PHOT2_ORYSJ
ID PHOT2_ORYSJ Reviewed; 907 AA.
AC Q9ST27; Q0JEA8; Q7XVR1;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Phototropin-2;
DE EC=2.7.11.1;
DE AltName: Full=Non-phototropic hypocotyl protein 1B;
DE Short=OsNPH1B;
GN Name=PHOT2; OrderedLocusNames=Os04g0304200, LOC_Os04g23890;
GN ORFNames=OSJNBa0079M09.13;
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], TISSUE SPECIFICITY, AND INDUCTION.
RC STRAIN=cv. Nohrin 8;
RX PubMed=10845454; DOI=10.1093/pcp/41.4.415;
RA Kanegae H., Tahir M., Savazzini F., Yamamoto K., Yano M., Sasaki T.,
RA Kanegae T., Wada M., Takano M.;
RT "Rice NPH1 homologues, OsNPH1a and OsNPH1b, are differently
RT photoregulated.";
RL Plant Cell Physiol. 41:415-423(2000).
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).
RN [6]
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=12068117; DOI=10.1104/pp.002410;
RA Kasahara M., Swartz T.E., Olney M.A., Onodera A., Mochizuki N.,
RA Fukuzawa H., Asamizu E., Tabata S., Kanegae H., Takano M., Christie J.M.,
RA Nagatani A., Briggs W.R.;
RT "Photochemical properties of the flavin mononucleotide-binding domains of
RT the phototropins from Arabidopsis, rice, and Chlamydomonas reinhardtii.";
RL Plant Physiol. 129:762-773(2002).
CC -!- FUNCTION: Protein kinase that acts as a blue light photoreceptor in a
CC signal-transduction pathway for phototropic responses. Regulates a wide
CC range of physiological activities in plants that maximize the
CC efficiency of photosynthesis, such as chloroplast relocations, stomata
CC opening, and leaf expansion (By similarity). {ECO:0000250}.
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 -!- 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;
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000250};
CC Note=Binds 2 FMN per subunit. {ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Absorption:
CC Abs(max)=450 nm {ECO:0000269|PubMed:12068117};
CC Note=Exhibits a smaller absorbance peak at 350 nm. The broad
CC fluorescence emission spectrum peaks at 490 nm.;
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed at low levels in leaves of dark-grown
CC seedlings. {ECO:0000269|PubMed:10845454}.
CC -!- INDUCTION: By white light in dark-grown seedlings.
CC {ECO:0000269|PubMed:10845454}.
CC -!- DOMAIN: The PAS (PER-ARNT-SIM) domains are required for the binding of
CC FMN chromophores. {ECO:0000250}.
CC -!- PTM: Autophosphorylated in response to blue light irradiation.
CC {ECO:0000250}.
CC -!- PTM: 2 molecules of FMN bind covalently to cysteines after exposure to
CC blue light and are reversed in the dark. {ECO:0000250}.
CC -!- MISCELLANEOUS: Undergoes a photocycle characterized by fluorescence and
CC absorption changes induced by blue light.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAF14329.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB018443; BAA84779.1; -; mRNA.
DR EMBL; AL731609; CAD40495.2; -; Genomic_DNA.
DR EMBL; AP008210; BAF14329.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP014960; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_015636457.1; XM_015780971.1.
DR RefSeq; XP_015636458.1; XM_015780972.1.
DR RefSeq; XP_015636459.1; XM_015780973.1.
DR RefSeq; XP_015636460.1; XM_015780974.1.
DR AlphaFoldDB; Q9ST27; -.
DR SMR; Q9ST27; -.
DR STRING; 4530.OS04T0304200-01; -.
DR PaxDb; Q9ST27; -.
DR PRIDE; Q9ST27; -.
DR GeneID; 4335426; -.
DR KEGG; osa:4335426; -.
DR eggNOG; ENOG502QPPH; Eukaryota.
