ID   SRK_ARATH               Reviewed;         853 AA.
AC   P0DH86; B0F2A9; B0F2B0; D6NTN9; D6NTP0; D6NTP1; D6NTP2; D6NTP6; D6NTP7;
AC   D6NTP8; O81904;
DT   19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT   19-OCT-2011, sequence version 1.
DT   02-SEP-2026, entry version 66.
DE   RecName: Full=G-type lectin S-receptor-like serine/threonine-protein kinase SRK;
DE            EC=2.7.11.1;
DE   Flags: Precursor;
GN   Name=SRK;
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], AND VARIANT THR-373.
RC   STRAIN=cv. Nok-0, and cv. Pog-0;
RX   PubMed=18179433; DOI=10.1111/j.1365-294x.2007.03605.x;
RA   Shimizu K.K., Shimizu-Inatsugi R., Tsuchimatsu T., Purugganan M.D.;
RT   "Independent origins of self-compatibility in Arabidopsis thaliana.";
RL   Mol. Ecol. 17:704-714(2008).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], VARIANTS ASN-45; TYR-269;
RP   THR-278; LYS-415; ALA-420; SER-438; ILE-562; ARG-612; ASP-630; GLN-676 AND
RP   829-SER--SER-837 DEL, AND FUNCTION.
RC   STRAIN=cv. Ca-0, cv. Co, cv. Di-1, cv. Fi-1, cv. Ge-1, cv. Gie, cv.
RC   Old-1, cv. Uk-3, cv. Wassilewskija, and cv. Wei-1;
RX   PubMed=20400945; DOI=10.1038/nature08927;
RA   Tsuchimatsu T., Suwabe K., Shimizu-Inatsugi R., Isokawa S., Pavlidis P.,
RA   Stadler T., Suzuki G., Takayama S., Watanabe M., Shimizu K.K.;
RT   "Evolution of self-compatibility in Arabidopsis by a mutation in the male
RT   specificity gene.";
RL   Nature 464:1342-1346(2010).
RN   [3]
RP   FUNCTION.
RX   PubMed=15505209; DOI=10.1073/pnas.0406970101;
RA   Nasrallah M.E., Liu P., Sherman-Broyles S., Boggs N.A., Nasrallah J.B.;
RT   "Natural variation in expression of self-incompatibility in Arabidopsis
RT   thaliana: implications for the evolution of selfing.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:16070-16074(2004).
RN   [4]
RP   FUNCTION, AND REVIEW.
RX   PubMed=17237349; DOI=10.1105/tpc.106.048199;
RA   Sherman-Broyles S., Boggs N., Farkas A., Liu P., Vrebalov J.,
RA   Nasrallah M.E., Nasrallah J.B.;
RT   "S locus genes and the evolution of self-fertility in Arabidopsis
RT   thaliana.";
RL   Plant Cell 19:94-106(2007).
RN   [5]
RP   FUNCTION.
RX   PubMed=17656687; DOI=10.1126/science.1143153;
RA   Tang C., Toomajian C., Sherman-Broyles S., Plagnol V., Guo Y.-L., Hu T.T.,
RA   Clark R.M., Nasrallah J.B., Weigel D., Nordborg M.;
RT   "The evolution of selfing in Arabidopsis thaliana.";
RL   Science 317:1070-1072(2007).
CC   -!- FUNCTION: Female specificity determinant of self-incompatibility.
CC       {ECO:0000269|PubMed:15505209, ECO:0000269|PubMed:17237349,
CC       ECO:0000269|PubMed:17656687, ECO:0000269|PubMed:20400945}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP +
CC         H(+); 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=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] +
CC         ADP + H(+); Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC         COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC       membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC   -!- CAUTION: Has been shown to be a pseudogene in cv. Columbia (AC P0DH87)
CC       due to a frameshift mutation that introduces a premature stop codon in
CC       this strain. The sequence shown is from strains cv. Pog-0 and cv. Wei-
CC       1. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Do it yourself - Issue 128
CC       of May 2011;
CC       URL="https://www.proteinspotlight.org/back_issues/128";
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; EF692484; ABU54597.1; -; Genomic_DNA.
DR   EMBL; EF692485; ABU54598.1; -; Genomic_DNA.
DR   EMBL; EF692488; ABU54595.1; -; mRNA.
DR   EMBL; EF692489; ABU54596.1; -; mRNA.
DR   EMBL; GU723782; ADG01645.1; -; mRNA.
DR   EMBL; GU723783; ADG01646.1; -; mRNA.
DR   EMBL; GU723784; ADG01647.1; -; mRNA.
