XIAO_ORYSJ
ID XIAO_ORYSJ Reviewed; 1157 AA.
AC G9LZD7; Q0JAU5; Q7XUH4;
DT 15-FEB-2017, integrated into UniProtKB/Swiss-Prot.
DT 22-FEB-2012, sequence version 1.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=Probable inactive leucine-rich repeat receptor kinase XIAO {ECO:0000305};
DE Flags: Precursor;
GN Name=XIAO {ECO:0000303|PubMed:22151303};
GN OrderedLocusNames=Os04g0576900 {ECO:0000312|EMBL:BAS90612.1},
GN LOC_Os04g48760 {ECO:0000305};
GN ORFNames=OSJNBa0020J04.8 {ECO:0000312|EMBL:CAD41303.2};
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 [GENOMIC DNA], FUNCTION, TISSUE SPECIFICITY, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=cv. Zhonghua 11;
RX PubMed=22151303; DOI=10.1111/j.1365-313x.2011.04877.x;
RA Jiang Y., Bao L., Jeong S.Y., Kim S.K., Xu C., Li X., Zhang Q.;
RT "XIAO is involved in the control of organ size by contributing to the
RT regulation of signaling and homeostasis of brassinosteroids and cell
RT cycling in rice.";
RL Plant J. 70:398-408(2012).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12447439; DOI=10.1038/nature01183;
RA Feng Q., Zhang Y., Hao P., Wang S., Fu G., Huang Y., Li Y., Zhu J., Liu Y.,
RA Hu X., Jia P., Zhang Y., Zhao Q., Ying K., Yu S., Tang Y., Weng Q.,
RA Zhang L., Lu Y., Mu J., Lu Y., Zhang L.S., Yu Z., Fan D., Liu X., Lu T.,
RA Li C., Wu Y., Sun T., Lei H., Li T., Hu H., Guan J., Wu M., Zhang R.,
RA Zhou B., Chen Z., Chen L., Jin Z., Wang R., Yin H., Cai Z., Ren S., Lv G.,
RA Gu W., Zhu G., Tu Y., Jia J., Zhang Y., Chen J., Kang H., Chen X., Shao C.,
RA Sun Y., Hu Q., Zhang X., Zhang W., Wang L., Ding C., Sheng H., Gu J.,
RA Chen S., Ni L., Zhu F., Chen W., Lan L., Lai Y., Cheng Z., Gu M., Jiang J.,
RA Li J., Hong G., Xue Y., Han B.;
RT "Sequence and analysis of rice chromosome 4.";
RL Nature 420:316-320(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).
CC -!- FUNCTION: Functions in the early stages of organ development by
CC regulating cell division rate. Is probably involved in the regulation
CC of a number of cell-cycle genes. May act as regulator of
CC brassinosteroid (BR) signaling and cell-cycle controlling organ growth.
CC {ECO:0000269|PubMed:22151303}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in developing culm, coleoptile, primary
CC root, young spikelet, young leaf blade and leaf sheath, floral meristem
CC primordia, stamen primordia, and lemma and palea primordia.
CC {ECO:0000269|PubMed:22151303}.
CC -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC inactive. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- DISRUPTION PHENOTYPE: Dwarf plants with erect leaves. Reduced organ
CC sizes due to decreased cell numbers resulting from reduced cell
CC division rate. {ECO:0000269|PubMed:22151303}.
CC -!- MISCELLANEOUS: Xiao means small in Chinese.
CC {ECO:0000305|PubMed:22151303}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAF15542.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAS90612.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAD41303.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; JQ234882; AEW49518.1; -; Genomic_DNA.
DR EMBL; AL606639; CAD41303.2; ALT_SEQ; Genomic_DNA.
DR EMBL; AP008210; BAF15542.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP014960; BAS90612.1; ALT_SEQ; Genomic_DNA.
DR AlphaFoldDB; G9LZD7; -.
DR SMR; G9LZD7; -.
DR STRING; 4530.OS04T0576900-01; -.
DR PRIDE; G9LZD7; -.
DR eggNOG; ENOG502QTHE; Eukaryota.
DR Proteomes; UP000000763; Chromosome 4.
DR Proteomes; UP000059680; Chromosome 4.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0009742; P:brassinosteroid mediated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0090696; P:post-embryonic plant organ development; IMP:UniProtKB.
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; IPR025875; Leu-rich_rpt_4.
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; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF12799; LRR_4; 1.
DR Pfam; PF13855; LRR_8; 6.
