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U1131_ARATH
ID   U1131_ARATH             Reviewed;         261 AA.
AC   Q9CAE4; Q0WQK5;
DT   09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 144.
DE   RecName: Full=U11/U12 small nuclear ribonucleoprotein 31 kDa protein;
DE            Short=U11/U12 snRNP 31 kDa protein;
DE            Short=U11/U12-31K;
GN   Name=SNRNP31; OrderedLocusNames=At3g10400; ORFNames=F13M14.33;
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=11130713; DOI=10.1038/35048706;
RA   Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA   Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA   Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA   Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA   Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA   Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA   Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA   Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA   Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA   Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA   Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA   de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA   Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA   Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA   Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA   Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA   Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA   Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA   Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA   Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA   Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA   Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL   Nature 408:820-822(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].
RA   Shinn P., Chen H., Cheuk R., Kim C.J., Ecker J.R.;
RT   "Arabidopsis cDNA clones.";
RL   Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Kim C.J., Chen H., Cheuk R., Shinn P., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
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   [6]
RP   IDENTIFICATION.
RX   PubMed=15987817; DOI=10.1261/rna.2440305;
RA   Lorkovic Z.J., Lehner R., Forstner C., Barta A.;
RT   "Evolutionary conservation of minor U12-type spliceosome between plants and
RT   humans.";
RL   RNA 11:1095-1107(2005).
RN   [7]
RP   FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=21148817; DOI=10.1105/tpc.110.079103;
RA   Kim W.Y., Jung H.J., Kwak K.J., Kim M.K., Oh S.H., Han Y.S., Kang H.;
RT   "The Arabidopsis U12-type spliceosomal protein U11/U12-31K is involved in
RT   U12 intron splicing via RNA chaperone activity and affects plant
RT   development.";
RL   Plant Cell 22:3951-3962(2010).
RN   [8]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=22912901; DOI=10.1371/journal.pone.0043707;
RA   Kwak K.J., Jung H.J., Lee K.H., Kim Y.S., Kim W.Y., Ahn S.J., Kang H.;
RT   "The minor spliceosomal protein U11/U12-31K is an RNA chaperone crucial for
RT   U12 intron splicing and the development of dicot and monocot plants.";
RL   PLoS ONE 7:E43707-E43707(2012).
CC   -!- FUNCTION: RNA chaperone required for proper U12 intron splicing and for
CC       normal growth and development of plants. Mainly responsible for
CC       meristem activity. Plays a role in regulating cell division.
CC       {ECO:0000269|PubMed:21148817, ECO:0000269|PubMed:22912901}.
CC   -!- SUBUNIT: Component of the U11/U12 snRNPs that are part of the U12-type
CC       spliceosome.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21148817}.
CC   -!- TISSUE SPECIFICITY: Ubiquitous. Abundantly expressed in the shoot
CC       apical neristem. {ECO:0000269|PubMed:21148817,
CC       ECO:0000269|PubMed:22912901}.
CC   -!- DISRUPTION PHENOTYPE: Embryo lethal when homozygous, and defective for
CC       seed maturation when heterozygous. {ECO:0000269|PubMed:21148817}.
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DR   EMBL; AC011560; AAG51392.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE74900.1; -; Genomic_DNA.
DR   EMBL; BT015938; AAV31168.1; -; mRNA.
DR   EMBL; BT021922; AAX49371.1; -; mRNA.
DR   EMBL; AK228689; BAF00594.1; -; mRNA.
DR   RefSeq; NP_187651.1; NM_111875.3.
DR   AlphaFoldDB; Q9CAE4; -.
DR   SMR; Q9CAE4; -.
DR   STRING; 3702.AT3G10400.1; -.
DR   iPTMnet; Q9CAE4; -.
DR   PaxDb; Q9CAE4; -.
DR   PRIDE; Q9CAE4; -.
DR   ProteomicsDB; 228535; -.
DR   EnsemblPlants; AT3G10400.1; AT3G10400.1; AT3G10400.
DR   GeneID; 820203; -.
DR   Gramene; AT3G10400.1; AT3G10400.1; AT3G10400.
DR   KEGG; ath:AT3G10400; -.
DR   Araport; AT3G10400; -.
DR   TAIR; locus:2075860; AT3G10400.
DR   eggNOG; KOG0118; Eukaryota.
DR   HOGENOM; CLU_059455_0_0_1; -.
DR   InParanoid; Q9CAE4; -.
DR   OMA; RFEDDNW; -.
DR   OrthoDB; 1422822at2759; -.
DR   PhylomeDB; Q9CAE4; -.
DR   PRO; PR:Q9CAE4; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9CAE4; differential.
DR   Genevisible; Q9CAE4; AT.
DR   GO; GO:0005634; C:nucleus; IDA:TAIR.
DR   GO; GO:0005689; C:U12-type spliceosomal complex; IBA:GO_Central.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0032502; P:developmental process; IMP:TAIR.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; IMP:TAIR.
DR   GO; GO:0051302; P:regulation of cell division; IMP:TAIR.
DR   CDD; cd12393; RRM_ZCRB1; 1.
DR   Gene3D; 3.30.70.330; -; 1.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR000504; RRM_dom.
DR   InterPro; IPR044598; ZCRB1.
DR   InterPro; IPR034219; ZCRB1_RRM.
DR   InterPro; IPR001878; Znf_CCHC.
DR   InterPro; IPR036875; Znf_CCHC_sf.
DR   PANTHER; PTHR46259; PTHR46259; 1.
DR   Pfam; PF00076; RRM_1; 1.
DR   Pfam; PF00098; zf-CCHC; 1.
DR   SMART; SM00360; RRM; 1.
DR   SMART; SM00343; ZnF_C2HC; 1.
DR   SUPFAM; SSF54928; SSF54928; 1.
DR   SUPFAM; SSF57756; SSF57756; 1.
DR   PROSITE; PS50102; RRM; 1.
DR   PROSITE; PS50158; ZF_CCHC; 1.
PE   2: Evidence at transcript level;
KW   Metal-binding; mRNA processing; mRNA splicing; Nucleus; Reference proteome;
KW   Ribonucleoprotein; RNA-binding; Spliceosome; Zinc; Zinc-finger.
FT   CHAIN           1..261
FT                   /note="U11/U12 small nuclear ribonucleoprotein 31 kDa
FT                   protein"
FT                   /id="PRO_0000429832"
FT   DOMAIN          57..135
FT                   /note="RRM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   ZN_FING         153..169
FT                   /note="CCHC-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT   REGION          18..51
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          165..261
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        176..195
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        225..255
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        107
FT                   /note="S -> P (in Ref. 5; BAF00594)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        138
FT                   /note="R -> L (in Ref. 5; BAF00594)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   261 AA;  29367 MW;  4A37767C92819D22 CRC64;
     MKKRKIHHSD DEEDDTFYYR YSSVAAPPPS NPKHQPSSSA KSSAPGGGSG GLAPSKSTLY
     VSNLDFSLTN SDIHTLFSTF GKVARVTVLK DRHTRQSRGV AFVLYVSRED AAKAARSMDA
     KILNGRKLTV SIAADNGRAS EFIKKRVYKD KSRCYECGDE GHLSYECPKN QLGPRERPPP
     PKKRGRRKEE EGEAEEISWS AAAPSLAVAE EEFEEENWAS VVDNEAGERL RKREAEEEEE
     RRMKRKEKKV SYFSDESDDE D
 
 
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