MSP1_ORYSJ
ID MSP1_ORYSJ Reviewed; 1294 AA.
AC Q8RZV7;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Leucine-rich repeat receptor protein kinase MSP1 {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000255};
DE AltName: Full=Protein MULTIPLE SPOROCYTE 1 {ECO:0000303|PubMed:12897248};
DE Flags: Precursor;
GN Name=MSP1 {ECO:0000303|PubMed:12897248};
GN OrderedLocusNames=Os01g0917500 {ECO:0000312|EMBL:BAF07116.1},
GN LOC_Os01g68870 {ECO:0000305};
GN ORFNames=P0413C03.22 {ECO:0000312|EMBL:BAB86144.1};
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 [MRNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Nipponbare;
RX PubMed=12897248; DOI=10.1105/tpc.012401;
RA Nonomura K., Miyoshi K., Eiguchi M., Suzuki T., Miyao A., Hirochika H.,
RA Kurata N.;
RT "The MSP1 gene is necessary to restrict the number of cells entering into
RT male and female sporogenesis and to initiate anther wall formation in
RT rice.";
RL Plant Cell 15:1728-1739(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12447438; DOI=10.1038/nature01184;
RA Sasaki T., Matsumoto T., Yamamoto K., Sakata K., Baba T., Katayose Y.,
RA Wu J., Niimura Y., Cheng Z., Nagamura Y., Antonio B.A., Kanamori H.,
RA Hosokawa S., Masukawa M., Arikawa K., Chiden Y., Hayashi M., Okamoto M.,
RA Ando T., Aoki H., Arita K., Hamada M., Harada C., Hijishita S., Honda M.,
RA Ichikawa Y., Idonuma A., Iijima M., Ikeda M., Ikeno M., Ito S., Ito T.,
RA Ito Y., Ito Y., Iwabuchi A., Kamiya K., Karasawa W., Katagiri S.,
RA Kikuta A., Kobayashi N., Kono I., Machita K., Maehara T., Mizuno H.,
RA Mizubayashi T., Mukai Y., Nagasaki H., Nakashima M., Nakama Y.,
RA Nakamichi Y., Nakamura M., Namiki N., Negishi M., Ohta I., Ono N., Saji S.,
RA Sakai K., Shibata M., Shimokawa T., Shomura A., Song J., Takazaki Y.,
RA Terasawa K., Tsuji K., Waki K., Yamagata H., Yamane H., Yoshiki S.,
RA Yoshihara R., Yukawa K., Zhong H., Iwama H., Endo T., Ito H., Hahn J.H.,
RA Kim H.-I., Eun M.-Y., Yano M., Jiang J., Gojobori T.;
RT "The genome sequence and structure of rice chromosome 1.";
RL Nature 420:312-316(2002).
RN [3]
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 [4]
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 [5]
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 [6]
RP INTERACTION WITH TDL1A, AND 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 plays important roles in
CC restricting the number of cells entering into male and female
CC sporogenesis. Involved in cell specification during anther development
CC and initiation of anther wall formation. {ECO:0000269|PubMed:12897248}.
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 -!- SUBUNIT: Interacts with TDL1A. {ECO:0000269|PubMed:18248596}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in anthers and ovules during meiosis.
CC {ECO:0000269|PubMed:18248596}.
CC -!- DISRUPTION PHENOTYPE: Male-sterile phenotype due to the absence of
CC tapetum. Presence of extra microsporocytes in the developing anthers
CC and ovules. {ECO:0000269|PubMed:12897248}.
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; AB103395; BAC81207.1; -; mRNA.
DR EMBL; AP003451; BAB86144.1; -; Genomic_DNA.
DR EMBL; AP008207; BAF07116.1; -; Genomic_DNA.
DR EMBL; AP014957; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_015622427.1; XM_015766941.1.
DR RefSeq; XP_015622428.1; XM_015766942.1.
DR AlphaFoldDB; Q8RZV7; -.
