UBP1C_ARATH
ID UBP1C_ARATH Reviewed; 427 AA.
AC Q9LJH8; Q8LAP3;
DT 19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 142.
DE RecName: Full=Oligouridylate-binding protein 1C;
DE Short=AtUBP1c;
DE AltName: Full=Polyuridylate-binding protein UBP1C;
DE Short=Poly(U)-binding protein UBP1C;
GN Name=UBP1C; OrderedLocusNames=At3g14100; ORFNames=MAG2.6;
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=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP INTERACTION WITH UBA1A AND UBA2A.
RX PubMed=12024044; DOI=10.1128/mcb.22.12.4346-4357.2002;
RA Lambermon M.H., Fu Y., Wieczorek Kirk D.A., Dupasquier M., Filipowicz W.,
RA Lorkovic Z.J.;
RT "UBA1 and UBA2, two proteins that interact with UBP1, a multifunctional
RT effector of pre-mRNA maturation in plants.";
RL Mol. Cell. Biol. 22:4346-4357(2002).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
CC -!- FUNCTION: Heterogeneous nuclear ribonucleoprotein (hnRNP)-like protein
CC that acts as a component of the pre-mRNA processing machinery.
CC Functions at multiple steps to facilitate the nuclear maturation of
CC plant pre-mRNAs (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with UBA1A and UBA2A. {ECO:0000269|PubMed:12024044}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
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DR EMBL; AP000600; BAB02974.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75468.1; -; Genomic_DNA.
DR EMBL; AY139775; AAM98093.1; -; mRNA.
DR EMBL; BT004540; AAO42786.1; -; mRNA.
DR EMBL; AY087692; AAM65229.1; -; mRNA.
DR RefSeq; NP_188026.1; NM_112266.4.
DR AlphaFoldDB; Q9LJH8; -.
DR SMR; Q9LJH8; -.
DR BioGRID; 5960; 1.
DR IntAct; Q9LJH8; 5.
DR STRING; 3702.AT3G14100.1; -.
DR iPTMnet; Q9LJH8; -.
DR PaxDb; Q9LJH8; -.
DR PRIDE; Q9LJH8; -.
DR ProteomicsDB; 233063; -.
DR EnsemblPlants; AT3G14100.1; AT3G14100.1; AT3G14100.
DR GeneID; 820626; -.
DR Gramene; AT3G14100.1; AT3G14100.1; AT3G14100.
DR KEGG; ath:AT3G14100; -.
DR Araport; AT3G14100; -.
DR TAIR; locus:2087457; AT3G14100.
DR eggNOG; KOG0118; Eukaryota.
DR HOGENOM; CLU_025000_0_0_1; -.
DR InParanoid; Q9LJH8; -.
DR OMA; PYLFNRQ; -.
DR OrthoDB; 1066369at2759; -.
DR PhylomeDB; Q9LJH8; -.
DR PRO; PR:Q9LJH8; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LJH8; baseline and differential.
DR Genevisible; Q9LJH8; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0071456; P:cellular response to hypoxia; IDA:TAIR.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0034063; P:stress granule assembly; IDA:TAIR.
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 1: Evidence at protein level;
KW mRNA processing; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW RNA-binding.
FT CHAIN 1..427
FT /note="Oligouridylate-binding protein 1C"
FT /id="PRO_0000425436"
FT DOMAIN 59..133
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 144..222
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 265..340
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 223..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..248
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 246
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LQI9"
FT CONFLICT 388
FT /note="Q -> P (in Ref. 4; AAM65229)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 427 AA; 47089 MW; AB89347B02B7C34D CRC64;
MQNPRLKQHQ QQQQQQAMMQ QQALMQQHSL YHPGVLAPPQ LEPVPSGNLP PGFDPSTCRS
VYVGNIHTQV TEPLLQEIFT STGPVESSKL IRKDKSSYGF VHYFDRRSAA LAILSLNGRH
LFGQPIKVNW AYATGQREDT SSHFNIFVGD LSPEVTDATL YQSFSVFSSC SDARVMWDQK
TGRSRGFGFV SFRNQQDAQT AINEMNGKWL SSRQIRCNWA TKGATSGDDK LSSDGKSVVE
LTTGSSEDGK ETLNEETPEN NSQFTTVYVG NLAPEVTQLD LHRYFHALGA GVIEEVRVQR
DKGFGFVRYN THPEAALAIQ MGNTQPYLFN RQIKCSWGNK PTPPGTASNP LPPPAPAPVP
GLSAADLLNY ERQLALSKMA SVNALMHQQG QHPLRQAHGI NAAGATAAMY DGGFQNVAAA
QQLMYYQ
