C71P1_ORYSJ
ID C71P1_ORYSJ Reviewed; 523 AA.
AC Q2QUC5; Q0IP04;
DT 20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Tryptamine 5-hydroxylase {ECO:0000303|PubMed:20150424};
DE EC=1.14.-.- {ECO:0000269|PubMed:20150424};
DE AltName: Full=Cytochrome P450 71P1 {ECO:0000303|PubMed:20150424};
DE AltName: Full=Protein SEKIGUCHI LESION {ECO:0000303|PubMed:20150424};
GN Name=CYP71P1 {ECO:0000303|PubMed:20150424};
GN Synonyms=SL {ECO:0000303|PubMed:20150424},
GN T5H {ECO:0000303|PubMed:23110463};
GN OrderedLocusNames=Os12g0268000 {ECO:0000312|EMBL:BAT16632.1},
GN LOC_Os12g16720 {ECO:0000312|EMBL:ABA97037.1};
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;
RN [1]
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 [2]
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 [3]
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 [4]
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 [5]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP THR-314 AND GLY-455.
RX PubMed=20150424; DOI=10.1074/jbc.m109.091371;
RA Fujiwara T., Maisonneuve S., Isshiki M., Mizutani M., Chen L., Wong H.L.,
RA Kawasaki T., Shimamoto K.;
RT "Sekiguchi lesion gene encodes a cytochrome P450 monooxygenase that
RT catalyzes conversion of tryptamine to serotonin in rice.";
RL J. Biol. Chem. 285:11308-11313(2010).
RN [6]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=21080162; DOI=10.1007/s00253-010-2994-4;
RA Park S., Kang K., Lee S.W., Ahn M.J., Bae J.M., Back K.;
RT "Production of serotonin by dual expression of tryptophan decarboxylase and
RT tryptamine 5-hydroxylase in Escherichia coli.";
RL Appl. Microbiol. Biotechnol. 89:1387-1394(2011).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, AND INDUCTION.
RX PubMed=23053415; DOI=10.1007/s00449-012-0787-0;
RA Park S., Kim Y.S., Rupasinghe S.G., Schuler M.A., Back K.;
RT "Rice P450 reductases differentially affect P450-mediated metabolism in
RT bacterial expression systems.";
RL Bioprocess Biosyst. Eng. 36:325-331(2013).
RN [8]
RP DEVELOPMENTAL STAGE.
RX PubMed=23110463; DOI=10.1111/jpi.12021;
RA Park S., Le T.N., Byeon Y., Kim Y.S., Back K.;
RT "Transient induction of melatonin biosynthesis in rice (Oryza sativa L.)
RT during the reproductive stage.";
RL J. Pineal Res. 55:40-45(2013).
RN [9]
RP FUNCTION.
RX PubMed=23521226; DOI=10.1111/jpi.12053;
RA Park S., Byeon Y., Back K.;
RT "Transcriptional suppression of tryptamine 5-hydroxylase, a terminal
RT serotonin biosynthetic gene, induces melatonin biosynthesis in rice (Oryza
RT sativa L.).";
RL J. Pineal Res. 55:131-137(2013).
CC -!- FUNCTION: Involved in serotonin biosynthesis. Catalyzes the conversion
CC of tryptamine to serotonin (PubMed:21080162, PubMed:23053415,
CC PubMed:20150424, PubMed:23521226). Accumulation of serotonin may play a
CC role in innate immunity (PubMed:20150424).
CC {ECO:0000269|PubMed:20150424, ECO:0000269|PubMed:21080162,
CC ECO:0000269|PubMed:23053415, ECO:0000269|PubMed:23521226}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=O2 + reduced [NADPH--hemoprotein reductase] + tryptamine =
CC H(+) + H2O + oxidized [NADPH--hemoprotein reductase] + serotonin;
CC Xref=Rhea:RHEA:52320, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:57887, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:350546; Evidence={ECO:0000269|PubMed:20150424,
CC ECO:0000269|PubMed:21080162, ECO:0000269|PubMed:23053415};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52321;
CC Evidence={ECO:0000269|PubMed:20150424, ECO:0000269|PubMed:21080162,
CC ECO:0000269|PubMed:23053415};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000305|PubMed:20150424}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- DEVELOPMENTAL STAGE: Expression increases in the panicle from 7 days
CC before flowering to flowering stage, to become undetectable 7 days
CC after flowering. {ECO:0000269|PubMed:23110463}.
