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U2AF2_SCHPO
ID   U2AF2_SCHPO             Reviewed;         517 AA.
AC   P36629; Q9UTU7;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   03-AUG-2022, entry version 169.
DE   RecName: Full=Splicing factor U2AF 59 kDa subunit;
DE   AltName: Full=U2 auxiliary factor 59 kDa subunit;
DE            Short=U2AF59;
DE   AltName: Full=U2 snRNP auxiliary factor large subunit;
GN   Name=prp2; Synonyms=mis11; ORFNames=SPBC146.07;
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 MUTAGENESIS OF CYS-387.
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=8211184; DOI=10.1126/science.8211184;
RA   Potashkin J., Naik K., Wentz-Hunter K.;
RT   "U2AF homolog required for splicing in vivo.";
RL   Science 262:573-575(1993).
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).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 1-168, AND SUBCELLULAR
RP   LOCATION.
RC   STRAIN=ATCC 38364 / 968;
RX   PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA   Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA   Hiraoka Y.;
RT   "Large-scale screening of intracellular protein localization in living
RT   fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL   Genes Cells 5:169-190(2000).
RN   [4]
RP   IDENTIFICATION OF SMALL SUBUNIT BINDING DOMAIN.
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   [5]
RP   INTERACTION WITH WAT1.
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11686295; DOI=10.1242/jcs.114.16.2911;
RA   Ochotorena I.L., Hirata D., Kominami K., Potashkin J., Sahin F.,
RA   Wentz-Hunter K., Gould K.L., Sato K., Yoshida Y., Vardy L., Toda T.;
RT   "Conserved Wat1/Pop3 WD-repeat protein of fission yeast secures genome
RT   stability through microtubule integrity and may be involved in mRNA
RT   maturation.";
RL   J. Cell Sci. 114:2911-2920(2001).
RN   [6]
RP   FUNCTION, AND INTERACTION WITH U2AF23 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 small 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 wat1/pop3. {ECO:0000269|PubMed:11686295,
CC       ECO:0000269|PubMed:12374752}.
CC   -!- INTERACTION:
CC       P36629; O74184: pop3; NbExp=4; IntAct=EBI-1024157, EBI-1564139;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10759889}.
CC   -!- SIMILARITY: Belongs to the splicing factor SR family. {ECO:0000305}.
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DR   EMBL; L22577; AAA03578.1; -; Genomic_DNA.
DR   EMBL; CU329671; CAB46760.1; -; Genomic_DNA.
DR   EMBL; AB027985; BAA87289.1; -; Genomic_DNA.
DR   PIR; A48250; A48250.
DR   RefSeq; NP_595396.1; NM_001021303.2.
DR   PDB; 4YH8; X-ray; 1.70 A; B=93-161.
DR   PDB; 7C06; X-ray; 3.02 A; B/E/H/K/N/Q/T/W/Z=93-161.
DR   PDB; 7C07; X-ray; 3.20 A; B/E/H/K/N/Q/T/W/Z=93-161.
DR   PDB; 7C08; X-ray; 3.35 A; B/E/H/K/N/Q/T/W/Z=93-161.
DR   PDBsum; 4YH8; -.
DR   PDBsum; 7C06; -.
DR   PDBsum; 7C07; -.
DR   PDBsum; 7C08; -.
DR   AlphaFoldDB; P36629; -.
DR   SMR; P36629; -.
DR   BioGRID; 276200; 25.
DR   IntAct; P36629; 3.
DR   STRING; 4896.SPBC146.07.1; -.
DR   iPTMnet; P36629; -.
DR   MaxQB; P36629; -.
DR   PaxDb; P36629; -.
DR   PRIDE; P36629; -.
DR   EnsemblFungi; SPBC146.07.1; SPBC146.07.1:pep; SPBC146.07.
DR   GeneID; 2539645; -.
DR   KEGG; spo:SPBC146.07; -.
DR   PomBase; SPBC146.07; prp2.
DR   VEuPathDB; FungiDB:SPBC146.07; -.
DR   eggNOG; KOG0120; Eukaryota.
