SERK1_ARATH
ID SERK1_ARATH Reviewed; 625 AA.
AC Q94AG2; C0LGI6; Q9M9G3;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Somatic embryogenesis receptor kinase 1 {ECO:0000303|PubMed:11706164};
DE Short=AtSERK1 {ECO:0000303|PubMed:11706164};
DE EC=2.7.10.1 {ECO:0000255|PROSITE-ProRule:PRU10027};
DE EC=2.7.11.1 {ECO:0000255|PROSITE-ProRule:PRU00159};
DE AltName: Full=Somatic embryogenesis receptor-like kinase 1 {ECO:0000303|PubMed:11706164};
DE Flags: Precursor;
GN Name=SERK1 {ECO:0000303|PubMed:11706164};
GN OrderedLocusNames=At1g71830 {ECO:0000312|Araport:AT1G71830};
GN ORFNames=F14O23.21 {ECO:0000312|EMBL:AAF43236.1},
GN F14O23_24 {ECO:0000312|EMBL:AAF43236.1};
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 / MRNA], DEVELOPMENTAL STAGE, AND TISSUE
RP SPECIFICITY.
RX PubMed=11706164; DOI=10.1104/pp.010324;
RA Hecht V.F.G., Vielle-Calzada J.-P., Hartog M.V., Schmidt E.D.L.,
RA Boutilier K., Grossniklaus U., de Vries S.C.;
RT "The Arabidopsis SOMATIC EMBRYOGENESIS RECEPTOR KINASE 1 gene is expressed
RT in developing ovules and embryos and enhances embryogenic competence in
RT culture.";
RL Plant Physiol. 127:803-816(2001).
RN [2]
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 [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 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 [6]
RP SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=11397085; DOI=10.1006/jmbi.2001.4706;
RA Shah K., Gadella T.W.J. Jr., van Erp H., Hecht V., de Vries S.C.;
RT "Subcellular localization and oligomerization of the Arabidopsis thaliana
RT somatic embryogenesis receptor kinase 1 protein.";
RL J. Mol. Biol. 309:641-655(2001).
RN [7]
RP FUNCTION, MUTAGENESIS OF LYS-330; THR-459; THR-462; THR-463 AND THR-468,
RP AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=11509554; DOI=10.1074/jbc.m102381200;
RA Shah K., Vervoort J., de Vries S.C.;
RT "Role of threonines in the Arabidopsis thaliana somatic embryogenesis
RT receptor kinase 1 activation loop in phosphorylation.";
RL J. Biol. Chem. 276:41263-41269(2001).
RN [8]
RP INTERACTION WITH KAPP, AND SUBUNIT.
RX PubMed=12101128; DOI=10.1101/gad.220402;
RA Shah K., Russinova E., Gadella T.W. Jr., Willemse J., de Vries S.C.;
RT "The Arabidopsis kinase-associated protein phosphatase controls
RT internalization of the somatic embryogenesis receptor kinase 1.";
RL Genes Dev. 16:1707-1720(2002).
RN [9]
RP INTERACTION WITH SERK2, SUBUNIT, TISSUE SPECIFICITY, SUBCELLULAR LOCATION,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=16284305; DOI=10.1105/tpc.105.036814;
RA Albrecht C., Russinova E., Hecht V.F.G., Baaijens E., de Vries S.;
RT "The Arabidopsis thaliana SOMATIC EMBRYOGENESIS RECEPTOR-LIKE KINASES1 and
RT 2 control male sporogenesis.";
RL Plant Cell 17:3337-3349(2005).
RN [10]
RP INTERACTION WITH CDC48A; GRF6 AND KAPP.
RX PubMed=15592873; DOI=10.1007/s00425-004-1447-7;
RA Rienties I.M., Vink J., Borst J.W., Russinova E., de Vries S.C.;
RT "The Arabidopsis SERK1 protein interacts with the AAA-ATPase AtCDC48, the
RT 14-3-3 protein GF14lambda and the PP2C phosphatase KAPP.";
RL Planta 221:394-405(2005).
RN [11]
RP SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RX PubMed=16231101; DOI=10.1007/s00709-005-0111-9;
RA Kwaaitaal M.A.C.J., de Vries S.C., Russinova E.;
RT "Arabidopsis thaliana somatic embryogenesis receptor kinase 1 protein is
RT present in sporophytic and gametophytic cells and undergoes endocytosis.";
RL Protoplasma 226:55-65(2005).
