PHOT_CHLRE
ID PHOT_CHLRE Reviewed; 749 AA.
AC Q8LPD9; A8IXU7; Q8LPE0;
DT 31-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Phototropin {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000269|PubMed:15695460, ECO:0000269|PubMed:24285544};
DE AltName: Full=Blue light receptor PHOT {ECO:0000305};
GN Name=PHOT {ECO:0000303|PubMed:12121468};
GN ORFNames=CHLRE_03g199000v5 {ECO:0000312|EMBL:PNW85943.1},
GN CHLREDRAFT_183965 {ECO:0000312|EMBL:EDP03413.1};
OS Chlamydomonas reinhardtii (Chlamydomonas smithii).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX NCBI_TaxID=3055;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=cw15;
RX PubMed=12121468; DOI=10.1034/j.1399-3054.2002.1150416.x;
RA Huang K.Y., Merkle T., Beck C.F.;
RT "Isolation and characterization of a Chlamydomonas gene that encodes a
RT putative blue-light photoreceptor of the phototropin family.";
RL Physiol. Plantarum 115:613-622(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC-503;
RX PubMed=17932292; DOI=10.1126/science.1143609;
RA Merchant S.S., Prochnik S.E., Vallon O., Harris E.H., Karpowicz S.J.,
RA Witman G.B., Terry A., Salamov A., Fritz-Laylin L.K., Marechal-Drouard L.,
RA Marshall W.F., Qu L.H., Nelson D.R., Sanderfoot A.A., Spalding M.H.,
RA Kapitonov V.V., Ren Q., Ferris P., Lindquist E., Shapiro H., Lucas S.M.,
RA Grimwood J., Schmutz J., Cardol P., Cerutti H., Chanfreau G., Chen C.L.,
RA Cognat V., Croft M.T., Dent R., Dutcher S., Fernandez E., Fukuzawa H.,
RA Gonzalez-Ballester D., Gonzalez-Halphen D., Hallmann A., Hanikenne M.,
RA Hippler M., Inwood W., Jabbari K., Kalanon M., Kuras R., Lefebvre P.A.,
RA Lemaire S.D., Lobanov A.V., Lohr M., Manuell A., Meier I., Mets L.,
RA Mittag M., Mittelmeier T., Moroney J.V., Moseley J., Napoli C.,
RA Nedelcu A.M., Niyogi K., Novoselov S.V., Paulsen I.T., Pazour G.J.,
RA Purton S., Ral J.P., Riano-Pachon D.M., Riekhof W., Rymarquis L.,
RA Schroda M., Stern D., Umen J., Willows R., Wilson N., Zimmer S.L.,
RA Allmer J., Balk J., Bisova K., Chen C.J., Elias M., Gendler K., Hauser C.,
RA Lamb M.R., Ledford H., Long J.C., Minagawa J., Page M.D., Pan J.,
RA Pootakham W., Roje S., Rose A., Stahlberg E., Terauchi A.M., Yang P.,
RA Ball S., Bowler C., Dieckmann C.L., Gladyshev V.N., Green P., Jorgensen R.,
RA Mayfield S., Mueller-Roeber B., Rajamani S., Sayre R.T., Brokstein P.,
RA Dubchak I., Goodstein D., Hornick L., Huang Y.W., Jhaveri J., Luo Y.,
RA Martinez D., Ngau W.C., Otillar B., Poliakov A., Porter A., Szajkowski L.,
RA Werner G., Zhou K., Grigoriev I.V., Rokhsar D.S., Grossman A.R.;
RT "The Chlamydomonas genome reveals the evolution of key animal and plant
RT functions.";
RL Science 318:245-250(2007).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=CC-503;
RG Chlamydomonas Annotation Team;
RG JGI Annotation Team;
RA Merchant S.S., Prochnik S.E., Vallon O., Harris E.H., Karpowicz S.J.,
RA Witman G.B., Terry A., Salamov A., Fritz-Laylin L.K., Marechal-Drouard L.,
RA Marshall W.F., Qu L.H., Nelson D.R., Sanderfoot A.A., Spalding M.H.,
RA Kapitonov V.V., Ren Q., Ferris P., Lindquist E., Shapiro H., Lucas S.M.,
RA Grimwood J., Schmutz J., Grigoriev I.V., Rokhsar D.S.;
RT "WGS assembly of Chlamydomonas reinhardtii.";
RL Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND AUTOPHOSPHORYLATION.
RX PubMed=15695460; DOI=10.1093/pcp/pci037;
RA Onodera A., Kong S.G., Doi M., Shimazaki K., Christie J., Mochizuki N.,
RA Nagatani A.;
RT "Phototropin from Chlamydomonas reinhardtii is functional in Arabidopsis
RT thaliana.";
RL Plant Cell Physiol. 46:367-374(2005).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF CYS-57; CYS-250 AND
RP ASP-547.
