ID SERK4_ARATH Reviewed; 620 AA.
AC Q9SKG5; Q0WW00; Q93ZV3;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 2.
DT 27-MAR-2024, entry version 157.
DE RecName: Full=Somatic embryogenesis receptor kinase 4 {ECO:0000303|PubMed:20064227};
DE Short=AtSERK4 {ECO:0000303|PubMed:20064227};
DE EC=2.7.10.1 {ECO:0000255|PROSITE-ProRule:PRU10027, ECO:0000269|PubMed:19105183, ECO:0000269|PubMed:19124768};
DE EC=2.7.11.1 {ECO:0000269|PubMed:19105183, ECO:0000269|PubMed:19124768};
DE AltName: Full=Protein BAK1-like 1 {ECO:0000303|PubMed:17600708};
DE Short=AtBKK1 {ECO:0000303|PubMed:17600708};
DE AltName: Full=Somatic embryogenesis receptor-like kinase 2 {ECO:0000303|PubMed:18667726};
DE Flags: Precursor;
GN Name=SERK4 {ECO:0000303|PubMed:20064227};
GN Synonyms=BKK1 {ECO:0000303|PubMed:17600708};
GN OrderedLocusNames=At2g13790 {ECO:0000312|Araport:AT2G13790};
GN ORFNames=F13J11.14 {ECO:0000312|EMBL:AAD28318.1};
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 [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].
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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., Hayashizaki Y.,
RA 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 FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17600708; DOI=10.1016/j.cub.2007.05.036;
RA He K., Gou X., Yuan T., Lin H., Asami T., Yoshida S., Russell S.D., Li J.;
RT "BAK1 and BKK1 regulate brassinosteroid-dependent growth and
RT brassinosteroid-independent cell-death pathways.";
RL Curr. Biol. 17:1109-1115(2007).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18667726; DOI=10.1104/pp.108.123216;
RA Albrecht C., Russinova E., Kemmerling B., Kwaaitaal M., de Vries S.C.;
RT "Arabidopsis SOMATIC EMBRYOGENESIS RECEPTOR KINASE proteins serve
RT brassinosteroid-dependent and -independent signaling pathways.";
RL Plant Physiol. 148:611-619(2008).
RN [8]
RP FUNCTION, AUTOPHOSPHORYLATION, AND CATALYTIC ACTIVITY.
RX PubMed=19124768; DOI=10.1073/pnas.0810249106;
RA Oh M.-H., Wang X., Kota U., Goshe M.B., Clouse S.D., Huber S.C.;
RT "Tyrosine phosphorylation of the BRI1 receptor kinase emerges as a
RT component of brassinosteroid signaling in Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:658-663(2009).
RN [9]
RP PHOSPHORYLATION AT SER-295, AND CATALYTIC ACTIVITY.
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 [10]
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 [11]
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).
RN [12]
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 [13]
RP FUNCTION, DISRUPTION PHENOTYPE, AND SUBUNIT.
RC STRAIN=cv. Columbia;
RX PubMed=34535661; DOI=10.1038/s41467-021-25580-w;
RA Hou S., Liu D., Huang S., Luo D., Liu Z., Xiang Q., Wang P., Mu R., Han Z.,
RA Chen S., Chai J., Shan L., He P.;
RT "The Arabidopsis MIK2 receptor elicits immunity by sensing a conserved
RT signature from phytocytokines and microbes.";
RL Nat. Commun. 12:5494-5494(2021).
CC -!- FUNCTION: Dual specificity kinase acting on both serine/threonine- and
CC tyrosine-containing substrates. Positively regulates the BR-dependent
CC plant growth pathway and negatively regulates the BR-independent cell-
CC death pathway. Required during SCOOP small peptides (e.g. SCOOP10 and
CC SCOOP12) perception and signaling; associates with MIK2 as a coreceptor
CC upon MIK2 perception of SCOOP peptides, and relays the signaling
CC through the activation of receptor-like cytosolic kinases (RLCKs) BIK1
CC and PBL1 (PubMed:34535661). {ECO:0000269|PubMed:17600708,
CC ECO:0000269|PubMed:18667726, ECO:0000269|PubMed:19124768,
CC ECO:0000269|PubMed:34535661}.