DR HOGENOM; CLU_006321_3_2_1; -.
DR InParanoid; Q9ST27; -.
DR OrthoDB; 529293at2759; -.
DR Proteomes; UP000000763; Chromosome 4.
DR Proteomes; UP000059680; Chromosome 4.
DR Genevisible; Q9ST27; OS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0009882; F:blue light photoreceptor activity; IDA:UniProtKB.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR CDD; cd00130; PAS; 2.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF13426; PAS_9; 2.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00086; PAC; 2.
DR SMART; SM00091; PAS; 2.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF55785; SSF55785; 2.
DR SUPFAM; SSF56112; SSF56112; 1.
DR TIGRFAMs; TIGR00229; sensory_box; 2.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 2.
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; Chromophore; Flavoprotein; FMN; Kinase; Nucleotide-binding;
KW Photoreceptor protein; Receptor; Reference proteome; Repeat;
KW Sensory transduction; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..907
FT /note="Phototropin-2"
FT /id="PRO_0000395004"
FT DOMAIN 89..162
FT /note="PAS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 163..217
FT /note="PAC 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00141"
FT DOMAIN 375..448
FT /note="PAS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 449..503
FT /note="PAC 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00141"
FT DOMAIN 576..863
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 28..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 332..363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 701
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 138..143
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 156
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 171
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 181
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 202
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 424..429
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 442
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 457
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 467
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 488
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 582..590
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 605
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 139
FT /note="S-4a-FMN cysteine"
FT /evidence="ECO:0000250"
FT MOD_RES 425
FT /note="S-4a-FMN cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 907 AA; 100224 MW; 7F8995A6FDD36AD6 CRC64;
MAGSSSSKEI VDAVEKWMAF PTSGGGGATA GLEIVAEDAP SGSSGAHQQQ AWRPVAPATA
GRDSGGTGSG KSSVDGGVGR ASHDSLPRVS QELKDALSSL QQTFVVSDAT RPDCPIIYAS
EGFFTMTGYS PREVVGRNCR FLQGPDTDAA EVAKIRDAVK HGRSFCGRLL NYRKDGAPFW
NLLTVTPIRD DNGKVIKFIG MQVEVSKYTE GLSDKRMRPN ELPVSLIRYD ERQKDKAMSS
MTEVVQTVKQ PRGARAPADA ALLTPPKMSD ADKMAAMSPV VAPGTPSGGG GGAGSFKSPL
WDLKKEESRL SRLASGRKSG RSSLMGFKIG KRSSVGSREA PAVVEEPAPA PPPAPEVVER
TDSWERAERE KDIRQGIDLA TTLERIEKNF VITDPRIPDN PIIFASDSFL ELTEYTREEI
LGRNCRFLQG PETDQGTVDK IREAIREQKE ITVQLINYTK SGKKFWNLFH LQPMRDQKGE
LQYFIGVQLD GSDHVEPLRN RLSENTEIQS AKLVKATAEN VDDAVRELPD ANLRPEDLWA
IHSMRVSPKP HKRNNPSWIA IEKATNLGEK IGLKHFKPVK PLGCGDTGSV HLVELQGSGE
LFAMKAMDKS VMLNRNKVHR ACIEREIYAL LDHPFLPTLY TSFQTPTHVC LITDFCPGGE
LFAVLDRQPM KIFREECARF YAAEVVIGLE YLHCLGIIYR DLKPENILLQ ADGHIVLTDF
DLSFLTTSKP HVIKNSTSLK RRRSQEFLPP TFVSEPSTPS NSFVGTEEYI APEVITGAGH
TSAIDWWALG ILLYEMLYGR TPFRGKNRKK TFYNILHKDL TFPSSIPVSL AAKQLIHGLL
QRDPSNRIGS NAGANDIKQH SFFQDINWPL IRCMSPPELD VPLKLIGKET QPKAKPDEDV
PLNLDTF
