SLC1_ORYSJ
ID SLC1_ORYSJ Reviewed; 383 AA.
AC Q6YYX9; A0A0P0XJT4; Q6YZJ5;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Probable 2-oxoglutarate-dependent dioxygenase SLC1 {ECO:0000305};
DE EC=1.14.11.- {ECO:0000255|PROSITE-ProRule:PRU00805};
DE AltName: Full=2-oxoglutarate-dependent dioxygenase 4 {ECO:0000303|PubMed:25728912};
DE AltName: Full=Gibberellin 20 oxidase 7 {ECO:0000303|PubMed:26706069};
DE Short=OsGA20ox7 {ECO:0000303|PubMed:26706069};
DE AltName: Full=Protein SLENDER AND CRINKLY LEAF 1 {ECO:0000303|PubMed:31701152};
GN Name=SLC1 {ECO:0000303|PubMed:31701152};
GN Synonyms=2ODD4 {ECO:0000303|PubMed:25728912},
GN GA20OX7 {ECO:0000303|PubMed:26706069};
GN OrderedLocusNames=Os08g0560000 {ECO:0000312|EMBL:BAF24420.1},
GN LOC_Os08g44590 {ECO:0000305};
GN ORFNames=P0562A06.31 {ECO:0000312|EMBL:BAD13144.1},
GN P0604E01.8 {ECO:0000312|EMBL:BAD13205.1};
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=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 [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [5]
RP NOMENCLATURE.
RX PubMed=25728912; DOI=10.1111/jpi.12220;
RA Byeon Y., Back K.;
RT "Molecular cloning of melatonin 2-hydroxylase responsible for 2-
RT hydroxymelatonin production in rice (Oryza sativa).";
RL J. Pineal Res. 58:343-351(2015).
RN [6]
RP NOMENCLATURE.
RX PubMed=26706069; DOI=10.1016/j.plantsci.2015.10.011;
RA Schmitz A.J., Begcy K., Sarath G., Walia H.;
RT "Rice Ovate Family Protein 2 (OFP2) alters hormonal homeostasis and
RT vasculature development.";
RL Plant Sci. 241:177-188(2015).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=31701152; DOI=10.1093/jxb/erz501;
RA Liu X., Cai W.J., Yin X., Yang D., Dong T., Feng Y.Q., Wu Y.;
RT "Two dioxygenases, SLC1 and SLC2, play essential roles in shoot development
RT of rice.";
RL J. Exp. Bot. 71:1387-1401(2020).
CC -!- FUNCTION: Involved in the regulation of shoot development and salicylic
CC acid (SA) homeostasis. {ECO:0000269|PubMed:31701152}.
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00805};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU00805};
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC Evidence={ECO:0000250|UniProtKB:D4N500};
CC -!- SUBUNIT: Interacts with OSH1. {ECO:0000269|PubMed:31701152}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:31701152}. Nucleus
CC {ECO:0000269|PubMed:31701152}.
CC -!- TISSUE SPECIFICITY: Expressed in coleoptiles, leaf sheaths, leaf blades
CC and root tips of young seedlings (PubMed:31701152). Expressed in
CC vascular bundles of mature leaf blades (PubMed:31701152). Expressed in
CC developing culms and nodes (PubMed:31701152).
CC {ECO:0000269|PubMed:31701152}.
CC -!- MISCELLANEOUS: Plants overexpressing SLC1 are infertile and exhibit
CC defects in shoot development characterized by slender and crinkly
CC leaves. {ECO:0000269|PubMed:31701152}.
CC -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAT06693.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AP005524; BAD13144.1; -; Genomic_DNA.
DR EMBL; AP005544; BAD13205.1; -; Genomic_DNA.
DR EMBL; AP008214; BAF24420.1; -; Genomic_DNA.
DR EMBL; AP014964; BAT06693.1; ALT_INIT; Genomic_DNA.
DR EMBL; AK107117; BAG97956.1; -; mRNA.
DR EMBL; AK107230; BAG98002.1; -; mRNA.
DR RefSeq; XP_015648463.1; XM_015792977.1.
DR AlphaFoldDB; Q6YYX9; -.
DR SMR; Q6YYX9; -.
DR STRING; 4530.OS08T0560000-01; -.
DR EnsemblPlants; Os08t0560000-01; Os08t0560000-01; Os08g0560000.
DR GeneID; 4346321; -.
DR Gramene; Os08t0560000-01; Os08t0560000-01; Os08g0560000.
DR KEGG; osa:4346321; -.
DR eggNOG; KOG0143; Eukaryota.
DR HOGENOM; CLU_010119_16_4_1; -.
DR InParanoid; Q6YYX9; -.
DR OrthoDB; 1005149at2759; -.
DR Proteomes; UP000000763; Chromosome 8.
DR Proteomes; UP000059680; Chromosome 8.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 2.60.120.330; -; 1.
DR InterPro; IPR026992; DIOX_N.
DR InterPro; IPR044861; IPNS-like_FE2OG_OXY.
DR InterPro; IPR027443; IPNS-like_sf.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR Pfam; PF03171; 2OG-FeII_Oxy; 1.
DR Pfam; PF14226; DIOX_N; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Developmental protein; Dioxygenase; Iron; Metal-binding;
KW Nucleus; Oxidoreductase; Reference proteome.
FT CHAIN 1..383
FT /note="Probable 2-oxoglutarate-dependent dioxygenase SLC1"
FT /id="PRO_0000449375"
FT DOMAIN 234..333
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 243
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:D4N500"
FT BINDING 258
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 260
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 314
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 324
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 326
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:D4N500"
SQ SEQUENCE 383 AA; 41832 MW; 6112561421BBC786 CRC64;
MAIVDLVNAG EQQQMGSKRA AAEDGDGGVD DSREYYCRRG VRHLCDSGIT RLPGNYVLPA
SDRPGQAAGA AAAAGGSVKL PVVDLSRLRV PSERGAVLRT LDAACREYGF FQVVNHGVGG
EVVGGMLDVA RRFFELPQPE RERYMSADVR APVRYGTSFN QVRDAVLCWR DFLKLACMPL
AAVVESWPTS PADLREVASR YAEANQRVFM EVMEAALEAL GVGGGGVMED LAAGTQMMTV
NCYPECPQPE LTLGMPPHSD YGFLTLVLQD EVAGLQVMHA GEWLTVDPLP GSFVVNVGDH
LEILSNGRYR SVLHRVKVNS RRLRVSVASF HSVAPERVVS PAPELIDDRH PRRYMDTDLA
TFLAYLASAA GNHKSFLHSR RLY
