SRK_ARATH
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 03-AUG-2022, entry version 55.
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. Old-1,
RC 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=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 -!- 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://web.expasy.org/spotlight/back_issues/128";
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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 PRIDE; P0DH86; -.
DR ExpressionAtlas; P0DH86; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005516; F:calmodulin binding; ISS:UniProtKB.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
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:UniProt.
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 Gene3D; 2.90.10.10; -; 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 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; SSF51110; 1.
DR SUPFAM; SSF56112; SSF56112; 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 823..838
FT /note="Polar residues"
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
