MSL1_ORYSJ
ID MSL1_ORYSJ Reviewed; 1413 AA.
AC Q7F8Q9; Q0E346;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Leucine-rich repeat receptor protein kinase MSL1 {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000255};
DE AltName: Full=MSP1 protein homolog 1 {ECO:0000305};
DE AltName: Full=MSP1-like protein 1 {ECO:0000303|PubMed:18248596};
DE Flags: Precursor;
GN Name=MSL1 {ECO:0000303|PubMed:18248596};
GN OrderedLocusNames=Os02g0194400 {ECO:0000312|EMBL:BAF08092.1},
GN LOC_Os02g10100 {ECO:0000305};
GN ORFNames=OsJ_05738 {ECO:0000312|EMBL:EAZ22074.1},
GN P0437H03.136 {ECO:0000312|EMBL:BAD15407.1};
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 952-1413.
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=18248596; DOI=10.1111/j.1365-313x.2008.03426.x;
RA Zhao X., de Palma J., Oane R., Gamuyao R., Luo M., Chaudhury A., Herve P.,
RA Xue Q., Bennett J.;
RT "OsTDL1A binds to the LRR domain of rice receptor kinase MSP1, and is
RT required to limit sporocyte numbers.";
RL Plant J. 54:375-387(2008).
CC -!- FUNCTION: Receptor-like kinase that may play a role male and female
CC sporogenesis. {ECO:0000250|UniProtKB:Q8RZV7}.
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:0000255};
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:0000255};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, shoots and spikelets.
CC {ECO:0000269|PubMed:18248596}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAF08092.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AP000366; BAD15407.1; -; Genomic_DNA.
DR EMBL; AP008208; BAF08092.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP014958; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CM000139; EAZ22074.1; -; Genomic_DNA.
DR EMBL; AK110011; -; NOT_ANNOTATED_CDS; mRNA.
DR AlphaFoldDB; Q7F8Q9; -.
DR SMR; Q7F8Q9; -.
DR STRING; 4530.OS02T0194400-01; -.
DR PaxDb; Q7F8Q9; -.
DR PRIDE; Q7F8Q9; -.
DR EnsemblPlants; Os02t0194400-02; Os02t0194400-02; Os02g0194400.
DR Gramene; Os02t0194400-02; Os02t0194400-02; Os02g0194400.
DR eggNOG; ENOG502QRD1; Eukaryota.
DR HOGENOM; CLU_000288_21_4_1; -.
DR InParanoid; Q7F8Q9; -.
DR Proteomes; UP000000763; Chromosome 2.
DR Proteomes; UP000007752; Chromosome 2.
DR Proteomes; UP000059680; Chromosome 2.
DR ExpressionAtlas; Q7F8Q9; baseline and differential.
DR Genevisible; Q7F8Q9; OS.
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: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 Gene3D; 3.80.10.10; -; 7.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
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; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00560; LRR_1; 1.
DR Pfam; PF13516; LRR_6; 1.
DR Pfam; PF13855; LRR_8; 5.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00369; LRR_TYP; 11.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 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; Glycoprotein; Kinase; Leucine-rich repeat;
KW Membrane; Nucleotide-binding; Receptor; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..1413
FT /note="Leucine-rich repeat receptor protein kinase MSL1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000432098"
FT TRANSMEM 1016..1036
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REPEAT 185..209
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 210..233
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 235..257
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 258..281
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT REPEAT 282..304
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT REPEAT 306..329
FT /note="LRR 6"
FT /evidence="ECO:0000255"
FT REPEAT 330..353
FT /note="LRR 7"
FT /evidence="ECO:0000255"
FT REPEAT 354..377
FT /note="LRR 8"
FT /evidence="ECO:0000255"
FT REPEAT 379..401
FT /note="LRR 9"
FT /evidence="ECO:0000255"
FT REPEAT 402..425
FT /note="LRR 10"
FT /evidence="ECO:0000255"
FT REPEAT 427..449
FT /note="LRR 11"
FT /evidence="ECO:0000255"
FT REPEAT 450..473
FT /note="LRR 12"
FT /evidence="ECO:0000255"
FT REPEAT 475..497
FT /note="LRR 13"
FT /evidence="ECO:0000255"
FT REPEAT 498..518
FT /note="LRR 14"
FT /evidence="ECO:0000255"
FT REPEAT 519..542
