LRSK7_ORYSJ
ID LRSK7_ORYSJ Reviewed; 695 AA.
AC A0A0P0VIP0; Q0E1D9; Q6K3K2;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2016, sequence version 1.
DT 03-AUG-2022, entry version 40.
DE RecName: Full=L-type lectin-domain containing receptor kinase S.7 {ECO:0000305};
DE Short=OsLecRK-S.7 {ECO:0000303|PubMed:31833176};
DE EC=2.7.11.1 {ECO:0000269|PubMed:31833176};
DE AltName: Full=Protein DEFECTIVE IN APERTURE FORMATION 1 {ECO:0000303|PubMed:32284546};
DE Short=OsDAF1 {ECO:0000303|PubMed:32284546};
DE Flags: Precursor;
GN Name=LECRKS7 {ECO:0000303|PubMed:31833176};
GN Synonyms=DAF1 {ECO:0000303|PubMed:32284546};
GN OrderedLocusNames=Os02g0459600 {ECO:0000312|EMBL:BAS78542.1},
GN LOC_Os02g26160 {ECO:0000305};
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, PHOSPHORYLATION AT
RP THR-376; SER-378; THR-386; THR-403 AND THR-657, DISRUPTION PHENOTYPE, AND
RP MUTAGENESIS OF LYS-418 AND GLU-560.
RX PubMed=31833176; DOI=10.1111/jipb.12897;
RA Peng X., Wang M., Li Y., Yan W., Chang Z., Chen Z., Xu C., Yang C.,
RA Deng X.W., Wu J., Tang X.;
RT "Lectin receptor kinase OsLecRK-S.7 is required for pollen development and
RT male fertility.";
RL J. Integr. Plant Biol. 62:1227-1245(2020).
RN [5]
RP FUNCTION, INTERACTION WITH INP1, AND DISRUPTION PHENOTYPE.
RX PubMed=32284546; DOI=10.1038/s41477-020-0630-6;
RA Zhang X., Zhao G., Tan Q., Yuan H., Betts N., Zhu L., Zhang D., Liang W.;
RT "Rice pollen aperture formation is regulated by the interplay between
RT OsINP1 and OsDAF1.";
RL Nat. Plants 6:394-403(2020).
CC -!- FUNCTION: Legume-lectin receptor-like kinase required for normal pollen
CC development and male fertility (PubMed:31833176, PubMed:32284546).
CC Regulates pollen exine assembly and aperture development
CC (PubMed:31833176, PubMed:32284546). Plays a critical role in annulus
CC formation, and may participate in the formation of the fibrillar-
CC granular layer underneath the operculum (PubMed:32284546). May function
CC by regulating the expression of genes involved in pollen exine
CC development (PubMed:31833176). Kinase activity is required for its
CC function in pollen development (PubMed:31833176).
CC {ECO:0000269|PubMed:31833176, ECO:0000269|PubMed:32284546}.
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:31833176};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990;
CC Evidence={ECO:0000269|PubMed:31833176};
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:31833176};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46609;
CC Evidence={ECO:0000269|PubMed:31833176};
CC -!- SUBUNIT: Interacts with INP1 (PubMed:32284546). Interaction with INP1
CC is required for DAF1 polar localization at the future aperture sites in
CC tetrads (PubMed:32284546). {ECO:0000269|PubMed:32284546}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:31833176,
CC ECO:0000269|PubMed:32284546}; Single-pass type I membrane protein
CC {ECO:0000255}. Cytoplasm, cytosol {ECO:0000269|PubMed:32284546}.
CC Note=During meiosis, localizes diffusely in the cytosol and plasma
CC membrane of microspore mother cells (MMCs). During tetrad development,
CC localizes at the corners. At late tetrad stage, accumulates to the four
CC corners of the tetrad, assembled into ring-like structures marking
CC future aperture sites. When microspores are released from tetrads and
CC preliminary aperture structures has formed, remains in a distinctly
CC ring-shaped distribution beneath the aperture in the plasma membrane
CC between the annulus and operculum. {ECO:0000269|PubMed:32284546}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, lemma, palea, pistil
CC and anthers. {ECO:0000269|PubMed:31833176}.
CC -!- PTM: Autophosphorylated at Thr-376; Ser-378; Thr-386; Thr-403 and Thr-
CC 657. {ECO:0000269|PubMed:31833176}.
CC -!- DISRUPTION PHENOTYPE: Male sterility due to aborted pollen grains with
CC abnormal exine an intine, and defective aperture (PubMed:32284546).
