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Database: UniProt
Entry: SERK5_ARATH
LinkDB: SERK5_ARATH
Original site: SERK5_ARATH 
ID   SERK5_ARATH             Reviewed;         601 AA.
AC   Q8LPS5; C0LGK2; Q9SKG4;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 2.
DT   27-MAR-2024, entry version 158.
DE   RecName: Full=Somatic embryogenesis receptor kinase 5;
DE            Short=AtSERK5;
DE            EC=2.7.11.1;
DE   AltName: Full=Somatic embryogenesis receptor-like kinase 5;
DE   Flags: Precursor;
GN   Name=SERK5; OrderedLocusNames=At2g13800; ORFNames=F13J11.15;
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 [MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=20064227; DOI=10.1186/1471-2164-11-19;
RA   Gou X., He K., Yang H., Yuan T., Lin H., Clouse S.D., Li J.;
RT   "Genome-wide cloning and sequence analysis of leucine-rich repeat receptor-
RT   like protein kinase genes in Arabidopsis thaliana.";
RL   BMC Genomics 11:19-19(2010).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(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] OF 5-601.
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   IDENTIFICATION.
RX   PubMed=11523644; DOI=10.1007/s004250000471;
RA   Baudino S., Hansen S., Brettschneider R., Hecht V.F.G., Dresselhaus T.,
RA   Loerz H., Dumas C., Rogowsky P.M.;
RT   "Molecular characterisation of two novel maize LRR receptor-like kinases,
RT   which belong to the SERK gene family.";
RL   Planta 213:1-10(2001).
RN   [6]
RP   AUTOPHOSPHORYLATION, AND PHOSPHORYLATION AT THR-441 AND SER-506.
RX   PubMed=19105183; DOI=10.1002/pmic.200701059;
RA   Karlova R., Boeren S., van Dongen W., Kwaaitaal M., Aker J., Vervoort J.,
RA   de Vries S.C.;
RT   "Identification of in vitro phosphorylation sites in the Arabidopsis
RT   thaliana somatic embryogenesis receptor-like kinases.";
RL   Proteomics 9:368-379(2009).
RN   [7]
RP   INTERACTION WITH TMK4/BARK1.
RX   PubMed=23921992; DOI=10.1093/pcp/pct106;
RA   Kim M.H., Kim Y., Kim J.W., Lee H.S., Lee W.S., Kim S.K., Wang Z.Y.,
RA   Kim S.H.;
RT   "Identification of Arabidopsis BAK1-associating receptor-like kinase 1
RT   (BARK1) and characterization of its gene expression and brassinosteroid-
RT   regulated root phenotypes.";
RL   Plant Cell Physiol. 54:1620-1634(2013).
CC   -!- FUNCTION: Serine/threonine-kinase of unknown function.
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   -!- 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;
CC   -!- SUBUNIT: Interacts with TMK4/BARK1 (PubMed:23921992).
CC       {ECO:0000269|PubMed:23921992}.
CC   -!- INTERACTION:
CC       Q8LPS5; C0LGI5: At1g69990; NbExp=2; IntAct=EBI-16887868, EBI-20651225;
CC       Q8LPS5; Q94F62: BAK1; NbExp=4; IntAct=EBI-16887868, EBI-617138;
CC       Q8LPS5; Q9ZWC8: BRL1; NbExp=2; IntAct=EBI-16887868, EBI-590903;
CC       Q8LPS5; Q9LJF3: BRL3; NbExp=2; IntAct=EBI-16887868, EBI-20651413;
CC       Q8LPS5; C0LGT6: EFR; NbExp=4; IntAct=EBI-16887868, EBI-8801168;
CC       Q8LPS5; Q42371: ERECTA; NbExp=3; IntAct=EBI-16887868, EBI-16940407;
CC       Q8LPS5; Q6XAT2: ERL2; NbExp=4; IntAct=EBI-16887868, EBI-16895926;
CC       Q8LPS5; C0LGQ5: GSO1; NbExp=2; IntAct=EBI-16887868, EBI-16905069;
CC       Q8LPS5; C0LGX3: HSL2; NbExp=2; IntAct=EBI-16887868, EBI-16904927;
CC       Q8LPS5; Q9ZVD4: LRR-RLK; NbExp=2; IntAct=EBI-16887868, EBI-20651739;
CC       Q8LPS5; Q9ZRF9: RPK1; NbExp=2; IntAct=EBI-16887868, EBI-1238953;
CC       Q8LPS5; Q9SKG5: SERK4; NbExp=4; IntAct=EBI-16887868, EBI-6290483;
CC       Q8LPS5; Q8LPS5: SERK5; NbExp=2; IntAct=EBI-16887868, EBI-16887868;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC       membrane protein {ECO:0000305}.
CC   -!- PTM: Autophosphorylated. {ECO:0000269|PubMed:19105183}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD28319.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; FJ708692; ACN59287.1; -; mRNA.
DR   EMBL; AC006436; AAD28319.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002685; AEC06260.1; -; Genomic_DNA.
DR   EMBL; CP002685; ANM62036.1; -; Genomic_DNA.
DR   EMBL; AY094412; AAM19787.1; -; mRNA.
DR   EMBL; BT001116; AAN64507.1; -; mRNA.
DR   PIR; H84510; H84510.
DR   RefSeq; NP_001318220.1; NM_001335399.1.
