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RRC1_ARATH
ID   RRC1_ARATH              Reviewed;         946 AA.
AC   Q9C5J3;
DT   13-APR-2016, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 148.
DE   RecName: Full=Protein RRC1 {ECO:0000303|PubMed:22324426};
DE   AltName: Full=Reduced red-light responses in cry1cry2 background 1 {ECO:0000303|PubMed:22324426};
GN   Name=RRC1 {ECO:0000303|PubMed:22324426};
GN   OrderedLocusNames=At5g25060 {ECO:0000312|Araport:AT5G25060};
GN   ORFNames=T11H3.70 {ECO:0000312|EMBL:AC005964};
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702 {ECO:0000312|EMBL:AAK25922.1};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130714; DOI=10.1038/35048507;
RA   Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA   Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA   Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA   Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA   O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA   Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA   Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA   Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA   Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA   Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA   Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA   Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA   Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA   Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA   Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA   McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA   Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA   Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA   Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA   Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA   Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA   Bevan M., Fransz P.F.;
RT   "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL   Nature 408:823-826(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [4]
RP   FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=22324426; DOI=10.1111/j.1365-313x.2012.04937.x;
RA   Shikata H., Shibata M., Ushijima T., Nakashima M., Kong S.G., Matsuoka K.,
RA   Lin C., Matsushita T.;
RT   "The RS domain of Arabidopsis splicing factor RRC1 is required for
RT   phytochrome B signal transduction.";
RL   Plant J. 70:727-738(2012).
RN   [5]
RP   DOMAIN.
RX   PubMed=22751357; DOI=10.4161/psb.20854;
RA   Shikata H., Nakashima M., Matsuoka K., Matsushita T.;
RT   "Deletion of the RS domain of RRC1 impairs phytochrome B signaling in
RT   Arabidopsis.";
RL   Plant Signal. Behav. 7:933-936(2012).
RN   [6]
RP   STRUCTURE BY NMR OF 789-842.
RA   He F., Muto Y., Inoue M., Kigawa T., Shirouzu M., Terada T., Yokoyama S.;
RT   "Solution structure of the cwf21 domain in protein AAK25922.";
RL   Submitted (DEC-2006) to the PDB data bank.
CC   -!- FUNCTION: SR-like splicing factor required for phytochrome B (phyB)
CC       signal transduction and involved in phyB-dependent alternative
CC       splicing. {ECO:0000269|PubMed:22324426}.
CC   -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:22324426}.
CC   -!- TISSUE SPECIFICITY: Expressed in leaves, inflorescence stems, roots,
CC       flower buds, open flowers and siliques. {ECO:0000269|PubMed:22324426}.
CC   -!- DOMAIN: The RS domain (871-946) is required for phytochrome B signal
CC       transduction through alternative splicing regulation.
CC       {ECO:0000269|PubMed:22751357}.
CC   -!- DISRUPTION PHENOTYPE: Dwarfism and sterile flowers when homozygous and
CC       semi-sterility when heterozygous under normal growth conditions.
CC       Reduced inhibition of hypocotyl elongation under continuous red light.
CC       {ECO:0000269|PubMed:22324426}.
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DR   EMBL; AC005964; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CP002688; AED93395.1; -; Genomic_DNA.
DR   EMBL; AF360212; AAK25922.1; -; mRNA.
DR   EMBL; AY040060; AAK64118.1; -; mRNA.
DR   RefSeq; NP_568464.1; NM_122415.2.
DR   PDB; 2E62; NMR; -; A=789-842.
DR   PDBsum; 2E62; -.
DR   AlphaFoldDB; Q9C5J3; -.
DR   SMR; Q9C5J3; -.
DR   IntAct; Q9C5J3; 2.
DR   STRING; 3702.AT5G25060.1; -.
DR   iPTMnet; Q9C5J3; -.
DR   PaxDb; Q9C5J3; -.
DR   PRIDE; Q9C5J3; -.
DR   ProteomicsDB; 236266; -.
DR   EnsemblPlants; AT5G25060.1; AT5G25060.1; AT5G25060.
DR   GeneID; 832577; -.
DR   Gramene; AT5G25060.1; AT5G25060.1; AT5G25060.
DR   KEGG; ath:AT5G25060; -.
DR   Araport; AT5G25060; -.
DR   TAIR; locus:2179295; AT5G25060.
DR   eggNOG; KOG0151; Eukaryota.
DR   HOGENOM; CLU_010743_2_0_1; -.
DR   InParanoid; Q9C5J3; -.
DR   OMA; VTTNLYI; -.
DR   OrthoDB; 523911at2759; -.
DR   PhylomeDB; Q9C5J3; -.
DR   EvolutionaryTrace; Q9C5J3; -.
DR   PRO; PR:Q9C5J3; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9C5J3; baseline and differential.
DR   GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR   CDD; cd12223; RRM_SR140; 1.