RN [12]
RP DISRUPTION PHENOTYPE.
RX PubMed=16284306; DOI=10.1105/tpc.105.036731;
RA Colcombet J., Boisson-Dernier A., Ros-Palau R., Vera C.E., Schroeder J.I.;
RT "Arabidopsis SOMATIC EMBRYOGENESIS RECEPTOR KINASES1 and 2 are essential
RT for tapetum development and microspore maturation.";
RL Plant Cell 17:3350-3361(2005).
RN [13]
RP INTERACTION WITH BRI1; BAK1/SERK3; CDC48A; GRF7 AND KAPP.
RX PubMed=16473966; DOI=10.1105/tpc.105.039412;
RA Karlova R., Boeren S., Russinova E., Aker J., Vervoort J., de Vries S.C.;
RT "The Arabidopsis SOMATIC EMBRYOGENESIS RECEPTOR-LIKE KINASE1 protein
RT complex includes BRASSINOSTEROID-INSENSITIVE1.";
RL Plant Cell 18:626-638(2006).
RN [14]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH CDC48A.
RX PubMed=16621602; DOI=10.1016/j.jsb.2006.03.004;
RA Aker J., Borst J.W., Karlova R., de Vries S.C.;
RT "The Arabidopsis thaliana AAA protein CDC48A interacts in vivo with the
RT somatic embryogenesis receptor-like kinase 1 receptor at the plasma
RT membrane.";
RL J. Struct. Biol. 156:62-71(2006).
RN [15]
RP FUNCTION, AND INTERACTION WITH CDC48A.
RX PubMed=17693538; DOI=10.1104/pp.107.103986;
RA Aker J., Hesselink R., Engel R., Karlova R., Borst J.W., Visser A.J.W.G.,
RA de Vries S.C.;
RT "In vivo hexamerization and characterization of the Arabidopsis AAA ATPase
RT CDC48A complex using forster resonance energy transfer-fluorescence
RT lifetime imaging microscopy and fluorescence correlation spectroscopy.";
RL Plant Physiol. 145:339-350(2007).
RN [16]
RP SUBUNIT.
RX PubMed=17905839; DOI=10.1529/biophysj.107.112003;
RA Hink M.A., Shah K., Russinova E., de Vries S.C., Visser A.J.;
RT "Fluorescence fluctuation analysis of Arabidopsis thaliana somatic
RT embryogenesis receptor-like kinase and brassinosteroid insensitive 1
RT receptor oligomerization.";
RL Biophys. J. 94:1052-1062(2008).
RN [17]
RP DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RX PubMed=18515128; DOI=10.1016/j.plaphy.2008.04.011;
RA Salaj J., von Recklinghausen I.R., Hecht V., de Vries S.C., Schel J.H.N.,
RA van Lammeren A.A.M.;
RT "AtSERK1 expression precedes and coincides with early somatic embryogenesis
RT in Arabidopsis thaliana.";
RL Plant Physiol. Biochem. 46:709-714(2008).
RN [18]
RP MUTAGENESIS OF THR-541; SER-562 AND SER-570, AND PHOSPHORYLATION AT
RP SER-291; SER-299; SER-303; THR-325; THR-337; THR-346; SER-352; SER-383;
RP SER-394; THR-402; SER-415; TYR-456; THR-459; THR-462; THR-463; THR-468;
RP TYR-476; SER-478; THR-479; SER-483; THR-541; TYR-543; THR-559; SER-606;
RP SER-612; THR-613; TYR-614 AND SER-622.
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 [19]
RP INTERACTION WITH EFR AND FLS2.
RC STRAIN=cv. Columbia;
RX PubMed=21693696; DOI=10.1105/tpc.111.084301;
RA Roux M., Schwessinger B., Albrecht C., Chinchilla D., Jones A., Holton N.,
RA Malinovsky F.G., Tor M., de Vries S., Zipfel C.;
RT "The Arabidopsis leucine-rich repeat receptor-like kinases BAK1/SERK3 and
RT BKK1/SERK4 are required for innate immunity to hemibiotrophic and
RT biotrophic pathogens.";
RL Plant Cell 23:2440-2455(2011).
