ID Q6ZF83_ORYSJ Unreviewed; 824 AA. AC Q6ZF83; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 28-JUN-2023, entry version 164. DE RecName: Full=Receptor-like serine/threonine-protein kinase {ECO:0000256|PIRNR:PIRNR000641}; DE EC=2.7.11.1 {ECO:0000256|PIRNR:PIRNR000641}; GN OrderedLocusNames=Os07g0553633 {ECO:0000313|EMBL:BAT02071.1}; GN ORFNames=OSNPB_070553633 {ECO:0000313|EMBL:BAT02071.1}; 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 {ECO:0000313|EMBL:BAT02071.1, ECO:0000313|Proteomes:UP000059680}; RN [1] {ECO:0000313|Proteomes:UP000059680} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Nipponbare {ECO:0000313|Proteomes:UP000059680}; RX PubMed=16100779; DOI=10.1038/nature03895; RG International rice genome sequencing project (IRGSP); RA Matsumoto T., Wu J., Kanamori H., Katayose Y., Fujisawa M., Namiki N., RA Mizuno H., Yamamoto K., Antonio B.A., Baba T., Sakata K., Nagamura Y., RA Aoki H., Arikawa K., Arita K., Bito T., Chiden Y., Fujitsuka N., RA Fukunaka R., Hamada M., Harada C., Hayashi A., Hijishita S., Honda M., RA Hosokawa S., Ichikawa Y., Idonuma A., Iijima M., Ikeda M., Ikeno M., RA Ito K., Ito S., Ito T., Ito Y., Ito Y., Iwabuchi A., Kamiya K., RA Karasawa W., Kurita K., Katagiri S., Kikuta A., Kobayashi H., Kobayashi N., RA Machita K., Maehara T., Masukawa M., Mizubayashi T., Mukai Y., Nagasaki H., RA Nagata Y., Naito S., Nakashima M., Nakama Y., Nakamichi Y., Nakamura M., RA Meguro A., Negishi M., Ohta I., Ohta T., Okamoto M., Ono N., Saji S., RA Sakaguchi M., Sakai K., Shibata M., Shimokawa T., Song J., Takazaki Y., RA Terasawa K., Tsugane M., Tsuji K., Ueda S., Waki K., Yamagata H., RA Yamamoto M., Yamamoto S., Yamane H., Yoshiki S., Yoshihara R., Yukawa K., RA Zhong H., Yano M., Yuan Q., Ouyang S., Liu J., Jones K.M., Gansberger K., RA Moffat K., Hill J., Bera J., Fadrosh D., Jin S., Johri S., Kim M., RA Overton L., Reardon M., Tsitrin T., Vuong H., Weaver B., Ciecko A., RA Tallon L., Jackson J., Pai G., Aken S.V., Utterback T., Reidmuller S., RA Feldblyum T., Hsiao J., Zismann V., Iobst S., de Vazeille A.R., Buell C.R., RA Ying K., Li Y., Lu T., Huang Y., Zhao Q., Feng Q., Zhang L., Zhu J., RA Weng Q., Mu J., Lu Y., Fan D., Liu Y., Guan J., Zhang Y., Yu S., Liu X., RA Zhang Y., Hong G., Han B., Choisne N., Demange N., Orjeda G., Samain S., RA Cattolico L., Pelletier E., Couloux A., Segurens B., Wincker P., D'Hont A., RA Scarpelli C., Weissenbach J., Salanoubat M., Quetier F., Yu Y., Kim H.R., RA Rambo T., Currie J., Collura K., Luo M., Yang T., Ammiraju J.S.S., RA Engler F., Soderlund C., Wing R.A., Palmer L.E., de la Bastide M., RA Spiegel L., Nascimento L., Zutavern T., O'Shaughnessy A., Dike S., RA Dedhia N., Preston R., Balija V., McCombie W.R., Chow T., Chen H., RA Chung M., Chen C., Shaw J., Wu H., Hsiao K., Chao Y., Chu M., Cheng C., RA Hour A., Lee P., Lin S., Lin Y., Liou J., Liu S., Hsing Y., Raghuvanshi S., RA Mohanty A., Bharti A.K., Gaur A., Gupta V., Kumar D., Ravi V., Vij S., RA Kapur A., Khurana P., Khurana P., Khurana J.P., Tyagi A.K., Gaikwad K., RA Singh A., Dalal