RX PubMed=24285544; DOI=10.1074/jbc.m113.515403;
RA Okajima K., Aihara Y., Takayama Y., Nakajima M., Kashojiya S., Hikima T.,
RA Oroguchi T., Kobayashi A., Sekiguchi Y., Yamamoto M., Suzuki T.,
RA Nagatani A., Nakasako M., Tokutomi S.;
RT "Light-induced conformational changes of LOV1 (light oxygen voltage-sensing
RT domain 1) and LOV2 relative to the kinase domain and regulation of kinase
RT activity in Chlamydomonas phototropin.";
RL J. Biol. Chem. 289:413-422(2014).
RN [6]
RP FUNCTION.
RX PubMed=27626383; DOI=10.1038/nature19358;
RA Petroutsos D., Tokutsu R., Maruyama S., Flori S., Greiner A., Magneschi L.,
RA Cusant L., Kottke T., Mittag M., Hegemann P., Finazzi G., Minagawa J.;
RT "A blue-light photoreceptor mediates the feedback regulation of
RT photosynthesis.";
RL Nature 537:563-566(2016).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 17-125 IN COMPLEX WITH FMN, AND
RP COFACTOR.
RX PubMed=12668455; DOI=10.1016/s0006-3495(03)75052-8;
RA Fedorov R., Schlichting I., Hartmann E., Domratcheva T., Fuhrmann M.,
RA Hegemann P.;
RT "Crystal structures and molecular mechanism of a light-induced signaling
RT switch: The Phot-LOV1 domain from Chlamydomonas reinhardtii.";
RL Biophys. J. 84:2474-2482(2003).
CC -!- FUNCTION: Protein kinase that acts as a blue light photoreceptor
CC (PubMed:15695460, PubMed:24285544). Required for non-photochemical
CC quenching (NPQ), a mechanism that converts and dissipates the harmful
CC excess absorbed light energy into heat and protect the photosynthetic
CC apparatus from photo-oxidative damage (PubMed:27626383). Controls the
CC energy-dependent chlorophyll fluorescence quenching (qE) activity of
CC chlorophyll excited states by inducing the expression of the qE
CC effector protein LHCSR3 in high light intensities (PubMed:27626383).
CC {ECO:0000269|PubMed:15695460, ECO:0000269|PubMed:24285544,
CC ECO:0000269|PubMed:27626383}.
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:0000269|PubMed:15695460, ECO:0000269|PubMed:24285544};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990;
CC Evidence={ECO:0000269|PubMed:15695460, ECO:0000269|PubMed:24285544};
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:0000269|PubMed:15695460,
CC ECO:0000269|PubMed:24285544};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46609;
CC Evidence={ECO:0000269|PubMed:15695460, ECO:0000269|PubMed:24285544};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000269|PubMed:12668455};
CC Note=Binds 2 FMN per subunit. {ECO:0000305|PubMed:12668455};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:12121468};
CC Peripheral membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8LPD9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8LPD9-2; Sequence=VSP_060225;
CC -!- TISSUE SPECIFICITY: Expressed in gametes, pre-gametes and gametes
CC generated by pre-gametes (at protein level).
CC {ECO:0000269|PubMed:12121468}.
CC -!- PTM: Autophosphorylated in response to blue light irradiation.
CC {ECO:0000269|PubMed:15695460}.
CC -!- PTM: 2 molecules of FMN bind covalently to cysteines after exposure to
CC blue light and are reversed in the dark. {ECO:0000305|PubMed:12668455}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. {ECO:0000305}.
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DR EMBL; AJ416556; CAC94940.1; -; Genomic_DNA.
DR EMBL; AJ416557; CAC94941.1; -; mRNA.
DR EMBL; DS496126; EDP03413.1; -; Genomic_DNA.
DR EMBL; CM008964; PNW85943.1; -; Genomic_DNA.
DR PDB; 1N9L; X-ray; 1.90 A; A=17-125.
DR PDB; 1N9N; X-ray; 2.30 A; A=17-125.
DR PDB; 1N9O; X-ray; 2.80 A; A=17-125.
DR PDBsum; 1N9L; -.
DR PDBsum; 1N9N; -.
DR PDBsum; 1N9O; -.
DR AlphaFoldDB; Q8LPD9; -.
DR SMR; Q8LPD9; -.
DR STRING; 3055.EDP03413; -.
DR PRIDE; Q8LPD9; -.
DR ProMEX; Q8LPD9; -.
DR EnsemblPlants; PNW85943; PNW85943; CHLRE_03g199000v5. [Q8LPD9-1]
DR Gramene; PNW85943; PNW85943; CHLRE_03g199000v5. [Q8LPD9-1]
DR eggNOG; ENOG502QPPH; Eukaryota.
DR HOGENOM; CLU_006321_3_1_1; -.
DR OMA; THVCLIS; -.
DR OrthoDB; 529293at2759; -.
DR Proteomes; UP000006906; Chromosome 3.
DR ExpressionAtlas; Q8LPD9; baseline and differential.
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; IDA:UniProtKB.
DR GO; GO:0009785; P:blue light signaling pathway; IDA:UniProtKB.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
DR CDD; cd00130; PAS; 2.