DR   HOGENOM; CLU_021795_2_0_1; -.
DR   InParanoid; P36629; -.
DR   OMA; MTQWDIK; -.
DR   PhylomeDB; P36629; -.
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:P36629; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0000243; C:commitment complex; IDA:PomBase.
DR   GO; GO:0016607; C:nuclear speck; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IDA:PomBase.
DR   GO; GO:0071004; C:U2-type prespliceosome; IDA:PomBase.
DR   GO; GO:0089701; C:U2AF complex; IDA:PomBase.
DR   GO; GO:0003729; F:mRNA binding; ISS:PomBase.
DR   GO; GO:0008187; F:poly-pyrimidine tract binding; IBA:GO_Central.
DR   GO; GO:0030628; F:pre-mRNA 3'-splice site binding; IBA:GO_Central.
DR   GO; GO:0000348; P:mRNA branch site recognition; ISS:PomBase.
DR   GO; GO:0045292; P:mRNA cis splicing, via spliceosome; IMP:PomBase.
DR   GO; GO:0000245; P:spliceosomal complex assembly; IMP:PomBase.
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   InterPro; IPR006529; U2AF_lg.
DR   Pfam; PF00076; RRM_1; 2.
DR   SMART; SM00360; RRM; 2.
DR   SUPFAM; SSF54928; SSF54928; 1.
DR   TIGRFAMs; TIGR01642; U2AF_lg; 1.
DR   PROSITE; PS50102; RRM; 2.
PE   1: Evidence at protein level;
KW   3D-structure; mRNA processing; mRNA splicing; Nucleus; Reference proteome;
KW   Repeat; RNA-binding.
FT   CHAIN           1..517
FT                   /note="Splicing factor U2AF 59 kDa subunit"
FT                   /id="PRO_0000081993"
FT   DOMAIN          310..388
FT                   /note="RRM 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          418..509
FT                   /note="RRM 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   REGION          1..112
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        13..90
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MUTAGEN         387
FT                   /note="C->Y: Temperature-sensitive."
FT                   /evidence="ECO:0000269|PubMed:8211184"
FT   HELIX           108..118
FT                   /evidence="ECO:0007829|PDB:4YH8"
FT   TURN            119..121
FT                   /evidence="ECO:0007829|PDB:4YH8"
FT   HELIX           125..127
FT                   /evidence="ECO:0007829|PDB:4YH8"
FT   TURN            140..143
FT                   /evidence="ECO:0007829|PDB:7C07"
FT   HELIX           147..152
FT                   /evidence="ECO:0007829|PDB:4YH8"
FT   STRAND          154..156
FT                   /evidence="ECO:0007829|PDB:7C08"
SQ   SEQUENCE   517 AA;  58933 MW;  B2E53EF633184731 CRC64;
     MDLSSRLSSG SSRIPKRHRD YRDEEPRRER GSGGIGREDP RGHYGSERPR RRRRDESDFR
     RHRESRERSY REDERPRRER RYDDYEPRSL RYSSVGRSRS PPPSRERSVR SIEQELEQLR
     DVTPINQWKR KRSLWDIKPP GYELVTADQA KMSGVFPLPG APRAAVTDPE KLLEFARSAE
     GSIIAPPPPL QPGASRQARR LVVTGIPNEF VEDAFVSFIE DLFISTTYHK PETKHFSSVN
     VCKEENFAIL EVATPEDATF LWGLQSESYS NDVFLKFQRI QNYIVPQITP EVSQKRSDDY
     AKNDVLDSKD KIYISNLPLN LGEDQVVELL KPFGDLLSFQ LIKNIADGSS KGFCFCEFKN
     PSDAEVAISG LDGKDTYGNK LHAQFACVGL NQAMIDKSNG MAILTELAKA SSQSIPTRVL
     QLHNLITGDE IMDVQEYEDI YESVKTQFSN YGPLIDIKIP RSIGTRNSGL GTGKVFVRYS
     DIRSAEVAME EMKGCKFNDR TIVIAFYGED CYKANAW
 
 
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