RN [20]
RP INTERACTION WITH ERECTA; ERL1 AND TMM.
RX PubMed=26320950; DOI=10.1016/j.cub.2015.07.068;
RA Meng X., Chen X., Mang H., Liu C., Yu X., Gao X., Torii K.U., He P.,
RA Shan L.;
RT "Differential function of Arabidopsis SERK family receptor-like kinases in
RT stomatal patterning.";
RL Curr. Biol. 25:2361-2372(2015).
RN [21]
RP FUNCTION, AND INTERACTION WITH RGI1/RGFR4/RCH2; RGI2/RGFR3/RCH1;
RP RGI3/RGFR1; RGI4/RGFR2/SKM2 AND RGI5/RGFR5.
RC STRAIN=cv. Columbia;
RX PubMed=27229311; DOI=10.1038/cr.2016.62;
RA Song W., Liu L., Wang J., Wu Z., Zhang H., Tang J., Lin G., Wang Y.,
RA Wen X., Li W., Han Z., Guo H., Chai J.;
RT "Signature motif-guided identification of receptors for peptide hormones
RT essential for root meristem growth.";
RL Cell Res. 26:674-685(2016).
RN [22]
RP X-RAY CRYSTALLOGRAPHY (1.53 ANGSTROMS) OF 24-213 IN COMPLEX WITH
RP BRASSINOLIDE AND BRI1, INTERACTION WITH BRI1, GLYCOSYLATION AT ASN-104;
RP ASN-150; ASN-163 AND ASN-184, AND DISULFIDE BONDS.
RX PubMed=23929946; DOI=10.1126/science.1242468;
RA Santiago J., Henzler C., Hothorn M.;
RT "Molecular mechanism for plant steroid receptor activation by somatic
RT embryogenesis co-receptor kinases.";
RL Science 341:889-892(2013).
RN [23]
RP X-RAY CRYSTALLOGRAPHY (2.66 ANGSTROMS) OF 1-213, FUNCTION, GLYCOSYLATION AT
RP ASN-150, DISULFIDE BONDS, AND INTERACTION WITH PSKR1.
RX PubMed=26308901; DOI=10.1038/nature14858;
RA Wang J., Li H., Han Z., Zhang H., Wang T., Lin G., Chang J., Yang W.,
RA Chai J.;
RT "Allosteric receptor activation by the plant peptide hormone
RT phytosulfokine.";
RL Nature 525:265-268(2015).
RN [24]
RP X-RAY CRYSTALLOGRAPHY (2.43 ANGSTROMS) OF 24-213, FUNCTION, DISRUPTION
RP PHENOTYPE, GLYCOSYLATION AT ASN-150 AND ASN-184, AND DISULFIDE BONDS.
RX PubMed=27058169; DOI=10.7554/elife.15075;
RA Santiago J., Brandt B., Wildhagen M., Hohmann U., Hothorn L.A.,
RA Butenko M.A., Hothorn M.;
RT "Mechanistic insight into a peptide hormone signaling complex mediating
RT floral organ abscission.";
RL Elife 5:0-0(2016).
RN [25]
RP X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) OF 24-208, AND DISULFIDE BONDS.
RX PubMed=29735985; DOI=10.1038/s41477-018-0150-9;
RA Hohmann U., Nicolet J., Moretti A., Hothorn L.A., Hothorn M.;
RT "The SERK3 elongated allele defines a role for BIR ectodomains in
RT brassinosteroid signalling.";
RL Nat. Plants 4:345-351(2018).
CC -!- FUNCTION: Dual specificity kinase acting on both serine/threonine- and
CC tyrosine-containing substrates. Phosphorylates BRI1 on 'Ser-887' and
CC CDC48 on at least one threonine residue and on 'Ser-41'. Confers
CC embryogenic competence. Acts redundantly with SERK2 as a control point
CC for sporophytic development controlling male gametophyte production.