DR   EMBL; GU723785; ADG01648.1; -; mRNA.
DR   EMBL; GU723786; ADG01649.1; -; mRNA.
DR   EMBL; GU723787; ADG01650.1; -; mRNA.
DR   EMBL; GU723788; ADG01651.1; -; mRNA.
DR   EMBL; GU723789; ADG01652.1; -; mRNA.
DR   EMBL; GU723790; ADG01653.1; -; mRNA.
DR   EMBL; GU723791; ADG01654.1; -; mRNA.
DR   EMBL; GU723866; ADG01729.1; -; Genomic_DNA.
DR   EMBL; GU723867; ADG01730.1; -; Genomic_DNA.
DR   EMBL; GU723870; ADG01731.1; -; Genomic_DNA.
DR   EMBL; GU723871; ADG01732.1; -; Genomic_DNA.
DR   EMBL; GU723872; ADG01733.1; -; Genomic_DNA.
DR   EMBL; GU723873; ADG01734.1; -; Genomic_DNA.
DR   EMBL; GU723874; ADG01735.1; -; Genomic_DNA.
DR   EMBL; GU723875; ADG01736.1; -; Genomic_DNA.
DR   EMBL; GU723876; ADG01737.1; -; Genomic_DNA.
DR   EMBL; GU723877; ADG01738.1; -; Genomic_DNA.
DR   AlphaFoldDB; P0DH86; -.
DR   SMR; P0DH86; -.
DR   TCDB; 1.A.87.2.16; the mechanosensitive calcium channel (mca) family.
DR   GlyCosmos; P0DH86; 5 sites, No reported glycans.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0005516; F:calmodulin binding; ISS:UniProtKB.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:UniProtKB-ARBA.
DR   GO; GO:0042742; P:defense response to bacterium; ISS:UniProtKB.
DR   GO; GO:0046777; P:protein autophosphorylation; ISS:UniProtKB.
DR   GO; GO:0048544; P:recognition of pollen; IEA:InterPro.
DR   CDD; cd00028; B_lectin; 1.
DR   CDD; cd01098; PAN_AP_plant; 1.
DR   CDD; cd14066; STKc_IRAK; 1.
DR   FunFam; 1.10.510.10:FF:000060; G-type lectin S-receptor-like serine/threonine-protein kinase; 1.
DR   FunFam; 3.30.200.20:FF:000195; G-type lectin S-receptor-like serine/threonine-protein kinase; 1.
DR   FunFam; 2.90.10.10:FF:000047; Putative inactive G-type lectin S-receptor-like serine/threonine-protein kinase SRK; 1.
DR   Gene3D; 2.90.10.10; Bulb-type lectin domain; 1.
DR   Gene3D; 3.30.200.20; Phosphorylase Kinase, domain 1; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 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   PANTHER; PTHR27002:SF956; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR27002; RECEPTOR-LIKE SERINE/THREONINE-PROTEIN KINASE SD1-8; 1.
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; PK_Tyr_Ser-Thr; 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; alpha-D-mannose-specific plant lectins; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 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   2: Evidence at transcript level;
KW   ATP-binding; Cell membrane; Disulfide bond; Glycoprotein; Kinase; Lectin;
KW   Membrane; Nucleotide-binding; Phosphoprotein; Receptor;
KW   Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..31
FT                   /evidence="ECO:0000255"
FT   CHAIN           32..853
FT                   /note="G-type lectin S-receptor-like serine/threonine-
FT                   protein kinase SRK"
FT                   /id="PRO_0000401305"
FT   TOPO_DOM        32..441
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        442..462
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        463..853
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          34..154
FT                   /note="Bulb-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00038"
FT   DOMAIN          293..329
FT                   /note="EGF-like; atypical"
FT   DOMAIN          348..428
FT                   /note="PAN"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00315"
FT   DOMAIN          524..802
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          613..631
FT                   /note="CaM-binding"
FT                   /evidence="ECO:0000250"
FT   REGION          807..838
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        822..832
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        650
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         530..538
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         552
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         558
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT   MOD_RES         654
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT   MOD_RES         667
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT   MOD_RES         684
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT   MOD_RES         831
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT   CARBOHYD        46
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        120
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        147
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        243
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        387
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        297..309
FT                   /evidence="ECO:0000250"
FT   DISULFID        303..317
FT                   /evidence="ECO:0000250"
FT   DISULFID        378..403
FT                   /evidence="ECO:0000250"
FT   DISULFID        382..388
FT                   /evidence="ECO:0000250"
FT   VARIANT         45
FT                   /note="S -> N (in strain: cv. Ge-1)"
FT                   /evidence="ECO:0000269|PubMed:20400945"
FT   VARIANT         269
FT                   /note="N -> Y (in strain: cv. Ge-1)"
FT                   /evidence="ECO:0000269|PubMed:20400945"
FT   VARIANT         278
FT                   /note="M -> T (in strain: cv. Old-1, cv. Uk-3 and cv.