DR InterPro; IPR000961; AGC-kinase_C.
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; 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; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 2.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding; Chromophore; Flavoprotein;
KW FMN; Kinase; Membrane; Nucleotide-binding; Photoreceptor protein; Receptor;
KW Reference proteome; Sensory transduction; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..749
FT /note="Phototropin"
FT /id="PRO_0000447660"
FT DOMAIN 7..80
FT /note="PAS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 81..135
FT /note="PAC 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00141"
FT DOMAIN 200..273
FT /note="PAS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 274..328
FT /note="PAC 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00141"
FT DOMAIN 404..712
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 713..749
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT REGION 563..591
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 729..749
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 576..591
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 529
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 56..61
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:12668455,
FT ECO:0007744|PDB:1N9L, ECO:0007744|PDB:1N9N,
FT ECO:0007744|PDB:1N9O"
FT BINDING 74
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:12668455,
FT ECO:0007744|PDB:1N9N, ECO:0007744|PDB:1N9O"
FT BINDING 89
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:12668455,
FT ECO:0007744|PDB:1N9L, ECO:0007744|PDB:1N9N,
FT ECO:0007744|PDB:1N9O"
FT BINDING 99
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:12668455,
FT ECO:0007744|PDB:1N9L, ECO:0007744|PDB:1N9N"
FT BINDING 120
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:12668455,
FT ECO:0007744|PDB:1N9L, ECO:0007744|PDB:1N9N"
FT BINDING 410..418
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 433
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 57
FT /note="S-4a-FMN cysteine"
FT /evidence="ECO:0000269|PubMed:12668455"
FT VAR_SEQ 631
FT /note="P -> PA (in isoform 2)"
FT /id="VSP_060225"
FT MUTAGEN 57
FT /note="C->A: No effect on blue light-induced kinase
FT activity."
FT /evidence="ECO:0000269|PubMed:24285544"
FT MUTAGEN 250
FT /note="C->A: Small decrease of blue light-induced kinase
FT activity."
FT /evidence="ECO:0000269|PubMed:24285544"
FT MUTAGEN 547
FT /note="D->N: Loss of kinase activity."
FT /evidence="ECO:0000269|PubMed:24285544"
FT CONFLICT 485
FT /note="D -> E (in Ref. 1; CAC94940)"
FT /evidence="ECO:0000305"
FT STRAND 21..26
FT /evidence="ECO:0007829|PDB:1N9L"
FT STRAND 34..37
FT /evidence="ECO:0007829|PDB:1N9L"
FT HELIX 39..45
FT /evidence="ECO:0007829|PDB:1N9L"
FT HELIX 49..52
FT /evidence="ECO:0007829|PDB:1N9L"
FT HELIX 57..60
FT /evidence="ECO:0007829|PDB:1N9L"
FT HELIX 67..79
FT /evidence="ECO:0007829|PDB:1N9L"
FT STRAND 83..90
FT /evidence="ECO:0007829|PDB:1N9L"
FT STRAND 96..107
FT /evidence="ECO:0007829|PDB:1N9L"
FT STRAND 113..122
FT /evidence="ECO:0007829|PDB:1N9L"
SQ SEQUENCE 749 AA; 81395 MW; 6F2E5FE88B85EAFF CRC64;
MAGVPAPASQ LTKVLAGLRH TFVVADATLP DCPLVYASEG FYAMTGYGPD EVLGHNCRFL
QGEGTDPKEV QKIRDAIKKG EACSVRLLNY RKDGTPFWNL LTVTPIKTPD GRVSKFVGVQ
VDVTSKTEGK ALADNSGVPL LVKYDHRLRD NVARTIVDDV TIAVEKAEGV EPGQASAVAA
AAPLGAKGPR GTAPKSFPRV ALDLATTVER IQQNFCISDP TLPDCPIVFA SDAFLELTGY
SREEVLGRNC RFLQGAGTDR GTVDQIRAAI KEGSELTVRI LNYTKAGKAF WNMFTLAPMR
DQDGHARFFV GVQVDVTAQS TSPDKAPVWN KTPEEEVAKA KMGAEAASLI SSALQGMAAP
TTANPWAAIS GVIMRRKPHK ADDKAYQALL QLQERDGKMK LMHFRRVKQL GAGDVGLVDL
VQLQGSELKF AMKTLDKFEM QERNKVARVL TESAILAAVD HPFLATLYCT IQTDTHLHFV
MEYCDGGELY GLLNSQPKKR LKEEHVRFYA SEVLTALQYL HLLGYVYRDL KPENILLHHT
GHVLLTDFDL SYSKGSTTPR IEKIGGAGAA GGSAPKSPKK SSSKSGGSSS GSALQLENYL
LLAEPSARAN SFVGTEEYLA PEVINAAGHG PAVDWWSLGI LIFELLYGTT PFRGARRDET
FENIIKSPLK FPSKPAVSEE CRDLIEKLLV KDVGARLGSR TGANEIKSHP WFKGINWALL
RHQQPPYVPR RASKAAGGSS TGGAAFDNY
