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RB47C_ARATH
ID   RB47C_ARATH             Reviewed;         432 AA.
AC   Q9SX79; F4HT91;
DT   22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 135.
DE   RecName: Full=Polyadenylate-binding protein RBP47C;
DE            Short=Poly(A)-binding protein RBP47C;
DE   AltName: Full=RNA-binding protein 47C;
DE            Short=AtRBP47C;
GN   Name=RBP47C; OrderedLocusNames=At1g47490; ORFNames=F16N3.24;
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(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] (ISOFORM 1).
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 11-310 (ISOFORM 2).
RC   STRAIN=cv. Columbia;
RX   PubMed=14993207; DOI=10.1101/gr.1515604;
RA   Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA   Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA   Weissenbach J., Salanoubat M.;
RT   "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT   combined approach to evaluate and improve Arabidopsis genome annotation.";
RL   Genome Res. 14:406-413(2004).
RN   [5]
RP   TISSUE SPECIFICITY, GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=11105760; DOI=10.1017/s1355838200001163;
RA   Lorkovic Z.J., Wieczorek Kirk D.A., Klahre U., Hemmings-Mieszczak M.,
RA   Filipowicz W.;
RT   "RBP45 and RBP47, two oligouridylate-specific hnRNP-like proteins
RT   interacting with poly(A)+ RNA in nuclei of plant cells.";
RL   RNA 6:1610-1624(2000).
RN   [6]
RP   GENE FAMILY.
RC   STRAIN=cv. Columbia, and cv. Wassilewskija;
RX   PubMed=21120628; DOI=10.1007/s10059-011-0001-2;
RA   Peal L., Jambunathan N., Mahalingam R.;
RT   "Phylogenetic and expression analysis of RNA-binding proteins with triple
RT   RNA recognition motifs in plants.";
RL   Mol. Cells 31:55-64(2011).
CC   -!- FUNCTION: Heterogeneous nuclear ribonucleoprotein (hnRNP)-protein
CC       binding the poly(A) tail of mRNA and probably involved in some steps of
CC       pre-mRNA maturation. {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with the poly(A) tail of mRNA in nucleus.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasmic granule
CC       {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9SX79-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9SX79-2; Sequence=VSP_042356, VSP_042357;
CC   -!- TISSUE SPECIFICITY: Expressed in leaves, stems, flowers, and seedlings.
CC       {ECO:0000269|PubMed:11105760}.
CC   -!- SIMILARITY: Belongs to the polyadenylate-binding RBP47 family.
CC       {ECO:0000305}.
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DR   EMBL; AC007519; AAD46038.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE32173.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE32174.1; -; Genomic_DNA.
DR   EMBL; AF344325; AAK06876.1; -; mRNA.
DR   EMBL; AY035180; AAK59684.1; -; mRNA.
DR   EMBL; AY062960; AAL33806.1; -; mRNA.
DR   EMBL; BX813781; -; NOT_ANNOTATED_CDS; mRNA.
DR   PIR; B96515; B96515.
DR   RefSeq; NP_175180.1; NM_103642.3. [Q9SX79-1]
DR   RefSeq; NP_973984.1; NM_202255.2. [Q9SX79-2]
DR   AlphaFoldDB; Q9SX79; -.
DR   SMR; Q9SX79; -.
DR   BioGRID; 26382; 1.
DR   STRING; 3702.AT1G47490.1; -.
DR   iPTMnet; Q9SX79; -.
DR   PaxDb; Q9SX79; -.
DR   PRIDE; Q9SX79; -.
DR   ProteomicsDB; 236220; -. [Q9SX79-1]
DR   EnsemblPlants; AT1G47490.1; AT1G47490.1; AT1G47490. [Q9SX79-1]
DR   EnsemblPlants; AT1G47490.2; AT1G47490.2; AT1G47490. [Q9SX79-2]
DR   GeneID; 841157; -.
DR   Gramene; AT1G47490.1; AT1G47490.1; AT1G47490. [Q9SX79-1]
DR   Gramene; AT1G47490.2; AT1G47490.2; AT1G47490. [Q9SX79-2]
DR   KEGG; ath:AT1G47490; -.
DR   Araport; AT1G47490; -.
DR   TAIR; locus:2015403; AT1G47490.
DR   eggNOG; KOG0118; Eukaryota.
DR   HOGENOM; CLU_016304_2_1_1; -.
DR   InParanoid; Q9SX79; -.
DR   OMA; YQNANNG; -.
DR   OrthoDB; 775799at2759; -.
DR   PhylomeDB; Q9SX79; -.
DR   PRO; PR:Q9SX79; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9SX79; baseline and differential.
DR   Genevisible; Q9SX79; AT.
DR   GO; GO:0010494; C:cytoplasmic stress granule; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR   GO; GO:0008143; F:poly(A) binding; ISS:UniProtKB.
DR   GO; GO:0034605; P:cellular response to heat; ISS:UniProtKB.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.70.330; -; 3.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR000504; RRM_dom.
DR   Pfam; PF00076; RRM_1; 3.
DR   SMART; SM00360; RRM; 3.
DR   SUPFAM; SSF54928; SSF54928; 2.
DR   PROSITE; PS50102; RRM; 3.
PE   2: Evidence at transcript level;
KW   Alternative splicing; mRNA processing; Nucleus; Reference proteome; Repeat;
KW   RNA-binding.
FT   CHAIN           1..432
FT                   /note="Polyadenylate-binding protein RBP47C"
FT                   /id="PRO_0000415769"
FT   DOMAIN          101..183
FT                   /note="RRM 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          197..276
FT                   /note="RRM 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          304..376
FT                   /note="RRM 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   REGION          1..55
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          271..293
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..18
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        19..35
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        277..291
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         306..310
FT                   /note="IFVGG -> VIVFP (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14993207"
FT                   /id="VSP_042356"
FT   VAR_SEQ         311..432
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14993207"
FT                   /id="VSP_042357"
SQ   SEQUENCE   432 AA;  48498 MW;  4C33874B16965D38 CRC64;
     MADVKIQSES ESSDSHPVVD NQPPPPPPPP QQPAKEEENQ PKTSPTPPPH WMRYPPTVII
     PHQMMYAPPP FPPYHQYPNH HHLHHQSRGN KHQNAFNGEN KTIWVGDLHH WMDEAYLNSS
     FASGDEREIV SVKVIRNKNN GLSEGYGFVE FESHDVADKV LREFNGTTMP NTDQPFRLNW
     ASFSTGEKRL ENNGPDLSIF VGDLSPDVSD NLLHETFSEK YPSVKAAKVV LDANTGRSKG
     YGFVRFGDEN ERTKAMTEMN GVKCSSRAMR IGPATPRKTN GYQQQGGYMP NGTLTRPEGD
     IMNTTIFVGG LDSSVTDEDL KQPFNEFGEI VSVKIPVGKG CGFVQFVNRP NAEEALEKLN
     GTVIGKQTVR LSWGRNPANK QPRDKYGNQW VDPYYGGQFY NGYGYMVPQP DPRMYPAAPY
     YPMYGGHQQQ VS
 
 
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