DR   Gene3D; 1.10.10.790; -; 1.
DR   Gene3D; 1.25.40.90; -; 1.
DR   Gene3D; 3.30.70.330; -; 1.
DR   InterPro; IPR006569; CID_dom.
DR   InterPro; IPR008942; ENTH_VHS.
DR   InterPro; IPR013170; mRNA_splic_Cwf21_dom.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR000504; RRM_dom.
DR   InterPro; IPR003034; SAP_dom.
DR   InterPro; IPR035009; SR140_RRM.
DR   InterPro; IPR000061; Surp.
DR   InterPro; IPR035967; SWAP/Surp_sf.
DR   Pfam; PF04818; CID; 1.
DR   Pfam; PF08312; cwf21; 1.
DR   Pfam; PF00076; RRM_1; 1.
DR   Pfam; PF01805; Surp; 1.
DR   SMART; SM01115; cwf21; 1.
DR   SMART; SM00582; RPR; 1.
DR   SMART; SM00360; RRM; 1.
DR   SMART; SM00648; SWAP; 1.
DR   SUPFAM; SSF109905; SSF109905; 1.
DR   SUPFAM; SSF48464; SSF48464; 1.
DR   SUPFAM; SSF54928; SSF54928; 1.
DR   PROSITE; PS51391; CID; 1.
DR   PROSITE; PS50102; RRM; 1.
DR   PROSITE; PS50800; SAP; 1.
DR   PROSITE; PS50128; SURP; 1.
PE   1: Evidence at protein level;
KW   3D-structure; mRNA processing; mRNA splicing; Nucleus; Reference proteome;
KW   RNA-binding.
FT   CHAIN           1..946
FT                   /note="Protein RRC1"
FT                   /id="PRO_0000436038"
FT   DOMAIN          179..260
FT                   /note="RRM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   REPEAT          329..372
FT                   /note="SURP motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00263"
FT   DOMAIN          437..582
FT                   /note="CID"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00724"
FT   DOMAIN          631..665
FT                   /note="SAP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00186"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          41..183
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          740..797
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          836..946
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        11..29
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        41..55
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        64..79
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        98..168
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        740..758
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        774..797
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        851..946
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   HELIX           792..816
FT                   /evidence="ECO:0007829|PDB:2E62"
FT   HELIX           821..838
FT                   /evidence="ECO:0007829|PDB:2E62"
SQ   SEQUENCE   946 AA;  108286 MW;  B531054388ABEB8B CRC64;
     MSSFSITRKK TPFQKHREEE EARKKKAEDE TARLYQEFVE SFQGDNATTK TFVRGGTINP
     GDKPKVDSEG EKSKDGGSVS KKGSRYVPSF LPPPLASKGK EPEKKREEER PREREKGKTR
     NIDNFMEELK REQEMRERRN QDRDRQGDSS PSSRFDELPD DFDPSGRPGS FDDGDPQTTN
     LYVGNLSPKV DENFLLRTFG RFGPIASVKI MWPRTDEEKR RQRNCGFVSF MNRADGQAAK
     DEMQGIIVYE YELKIGWGKA VSLPSQALPA PPPGHMAIRS KEGCNLVFSG QTGPPIITSV
     PNQNSELVLT PNVPDITVVT PEDEHLRHVI DTLALYVLDG ECAFEQAIME RGRGNPLFKF
     MFELGSKEHT YYVWRLYSFA QGDTLQRWRT EPYIMITGSG RWIPPPLPVT RTQEHEKESA
     STYAAGRTRR AEVERTLTDP QRDEFEDMLR ALTLERSQIK EAMGFALDNA DAAGEVVEVL
     TESLTLKETS IPTKVARLML VSDILHNSSA RVKNASAYRT KFEATLPDIM ESFNDLYRSI
     TGRITAEALK ERVLKVLQVW ADWFLFSDAY IYGLRSTFLR SGVSGVTSFH SICGDAPEIE
     NKSYADNMSD IGKINPDAAL AIGKGAARQE LMNLPIAELE RRCRHNGLSL VGGRVMMVTR
     LLSLEDTEKQ RGYEAVDEIP KHPQNHSTWE EVKSEREHIK NSYAEVEMKE PVNLPTTIPI
     PQPELKAFVG KEKNELILPA SKWARDDDEA DDEQKRSSSS GSDNTGGITF KADGEDLKGN
     DCVRAQPDNG MDEEQRQKRR RIEVALIEYR ETLEEQGMKN PEEIERKVEI NRKRLEVDYG
     LSGPNEGNRN QKSIIERKEK REDSQESSKK RHRGENKSQS PPRKSSTRER DHDLGRDRDR
     ERHRDRDRQH DLNRDRDRRE KSSSHDRDDN DRSKERDRDW RRRGTR
 
 
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