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SCL7_ORYSJ
ID   SCL7_ORYSJ              Reviewed;         578 AA.
AC   Q53K16;
DT   20-DEC-2017, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=SCARECROW-LIKE protein 7 {ECO:0000303|PubMed:27081181};
DE   AltName: Full=Os-SCL7 {ECO:0000303|PubMed:27081181};
GN   Name=SCL7 {ECO:0000303|PubMed:27081181};
GN   OrderedLocusNames=LOC_Os03g51330 {ECO:0000312|EMBL:ABF98609.1},
GN   Os03g0723000 {ECO:0000312|EMBL:BAF13029.1, ECO:0000312|EMBL:BAS86141.1};
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 {ECO:0000312|EMBL:AAX95685.1};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16109971; DOI=10.1101/gr.3869505;
RG   The rice chromosome 3 sequencing consortium;
RA   Buell C.R., Yuan Q., Ouyang S., Liu J., Zhu W., Wang A., Maiti R., Haas B.,
RA   Wortman J., Pertea M., Jones K.M., Kim M., Overton L., Tsitrin T.,
RA   Fadrosh D., Bera J., Weaver B., Jin S., Johri S., Reardon M., Webb K.,
RA   Hill J., Moffat K., Tallon L., Van Aken S., Lewis M., Utterback T.,
RA   Feldblyum T., Zismann V., Iobst S., Hsiao J., de Vazeille A.R.,
RA   Salzberg S.L., White O., Fraser C.M., Yu Y., Kim H., Rambo T., Currie J.,
RA   Collura K., Kernodle-Thompson S., Wei F., Kudrna K., Ammiraju J.S.S.,
RA   Luo M., Goicoechea J.L., Wing R.A., Henry D., Oates R., Palmer M.,
RA   Pries G., Saski C., Simmons J., Soderlund C., Nelson W., de la Bastide M.,
RA   Spiegel L., Nascimento L., Huang E., Preston R., Zutavern T., Palmer L.,
RA   O'Shaughnessy A., Dike S., McCombie W.R., Minx P., Cordum H., Wilson R.,
RA   Jin W., Lee H.R., Jiang J., Jackson S.;
RT   "Sequence, annotation, and analysis of synteny between rice chromosome 3
RT   and diverged grass species.";
RL   Genome Res. 15:1284-1291(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   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   [6] {ECO:0007744|PDB:5HYZ}
RP   X-RAY CRYSTALLOGRAPHY (1.82 ANGSTROMS) OF 204-578, FUNCTION, DNA-BINDING,
RP   SUBUNIT, DOMAIN, AND MUTAGENESIS OF LYS-284; ARG-478; ARG-485; LYS-549 AND
RP   LYS-551.
RX   PubMed=27081181; DOI=10.1105/tpc.16.00018;
RA   Li S., Zhao Y., Zhao Z., Wu X., Sun L., Liu Q., Wu Y.;
RT   "Crystal structure of the GRAS domain of SCARECROW-LIKE7 in Oryza sativa.";
RL   Plant Cell 28:1025-1034(2016).
CC   -!- FUNCTION: Probable transcription factor involved in plant development
CC       (By similarity). Involved in environmental abiotic stress resistance.
CC       May increase the expression of stress-responsive genes (By similarity).
CC       Binds DNA in vitro (PubMed:27081181).
CC       {ECO:0000250|UniProtKB:A0A024B7I0, ECO:0000250|UniProtKB:Q9SCR0,
CC       ECO:0000269|PubMed:27081181}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:27081181}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:A0A024B7I0}.
CC   -!- DOMAIN: The GRAS domain is involved in DNA-binding.
CC       {ECO:0000269|PubMed:27081181}.
CC   -!- SIMILARITY: Belongs to the GRAS family. {ECO:0000255|PROSITE-
CC       ProRule:PRU01191, ECO:0000303|PubMed:27081181}.
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DR   EMBL; AC146936; AAX95685.1; -; Genomic_DNA.
DR   EMBL; DP000009; ABF98609.1; -; Genomic_DNA.
DR   EMBL; AP008209; BAF13029.1; -; Genomic_DNA.
DR   EMBL; AP014959; BAS86141.1; -; Genomic_DNA.
