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 03-AUG-2022, entry version 151.
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.AT2G13800.1; -.
DR iPTMnet; Q8LPS5; -.
DR PaxDb; Q8LPS5; -.
DR PRIDE; Q8LPS5; -.
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; locus:2040471; AT2G13800.
DR eggNOG; KOG1187; Eukaryota.
DR HOGENOM; CLU_000288_92_7_1; -.
DR InParanoid; Q8LPS5; -.
DR OrthoDB; 684563at2759; -.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0005102; F:signaling receptor binding; IEA:InterPro.
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; -; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
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; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR031048; SERK.
DR PANTHER; PTHR47988:SF38; PTHR47988:SF38; 1.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 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