CC Involved in the brassinolide signaling pathway. Probably required
CC during small peptide (e.g. RGF1) signaling (Probable). Involved in the
CC perception of phytosulfokine and subsequent signal transduction
CC (PubMed:26308901). Acts as a RLK5 coreceptor and promotes high-affinity
CC IDA sensing, thus being a positive regulator of floral abscission
CC (PubMed:27058169). {ECO:0000269|PubMed:11509554,
CC ECO:0000269|PubMed:17693538, ECO:0000269|PubMed:26308901,
CC ECO:0000269|PubMed:27058169, ECO:0000305|PubMed:27229311}.
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:0000255|PROSITE-ProRule:PRU00159};
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:0000255|PROSITE-ProRule:PRU00159};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10027};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC -!- ACTIVITY REGULATION: Inhibited by manganese.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=4 uM for ATP {ECO:0000269|PubMed:11509554};
CC -!- SUBUNIT: Monomer, homo- and heterodimer. Interacts with KAPP, CDC48A,
CC GRF6 or GRF7, SERK2, BRI1 and SERK3/BAK1 to form the SERK1 signaling
CC complex. Bind to BRI1 in a brassinolide-dependent manner
CC (PubMed:23929946). Heterodimer with PSKR1 (PubMed:26308901). Interacts
CC with the EF-Tu receptor EFR and FLS2 in a specific ligand-induced
CC manner. Interacts with ERECTA in a EPF2-induced manner. Interacts with
CC ERL1 in a EPF1-induced manner. Interacts with TMM (PubMed:26320950). In
CC the presence of the signal peptide RGF1, interacts with
CC RGI1/RGFR4/RCH2, RGI2/RGFR3/RCH1, RGI3/RGFR1, RGI4/RGFR2/SKM2 and
CC RGI5/RGFR5 (PubMed:27229311). {ECO:0000269|PubMed:11397085,
CC ECO:0000269|PubMed:12101128, ECO:0000269|PubMed:15592873,
CC ECO:0000269|PubMed:16284305, ECO:0000269|PubMed:16473966,
CC ECO:0000269|PubMed:16621602, ECO:0000269|PubMed:17693538,
CC ECO:0000269|PubMed:17905839, ECO:0000269|PubMed:21693696,
CC ECO:0000269|PubMed:23929946, ECO:0000269|PubMed:26308901,
CC ECO:0000269|PubMed:26320950, ECO:0000269|PubMed:27229311}.
CC -!- INTERACTION:
CC Q94AG2; Q8VYT3: At4g30520; NbExp=2; IntAct=EBI-1555537, EBI-16902452;
CC Q94AG2; Q9ASS4: At5g48380; NbExp=2; IntAct=EBI-1555537, EBI-6298290;
CC Q94AG2; Q9FN93: At5g59680; NbExp=2; IntAct=EBI-1555537, EBI-20653513;
CC Q94AG2; Q94F62: BAK1; NbExp=6; IntAct=EBI-1555537, EBI-617138;
CC Q94AG2; O22476: BRI1; NbExp=7; IntAct=EBI-1555537, EBI-1797828;
CC Q94AG2; P54609: CDC48A; NbExp=12; IntAct=EBI-1555537, EBI-1563238;
CC Q94AG2; Q6XAT2: ERL2; NbExp=4; IntAct=EBI-1555537, EBI-16895926;
CC Q94AG2; P48349: GRF6; NbExp=6; IntAct=EBI-1555537, EBI-1633785;
CC Q94AG2; Q9C8I6: IOS1; NbExp=4; IntAct=EBI-1555537, EBI-16924837;
CC Q94AG2; Q9ZVD4: LRR-RLK; NbExp=2; IntAct=EBI-1555537, EBI-20651739;
CC Q94AG2; Q9ZVR7: PSKR1; NbExp=4; IntAct=EBI-1555537, EBI-16172949;
CC Q94AG2; Q94AG2: SERK1; NbExp=7; IntAct=EBI-1555537, EBI-1555537;
CC Q94AG2; Q9SKG5: SERK4; NbExp=4; IntAct=EBI-1555537, EBI-6290483;
CC Q94AG2; Q9C8M9: SRF6; NbExp=3; IntAct=EBI-1555537, EBI-16954301;
CC Q94AG2; Q8RWZ1: SUB; NbExp=4; IntAct=EBI-1555537, EBI-17072125;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11397085,
CC ECO:0000269|PubMed:16231101, ECO:0000269|PubMed:16284305,
CC ECO:0000269|PubMed:16621602}; Single-pass type I membrane protein
CC {ECO:0000255}. Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:16231101}; Single-pass type I membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in flowers, tapetum, developing
CC microspores, all cells of the embryo sac, provascular strands and
CC developing vascular bundles. Low expression in adult vascular tissue.