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:19105183, ECO:0000269|PubMed:19124768};
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:19105183,
CC ECO:0000269|PubMed:19124768};
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 ECO:0000269|PubMed:19105183, ECO:0000269|PubMed:19124768};
CC -!- SUBUNIT: Interacts with the EF-Tu receptor EFR and FLS2 in a specific
CC ligand-induced manner (PubMed:21693696). Interacts with TMK4/BARK1
CC (PubMed:23921992). Interacts with ERECTA in a EPF2-induced manner.
CC Interacts with ERL1 in a EPF1-induced manner. Interacts with TMM
CC (PubMed:26320950). Forms a complex with MIK2 in response to SCOOP12
CC perception (PubMed:34535661). {ECO:0000269|PubMed:21693696,
CC ECO:0000269|PubMed:23921992, ECO:0000269|PubMed:26320950,
CC ECO:0000269|PubMed:34535661}.
CC -!- INTERACTION:
CC Q9SKG5; C0LGI5: At1g69990; NbExp=4; IntAct=EBI-6290483, EBI-20651225;
CC Q9SKG5; Q8VYT3: At4g30520; NbExp=2; IntAct=EBI-6290483, EBI-16902452;
CC Q9SKG5; Q9ASS4: At5g48380; NbExp=2; IntAct=EBI-6290483, EBI-6298290;
CC Q9SKG5; Q94F62: BAK1; NbExp=4; IntAct=EBI-6290483, EBI-617138;
CC Q9SKG5; Q42371: ERECTA; NbExp=2; IntAct=EBI-6290483, EBI-16940407;
CC Q9SKG5; C0LGW6: ERL1; NbExp=4; IntAct=EBI-6290483, EBI-16914248;
CC Q9SKG5; Q6XAT2: ERL2; NbExp=3; IntAct=EBI-6290483, EBI-16895926;
CC Q9SKG5; Q9C8I6: IOS1; NbExp=4; IntAct=EBI-6290483, EBI-16924837;
CC Q9SKG5; Q9ZVD4: LRR-RLK; NbExp=2; IntAct=EBI-6290483, EBI-20651739;
CC Q9SKG5; Q9LFS4: NIK1; NbExp=4; IntAct=EBI-6290483, EBI-16146189;
CC Q9SKG5; Q94AG2: SERK1; NbExp=4; IntAct=EBI-6290483, EBI-1555537;
CC Q9SKG5; Q8LPS5: SERK5; NbExp=4; IntAct=EBI-6290483, EBI-16887868;
CC Q9SKG5; Q9LUL4: SRF7; NbExp=4; IntAct=EBI-6290483, EBI-16964596;
CC Q9SKG5; Q8RWZ1: SUB; NbExp=4; IntAct=EBI-6290483, EBI-17072125;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- PTM: Autophosphorylated on Thr and Tyr residues.
CC {ECO:0000269|PubMed:19105183, ECO:0000269|PubMed:19124768}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype; due to the redundancy with
CC BAK1. Compromised SCOOP10- and SCOOP12-induced root growth inhibition
CC and reactive oxygen species (ROS) production in the double mutant bak1-
CC 5 serk4 (PubMed:34535661). Bak1 and bkk1 double mutants are seedling
CC lethal. {ECO:0000269|PubMed:17600708, ECO:0000269|PubMed:18667726,
CC ECO:0000269|PubMed:34535661}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD28318.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAE98698.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FJ708691; ACN59286.1; -; mRNA.
DR EMBL; AC006436; AAD28318.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC06259.1; -; Genomic_DNA.
DR EMBL; AY056243; AAL07092.1; -; mRNA.
DR EMBL; AK226573; BAE98698.1; ALT_SEQ; mRNA.
DR PIR; G84510; G84510.
DR RefSeq; NP_178999.2; NM_126955.5.
DR AlphaFoldDB; Q9SKG5; -.
DR SMR; Q9SKG5; -.
DR BioGRID; 1223; 14.
DR IntAct; Q9SKG5; 28.
DR STRING; 3702.Q9SKG5; -.
DR GlyCosmos; Q9SKG5; 4 sites, No reported glycans.
DR iPTMnet; Q9SKG5; -.