FT                   Wassilewskija)"
FT                   /evidence="ECO:0000269|PubMed:20400945"
FT   VARIANT         373
FT                   /note="I -> T (in strain: cv. Nok-0)"
FT                   /evidence="ECO:0000269|PubMed:18179433"
FT   VARIANT         415
FT                   /note="N -> K (in strain: cv. Ca-0 and cv. Co)"
FT                   /evidence="ECO:0000269|PubMed:20400945"
FT   VARIANT         420
FT                   /note="G -> A (in strain: cv. Fi-1)"
FT                   /evidence="ECO:0000269|PubMed:20400945"
FT   VARIANT         438
FT                   /note="I -> S (in strain: cv. Old-1, cv. Uk-3 and cv.
FT                   Wassilewskija)"
FT                   /evidence="ECO:0000269|PubMed:20400945"
FT   VARIANT         562
FT                   /note="T -> I (in strain: cv. Ca-0)"
FT                   /evidence="ECO:0000269|PubMed:20400945"
FT   VARIANT         612
FT                   /note="T -> R (in strain: cv. Di-1, cv. Fi-1, cv. Gie, cv.
FT                   Old-1, cv. Uk-3 and cv. Wassilewskija)"
FT                   /evidence="ECO:0000269|PubMed:20400945"
FT   VARIANT         630
FT                   /note="G -> D (in strain: cv. Ca-0)"
FT                   /evidence="ECO:0000269|PubMed:20400945"
FT   VARIANT         676
FT                   /note="E -> Q (in strain: cv. Di-1, cv. Fi-1, cv. Gie, cv.
FT                   Old-1, cv. Uk-3 and cv. Wassilewskija)"
FT                   /evidence="ECO:0000269|PubMed:20400945"
FT   VARIANT         829..837
FT                   /note="Missing (in strain: cv. Fi-1, cv. Gie, cv. Old-1,
FT                   cv. Uk-3 and cv. Wassilewskija)"
FT                   /evidence="ECO:0000269|PubMed:20400945"
SQ   SEQUENCE   853 AA;  96764 MW;  9A74E475EEA40204 CRC64;
     MRGELPNKHH SYTFFVFLFF FLILFPDLSI SVNTLSATES LTISSNKTIV SPGGVFELGF
     FRILGDSWYL GIWYKKISQR TYVWVANRDT PLSNPIGILK ISNANLVILD NSDTHVWSTN
     LTGAVRSSVV AELLDNGNFV LRGSKINESD EFLWQSFDFP TDTLLPQMKL GRDHKRGLNR
     FVTSWKSSFD PSSGSFMFKL ETLGLPEFFG FTSFLEVYRS GPWDGLRFSG ILEMQQWDDI
     IYNFTENREE VAYTFRVTDH NSYSRLTINT VGRLEGFMWE PTQQEWNMFW FMPKDTCDLY
     GICGPYAYCD MSTSPTCNCI KGFQPLSPQD WASGDVTGRC RRKTQLTCGE DRFFRLMNMK
     IPATTAAIVD KRIGLKECEE KCKTHCNCTA YANSDIRNGG SGCIIWIGEF RDIRNYAADG
     QDLFVRLAAA EFGERRTIRG KIIGLIIGIS LMLVLSFIIY CFWKKKQKRA RATAAPIGYR
     DRIQELIITN GVVMSSGRRL LGEEEDLELP LTEFETVVMA TENFSDSNIL GRGGFGIVYK
     GRLLDGQEIA VKRLSEMSSQ GTNEFKNEVR LIARLQHINL VRLLSCCIYA DEKILIYEYL
     ENGSLDSHLF ETTQSSNKLN WQTRFSIING IARGLLYLHQ DSRFKIIHRD LKASNVLLDK
     NMTPKISDFG MARIFERDET EANTRKVVGT YGYMSPEYAM EGIFSVKSDV FSFGVLVLEI
     VSGKRNRGFH NSGQDNNLLG YTWENWKEGK GLEIVDSIIV DSSSSMSLFQ PHEVLRCIQI
     GLLCVQERAE DRPKMSSVVL MLGSEKGEIP QPKRPGYCVG RSSLDTADSS SSTKRDSESL
     TVNQITVSVI NAR
//