DR   EMBL; AK064022; BAG88969.1; -; mRNA.
DR   EMBL; AK101603; BAG95146.1; -; mRNA.
DR   EMBL; AK102857; BAG95752.1; -; mRNA.
DR   RefSeq; XP_015628849.1; XM_015773363.1.
DR   PDB; 5HYZ; X-ray; 1.82 A; A=204-578.
DR   PDBsum; 5HYZ; -.
DR   AlphaFoldDB; Q53K16; -.
DR   SMR; Q53K16; -.
DR   STRING; 4530.OS03T0723000-01; -.
DR   PaxDb; Q53K16; -.
DR   PRIDE; Q53K16; -.
DR   EnsemblPlants; Os03t0723000-01; Os03t0723000-01; Os03g0723000.
DR   EnsemblPlants; Os03t0723000-02; Os03t0723000-02; Os03g0723000.
DR   GeneID; 4333948; -.
DR   Gramene; Os03t0723000-01; Os03t0723000-01; Os03g0723000.
DR   Gramene; Os03t0723000-02; Os03t0723000-02; Os03g0723000.
DR   KEGG; osa:4333948; -.
DR   eggNOG; ENOG502QTXA; Eukaryota.
DR   HOGENOM; CLU_011924_0_5_1; -.
DR   InParanoid; Q53K16; -.
DR   OMA; FSACPNR; -.
DR   OrthoDB; 690313at2759; -.
DR   Proteomes; UP000000763; Chromosome 3.
DR   Proteomes; UP000059680; Chromosome 3.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR   InterPro; IPR005202; TF_GRAS.
DR   PANTHER; PTHR31636; PTHR31636; 1.
DR   Pfam; PF03514; GRAS; 1.
DR   PROSITE; PS50985; GRAS; 1.
PE   1: Evidence at protein level;
KW   3D-structure; DNA-binding; Nucleus; Reference proteome; Stress response;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..578
FT                   /note="SCARECROW-LIKE protein 7"
FT                   /id="PRO_0000442600"
FT   DOMAIN          198..578
FT                   /note="GRAS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT   REGION          18..84
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          146..173
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          205..264
FT                   /note="Leucine repeat I (LRI)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT   REGION          283..349
FT                   /note="VHIID"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT   REGION          365..397
FT                   /note="Leucine repeat II (LRII)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT   REGION          406..497
FT                   /note="PFYRE"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT   REGION          500..578
FT                   /note="SAW"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT   MOTIF           314..318
FT                   /note="VHIID"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT   MOTIF           414..418
FT                   /note="LXXLL motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT   MUTAGEN         284
FT                   /note="K->A: Does not affect DNA-binding."
FT                   /evidence="ECO:0000269|PubMed:27081181"
FT   MUTAGEN         284
FT                   /note="K->E: Loss of DNA-binding."
FT                   /evidence="ECO:0000269|PubMed:27081181"
FT   MUTAGEN         478
FT                   /note="R->A: Loss of DNA-binding."
FT                   /evidence="ECO:0000269|PubMed:27081181"
FT   MUTAGEN         485
FT                   /note="R->A: Loss of DNA-binding."
FT                   /evidence="ECO:0000269|PubMed:27081181"
FT   MUTAGEN         549
FT                   /note="K->A,E: Loss of DNA-binding."
FT                   /evidence="ECO:0000269|PubMed:27081181"
FT   MUTAGEN         551
FT                   /note="K->A: Loss of DNA-binding."