DR PaxDb; 3702-AT2G13790-1; -.
DR ProteomicsDB; 234542; -.
DR EnsemblPlants; AT2G13790.1; AT2G13790.1; AT2G13790.
DR GeneID; 815862; -.
DR Gramene; AT2G13790.1; AT2G13790.1; AT2G13790.
DR KEGG; ath:AT2G13790; -.
DR Araport; AT2G13790; -.
DR TAIR; AT2G13790; SERK4.
DR eggNOG; KOG1187; Eukaryota.
DR HOGENOM; CLU_000288_92_7_1; -.
DR InParanoid; Q9SKG5; -.
DR OMA; IAFAWWI; -.
DR OrthoDB; 672884at2759; -.
DR PhylomeDB; Q9SKG5; -.
DR PRO; PR:Q9SKG5; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SKG5; baseline and differential.
DR Genevisible; Q9SKG5; AT.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; ISS:TAIR.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0009742; P:brassinosteroid mediated signaling pathway; IGI:TAIR.
DR GO; GO:0008219; P:cell death; IGI:TAIR.
DR GO; GO:0071456; P:cellular response to hypoxia; HEP:TAIR.
DR GO; GO:0010150; P:leaf senescence; IGI:TAIR.
DR GO; GO:0006468; P:protein phosphorylation; ISS:TAIR.
DR GO; GO:0090351; P:seedling development; IMP:UniProtKB.
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; Tyrosine-protein kinase.
FT SIGNAL 1..33
FT /evidence="ECO:0000255"
FT CHAIN 34..620
FT /note="Somatic embryogenesis receptor kinase 4"
FT /id="PRO_0000380726"
FT TOPO_DOM 34..234
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 235..255
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 256..620
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 100..122
FT /note="LRR 1"
FT REPEAT 124..146
FT /note="LRR 2"
FT REPEAT 148..170
FT /note="LRR 3"
FT REPEAT 171..193
FT /note="LRR 4"
FT REPEAT 194..215
FT /note="LRR 5"
FT DOMAIN 294..591
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 205..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..225
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 421
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 300..308
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 322
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 291
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9LSI9"
FT MOD_RES 295
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19105183"
FT MOD_RES 375
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT MOD_RES 378
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LSI9"
FT MOD_RES 454
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q94F62"
FT MOD_RES 455
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q94F62"
FT MOD_RES 460
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q94F62"
FT MOD_RES 468
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT MOD_RES 470
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT MOD_RES 471
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT MOD_RES 475
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT MOD_RES 551
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT CARBOHYD 110
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 156
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 189
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 202
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 620 AA; 68635 MW; 3BFDC6D10E3B9CC7 CRC64;
MTSSKMEQRS LLCFLYLLLL FNFTLRVAGN AEGDALTQLK NSLSSGDPAN NVLQSWDATL
VTPCTWFHVT CNPENKVTRV DLGNAKLSGK LVPELGQLLN LQYLELYSNN ITGEIPEELG
DLVELVSLDL YANSISGPIP SSLGKLGKLR FLRLNNNSLS GEIPMTLTSV QLQVLDISNN
RLSGDIPVNG SFSLFTPISF ANNSLTDLPE PPPTSTSPTP PPPSGGQMTA AIAGGVAAGA
ALLFAVPAIA FAWWLRRKPQ DHFFDVPAEE DPEVHLGQLK RFTLRELLVA TDNFSNKNVL
GRGGFGKVYK GRLADGNLVA VKRLKEERTK GGELQFQTEV EMISMAVHRN LLRLRGFCMT
PTERLLVYPY MANGSVASCL RERPEGNPAL DWPKRKHIAL GSARGLAYLH DHCDQKIIHR
DVKAANILLD EEFEAVVGDF GLAKLMNYND SHVTTAVRGT IGHIAPEYLS TGKSSEKTDV
FGYGVMLLEL ITGQKAFDLA RLANDDDIML LDWVKEVLKE KKLESLVDAE LEGKYVETEV
EQLIQMALLC TQSSAMERPK MSEVVRMLEG DGLAERWEEW QKEEMPIHDF NYQAYPHAGT
DWLIPYSNSL IENDYPSGPR
//