CC Detected in root meristem. {ECO:0000269|PubMed:11706164,
CC ECO:0000269|PubMed:16231101, ECO:0000269|PubMed:16284305,
CC ECO:0000269|PubMed:18515128}.
CC -!- DEVELOPMENTAL STAGE: Expressed during pollen development and
CC megasporogenesis in the nucellus of developing ovules, in all cells of
CC the embryo sac up to fertilization and in all cells of the developing
CC embryo until the heart-shaped stage. Found in epidermal and vascular
CC cells of the late torpedo and cotyledon stages embryos.
CC {ECO:0000269|PubMed:11706164, ECO:0000269|PubMed:16231101,
CC ECO:0000269|PubMed:18515128}.
CC -!- DOMAIN: The extracellular domain (26-234) is required for dimerization.
CC -!- PTM: Glycosylated. Important for targeting to the plasma membrane.
CC -!- PTM: Intermolecular autophosphorylation. The catalytic activity of
CC SERK1 depends on the presence of a phosphorylated Thr residue in SERK1.
CC The phosphorylation is induced by brassinosteroids.
CC Transphosphorylation by BRI1 occurs only on Ser-299 and Thr-462.
CC Dephosphorylation of threonine residues by the kinase-associated
CC protein phosphatase (KAPP) is involved in SERK1 endocytosis.
CC {ECO:0000269|PubMed:19105183}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype. Serk1 and serk2 double
CC mutants are completely male sterile due to a failure in tapetum
CC specification. Delayed floral abscission (PubMed:27058169).
CC {ECO:0000269|PubMed:16284305, ECO:0000269|PubMed:16284306,
CC ECO:0000269|PubMed:27058169}.
CC -!- MISCELLANEOUS: Seems to be related with early development of tissues in
CC general rather than with embryogenesis.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF43236.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; A67827; CAB42254.1; -; Unassigned_DNA.
DR EMBL; A67815; -; NOT_ANNOTATED_CDS; Unassigned_DNA.
DR EMBL; FJ708676; ACN59271.1; -; mRNA.
DR EMBL; AC012654; AAF43236.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE35238.1; -; Genomic_DNA.
DR EMBL; AY048200; AAK82463.1; -; mRNA.
DR EMBL; BT002217; AAN72307.1; -; mRNA.
DR PIR; H96740; H96740.
DR RefSeq; NP_177328.1; NM_105841.4.
DR PDB; 4LSC; X-ray; 1.53 A; A=24-213.
DR PDB; 4LSX; X-ray; 3.30 A; C/D=24-213.
DR PDB; 4Z64; X-ray; 2.66 A; C=1-213.
DR PDB; 5IYX; X-ray; 2.43 A; C=24-213.
DR PDB; 6FG8; X-ray; 1.25 A; A=24-208.
DR PDB; 7ODV; X-ray; 2.31 A; BBB/EEE=24-211.
DR PDB; 7OGO; X-ray; 2.38 A; BBB/EEE=24-211.
DR PDB; 7OGQ; X-ray; 2.20 A; BBB=24-211.
DR PDB; 7OGU; X-ray; 2.87 A; BBB/EEE/HHH/KKK=24-211.
DR PDB; 7OGZ; X-ray; 2.70 A; BBB/EEE=24-213.
DR PDBsum; 4LSC; -.
DR PDBsum; 4LSX; -.
DR PDBsum; 4Z64; -.
DR PDBsum; 5IYX; -.
DR PDBsum; 6FG8; -.
DR PDBsum; 7ODV; -.
DR PDBsum; 7OGO; -.
DR PDBsum; 7OGQ; -.
DR PDBsum; 7OGU; -.
DR PDBsum; 7OGZ; -.
DR AlphaFoldDB; Q94AG2; -.
DR SMR; Q94AG2; -.
DR BioGRID; 28733; 30.
DR DIP; DIP-38028N; -.
DR IntAct; Q94AG2; 34.