V., Srivastava S., Dixit A., Pal A.K., Ghazi I.A., RA Yadav M., Pandit A., Bhargava A., Sureshbabu K., Batra K., Sharma T.R., RA Mohapatra T., Singh N.K., Messing J., Nelson A.B., Fuks G., Kavchok S., RA Keizer G., Linton E., Llaca V., Song R., Tanyolac B., Young S., Ho-Il K., RA Hahn J.H., Sangsakoo G., Vanavichit A., de Mattos Luiz.A.T., Zimmer P.D., RA Malone G., Dellagostin O., de Oliveira A.C., Bevan M., Bancroft I., RA Minx P., Cordum H., Wilson R., Cheng Z., Jin W., Jiang J., Leong S.A., RA Iwama H., Gojobori T., Itoh T., Niimura Y., Fujii Y., Habara T., Sakai H., RA Sato Y., Wilson G., Kumar K., McCouch S., Juretic N., Hoen D., Wright S., RA Bruskiewich R., Bureau T., Miyao A., Hirochika H., Nishikawa T., RA Kadowaki K., Sugiura M., Burr B., Sasaki T.; RT "The map-based sequence of the rice genome."; RL Nature 436:793-800(2005). RN [2] {ECO:0000313|EMBL:BAH00857.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Leaf of seedling {ECO:0000313|EMBL:BAH00857.1}; RA Kikuchi S.; RT "Oryza sativa full length cDNA."; RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:BAT02071.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=23299411; DOI=10.1093/pcp/pcs183; RA Sakai H., Lee S.S., Tanaka T., Numa H., Kim J., Kawahara Y., Wakimoto H., RA Yang C.C., Iwamoto M., Abe T., Yamada Y., Muto A., Inokuchi H., Ikemura T., RA Matsumoto T., Sasaki T., Itoh T.; RT "Rice Annotation Project Database (RAP-DB): an integrative and interactive RT database for rice genomics."; RL Plant Cell Physiol. 54:E6-E6(2013). RN [4] {ECO:0000313|EMBL:BAT02071.1, ECO:0000313|Proteomes:UP000059680} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Nipponbare {ECO:0000313|Proteomes:UP000059680}; 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 [5] {ECO:0000313|EMBL:BAT02071.1} RP NUCLEOTIDE SEQUENCE. RA Sakai H., Kawahara Y., Matsumoto T., Buell C.R., Itoh T.; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. 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:0000256|ARBA:ARBA00001433, CC ECO:0000256|PIRNR:PIRNR000641}; 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:0000256|ARBA:ARBA00000775, CC ECO:0000256|PIRNR:PIRNR000641}; CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single- CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein CC kinase family. {ECO:0000256|PIRNR:PIRNR000641}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AK240758; BAH00857.1; -; mRNA. DR EMBL; AP014963; BAT02071.1; -; Genomic_DNA. DR RefSeq; XP_015646909.1; XM_015791423.1. DR STRING; 39947.Q6ZF83; -. DR EnsemblPlants; Os07t0553633-01; Os07t0553633-01; Os07g0553633. DR GeneID; 9269356; -. DR Gramene; Os07t0553633-01; Os07t0553633-01; Os07g0553633. DR KEGG; osa:9269356; -. DR eggNOG; ENOG502QUMK; Eukaryota. DR HOGENOM; CLU_000288_116_2_1; -. DR OMA; FSQKFQS; -. DR OrthoDB; 337883at2759; -. DR Proteomes; UP000059680; Chromosome 7. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. 