U2AF1_SCHPO
ID U2AF1_SCHPO Reviewed; 216 AA.
AC Q09176;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Splicing factor U2AF 23 kDa subunit;
DE AltName: Full=U2 auxiliary factor 23 kDa subunit;
DE Short=U2AF23;
DE AltName: Full=U2 snRNP auxiliary factor small subunit;
GN ORFNames=SPAP8A3.06;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RC STRAIN=972 / ATCC 24843;
RX PubMed=8657565; DOI=10.1093/nar/24.10.1849;
RA Wentz-Hunter K., Potashkin J.;
RT "The small subunit of the splicing factor U2AF is conserved in fission
RT yeast.";
RL Nucleic Acids Res. 24:1849-1854(1996).
RN [2]
RP SEQUENCE REVISION.
RA Potashkin J.;
RL Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [4]
RP INTERACTION WITH CWF13.
RX PubMed=11414703; DOI=10.1006/bbrc.2001.5108;
RA Ambrozkova M., Puta F., Fukova I., Skruzny M., Brabek J., Folk P.;
RT "The fission yeast ortholog of the coregulator SKIP interacts with the
RT small subunit of U2AF.";
RL Biochem. Biophys. Res. Commun. 284:1148-1154(2001).
RN [5]
RP FUNCTION, AND INTERACTION WITH U2AF59 AND SF1.
RX PubMed=12374752; DOI=10.1093/emboj/cdf555;
RA Huang T., Vilardell J., Query C.C.;
RT "Pre-spliceosome formation in S.pombe requires a stable complex of SF1-
RT U2AF(59)-U2AF(23).";
RL EMBO J. 21:5516-5526(2002).
CC -!- FUNCTION: Necessary for the splicing of pre-mRNA. The SF1-U2AF59-U2AF23
CC complex has a role in the recognition of the branch site (5'-UACUAAC-
CC 3'), the pyrimidine tract and the 3'-splice site at the 3'-end of
CC introns. {ECO:0000269|PubMed:12374752}.
CC -!- SUBUNIT: Forms a heterodimer with the U2AF large subunit. Can also form
CC a homodimer. U2AF large subunit (U2AF59), U2AF small subunit (U2AF23)
CC and SF1 (bpb1) interact to form a complex required for complex A
CC formation. Interacts with cwf13. {ECO:0000269|PubMed:11414703,
CC ECO:0000269|PubMed:12374752}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U48234; AAC49805.1; -; Genomic_DNA.
DR EMBL; CU329670; CAB55173.1; -; Genomic_DNA.
DR PIR; T39243; T39243.
DR RefSeq; NP_594945.1; NM_001020376.2.
DR PDB; 4YH8; X-ray; 1.70 A; A=1-216.
DR PDB; 7C06; X-ray; 3.02 A; A/D/G/J/M/P/S/V/Y=1-216.
DR PDB; 7C07; X-ray; 3.20 A; A/D/G/J/M/P/S/V/Y=1-216.
DR PDB; 7C08; X-ray; 3.35 A; A/D/G/J/M/P/S/V/Y=1-216.
DR PDBsum; 4YH8; -.
DR PDBsum; 7C06; -.
DR PDBsum; 7C07; -.
DR PDBsum; 7C08; -.
DR AlphaFoldDB; Q09176; -.
DR SMR; Q09176; -.
DR BioGRID; 278942; 14.
DR IntAct; Q09176; 1.
DR STRING; 4896.SPAP8A3.06.1; -.
DR iPTMnet; Q09176; -.
DR MaxQB; Q09176; -.
DR PaxDb; Q09176; -.
DR PRIDE; Q09176; -.
DR EnsemblFungi; SPAP8A3.06.1; SPAP8A3.06.1:pep; SPAP8A3.06.
DR GeneID; 2542482; -.
DR KEGG; spo:SPAP8A3.06; -.
DR PomBase; SPAP8A3.06; -.
DR VEuPathDB; FungiDB:SPAP8A3.06; -.
DR eggNOG; KOG2202; Eukaryota.
DR HOGENOM; CLU_059852_1_0_1; -.
DR InParanoid; Q09176; -.
DR OMA; NDGEDRW; -.
DR PhylomeDB; Q09176; -.
DR Reactome; R-SPO-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-SPO-72187; mRNA 3'-end processing.
DR PRO; PR:Q09176; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0000243; C:commitment complex; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005681; C:spliceosomal complex; IBA:GO_Central.
DR GO; GO:0071004; C:U2-type prespliceosome; IDA:PomBase.
DR GO; GO:0089701; C:U2AF complex; IDA:PomBase.
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:0045292; P:mRNA cis splicing, via spliceosome; IMP:PomBase.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
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 3D-structure; Metal-binding; mRNA processing; mRNA splicing; Nucleus;
KW Reference proteome; Repeat; RNA-binding; Zinc; Zinc-finger.
FT CHAIN 1..216
FT /note="Splicing factor U2AF 23 kDa subunit"
FT /id="PRO_0000081998"
FT DOMAIN 44..141
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 143..170
FT /note="C3H1-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT REGION 194..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 15..17
FT /evidence="ECO:0007829|PDB:7C06"
FT HELIX 19..24
FT /evidence="ECO:0007829|PDB:4YH8"
FT HELIX 30..32
FT /evidence="ECO:0007829|PDB:4YH8"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:4YH8"
FT STRAND 44..48
FT /evidence="ECO:0007829|PDB:4YH8"
FT HELIX 55..57
FT /evidence="ECO:0007829|PDB:4YH8"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:7C08"
FT HELIX 61..63
FT /evidence="ECO:0007829|PDB:4YH8"
FT HELIX 66..84
FT /evidence="ECO:0007829|PDB:4YH8"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:4YH8"
FT STRAND 90..96
FT /evidence="ECO:0007829|PDB:4YH8"
FT TURN 101..105
FT /evidence="ECO:0007829|PDB:4YH8"
FT STRAND 107..113
FT /evidence="ECO:0007829|PDB:4YH8"
FT HELIX 114..124
FT /evidence="ECO:0007829|PDB:4YH8"
FT STRAND 128..133
FT /evidence="ECO:0007829|PDB:7C06"
FT STRAND 137..139
FT /evidence="ECO:0007829|PDB:4YH8"
FT HELIX 144..147
FT /evidence="ECO:0007829|PDB:4YH8"
FT HELIX 150..154
FT /evidence="ECO:0007829|PDB:4YH8"
FT HELIX 160..162
FT /evidence="ECO:0007829|PDB:4YH8"
FT STRAND 164..166
FT /evidence="ECO:0007829|PDB:7C06"
FT HELIX 173..191
FT /evidence="ECO:0007829|PDB:4YH8"
SQ SEQUENCE 216 AA; 25030 MW; AAEDD3DE2DF3507D CRC64;
MASHLASIYG TEQDKVNCSF YYKIGACRHG ERCSRKHVKP NFSQTILCPN MYKNPIHEPN
GKKFTQRELA EQFDAFYEDM FCEFSKYGEV EQLVVCDNVG DHLVGNVYVR FKYEESAQNA
IDDLNSRWYS QRPVYAELSP VTDFREACCR QHETSECQRG GLCNFMHAKK PSPQLLRDLV
LAQRKYLALN AAEEMKKEPN SDSTNRWVSV TAERKN