DR STRING; 3702.AT1G71830.1; -.
DR iPTMnet; Q94AG2; -.
DR PaxDb; Q94AG2; -.
DR PRIDE; Q94AG2; -.
DR ProteomicsDB; 232575; -.
DR EnsemblPlants; AT1G71830.1; AT1G71830.1; AT1G71830.
DR GeneID; 843513; -.
DR Gramene; AT1G71830.1; AT1G71830.1; AT1G71830.
DR KEGG; ath:AT1G71830; -.
DR Araport; AT1G71830; -.
DR TAIR; locus:2013021; AT1G71830.
DR eggNOG; ENOG502QQ7B; Eukaryota.
DR HOGENOM; CLU_000288_92_7_1; -.
DR InParanoid; Q94AG2; -.
DR OMA; TIHVAFI; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; Q94AG2; -.
DR SABIO-RK; Q94AG2; -.
DR PRO; PR:Q94AG2; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q94AG2; baseline and differential.
DR Genevisible; Q94AG2; AT.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
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; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IPI:TAIR.
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:0033612; F:receptor serine/threonine kinase binding; IPI:UniProtKB.
DR GO; GO:0005102; F:signaling receptor binding; IPI:UniProtKB.
DR GO; GO:0004675; F:transmembrane receptor protein serine/threonine kinase activity; IDA:TAIR.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0009742; P:brassinosteroid mediated signaling pathway; IMP:TAIR.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
DR GO; GO:0010227; P:floral organ abscission; IGI:TAIR.
DR GO; GO:0007030; P:Golgi organization; IGI:TAIR.
DR GO; GO:0009556; P:microsporogenesis; IMP:TAIR.
DR GO; GO:0010152; P:pollen maturation; IMP:TAIR.
DR GO; GO:0046777; P:protein autophosphorylation; TAS:TAIR.
DR GO; GO:0006468; P:protein phosphorylation; IDA: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:SF34; PTHR47988:SF34; 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 3D-structure; ATP-binding; Cell membrane; Disulfide bond;
KW Endoplasmic reticulum; Glycoprotein; Kinase; Leucine-rich repeat; Membrane;
KW Nucleotide-binding; Phosphoprotein; Receptor; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
KW Transmembrane helix; Tyrosine-protein kinase.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..625
FT /note="Somatic embryogenesis receptor kinase 1"
FT /id="PRO_0000379596"
FT TOPO_DOM 27..238
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 239..259
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 260..625
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 92..116
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 118..140
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 141..164
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 165..189
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT DOMAIN 302..589
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 59..78
FT /note="Leucine-rich repeat receptor-like protein kinase
FT binding"
FT /evidence="ECO:0000269|PubMed:26308901,
FT ECO:0000269|PubMed:29735985, ECO:0007744|PDB:4LSX,
FT ECO:0007744|PDB:6FG8"
FT REGION 97..102
FT /note="Leucine-rich repeat receptor-like protein kinase
FT binding"
FT /evidence="ECO:0000269|PubMed:23929946,
FT ECO:0000269|PubMed:29735985, ECO:0007744|PDB:4LSX,
FT ECO:0007744|PDB:6FG8"
FT REGION 123..126
FT /note="Leucine-rich repeat receptor-like protein kinase
FT binding"
FT /evidence="ECO:0000269|PubMed:23929946,
FT ECO:0000269|PubMed:29735985, ECO:0007744|PDB:4LSX,
FT ECO:0007744|PDB:6FG8"
FT REGION 145..147
FT /note="Leucine-rich repeat receptor-like protein kinase
FT binding"
FT /evidence="ECO:0000269|PubMed:23929946,
FT ECO:0000269|PubMed:29735985, ECO:0007744|PDB:4LSX,
FT ECO:0007744|PDB:6FG8"
FT REGION 171..194
FT /note="Leucine-rich repeat receptor-like protein kinase
FT binding"
FT /evidence="ECO:0000269|PubMed:29735985,
FT ECO:0007744|PDB:6FG8"
FT ACT_SITE 429
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 61..62
FT /ligand="brassinolide"
FT /ligand_id="ChEBI:CHEBI:28277"
FT /evidence="ECO:0000269|PubMed:23929946,
FT ECO:0007744|PDB:4LSX"
FT BINDING 308..316
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 330
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 291
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19105183"
FT MOD_RES 299
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19105183"
FT MOD_RES 303
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19105183"