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:0048544; P:recognition of pollen; IEA:InterPro. DR GO; GO:0051707; P:response to other organism; IEA:UniProt. DR CDD; cd00028; B_lectin; 1. DR CDD; cd01098; PAN_AP_plant; 1. DR CDD; cd14066; STKc_IRAK; 1. DR Gene3D; 2.90.10.10; Bulb-type lectin domain; 1. DR Gene3D; 3.50.4.10; Hepatocyte Growth Factor; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 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; IPR000858; S_locus_glycoprot_dom. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR InterPro; IPR024171; SRK-like_kinase. DR PANTHER; PTHR47974; OS07G0415500 PROTEIN; 1. DR PANTHER; PTHR47974:SF19; RECEPTOR-LIKE SERINE/THREONINE-PROTEIN KINASE; 1. DR Pfam; PF01453; B_lectin; 1. DR Pfam; PF08276; PAN_2; 1. DR Pfam; PF00069; Pkinase; 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; alpha-D-mannose-specific plant lectins; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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 {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR000641}; KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157}; KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536}; KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR000641}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, KW ECO:0000256|PIRNR:PIRNR000641}; Receptor {ECO:0000256|ARBA:ARBA00023170}; KW Reference proteome {ECO:0000313|Proteomes:UP000059680}; KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527, KW ECO:0000256|PIRNR:PIRNR000641}; KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000641}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT SIGNAL 1..18 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 19..824 FT /note="Receptor-like serine/threonine-protein kinase" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5013533632" FT TRANSMEM 439..463 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 19..149 FT /note="Bulb-type lectin" FT /evidence="ECO:0000259|PROSITE:PS50927" FT DOMAIN 342..426 FT /note="Apple" FT /evidence="ECO:0000259|PROSITE:PS50948" FT DOMAIN 495..767 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT REGION 795..824 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 523 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141" SQ SEQUENCE 824 AA; 90414 MW; 36AF62D305910290 CRC64; MAPVFFLLLF SQIFLCTAVD TINSTTPLSG TQKIVSKGGR FALGFYTPPQ GNNTASGTGN YYIAIWYNNI PLQTTVWTAN SDVPVSDPTT ASLSIGSDGN LVLLDQSKNR QLWSTNVSVA SNSTVAVIQD GGSLDLMDAT NSSIVYWRSI DHPTNTWLPG GKLGLNKTTG VSQRLVPWRN NANPSPGLFS LELDPNGTTQ YFIQWNDSIT YWTSGPWNGN IFSLVPEMTA GYNYNFRFIN NVSESYFIYS MKDDSIISRF TIDVNGQIKQ WTWVPASENW ILFWSQPRTQ CEVYGLCGAY GSCNLNVLPF CNCIKGFSQK FQSDWDLQDF TGGCKRNVPL QCQTNSSSAQ TQPDKFYSMV SVRLPDNAQS AVAASSQACQ VACLNNCSCN AYTYNSSGCF VWHGDLINLQ DQYNGNGGGT LFLRLAASEL PDSKKSKKMI IGAVVGGVAA ALIILAIVLF IVFQKCRRDR TLRISKTTGG ALIAFRYSDL QHVTSNFSEK LGGGAFGTVF KGKLPDSTAI AVKRLDGLSQ GEKQFRAEVS TIGTIQHVNL VRLLGFCSEG SRRLLVYEYM PKGSLELQLF HGETTALNWA IRYQIALGTA RGLNYLHEKC RDCIIHCDVK PDNILLDESF VPKVSDFGLA KLLGRDFSRV LTTMRGTRGY LAPEWISGVP ITPKADVFSY GMMLFELISG RRNADLGEEG KSSFFPTLAV NKLQEGDVQT LLDPRLNGDA SADELTKACK VACWCIQDDE NGRPTMGQVV QILEGFLDVN MPPVPRSLKV LDESPDVINF FSDVSSSQTS QMHNSTASSQ TKSSTSGGSQ FQST //