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; PS51450; LRR; 19.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Brassinosteroid signaling pathway; Cell membrane;
KW Glycoprotein; Leucine-rich repeat; Membrane; Nucleotide-binding; Receptor;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..1157
FT /note="Probable inactive leucine-rich repeat receptor
FT kinase XIAO"
FT /id="PRO_5003523412"
FT TRANSMEM 765..785
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REPEAT 101..125
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 127..149
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 150..172
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 173..196
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT REPEAT 198..220
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT REPEAT 221..245
FT /note="LRR 6"
FT /evidence="ECO:0000255"
FT REPEAT 247..269
FT /note="LRR 7"
FT /evidence="ECO:0000255"
FT REPEAT 270..293
FT /note="LRR 8"
FT /evidence="ECO:0000255"
FT REPEAT 296..319
FT /note="LRR 9"
FT /evidence="ECO:0000255"
FT REPEAT 320..343
FT /note="LRR 10"
FT /evidence="ECO:0000255"
FT REPEAT 344..367
FT /note="LRR 11"
FT /evidence="ECO:0000255"
FT REPEAT 368..391
FT /note="LRR 12"
FT /evidence="ECO:0000255"
FT REPEAT 393..414
FT /note="LRR 13"
FT /evidence="ECO:0000255"
FT REPEAT 415..439
FT /note="LRR 14"
FT /evidence="ECO:0000255"
FT REPEAT 440..463
FT /note="LRR 15"
FT /evidence="ECO:0000255"
FT REPEAT 464..487
FT /note="LRR 16"
FT /evidence="ECO:0000255"
FT REPEAT 489..511
FT /note="LRR 17"
FT /evidence="ECO:0000255"
FT REPEAT 513..536
FT /note="LRR 18"
FT /evidence="ECO:0000255"
FT REPEAT 537..559
FT /note="LRR 19"
FT /evidence="ECO:0000255"
FT REPEAT 561..583
FT /note="LRR 20"
FT /evidence="ECO:0000255"
FT REPEAT 584..608
FT /note="LRR 21"
FT /evidence="ECO:0000255"
FT REPEAT 609..631
FT /note="LRR 22"
FT /evidence="ECO:0000255"
FT REPEAT 632..656
FT /note="LRR 23"
FT /evidence="ECO:0000255"
FT REPEAT 658..680
FT /note="LRR 24"
FT /evidence="ECO:0000255"
FT REPEAT 681..704
FT /note="LRR 25"
FT /evidence="ECO:0000255"
FT REPEAT 706..728
FT /note="LRR 26"
FT /evidence="ECO:0000255"
FT DOMAIN 849..1144
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 804..825
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 855..863
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 930..932
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT BINDING 936..939
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT BINDING 980..985
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT BINDING 998
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT CARBOHYD 58
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 149
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 204
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 244
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 296
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 438
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 465
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 494
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 524
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 607
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 610
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 655
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 679
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 692
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 711
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CONFLICT 179
FT /note="D -> E (in Ref. 2; CAD41303)"
FT /evidence="ECO:0000305"
FT CONFLICT 206..207
FT /note="SF -> AV (in Ref. 2; CAD41303)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1157 AA; 122421 MW; 6F80B3B6BAF3CD2B CRC64;
MPPPPRLLFL LVMLLVVAAP GAPVFGANAP PEVKAEIDAL LMFRSGLRDP YAAMSGWNAS
SPSAPCSWRG VACAAGTGRV VELALPKLRL SGAISPALSS LVYLEKLSLR SNSLSGTIPA
SLSRISSLRA VYLQYNSLSG PIPQSFLANL TNLQTFDVSG NLLSGPVPVS FPPSLKYLDL
SSNAFSGTIP ANVSASATSL QFLNLSFNRL RGTVPASLGT LQDLHYLWLD GNLLEGTIPS
ALSNCSALLH LSLQGNALRG ILPPAVAAIP SLQILSVSRN RLTGAIPAAA FGGVGNSSLR
IVQVGGNAFS QVDVPVSLGK DLQVVDLRAN KLAGPFPSWL AGAGGLTVLD LSGNAFTGEV
PPAVGQLTAL QELRLGGNAF TGTVPAEIGR CGALQVLDLE DNRFSGEVPA ALGGLRRLRE
VYLGGNSFSG QIPASLGNLS WLEALSTPGN RLTGDLPSEL FVLGNLTFLD LSDNKLAGEI
PPSIGNLAAL QSLNLSGNSF SGRIPSNIGN LLNLRVLDLS GQKNLSGNLP AELFGLPQLQ
YVSLAGNSFS GDVPEGFSSL WSLRHLNLSV NSFTGSMPAT YGYLPSLQVL SASHNRICGE
LPVELANCSN LTVLDLRSNQ LTGPIPGDFA RLGELEELDL SHNQLSRKIP PEISNCSSLV
TLKLDDNHLG GEIPASLSNL SKLQTLDLSS NNLTGSIPAS LAQIPGMLSL NVSQNELSGE
IPAMLGSRFG TPSVFASNPN LCGPPLENEC SAYRQHRRRQ RLQRLALLIG VVAATVLLLV
LFCCCCVYSL LRWRRRFIEK RDGVKKRRRS PGRGSGSSGT STDSVSQPKL IMFNSRITYA
DTVEATRQFD EENVLSRGRH GLVFKACYND GTVLAILRLP STSSDGAVVI EEGSFRKEAE
SLGKVKHRNL TVLRGYYAGP PPDVRLLVYD YMPNGNLATL LQEASHQDGH ILNWPMRHLI
ALGVSRGLAF LHQSGVVHGD VKPQNILFDA DFEPHLSDFG LEPMVVTAGA AAAAAAASTS
ATTTVGSLGY VAPDAAAAGQ ATREGDVYSF GIVLLELLTG RRPGMFAGED EDIVKWVKRQ
LQRGAVAELL EPGLLELDPE SSEWEEFLLG IKVGLLCTAP DPLDRPAMGD VVFMLEGCRV
GPDIPSSADP TSQPSPA