FT MOD_RES 325
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:19105183"
FT MOD_RES 337
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:19105183"
FT MOD_RES 346
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:19105183"
FT MOD_RES 352
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19105183"
FT MOD_RES 383
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19105183"
FT MOD_RES 386
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LSI9"
FT MOD_RES 394
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19105183"
FT MOD_RES 402
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:19105183"
FT MOD_RES 415
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19105183"
FT MOD_RES 456
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:19105183"
FT MOD_RES 459
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:19105183"
FT MOD_RES 462
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:19105183"
FT MOD_RES 463
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:19105183"
FT MOD_RES 468
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:19105183"
FT MOD_RES 476
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:19105183"
FT MOD_RES 478
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19105183"
FT MOD_RES 479
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:19105183"
FT MOD_RES 483
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19105183"
FT MOD_RES 541
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:19105183"
FT MOD_RES 543
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:19105183"
FT MOD_RES 559
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:19105183"
FT MOD_RES 606
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19105183"
FT MOD_RES 612
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19105183"
FT MOD_RES 613
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:19105183"
FT MOD_RES 614
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:19105183"
FT MOD_RES 622
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19105183"
FT CARBOHYD 104
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|PubMed:23929946, ECO:0007744|PDB:4LSC,
FT ECO:0007744|PDB:4LSX"
FT CARBOHYD 115
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 150
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|PubMed:23929946, ECO:0000269|PubMed:26308901,
FT ECO:0000269|PubMed:27058169, ECO:0007744|PDB:4LSC,
FT ECO:0007744|PDB:4LSX, ECO:0007744|PDB:4Z64,
FT ECO:0007744|PDB:5IYX"
FT CARBOHYD 163
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|PubMed:23929946, ECO:0007744|PDB:4LSX"
FT CARBOHYD 184
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|PubMed:23929946, ECO:0000269|PubMed:27058169,
FT ECO:0007744|PDB:4LSC, ECO:0007744|PDB:5IYX"
FT DISULFID 58..65
FT /evidence="ECO:0000269|PubMed:23929946,
FT ECO:0000269|PubMed:26308901, ECO:0000269|PubMed:27058169,
FT ECO:0000269|PubMed:29735985, ECO:0007744|PDB:4LSC,
FT ECO:0007744|PDB:4LSX, ECO:0007744|PDB:4Z64,
FT ECO:0007744|PDB:5IYX, ECO:0007744|PDB:6FG8"
FT DISULFID 202..210
FT /evidence="ECO:0000269|PubMed:23929946,
FT ECO:0000269|PubMed:26308901, ECO:0000269|PubMed:27058169,
FT ECO:0000269|PubMed:29735985, ECO:0007744|PDB:4LSC,
FT ECO:0007744|PDB:4LSX, ECO:0007744|PDB:4Z64,
FT ECO:0007744|PDB:5IYX"
FT MUTAGEN 330
FT /note="K->E: Loss of kinase activity."
FT /evidence="ECO:0000269|PubMed:11509554"
FT MUTAGEN 459
FT /note="T->A,E: No effect."
FT /evidence="ECO:0000269|PubMed:11509554"
FT MUTAGEN 462
FT /note="T->A,E: Decreased kinase activity. Loss of kinase
FT activity; when associated with A,E-463 and A,E-468."
FT /evidence="ECO:0000269|PubMed:11509554"
FT MUTAGEN 463
FT /note="T->A,E: Loss of autophosphorylation. Loss of kinase
FT activity; when associated with A,E-462 and A,E-468."
FT /evidence="ECO:0000269|PubMed:11509554"
FT MUTAGEN 468
FT /note="T->A,E: Loss of kinase activity. Loss of kinase
FT activity; when associated with A,E-462 and A,E-463."
FT /evidence="ECO:0000269|PubMed:11509554"
FT MUTAGEN 541
FT /note="T->A: No effect. Reduction of autophosphorylation;
FT when associated with A-570."
FT /evidence="ECO:0000269|PubMed:19105183"
FT MUTAGEN 562
FT /note="S->A: Loss of autophosphorylation."
