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U2AFA_ARATH
ID   U2AFA_ARATH             Reviewed;         296 AA.
AC   Q9S709; Q945S1;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 155.
DE   RecName: Full=Splicing factor U2af small subunit A;
DE   AltName: Full=U2 auxiliary factor 35 kDa subunit A;
DE   AltName: Full=U2 small nuclear ribonucleoprotein auxiliary factor small subunit A;
DE            Short=U2 snRNP auxiliary factor small subunit A;
DE   AltName: Full=Zinc finger CCCH domain-containing protein 8;
DE            Short=AtC3H8;
GN   Name=U2AF35A; Synonyms=AUSA; OrderedLocusNames=At1g27650;
GN   ORFNames=T17H3.14, T22C5.10;
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=Root;
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=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   [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   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   [6]
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   [7]
RP   INTERACTION WITH RNU1; SR45 AND U2AF35B, 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 U2AF35B, RNU1 and SR45. {ECO:0000269|PubMed:22563826}.
CC   -!- INTERACTION:
CC       Q9S709; F4ILE1: At2g16940; NbExp=3; IntAct=EBI-15193047, EBI-25522131;
CC   -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:16407443,
CC       ECO:0000269|PubMed:22563826}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms are produced. According to EST
CC         sequences.;
CC       Name=1;
CC         IsoId=Q9S709-1; Sequence=Displayed;
CC   -!- SIMILARITY: Belongs to the splicing factor SR family. {ECO:0000305}.
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DR   EMBL; AF409139; AAL06331.1; -; mRNA.
DR   EMBL; AC005916; AAD46002.1; -; Genomic_DNA.
DR   EMBL; AC012375; AAF24943.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE30858.1; -; Genomic_DNA.
DR   EMBL; AF344324; AAK06875.1; -; mRNA.
DR   EMBL; AY065202; AAL38678.1; -; mRNA.
DR   EMBL; AY090343; AAL91249.1; -; mRNA.
DR   EMBL; AY096507; AAM20157.1; -; mRNA.
DR   EMBL; AY122894; AAM67427.1; -; mRNA.
DR   EMBL; AY088540; AAM66073.1; -; mRNA.
DR   RefSeq; NP_174086.1; NM_102530.3. [Q9S709-1]
DR   AlphaFoldDB; Q9S709; -.
DR   SMR; Q9S709; -.
DR   BioGRID; 24892; 12.
DR   IntAct; Q9S709; 6.
DR   STRING; 3702.AT1G27650.1; -.
DR   iPTMnet; Q9S709; -.
DR   PaxDb; Q9S709; -.
DR   PRIDE; Q9S709; -.
DR   ProteomicsDB; 234642; -. [Q9S709-1]
DR   EnsemblPlants; AT1G27650.1; AT1G27650.1; AT1G27650. [Q9S709-1]
DR   GeneID; 839657; -.
DR   Gramene; AT1G27650.1; AT1G27650.1; AT1G27650. [Q9S709-1]
DR   KEGG; ath:AT1G27650; -.
DR   Araport; AT1G27650; -.
DR   TAIR; locus:2196929; AT1G27650.
DR   eggNOG; KOG2202; Eukaryota.
DR   HOGENOM; CLU_059852_2_1_1; -.
DR   InParanoid; Q9S709; -.
DR   OMA; NDGEDRW; -.
DR   PhylomeDB; Q9S709; -.
DR   PRO; PR:Q9S709; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9S709; baseline and differential.
DR   Genevisible; Q9S709; 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   Alternative splicing; DNA-binding; Metal-binding; mRNA processing;
KW   mRNA splicing; Nucleus; Reference proteome; Repeat; RNA-binding;
KW   Spliceosome; Zinc; Zinc-finger.
FT   CHAIN           1..296
FT                   /note="Splicing factor U2af small subunit A"
FT                   /id="PRO_0000371961"
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..296
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        205..258
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        269..296
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        163
FT                   /note="N -> Y (in Ref. 1; AAL06331)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        185
FT                   /note="F -> S (in Ref. 1; AAL06331)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   296 AA;  34572 MW;  F284D29BF68445BF CRC64;
     MAEHLASIFG TEKDRVNCPF YFKIGACRHG DRCSRLHNRP TISPTLLLSN MYQRPDMITP
     GVDAQGQPLD PRKIQEHFED FFEDLFEELG KFGEIESLNI CDNLADHMIG NVYVQFKEED
     QAAAALQALQ GRFYSGRPII ADFSPVTDFR EATCRQYEEN NCNRGGYCNF MHVKLVSREL
     RRKLFGRYRR SYRRGSRSRS RSRSISPRNK RDNDRRDPSH REFSHRDRDR EFYRHGSGKR
     SSERSERQER DGSRGRRQAS PKRGGSPGGG REGSEERRAR IEQWNREREE KEEGGA
 
 
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