DR SMR; Q8RZV7; -.
DR STRING; 4530.OS01T0917500-01; -.
DR PaxDb; Q8RZV7; -.
DR PRIDE; Q8RZV7; -.
DR EnsemblPlants; Os01t0917500-01; Os01t0917500-01; Os01g0917500.
DR GeneID; 4324355; -.
DR Gramene; Os01t0917500-01; Os01t0917500-01; Os01g0917500.
DR KEGG; osa:4324355; -.
DR eggNOG; ENOG502QRD1; Eukaryota.
DR HOGENOM; CLU_000288_22_1_1; -.
DR InParanoid; Q8RZV7; -.
DR OrthoDB; 95617at2759; -.
DR PlantReactome; R-OSA-8986768; Anther and pollen development.
DR Proteomes; UP000000763; Chromosome 1.
DR Proteomes; UP000059680; Chromosome 1.
DR Genevisible; Q8RZV7; 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; ISS:Gramene.
DR GO; GO:0048658; P:anther wall tapetum development; IMP:Gramene.
DR GO; GO:0009554; P:megasporogenesis; IMP:Gramene.
DR GO; GO:0009556; P:microsporogenesis; IMP:Gramene.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR Gene3D; 3.80.10.10; -; 5.
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; PF13855; LRR_8; 3.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00369; LRR_TYP; 10.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51450; LRR; 17.
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; Cell membrane; Glycoprotein; Kinase; Leucine-rich repeat;
KW Meiosis; Membrane; Nucleotide-binding; Receptor; Reference proteome;
KW Repeat; Serine/threonine-protein kinase; Signal; Transferase;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..1294
FT /note="Leucine-rich repeat receptor protein kinase MSP1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000432097"
FT TRANSMEM 917..937
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REPEAT 88..112
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 113..136
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 138..160
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 161..184
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT REPEAT 186..207
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT REPEAT 232..256
FT /note="LRR 6"
FT /evidence="ECO:0000255"
FT REPEAT 258..280
FT /note="LRR 7"
FT /evidence="ECO:0000255"
FT REPEAT 282..304
FT /note="LRR 8"
FT /evidence="ECO:0000255"
FT REPEAT 305..328
FT /note="LRR 9"
FT /evidence="ECO:0000255"
FT REPEAT 330..352
FT /note="LRR 10"
FT /evidence="ECO:0000255"
FT REPEAT 353..376
FT /note="LRR 11"
FT /evidence="ECO:0000255"
FT REPEAT 378..400
FT /note="LRR 12"
FT /evidence="ECO:0000255"
FT REPEAT 401..422
FT /note="LRR 13"
FT /evidence="ECO:0000255"
FT REPEAT 423..446
FT /note="LRR 14"
FT /evidence="ECO:0000255"
FT REPEAT 447..469
FT /note="LRR 15"
FT /evidence="ECO:0000255"
FT REPEAT 471..493
FT /note="LRR 16"
FT /evidence="ECO:0000255"
FT REPEAT 494..517
FT /note="LRR 17"
FT /evidence="ECO:0000255"
FT REPEAT 519..541
FT /note="LRR 18"
FT /evidence="ECO:0000255"
FT REPEAT 542..565
FT /note="LRR 19"
FT /evidence="ECO:0000255"
FT REPEAT 566..589
FT /note="LRR 20"
FT /evidence="ECO:0000255"
FT REPEAT 591..613
FT /note="LRR 21"
FT /evidence="ECO:0000255"
FT REPEAT 614..637
FT /note="LRR 22"
FT /evidence="ECO:0000255"
FT REPEAT 649..673
FT /note="LRR 23"