FT /evidence="ECO:0000269|PubMed:19105183"
FT MUTAGEN 570
FT /note="S->A: No effect. Reduction of autophosphorylation;
FT when associated with A-541."
FT /evidence="ECO:0000269|PubMed:19105183"
FT CONFLICT 53
FT /note="T -> R (in Ref. 5; AAK82463/AAN72307)"
FT /evidence="ECO:0000305"
FT CONFLICT 251
FT /note="L -> P (in Ref. 1; CAB42254)"
FT /evidence="ECO:0000305"
FT CONFLICT 266
FT /note="K -> S (in Ref. 1; CAB42254)"
FT /evidence="ECO:0000305"
FT CONFLICT 327
FT /note="V -> I (in Ref. 5; AAK82463/AAN72307)"
FT /evidence="ECO:0000305"
FT HELIX 28..39
FT /evidence="ECO:0007829|PDB:6FG8"
FT TURN 46..49
FT /evidence="ECO:0007829|PDB:6FG8"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:5IYX"
FT HELIX 57..59
FT /evidence="ECO:0007829|PDB:6FG8"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:6FG8"
FT STRAND 71..75
FT /evidence="ECO:0007829|PDB:6FG8"
FT STRAND 82..84
FT /evidence="ECO:0007829|PDB:6FG8"
FT HELIX 87..91
FT /evidence="ECO:0007829|PDB:6FG8"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:6FG8"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:6FG8"
FT HELIX 111..115
FT /evidence="ECO:0007829|PDB:6FG8"
FT STRAND 120..123
FT /evidence="ECO:0007829|PDB:6FG8"
FT STRAND 126..131
FT /evidence="ECO:0007829|PDB:6FG8"
FT HELIX 135..139
FT /evidence="ECO:0007829|PDB:6FG8"
FT STRAND 145..147
FT /evidence="ECO:0007829|PDB:6FG8"
FT STRAND 150..155
FT /evidence="ECO:0007829|PDB:6FG8"
FT HELIX 159..163
FT /evidence="ECO:0007829|PDB:6FG8"
FT STRAND 168..171
FT /evidence="ECO:0007829|PDB:6FG8"
FT STRAND 174..180
FT /evidence="ECO:0007829|PDB:6FG8"
FT HELIX 185..189
FT /evidence="ECO:0007829|PDB:6FG8"
FT HELIX 192..194
FT /evidence="ECO:0007829|PDB:6FG8"
FT STRAND 199..203
FT /evidence="ECO:0007829|PDB:6FG8"
FT TURN 204..207
FT /evidence="ECO:0007829|PDB:6FG8"
SQ SEQUENCE 625 AA; 69022 MW; 98F6B69126DB664A CRC64;
MESSYVVFIL LSLILLPNHS LWLASANLEG DALHTLRVTL VDPNNVLQSW DPTLVNPCTW
FHVTCNNENS VIRVDLGNAE LSGHLVPELG VLKNLQYLEL YSNNITGPIP SNLGNLTNLV
SLDLYLNSFS GPIPESLGKL SKLRFLRLNN NSLTGSIPMS LTNITTLQVL DLSNNRLSGS
VPDNGSFSLF TPISFANNLD LCGPVTSHPC PGSPPFSPPP PFIQPPPVST PSGYGITGAI
AGGVAAGAAL LFAAPAIAFA WWRRRKPLDI FFDVPAEEDP EVHLGQLKRF SLRELQVASD
GFSNKNILGR GGFGKVYKGR LADGTLVAVK RLKEERTPGG ELQFQTEVEM ISMAVHRNLL
RLRGFCMTPT ERLLVYPYMA NGSVASCLRE RPPSQPPLDW PTRKRIALGS ARGLSYLHDH
CDPKIIHRDV KAANILLDEE FEAVVGDFGL AKLMDYKDTH VTTAVRGTIG HIAPEYLSTG
KSSEKTDVFG YGIMLLELIT GQRAFDLARL ANDDDVMLLD WVKGLLKEKK LEMLVDPDLQ
TNYEERELEQ VIQVALLCTQ GSPMERPKMS EVVRMLEGDG LAEKWDEWQK VEILREEIDL
SPNPNSDWIL DSTYNLHAVE LSGPR