DR   RefSeq; NP_001324219.1; NM_001335400.1.
DR   RefSeq; NP_001324220.1; NM_001335401.1.
DR   RefSeq; NP_179000.3; NM_126956.4.
DR   AlphaFoldDB; Q8LPS5; -.
DR   SMR; Q8LPS5; -.
DR   BioGRID; 1224; 36.
DR   IntAct; Q8LPS5; 46.
DR   STRING; 3702.Q8LPS5; -.
DR   GlyCosmos; Q8LPS5; 6 sites, No reported glycans.
DR   iPTMnet; Q8LPS5; -.
DR   PaxDb; 3702-AT2G13800-1; -.
DR   ProteomicsDB; 234485; -.
DR   EnsemblPlants; AT2G13800.1; AT2G13800.1; AT2G13800.
DR   EnsemblPlants; AT2G13800.3; AT2G13800.3; AT2G13800.
DR   GeneID; 815863; -.
DR   Gramene; AT2G13800.1; AT2G13800.1; AT2G13800.
DR   Gramene; AT2G13800.3; AT2G13800.3; AT2G13800.
DR   KEGG; ath:AT2G13800; -.
DR   Araport; AT2G13800; -.
DR   TAIR; AT2G13800; SERK5.
DR   eggNOG; KOG1187; Eukaryota.
DR   HOGENOM; CLU_000288_92_7_1; -.
DR   InParanoid; Q8LPS5; -.
DR   OrthoDB; 672884at2759; -.
DR   PhylomeDB; Q8LPS5; -.
DR   PRO; PR:Q8LPS5; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q8LPS5; baseline and differential.
DR   Genevisible; Q8LPS5; AT.
DR   GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004675; F:transmembrane receptor protein serine/threonine kinase activity; ISS:TAIR.
DR   GO; GO:0006468; P:protein phosphorylation; ISS:TAIR.
DR   Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   InterPro; IPR013210; LRR_N_plant-typ.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR47988; SOMATIC EMBRYOGENESIS RECEPTOR KINASE 1; 1.
DR   PANTHER; PTHR47988:SF91; SOMATIC EMBRYOGENESIS RECEPTOR KINASE 4-RELATED; 1.
DR   Pfam; PF00560; LRR_1; 4.
DR   Pfam; PF08263; LRRNT_2; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF52058; L domain-like; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 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; Glycoprotein; Kinase; Leucine-rich repeat;
KW   Membrane; Nucleotide-binding; Phosphoprotein; Receptor; Reference proteome;
KW   Repeat; Serine/threonine-protein kinase; Signal; Transferase;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..601
FT                   /note="Somatic embryogenesis receptor kinase 5"
FT                   /id="PRO_0000380727"
FT   TOPO_DOM        25..215
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        216..236
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        237..601
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REPEAT          71..94
FT                   /note="LRR 1"
FT   REPEAT          95..118
FT                   /note="LRR 2"
FT   REPEAT          119..141
FT                   /note="LRR 3"
FT   REPEAT          143..165
FT                   /note="LRR 4"
FT   REPEAT          166..188
FT                   /note="LRR 5"
FT   DOMAIN          275..572
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   ACT_SITE        402
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         281..289
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         303
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         272
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9LSI9"
FT   MOD_RES         298
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q94F62"
FT   MOD_RES         356
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT   MOD_RES         359
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9LSI9"
FT   MOD_RES         435
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q94F62"
FT   MOD_RES         436
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q94F62"
FT   MOD_RES         441
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000269|PubMed:19105183"
FT   MOD_RES         449
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT   MOD_RES         451
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT   MOD_RES         452
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT   MOD_RES         456
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT   MOD_RES         506
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:19105183"
FT   MOD_RES         532
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT   CARBOHYD        52
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        81
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        105
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        129
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        151
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        184
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   601 AA;  66981 MW;  EA5CA79DAA12EA55 CRC64;
     MEHGSSRGFI WLILFLDFVS RVTGKTQVDA LIALRSSLSS GDHTNNILQS WNATHVTPCS
     WFHVTCNTEN SVTRLDLGSA NLSGELVPQL AQLPNLQYLE LFNNNITGEI PEELGDLMEL
     VSLDLFANNI SGPIPSSLGK LGKLRFLRLY NNSLSGEIPR SLTALPLDVL DISNNRLSGD
     IPVNGSFSQF TSMSFANNKL RPRPASPSPS PSGTSAAIVV GVAAGAALLF ALAWWLRRKL
     QGHFLDVPAE EDPEVYLGQF KRFSLRELLV ATEKFSKRNV LGKGRFGILY KGRLADDTLV
     AVKRLNEERT KGGELQFQTE VEMISMAVHR NLLRLRGFCM TPTERLLVYP YMANGSVASC
     LRERPEGNPA LDWPKRKHIA LGSARGLAYL HDHCDQKIIH LDVKAANILL DEEFEAVVGD
     FGLAKLMNYN DSHVTTAVRG TIGHIAPEYL STGKSSEKTD VFGYGVMLLE LITGQKAFDL
     ARLANDDDIM LLDWVKEVLK EKKLESLVDA ELEGKYVETE VEQLIQMALL CTQSSAMERP
     KMSEVVRMLE GDGLAERWEE WQKEEMPIHD FNYQAYPHAG TDWLIPYSNS LIENDYPSGP
     R
//
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