U2AFB_ARATH
ID U2AFB_ARATH Reviewed; 283 AA.
AC Q9FMY5; Q945S0;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Splicing factor U2af small subunit B;
DE AltName: Full=U2 auxiliary factor 35 kDa subunit B;
DE AltName: Full=U2 small nuclear ribonucleoprotein auxiliary factor small subunit B;
DE Short=U2 snRNP auxiliary factor small subunit B;
DE AltName: Full=Zinc finger CCCH domain-containing protein 60;
DE Short=AtC3H60;
GN Name=U2AF35B; Synonyms=AUSB; OrderedLocusNames=At5g42820;
GN ORFNames=MJB21.20;
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 [MRNA], AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia; TISSUE=Leaf;
RX PubMed=16407443; DOI=10.1104/pp.105.073858;
RA Wang B.-B., Brendel V.;
RT "Molecular characterization and phylogeny of U2AF35 homologs in plants.";
RL Plant Physiol. 140:624-636(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9501997; DOI=10.1093/dnares/4.6.401;
RA Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. III. Sequence
RT features of the regions of 1,191,918 bp covered by seventeen physically
RT assigned P1 clones.";
RL DNA Res. 4:401-414(1997).
RN [3]
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 [4]
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 [5]
RP NOMENCLATURE.
RX PubMed=18221561; DOI=10.1186/1471-2164-9-44;
RA Wang D., Guo Y., Wu C., Yang G., Li Y., Zheng C.;
RT "Genome-wide analysis of CCCH zinc finger family in Arabidopsis and rice.";
RL BMC Genomics 9:44-44(2008).
RN [6]
RP INTERACTION WITH RNU1; SR45 AND U2AF35A, AND SUBCELLULAR LOCATION.
RX PubMed=22563826; DOI=10.1111/j.1365-313x.2012.05042.x;
RA Day I.S., Golovkin M., Palusa S.G., Link A., Ali G.S., Thomas J.,
RA Richardson D.N., Reddy A.S.;
RT "Interactions of SR45, an SR-like protein, with spliceosomal proteins and
RT an intronic sequence: insights into regulated splicing.";
RL Plant J. 71:936-947(2012).
CC -!- FUNCTION: Necessary for the splicing of pre-mRNA (By similarity).
CC Probably active at the 3' splice sites. {ECO:0000250}.
CC -!- SUBUNIT: Component of the spliceosome. Homo- and heterodimer. Interacts
CC with RNU1, U2AF35A and SR45. {ECO:0000269|PubMed:22563826}.
CC -!- INTERACTION:
CC Q9FMY5; O23090: BHLH14; NbExp=3; IntAct=EBI-4448718, EBI-15193049;
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:16407443,
CC ECO:0000269|PubMed:22563826}.
CC -!- SIMILARITY: Belongs to the splicing factor SR family. {ECO:0000305}.
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DR EMBL; AF409140; AAL06332.1; -; mRNA.
DR EMBL; AB007647; BAB10638.1; -; Genomic_DNA.
DR EMBL; AB008264; BAB10638.1; JOINED; Genomic_DNA.
DR EMBL; CP002688; AED94868.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94869.1; -; Genomic_DNA.
DR EMBL; AY136436; AAM97101.1; -; mRNA.
DR EMBL; BT000219; AAN15538.1; -; mRNA.
DR RefSeq; NP_199096.1; NM_123647.3.
DR RefSeq; NP_974870.1; NM_203141.2.
DR AlphaFoldDB; Q9FMY5; -.
DR SMR; Q9FMY5; -.
DR BioGRID; 19543; 14.
DR IntAct; Q9FMY5; 9.
DR STRING; 3702.AT5G42820.2; -.
DR PaxDb; Q9FMY5; -.
DR PRIDE; Q9FMY5; -.
DR ProteomicsDB; 243233; -.
DR EnsemblPlants; AT5G42820.1; AT5G42820.1; AT5G42820.
DR EnsemblPlants; AT5G42820.2; AT5G42820.2; AT5G42820.
DR GeneID; 834293; -.
DR Gramene; AT5G42820.1; AT5G42820.1; AT5G42820.
DR Gramene; AT5G42820.2; AT5G42820.2; AT5G42820.
DR KEGG; ath:AT5G42820; -.
DR Araport; AT5G42820; -.
DR TAIR; locus:2165447; AT5G42820.
DR eggNOG; KOG2202; Eukaryota.
DR HOGENOM; CLU_059852_2_1_1; -.
DR InParanoid; Q9FMY5; -.
DR OMA; HERSGRF; -.
DR OrthoDB; 1340384at2759; -.
DR PhylomeDB; Q9FMY5; -.
DR PRO; PR:Q9FMY5; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FMY5; baseline and differential.
DR Genevisible; Q9FMY5; AT.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0005681; C:spliceosomal complex; IBA:GO_Central.
DR GO; GO:0089701; C:U2AF complex; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030628; F:pre-mRNA 3'-splice site binding; IBA:GO_Central.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0048573; P:photoperiodism, flowering; IMP:TAIR.
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; IPR003954; RRM_dom_euk.
DR InterPro; IPR009145; U2AF_small.
DR InterPro; IPR000571; Znf_CCCH.
DR PANTHER; PTHR12620; PTHR12620; 1.
DR Pfam; PF00076; RRM_1; 1.
DR Pfam; PF00642; zf-CCCH; 2.
DR PRINTS; PR01848; U2AUXFACTOR.
DR SMART; SM00361; RRM_1; 1.
DR SMART; SM00356; ZnF_C3H1; 2.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
DR PROSITE; PS50103; ZF_C3H1; 2.
PE 1: Evidence at protein level;
KW DNA-binding; Metal-binding; mRNA processing; mRNA splicing; Nucleus;
KW Reference proteome; Repeat; RNA-binding; Spliceosome; Zinc; Zinc-finger.
FT CHAIN 1..283
FT /note="Splicing factor U2af small subunit B"
FT /id="PRO_0000371962"
FT DOMAIN 44..146
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT ZN_FING 12..40
FT /note="C3H1-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 148..175
FT /note="C3H1-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT REGION 191..283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..206
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..247
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 256..283
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 102
FT /note="D -> V (in Ref. 1; AAL06332)"
FT /evidence="ECO:0000305"
FT CONFLICT 167
FT /note="Y -> C (in Ref. 1; AAL06332)"
FT /evidence="ECO:0000305"
FT CONFLICT 239
FT /note="H -> Y (in Ref. 1; AAL06332)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 283 AA; 33232 MW; 45407ABBFC1624A5 CRC64;
MAEHLASIFG TEKDRVNCPF YFKIGACRHG DRCSRLHNRP TISPTLLLSN MYQRPDMITP
GVDPQGQPLD PSKIQDHFED FYEDIFEELN KFGEVESLNV CDNLADHMIG NVYVLFKEED
HAAAALQALQ GRFYSGRPII ADFSPVTDFR EATCRQYEEN SCNRGGYCNF MHVKQISREL
RRKLFGRYRR SYRRGSRSRS RSISPRRKRE HSRERERGDV RDRDRHGNGK RSSDRSERHD
RDGGGRRRHG SPKRSRSPRN VREGSEERRA RIEQWNRERD EGV
