376    401       {ECO:0000250}.
FT   DISULFID    380    386       {ECO:0000250}.
FT   CONFLICT     11     11       Y -> YF (in Ref. 1; no nucleotide entry).
FT                                {ECO:0000305}.
FT   CONFLICT    328    328       A -> AW (in Ref. 1; no nucleotide entry).
FT                                {ECO:0000305}.
FT   CONFLICT    445    445       I -> L (in Ref. 1; no nucleotide entry).
FT                                {ECO:0000305}.
FT   CONFLICT    478    478       L -> LQ (in Ref. 1; no nucleotide entry).
FT                                {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
//
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