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R47CP_ARATH
ID   R47CP_ARATH             Reviewed;         434 AA.
AC   Q9SX80;
DT   22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 136.
DE   RecName: Full=Polyadenylate-binding protein RBP47C';
DE            Short=Poly(A)-binding protein RBP47C';
DE   AltName: Full=RNA-binding protein 47C';
DE            Short=AtRBP47C prime;
DE            Short=AtRBP47C';
GN   Name=RBP47C'; OrderedLocusNames=At1g47500; ORFNames=F16N3.23;
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].
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Bautista V.R., Kim C.J., Chen H., Wu S.Y., De Los Reyes C., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   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   -!- SIMILARITY: Belongs to the polyadenylate-binding RBP47 family.
CC       {ECO:0000305}.
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DR   EMBL; AC007519; AAD46037.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE32178.1; -; Genomic_DNA.
DR   EMBL; AK227406; BAE99410.1; -; mRNA.
DR   EMBL; BT030029; ABN04767.1; -; mRNA.
DR   PIR; C96515; C96515.
DR   RefSeq; NP_175181.1; NM_103643.3.
DR   AlphaFoldDB; Q9SX80; -.
DR   SMR; Q9SX80; -.
DR   STRING; 3702.AT1G47500.1; -.
DR   iPTMnet; Q9SX80; -.
DR   PaxDb; Q9SX80; -.
DR   PRIDE; Q9SX80; -.
DR   ProteomicsDB; 224873; -.
DR   EnsemblPlants; AT1G47500.1; AT1G47500.1; AT1G47500.
DR   GeneID; 841159; -.
DR   Gramene; AT1G47500.1; AT1G47500.1; AT1G47500.
DR   KEGG; ath:AT1G47500; -.
DR   Araport; AT1G47500; -.
DR   TAIR; locus:2015398; AT1G47500.
DR   eggNOG; KOG0118; Eukaryota.
DR   HOGENOM; CLU_016304_2_1_1; -.
DR   OMA; RADYSNQ; -.
DR   OrthoDB; 775799at2759; -.
DR   PhylomeDB; Q9SX80; -.
DR   PRO; PR:Q9SX80; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9SX80; baseline and differential.
DR   Genevisible; Q9SX80; 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   mRNA processing; Nucleus; Reference proteome; Repeat; RNA-binding.
FT   CHAIN           1..434
FT                   /note="Polyadenylate-binding protein RBP47C'"
FT                   /id="PRO_0000415770"
FT   DOMAIN          103..185
FT                   /note="RRM 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          199..278
FT                   /note="RRM 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          306..378
FT                   /note="RRM 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   REGION          1..50
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..19
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        22..50
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   434 AA;  48632 MW;  B0D7D84DF69D31BD CRC64;
     MADVKVQSES ESSDSHPLVD YQSLPPYPPP HPPVEVEENQ PKTSPTPPPP HWMRYPPVLM
     PQMMYAPPPP MPFSPYHQYP NHHHFHHQSR GNKHQNAFNG ENKTIWVGDL QNWMDEAYLN
     SAFTSAEERE IVSLKVIRNK HNGSSEGYGF VEFESHDVAD KVLQEFNGAP MPNTDQPFRL
     NWASFSTGEK RLENNGPDLS IFVGDLAPDV SDALLHETFS EKYPSVKAAK VVLDANTGRS
     KGYGFVRFGD ENERTKAMTE MNGVKCSSRA MRIGPATPRK TNGYQQQGGY MPSGAFTRSE
     GDTINTTIFV GGLDSSVTDE DLKQPFSEFG EIVSVKIPVG KGCGFVQFVN RPNAEEALEK
     LNGTVIGKQT VRLSWGRNPA NKQPRDKYGN QWVDPYYGGQ FYNGYGYMVP QPDPRMYPAA
     PYYPMYGGHQ QQVS
 
 
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