SRK6_BRAOV
ID SRK6_BRAOV Reviewed; 857 AA.
AC Q09092;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Putative serine/threonine-protein kinase receptor;
DE EC=2.7.11.1;
DE AltName: Full=S-receptor kinase;
DE Short=SRK;
DE Flags: Precursor;
GN Name=SRK6;
OS Brassica oleracea var. viridis (Flowering kale) (Brassica oleracea var.
OS acephala).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX NCBI_TaxID=3713;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=S6S6; TISSUE=Stigma;
RX PubMed=1681543; DOI=10.1073/pnas.88.19.8816;
RA Stein J.C., Howlett B., Boyes D.C., Nasrallah M.E.;
RT "Molecular cloning of a putative receptor protein kinase gene encoded at
RT the self-incompatibility locus of Brassica oleracea.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:8816-8820(1991).
CC -!- FUNCTION: Involved in sporophytic self-incompatibility system (the
CC inability of flowering plants to achieve self-fertilization), probably
CC acting in combination with S-locus-specific glycoproteins. Interaction
CC with a ligand in the extracellular domain triggers the protein kinase
CC activity of the cytoplasmic domain.
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 -!- INTERACTION:
CC Q09092; Q09092: SRK6; NbExp=2; IntAct=EBI-15646168, EBI-15646168;
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- TISSUE SPECIFICITY: Predominantly in the pistil and anther.
CC -!- POLYMORPHISM: There are a number of different S alleles in B.oleracea,
CC possibly providing the recognition specificity.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; M76647; AAA33000.1; -; mRNA.
DR PIR; A41369; A41369.
DR AlphaFoldDB; Q09092; -.
DR SMR; Q09092; -.
DR DIP; DIP-60975N; -.
DR IntAct; Q09092; 3.
DR PRIDE; Q09092; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0060320; P:rejection of self pollen; IEA:UniProtKB-KW.
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 1: Evidence at protein level;
KW ATP-binding; Disulfide bond; Glycoprotein; Kinase; Membrane;
KW Nucleotide-binding; Receptor; Self-incompatibility;
KW Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..32
FT /evidence="ECO:0000255"
FT CHAIN 33..857
FT /note="Putative serine/threonine-protein kinase receptor"
FT /id="PRO_0000024385"
FT TOPO_DOM 33..446
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 447..466
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 467..857
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 35..155
FT /note="Bulb-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00038"
FT DOMAIN 350..433
FT /note="PAN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00315"
FT DOMAIN 528..779
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 653
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 534..542
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 556
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 47
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 196
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 260
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 389
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 442
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 380..405
FT /evidence="ECO:0000250"
FT DISULFID 388..390
FT /evidence="ECO:0000250"
SQ SEQUENCE 857 AA; 98078 MW; 8931F0DBFA834030 CRC64;
MKGARNIYHH SYMSFLLVFV VMILIHPALS IYINTLSSTE SLTISSNKTL VSPGSIFEVG
FFRTNSRWYL GMWYKKVSDR TYVWVANRDN PLSNAIGTLK ISGNNLVLLD HSNKPVWWTN
LTRGNERSPV VAELLANGNF VMRDSSNNDA SEYLWQSFDY PTDTLLPEMK LGYNLKTGLN
RFLTSWRSSD DPSSGNFSYK LETQSLPEFY LSRENFPMHR SGPWNGIRFS GIPEDQKLSY
MVYNFIENNE EVAYTFRMTN NSFYSRLTLI SEGYFQRLTW YPSIRIWNRF WSSPVDPQCD
TYIMCGPYAY CDVNTSPVCN CIQGFNPRNI QQWDQRVWAG GCIRRTQLSC SGDGFTRMKK
MKLPETTMAT VDRSIGVKEC KKRCISDCNC TAFANADIRN GGSGCVIWTE RLEDIRNYAT
DAIDGQDLYV RLAAADIAKK RNASGKIISL TVGVSVLLLL IMFCLWKRKQ KRAKASAISI
ANTQRNQNLP MNEMVLSSKR EFSGEYKFEE LELPLIEMET VVKATENFSS CNKLGQGGFG
IVYKGRLLDG KEIAVKRLSK TSVQGTDEFM NEVTLIARLQ HINLVQVLGC CIEGDEKMLI
YEYLENLSLD SYLFGKTRRS KLNWNERFDI TNGVARGLLY LHQDSRFRII HRDLKVSNIL
LDKNMIPKIS DFGMARIFER DETEANTMKV VGTYGYMSPE YAMYGIFSEK SDVFSFGVIV
LEIVSGKKNR GFYNLDYEND LLSYVWSRWK EGRALEIVDP VIVDSLSSQP SIFQPQEVLK
CIQIGLLCVQ ELAEHRPAMS SVVWMFGSEA TEIPQPKPPG YCVRRSPYEL DPSSSWQCDE
NESWTVNQYT CSVIDAR