FT /evidence="ECO:0000255"
FT REPEAT 675..697
FT /note="LRR 24"
FT /evidence="ECO:0000255"
FT REPEAT 698..721
FT /note="LRR 25"
FT /evidence="ECO:0000255"
FT REPEAT 722..745
FT /note="LRR 26"
FT /evidence="ECO:0000255"
FT REPEAT 746..770
FT /note="LRR 27"
FT /evidence="ECO:0000255"
FT REPEAT 772..794
FT /note="LRR 28"
FT /evidence="ECO:0000255"
FT REPEAT 822..846
FT /note="LRR 29"
FT /evidence="ECO:0000255"
FT REPEAT 848..870
FT /note="LRR 30"
FT /evidence="ECO:0000255"
FT DOMAIN 1002..1282
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 1129
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 1008..1016
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 1030
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 198
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 207
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 220
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 330
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 359
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 458
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 472
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 567
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 570
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 687
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 699
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 704
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 805
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 821
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 832
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 1294 AA; 141319 MW; 886583E4859982A1 CRC64;
MVSNSFWLFI LLVSFIPISA WAESRDISTL FTLRDSITEG KGFLRNWFDS ETPPCSWSGI
TCIGHNVVAI DLSSVPLYAP FPLCIGAFQS LVRLNFSGCG FSGELPEALG NLQNLQYLDL
SNNELTGPIP ISLYNLKMLK EMVLDYNSLS GQLSPAIAQL QHLTKLSISM NSISGSLPPD
LGSLKNLELL DIKMNTFNGS IPATFGNLSC LLHFDASQNN LTGSIFPGIT SLTNLLTLDL
SSNSFEGTIP REIGQLENLE LLILGKNDLT GRIPQEIGSL KQLKLLHLEE CQFTGKIPWS
ISGLSSLTEL DISDNNFDAE LPSSMGELGN LTQLIAKNAG LSGNMPKELG NCKKLTVINL
SFNALIGPIP EEFADLEAIV SFFVEGNKLS GRVPDWIQKW KNARSIRLGQ NKFSGPLPVL
PLQHLLSFAA ESNLLSGSIP SHICQANSLH SLLLHHNNLT GTIDEAFKGC TNLTELNLLD
NHIHGEVPGY LAELPLVTLE LSQNKFAGML PAELWESKTL LEISLSNNEI TGPIPESIGK
LSVLQRLHID NNLLEGPIPQ SVGDLRNLTN LSLRGNRLSG IIPLALFNCR KLATLDLSYN
NLTGNIPSAI SHLTLLDSLI LSSNQLSGSI PAEICVGFEN EAHPDSEFLQ HHGLLDLSYN
QLTGQIPTSI KNCAMVMVLN LQGNLLNGTI PVELGELTNL TSINLSFNEF VGPMLPWSGP
LVQLQGLILS NNHLDGSIPA KIGQILPKIA VLDLSSNALT GTLPQSLLCN NYLNHLDVSN
NHLSGHIQFS CPDGKEYSST LLFFNSSSNH FSGSLDESIS NFTQLSTLDI HNNSLTGRLP
SALSDLSSLN YLDLSSNNLY GAIPCGICNI FGLSFANFSG NYIDMYSLAD CAAGGICSTN
GTDHKALHPY HRVRRAITIC AFTFVIIIVL VLLAVYLRRK LVRSRPLAFE SASKAKATVE
PTSTDELLGK KSREPLSINL ATFEHALLRV TADDILKATE NFSKVHIIGD GGFGTVYKAA
LPEGRRVAIK RLHGGHQFQG DREFLAEMET IGKVKHPNLV PLLGYCVCGD ERFLIYEYME
NGSLEMWLRN RADALEALGW PDRLKICLGS ARGLAFLHHG FVPHIIHRDM KSSNILLDEN
FEPRVSDFGL ARIISACETH VSTDIAGTFG YIPPEYGLTM KSTTKGDVYS FGVVMLELLT
GRPPTGQEEV QGGGNLVGWV RWMIARGKQN ELFDPCLPVS SVWREQMARV LAIARDCTAD
EPFKRPTMLE VVKGLKMTHG MECGPLVVTV SRDM