FT /note="LRR 15"
FT /evidence="ECO:0000255"
FT REPEAT 543..565
FT /note="LRR 16"
FT /evidence="ECO:0000255"
FT REPEAT 567..589
FT /note="LRR 17"
FT /evidence="ECO:0000255"
FT REPEAT 590..613
FT /note="LRR 18"
FT /evidence="ECO:0000255"
FT REPEAT 615..636
FT /note="LRR 19"
FT /evidence="ECO:0000255"
FT REPEAT 637..661
FT /note="LRR 20"
FT /evidence="ECO:0000255"
FT REPEAT 662..685
FT /note="LRR 21"
FT /evidence="ECO:0000255"
FT REPEAT 687..709
FT /note="LRR 22"
FT /evidence="ECO:0000255"
FT REPEAT 710..733
FT /note="LRR 23"
FT /evidence="ECO:0000255"
FT REPEAT 745..769
FT /note="LRR 24"
FT /evidence="ECO:0000255"
FT REPEAT 771..793
FT /note="LRR 25"
FT /evidence="ECO:0000255"
FT REPEAT 794..817
FT /note="LRR 26"
FT /evidence="ECO:0000255"
FT REPEAT 818..841
FT /note="LRR 27"
FT /evidence="ECO:0000255"
FT REPEAT 843..866
FT /note="LRR 28"
FT /evidence="ECO:0000255"
FT REPEAT 868..890
FT /note="LRR 29"
FT /evidence="ECO:0000255"
FT REPEAT 918..942
FT /note="LRR 30"
FT /evidence="ECO:0000255"
FT REPEAT 944..966
FT /note="LRR 31"
FT /evidence="ECO:0000255"
FT DOMAIN 1107..1401
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 1234
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 1113..1121
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 1135
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 153
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 192
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 304
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 317
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 461
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 496
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 499
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 554
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 568
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 601
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 663
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 697
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 768
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 795
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 878
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 901
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 917
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 928
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 973
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CONFLICT 1262
FT /note="C -> R (in Ref. 5; AK110011)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1413 AA; 152675 MW; CDDE97F47D087981 CRC64;
MAPMLSIASR SPSPALIAPH ASARATGLRA PFAGNRIVGW GWGDQTKSGT DRNRASICVV
LFLRVRSGEP TQAPRDPPAA VGGGGCYVRL PAPPRDRDAV LYHVCLFTLL LCFIPITALA
ESDIKNLFAL RKAIAVGKGF LHNWFELETP PCNWSGISCV GLTVVAIDLS STPLYVDFPS
QIIAFQSLVR LNVSGCGFSG ELPEAMVNLQ HLQHLDLSDN QLGGPLPASL FDLKMLKVMV
LDNNMFSGQL SPAIAHLQQL TVLSISTNSF SGGLPPELGS LKNLEYLDIH TNAFSGSIPA
SFSNLSRLLY LDANNNNLTG SIFPGIRALV NLVKLDLSSN GLVGAIPKEL CQLKNLQSLI
LSDNELTGSI PEEIGNLKQL EVLNLLKCNL MDTVPLSIGN LEILEGLYIS FNSFSGELPA
SVGELRNLRQ LMAKSAGFTG SIPKELGNCK KLTTLVLSGN NFTGTIPEEL ADLVAVVLFD
VEGNRLSGHI PDWIQNWSNV SSISLAQNMF DGPLPGLPLH LVSFSAESNR LSGSIPAKIC
QGTFLQILRL NDNNLTGSID ETFKGCKNLT ELSLLDNHLH GEIPEYLALL PLVSLDLSHN
NFTGMIPDRL WESSTILDIS LSDNQLTGMI TESIGKLLSL QSLSIDRNYL QGPLPRSIGA
LRNLTALSLS GNMLSEDIPI QLFNCRNLVT LDLSCNNLTG HIPKAISHLT KLNTLVLSRN
RLSGAIPSEL CVAFSRESHS ELEYVQHIGL IDLSRNRLTG HIPRAINNCS ILVELHLQDN
LLSGTIPVEL AELRNITTID LSSNALVGPV LPWPVPLASL QGLLLSNNRL SGSIPSGIGN
ILPQITMLDL SGNALTGTLP LDLLCKESLN HLDVSDNNIS GQIPFSCHED KESPIPLIFF
NASSNHFSGS LDESISNFTK LTYLDLHNNS LTGRLPSAIA RVTSLYYLDL SSNDFSGTIP
CGICGMFGLT FANFSGNRDG GTFTLADCAA EEGGVCAANR VDRKMPDHPF HVLEATICCI
ATAIVIVLVV ILVVYLRRRR KMLRRRQFVL VPAGDNAMAD HETTLSNNLL GRRRMKKREP
PSINLATFEH APVRVTVDEI MRATGNFDGM HVVGDGGFGT VYRAELPGGR RVAVKRLHGV
GRRFQGGERE FRAEMETVGK VRHPNLVPLL GYCAAGDERF LVYEYMEHGS LEDRLRGGGG
AALGWPERLT ICGGAARGLA FLHHGFVPHV IHRDVKSSNV LLGEGLQPRV SDFGLARIIS
ACETHVSTVL AGTLGYIPPE YALAMRCTAK GDVYSFGVVM LELLTGRPPT WSSAEVTAEG
DDERGGGGSL VGWVRWMAAR GRGGEVFDAC LPVSGAEREQ MARVLDVARD CTADEPWRRP
TMAEVARRVG AIEAMEYGPL VVAVSSGEPP AMP