FT                   /evidence="ECO:0000269|PubMed:27081181"
FT   HELIX           206..219
FT                   /evidence="ECO:0007829|PDB:5HYZ"
FT   STRAND          220..222
FT                   /evidence="ECO:0007829|PDB:5HYZ"
FT   HELIX           226..235
FT                   /evidence="ECO:0007829|PDB:5HYZ"
FT   HELIX           242..260
FT                   /evidence="ECO:0007829|PDB:5HYZ"
FT   HELIX           277..289
FT                   /evidence="ECO:0007829|PDB:5HYZ"
FT   HELIX           292..307
FT                   /evidence="ECO:0007829|PDB:5HYZ"
FT   TURN            308..310
FT                   /evidence="ECO:0007829|PDB:5HYZ"
FT   STRAND          312..321
FT                   /evidence="ECO:0007829|PDB:5HYZ"
FT   HELIX           325..335
FT                   /evidence="ECO:0007829|PDB:5HYZ"
FT   STRAND          343..351
FT                   /evidence="ECO:0007829|PDB:5HYZ"
FT   HELIX           353..355
FT                   /evidence="ECO:0007829|PDB:5HYZ"
FT   HELIX           360..376
FT                   /evidence="ECO:0007829|PDB:5HYZ"
FT   STRAND          380..385
FT                   /evidence="ECO:0007829|PDB:5HYZ"
FT   HELIX           390..392
FT                   /evidence="ECO:0007829|PDB:5HYZ"
FT   HELIX           395..398
FT                   /evidence="ECO:0007829|PDB:5HYZ"
FT   STRAND          404..412
FT                   /evidence="ECO:0007829|PDB:5HYZ"
FT   HELIX           414..417
FT                   /evidence="ECO:0007829|PDB:5HYZ"
FT   STRAND          420..422
FT                   /evidence="ECO:0007829|PDB:5HYZ"
FT   HELIX           423..434
FT                   /evidence="ECO:0007829|PDB:5HYZ"
FT   STRAND          438..445
FT                   /evidence="ECO:0007829|PDB:5HYZ"
FT   STRAND          449..452
FT                   /evidence="ECO:0007829|PDB:5HYZ"
FT   HELIX           454..475
FT                   /evidence="ECO:0007829|PDB:5HYZ"
FT   HELIX           481..489
FT                   /evidence="ECO:0007829|PDB:5HYZ"
FT   HELIX           491..499
FT                   /evidence="ECO:0007829|PDB:5HYZ"
FT   HELIX           504..506
FT                   /evidence="ECO:0007829|PDB:5HYZ"
FT   HELIX           514..523
FT                   /evidence="ECO:0007829|PDB:5HYZ"
FT   STRAND          527..529
FT                   /evidence="ECO:0007829|PDB:5HYZ"
FT   HELIX           535..542
FT                   /evidence="ECO:0007829|PDB:5HYZ"
FT   TURN            543..545
FT                   /evidence="ECO:0007829|PDB:5HYZ"
FT   STRAND          552..557
FT                   /evidence="ECO:0007829|PDB:5HYZ"
FT   TURN            558..560
FT                   /evidence="ECO:0007829|PDB:5HYZ"
FT   STRAND          561..566
FT                   /evidence="ECO:0007829|PDB:5HYZ"
FT   STRAND          569..578
FT                   /evidence="ECO:0007829|PDB:5HYZ"
SQ   SEQUENCE   578 AA;  62478 MW;  DA75DDB01B373A68 CRC64;
     MAYMCADSGN LMAIAQQVIQ QQQQQQQQQQ RHHHHHHLPP PPPPQSMAPH HHQQKHHHHH
     QQMPAMPQAP PSSHGQIPGQ LAYGGGAAWP AGEHFFADAF GASAGDAVFS DLAAAADFDS
     DGWMESLIGD APFQDSDLER LIFTTPPPPV PSPPPTHAAA TATATAATAA PRPEAAPALL
     PQPAAATPVA CSSPSPSSAD ASCSAPILQS LLSCSRAAAT DPGLAAAELA SVRAAATDAG
     DPSERLAFYF ADALSRRLAC GTGAPPSAEP DARFASDELT LCYKTLNDAC PYSKFAHLTA
     NQAILEATGA ATKIHIVDFG IVQGIQWAAL LQALATRPEG KPTRIRITGV PSPLLGPQPA
     ASLAATNTRL RDFAKLLGVD FEFVPLLRPV HELNKSDFLV EPDEAVAVNF MLQLYHLLGD
     SDELVRRVLR LAKSLSPAVV TLGEYEVSLN RAGFVDRFAN ALSYYRSLFE SLDVAMTRDS
     PERVRVERWM FGERIQRAVG PEEGADRTER MAGSSEWQTL MEWCGFEPVP LSNYARSQAD
     LLLWNYDSKY KYSLVELPPA FLSLAWEKRP LLTVSAWR
 
 
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