CC -!- INDUCTION: Induced by N-acetylchitooligosaccharide elicitor and
CC infection with a compatible race of the rice blast fungus Magnaporthe
CC oryzae (PubMed:20150424). Induced by salt stress, methyl viologen,
CC acifluorfen and cadmium (PubMed:23053415).
CC {ECO:0000269|PubMed:20150424, ECO:0000269|PubMed:23053415}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAF29561.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; DP000011; ABA97037.1; -; Genomic_DNA.
DR EMBL; AP008218; BAF29561.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP014968; BAT16632.1; -; Genomic_DNA.
DR EMBL; AK071599; BAG92576.1; -; mRNA.
DR RefSeq; XP_015618264.1; XM_015762778.1.
DR AlphaFoldDB; Q2QUC5; -.
DR SMR; Q2QUC5; -.
DR STRING; 4530.OS12T0268000-01; -.
DR PaxDb; Q2QUC5; -.
DR PRIDE; Q2QUC5; -.
DR EnsemblPlants; Os12t0268000-01; Os12t0268000-01; Os12g0268000.
DR GeneID; 4351945; -.
DR Gramene; Os12t0268000-01; Os12t0268000-01; Os12g0268000.
DR KEGG; osa:4351945; -.
DR eggNOG; KOG0156; Eukaryota.
DR HOGENOM; CLU_001570_4_0_1; -.
DR OMA; WPVDIFP; -.
DR OrthoDB; 702827at2759; -.
DR Proteomes; UP000000763; Chromosome 12.
DR Proteomes; UP000059680; Chromosome 12.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IDA:UniProtKB.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0006587; P:serotonin biosynthetic process from tryptophan; IDA:UniProtKB.
DR Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR002401; Cyt_P450_E_grp-I.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; SSF48264; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW Oxidoreductase; Plant defense; Reference proteome; Serotonin biosynthesis;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..523
FT /note="Tryptamine 5-hydroxylase"
FT /id="PRO_0000444625"
FT TRANSMEM 5..25
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 453
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P04798"
FT MUTAGEN 314
FT /note="T->I: Sekiguchi lesion phenotype."
FT /evidence="ECO:0000269|PubMed:20150424"
FT MUTAGEN 455
FT /note="G->D: Sekiguchi lesion phenotype."
FT /evidence="ECO:0000269|PubMed:20150424"
SQ SEQUENCE 523 AA; 57765 MW; A3167C97B25BD145 CRC64;
MELTMASTMS LALLVLSAAY VLVALRRSRS SSSKPRRLPP SPPGWPVIGH LHLMSGMPHH
ALAELARTMR APLFRMRLGS VPAVVISKPD LARAALTTND AALASRPHLL SGQFLSFGCS
DVTFAPAGPY HRMARRVVVS ELLSARRVAT YGAVRVKELR RLLAHLTKNT SPAKPVDLSE
CFLNLANDVL CRVAFGRRFP HGEGDKLGAV LAEAQDLFAG FTIGDFFPEL EPVASTVTGL
RRRLKKCLAD LREACDVIVD EHISGNRQRI PGDRDEDFVD VLLRVQKSPD LEVPLTDDNL
KALVLDMFVA GTDTTFATLE WVMTELVRHP RILKKAQEEV RRVVGDSGRV EESHLGELHY
MRAIIKETFR LHPAVPLLVP RESVAPCTLG GYDIPARTRV FINTFAMGRD PEIWDNPLEY
SPERFESAGG GGEIDLKDPD YKLLPFGGGR RGCPGYTFAL ATVQVSLASL LYHFEWALPA
GVRAEDVNLD ETFGLATRKK EPLFVAVRKS DAYEFKGEEL SEV
