UAP2_SCHPO
ID UAP2_SCHPO Reviewed; 367 AA.
AC O43120;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Splicing factor U2AF-associated protein 2;
DE AltName: Full=Cold sensitive U2 snRNA suppressor 2 homolog;
GN Name=uap2; ORFNames=SPBC1289.02c;
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], FUNCTION, AND SUBUNIT.
RC STRAIN=972 / ATCC 24843;
RX PubMed=9371883; DOI=10.1007/s002940050284;
RA McKinny R., Wentz-Hunter K., Schmidt H., Potashkin J.;
RT "Molecular characterization of a novel fission yeast gene spUAP2 that
RT interacts with the splicing factor spU2AF59.";
RL Curr. Genet. 32:323-330(1997).
RN [2]
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).
CC -!- FUNCTION: Has a role in pre-mRNA splicing.
CC {ECO:0000269|PubMed:9371883}.
CC -!- SUBUNIT: Interacts with the U2AF large and U2AF small subunits.
CC {ECO:0000269|PubMed:9371883}.
CC -!- SIMILARITY: Belongs to the HTATSF1 family. {ECO:0000305}.
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DR EMBL; U97681; AAC04326.1; -; Genomic_DNA.
DR EMBL; CU329671; CAB38682.1; -; Genomic_DNA.
DR PIR; T39353; T39353.
DR RefSeq; NP_596826.1; NM_001023847.2.
DR AlphaFoldDB; O43120; -.
DR BioGRID; 276333; 62.
DR IntAct; O43120; 1.
DR STRING; 4896.SPBC1289.02c.1; -.
DR iPTMnet; O43120; -.
DR MaxQB; O43120; -.
DR PaxDb; O43120; -.
DR PRIDE; O43120; -.
DR EnsemblFungi; SPBC1289.02c.1; SPBC1289.02c.1:pep; SPBC1289.02c.
DR GeneID; 2539783; -.
DR KEGG; spo:SPBC1289.02c; -.
DR PomBase; SPBC1289.02c; uap2.
DR VEuPathDB; FungiDB:SPBC1289.02c; -.
DR eggNOG; KOG1548; Eukaryota.
DR HOGENOM; CLU_026945_0_2_1; -.
DR InParanoid; O43120; -.
DR OMA; DTDFRFG; -.
DR PhylomeDB; O43120; -.
DR PRO; PR:O43120; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005686; C:U2 snRNP; IPI:PomBase.
DR GO; GO:0005684; C:U2-type spliceosomal complex; IPI:PomBase.
DR GO; GO:0003723; F:RNA binding; ISM:PomBase.
DR GO; GO:0045292; P:mRNA cis splicing, via spliceosome; TAS:PomBase.
DR CDD; cd12281; RRM1_TatSF1_like; 1.
DR Gene3D; 3.30.70.330; -; 2.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR034393; TatSF1-like.
DR InterPro; IPR034392; TatSF1-like_RRM1.
DR PANTHER; PTHR15608; PTHR15608; 1.
DR Pfam; PF00076; RRM_1; 2.
DR SMART; SM00360; RRM; 2.
DR SUPFAM; SSF54928; SSF54928; 2.
DR PROSITE; PS50102; RRM; 2.
PE 1: Evidence at protein level;
KW mRNA processing; mRNA splicing; Reference proteome; Repeat; RNA-binding.
FT CHAIN 1..367
FT /note="Splicing factor U2AF-associated protein 2"
FT /id="PRO_0000082003"
FT DOMAIN 112..193
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 268..329
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 36..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..63
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..79
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..104
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 367 AA; 41964 MW; AAA72B803E5AABC9 CRC64;
MSSQPFWDER IHRWRCLGSE GNELIYIDEE QTWKDYDPNS LKMNKAGSTG AEVSDVTAEA
TEGKESSNGE DRHTKRLYES TSAEGYPSGS RNKKSKSENS EASPAPVINK AVYIQGLPLD
VTVDEIEEVF KKCGVIAKNI DNGTPRIKIY RTEDGTPKGD ALIVFFRSES VELAEQLFDD
TEFRYGSGQK MRVQKANIDY KKEKTVNKDV GGALKKKALR LRQQQMQQIS SWDDVDEEVD
DKRKKRFNKI VVLKHIFTLE ELDKTPELLI DLKDDITEEA EKCGRVTNVV LYDKEPDGVV
TVRFSNNEEA EACVRLMQGR YFDGRVVEAS IYDGKVRFQK SGKHTLDDEE DEEKRLEKFA
DWLENSN
