PHT1A_ORYSJ
ID PHT1A_ORYSJ Reviewed; 921 AA.
AC Q2QYY8; Q9ST26;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Phototropin-1A;
DE EC=2.7.11.1;
DE AltName: Full=Non-phototropic hypocotyl protein 1A;
DE Short=OsNPH1a;
GN Name=PHOT1A; OrderedLocusNames=Os12g0101800, LOC_Os12g01140;
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=16188032; DOI=10.1186/1741-7007-3-20;
RG The rice chromosomes 11 and 12 sequencing consortia;
RT "The sequence of rice chromosomes 11 and 12, rich in disease resistance
RT genes and recent gene duplications.";
RL BMC Biol. 3:20-20(2005).
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: Highly expressed in coleoptiles of dark-grown
CC seedlings. {ECO:0000269|PubMed:10845454}.
CC -!- INDUCTION: Down-regulated 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}.
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DR EMBL; AB018444; BAA84780.1; -; mRNA.
DR EMBL; DP000011; ABA95572.2; -; Genomic_DNA.
DR EMBL; AP008218; BAF28932.1; -; Genomic_DNA.
DR EMBL; AP014968; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_015620213.1; XM_015764727.1.
DR AlphaFoldDB; Q2QYY8; -.
DR SMR; Q2QYY8; -.
DR STRING; 39947.Q2QYY8; -.
DR PaxDb; Q2QYY8; -.
DR PRIDE; Q2QYY8; -.
DR GeneID; 4351240; -.
DR KEGG; osa:4351240; -.
DR InParanoid; Q2QYY8; -.
DR OrthoDB; 529293at2759; -.
DR Proteomes; UP000000763; Chromosome 12.
DR Proteomes; UP000059680; Chromosome 12.
DR Genevisible; Q2QYY8; 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..921
FT /note="Phototropin-1A"
FT /id="PRO_0000395002"
FT DOMAIN 123..197
FT /note="PAS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 197..251
FT /note="PAC 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00141"
FT DOMAIN 400..473
FT /note="PAS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 474..528
FT /note="PAC 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00141"
FT DOMAIN 594..881
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 87..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 286..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 364..390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..118
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..315
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..344
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 719
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 172..177
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 190
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 205
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 215
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 236
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 449..454
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 482
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 492
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 513
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 600..608
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 623
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 173
FT /note="S-4a-FMN cysteine"
FT /evidence="ECO:0000250"
FT MOD_RES 450
FT /note="S-4a-FMN cysteine"
FT /evidence="ECO:0000250"
FT CONFLICT 133
FT /note="A -> V (in Ref. 1; BAA84780)"
FT /evidence="ECO:0000305"
FT CONFLICT 916
FT /note="N -> T (in Ref. 1; BAA84780)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 921 AA; 103382 MW; D8BA98ED7D278674 CRC64;
MASKGTEGGH GGVERKEQQQ QRGYQLPRDS RGSLEVFNPS SASSFRTAAA APKSASPFLA
IPDREEDNVV AQQRAAEWGL VLQTDHHTGL PQGVSARPSS GSARTSSEDN PQQQQSAAAI
PRVSEELRAA LSAFQQTFVV SDATHPNHPI MYASAGFFNM TGYTSKEVVG RNCRFLQGSG
TDPHEIDKIR QSLANGSNYC GRILNYKKDG TPFWNLLTIA PIKDEDGRLL KFIGMQVEVS
KYTEGKKDTV VRPNGLSESL IKYDARQKDH ARSSVSELLL ALKNPRSLSE SSNNTLKRKS
QESLSMSMTE VPSKRSSESG SRRNSRSGTR SSLQKINEVP DQGNRTRKSG LRAFMGFLGM
GHGSVEKNML KPRDEDPLID SDDERPESFE DEFRRKEMRR GIDLATTLER IEKNFVITDP
RLPDNPIIFA SDSFLQLTEY NREEILGRNC RFLQGPETDR ATVRKIRDAI DNQAEVTVQL
INYTKSGKKF WNLFHLQPMR DQKGDVQYFI GVQLDGTEHV QDDAAKEGVV LVKKTADNID
EAAKELPDAN LRPEDLWANH SKVVLPNPHM KDTASWRAIQ KVLESGESIG LKHFRPVKPL
GSGDTGSVHL VELLNTGEYF AMKAMDKSIM LNRNKVHRAT AERQILDLLD HPFLPTLYAS
FQTKTHICLI TDYCPGGELF VLLDNQPLKV LHEDAVRFYA AEVVVALEYL HCQGIIYRDL
KPENILLHRD GHISLTDFDL SCLTSCRPQV FLPEDADEKK GRKNGSYPIF FAEPMRASNS
FVGTEEYIAP EIITGAGHTS AVDWWALGIL LYEMLYGYTP FRGKTRQRTF ANILHKDIRF
PASISVSLAA RQLMYRLLHR DPANRLGSYE GANEIKGHPF FRGINWPLIR ATAPPKLEIP
LFSKDDMEKK GLVTNNRTDM F