CC Aborted pollen grains with defective apertures and intine formation,
CC and male sterility (PubMed:32284546). {ECO:0000269|PubMed:32284546}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the leguminous lectin
CC family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the protein kinase
CC superfamily. Ser/Thr protein kinase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD19984.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAF08699.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AP005650; BAD19984.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP008208; BAF08699.2; ALT_INIT; Genomic_DNA.
DR EMBL; AP014958; BAS78542.1; -; Genomic_DNA.
DR RefSeq; XP_015624294.1; XM_015768808.1.
DR RefSeq; XP_015624296.1; XM_015768810.1.
DR AlphaFoldDB; A0A0P0VIP0; -.
DR SMR; A0A0P0VIP0; -.
DR STRING; 4530.OS02T0459600-00; -.
DR PaxDb; A0A0P0VIP0; -.
DR EnsemblPlants; Os02t0459600-00; Os02t0459600-00; Os02g0459600.
DR GeneID; 4329292; -.
DR Gramene; Os02t0459600-00; Os02t0459600-00; Os02g0459600.
DR KEGG; osa:4329292; -.
DR eggNOG; KOG1187; Eukaryota.
DR HOGENOM; CLU_000288_62_6_1; -.
DR OMA; TEFATMV; -.
DR OrthoDB; 684563at2759; -.
DR Proteomes; UP000000763; Chromosome 2.
DR Proteomes; UP000059680; Chromosome 2.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0062074; C:pollen aperture; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IDA:UniProtKB.
DR GO; GO:0004675; F:transmembrane receptor protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0042742; P:defense response to bacterium; IBA:GO_Central.
DR GO; GO:0002229; P:defense response to oomycetes; IBA:GO_Central.
DR GO; GO:0062075; P:pollen aperture formation; IMP:UniProtKB.
DR GO; GO:0009555; P:pollen development; IMP:UniProtKB.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
DR CDD; cd06899; lectin_legume_LecRK_Arcelin_ConA; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001220; Legume_lectin_dom.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00139; Lectin_legB; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00307; LECTIN_LEGUME_BETA; 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; Cytoplasm; Glycoprotein; Kinase; Lectin;
KW Membrane; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..695
FT /note="L-type lectin-domain containing receptor kinase S.7"
FT /id="PRO_5006056350"
FT TOPO_DOM 24..331
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 332..352
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 353..695
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 389..661
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 37..276
FT /note="Legume-lectin like"
FT /evidence="ECO:0000255"
FT REGION 286..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..319
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 514
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 395..403
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 418
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 376
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:31833176"
FT MOD_RES 378
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:31833176"
FT MOD_RES 386
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:31833176"
FT MOD_RES 403
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:31833176"
FT MOD_RES 657
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:31833176"
FT CARBOHYD 45
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 279
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT MUTAGEN 418
FT /note="K->E: Loss of kinase activity."
FT /evidence="ECO:0000269|PubMed:31833176"
FT MUTAGEN 560
FT /note="E->K: In s13283; loss of kinase activity and male
FT sterile phenotype."
FT /evidence="ECO:0000269|PubMed:31833176"
SQ SEQUENCE 695 AA; 74135 MW; 2F534B41133DB0C5 CRC64;
MPPRCRRLPL LFILLLAVRP LSAAAASSIA AAPASSYRRI SWASNLTLLG SASLLPGAAG
VALTTPSRDG VGAGRALFSE PVRLLLPQDA AASASASRAA TPASFSTRFT FRITPSPTYG
DGLAFLLTSS RTFLGASNGF LGLFPSSSAS DEGELRDVST VAVEIDTHLD VALHDPDGNH
VALDAGSIFS VASAQPGVDL KAGVPITAWV EYRAPRRRLN VWLSYSPSRR PEKPALSADV
DLSGLLRTYM YAGFSASNGN GAALHVVERW TFRTFGFPNS SYAPPPTKYI GPMPPNNQPL
PPPPSPSPSP PPPSPPPPPH PNHRRRHLFY KVLGGVLGGM VLLGLVVVGS AVLLGRSVRR
KNQEHAVASE DMGEATLSME VARAATKGFD SGNVIGVGGS GATVYEGVLP SGSRVAVKRF
QAIGSCTKAF DSELKAMLNC PHHPNLVPLA GWCRSKDELV LVYEFMPNGN LDSALHTLGG
ATLPWEARFR AVYGVASALA YLHDECENRI IHRDVKSSNV MLDAEFNARL GDFGLARTVS
HGGLPLTTQP AGTLGYLAPE YVHTGVATER SDVYSFGVLA LEVATGRRPA ERGISVVNWV
WTLWGRRRLV DAADRRLQGR FVADEMRRVL LVGLCCVHPD CRKRPGMRRV VSMLDGTAPL
ILVPDKMPPV LLQPVPNASS MNSADTANTA FFSCR
