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PRP38_YEAST
ID   PRP38_YEAST             Reviewed;         242 AA.
AC   Q00723; D6VUK7;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   03-AUG-2022, entry version 168.
DE   RecName: Full=Pre-mRNA-splicing factor 38;
DE   AltName: Full=Pre-mRNA-processing factor 38;
GN   Name=PRP38; OrderedLocusNames=YGR075C;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX   PubMed=1508195; DOI=10.1128/mcb.12.9.3939-3947.1992;
RA   Blanton S., Srinivasan A., Rymond B.C.;
RT   "PRP38 encodes a yeast protein required for pre-mRNA splicing and
RT   maintenance of stable U6 small nuclear RNA levels.";
RL   Mol. Cell. Biol. 12:3939-3947(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169869;
RA   Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA   Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA   Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA   Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA   Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA   Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA   Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA   Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA   Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA   Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA   Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA   Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA   Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA   Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA   Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA   Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA   Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA   Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA   Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA   Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA   Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA   Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL   Nature 387:81-84(1997).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA   Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA   Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA   LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-encoding
RT   clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [5]
RP   FUNCTION, INTERACTION WITH U4/U6.U5 TRI-SNRNP COMPLEX, AND MUTAGENESIS OF
RP   CYS-87.
RX   PubMed=9582287; DOI=10.1093/emboj/17.10.2938;
RA   Xie J., Beickman K., Otte E., Rymond B.C.;
RT   "Progression through the spliceosome cycle requires Prp38p function for
RT   U4/U6 snRNA dissociation.";
RL   EMBO J. 17:2938-2946(1998).
RN   [6]
RP   SUBUNIT, IDENTIFICATION IN THE U4/U5/U6 TRI-SNRNP COMPLEX, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=10449419; DOI=10.1093/emboj/18.16.4535;
RA   Gottschalk A., Neubauer G., Banroques J., Mann M., Luehrmann R.,
RA   Fabrizio P.;
RT   "Identification by mass spectrometry and functional analysis of novel
RT   proteins of the yeast [U4/U6.U5] tri-snRNP.";
RL   EMBO J. 18:4535-4548(1999).
RN   [7]
RP   IDENTIFICATION IN U4/U6.U5 TRI-SNRNP COMPLEX BY MASS SPECTROMETRY.
RX   PubMed=10377396; DOI=10.1073/pnas.96.13.7226;
RA   Stevens S.W., Abelson J.;
RT   "Purification of the yeast U4/U6.U5 small nuclear ribonucleoprotein
RT   particle and identification of its proteins.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:7226-7231(1999).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=11804584; DOI=10.1016/s1097-2765(02)00436-7;
RA   Stevens S.W., Ryan D.E., Ge H.Y., Moore R.E., Young M.K., Lee T.D.,
RA   Abelson J.;
RT   "Composition and functional characterization of the yeast spliceosomal
RT   penta-snRNP.";
RL   Mol. Cell 9:31-44(2002).
RN   [9]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
RN   [10]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
CC   -!- FUNCTION: Required for pre-mRNA splicing and maintenance of stable U6
CC       small nuclear RNA levels. Implicated in the formation of stable and
CC       biologically active snRNP structures. As part of the U4/U6.U5 tri-snRNP
CC       particle, dispensible for spliceosome assembly, but required for
CC       conformational changes, which result in U4 snRNA release and the
CC       subsequent catalytic activation of the spliceosome.
CC       {ECO:0000269|PubMed:1508195, ECO:0000269|PubMed:9582287}.
CC   -!- SUBUNIT: Component of the U4/U6-U5 tri-snRNP complex composed of the
CC       U4, U6 and U5 snRNAs and at least PRP3, PRP4, PRP6, PRP8, PRP18, PRP31,
CC       PRP38, SNU13, SNU23, SNU66, SNU114, SPP381, SMB1, SMD1, SMD2, SMD3,
CC       SMX2, SMX3, LSM2, LSM3, LSM4, LSM5, LSM6, LSM7, LSM8, BRR2 and DIB1.
CC       {ECO:0000269|PubMed:10377396, ECO:0000269|PubMed:10449419}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC   -!- MISCELLANEOUS: Present with 2380 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the PRP38 family. {ECO:0000305}.
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DR   EMBL; L04669; AAA35054.1; -; Genomic_DNA.
DR   EMBL; M95921; AAA34913.1; -; Genomic_DNA.
DR   EMBL; Z72858; CAA97077.1; -; Genomic_DNA.
DR   EMBL; AY558507; AAS56833.1; -; Genomic_DNA.
DR   EMBL; BK006941; DAA08168.1; -; Genomic_DNA.
DR   PIR; S30888; S30888.
DR   RefSeq; NP_011589.3; NM_001181204.3.
DR   PDB; 5NRL; EM; 7.20 A; M=1-242.
DR   PDB; 5ZWO; EM; 3.90 A; 0=1-242.
DR   PDBsum; 5NRL; -.
DR   PDBsum; 5ZWO; -.
DR   AlphaFoldDB; Q00723; -.
DR   SMR; Q00723; -.
DR   BioGRID; 33317; 127.
DR   ComplexPortal; CPX-25; U4/U6.U5 tri-small nuclear ribonucleoprotein complex.
DR   DIP; DIP-1648N; -.
DR   IntAct; Q00723; 9.
DR   MINT; Q00723; -.
DR   STRING; 4932.YGR075C; -.
DR   MaxQB; Q00723; -.
DR   PaxDb; Q00723; -.
DR   PRIDE; Q00723; -.
DR   EnsemblFungi; YGR075C_mRNA; YGR075C; YGR075C.
DR   GeneID; 852966; -.
DR   KEGG; sce:YGR075C; -.
DR   SGD; S000003307; PRP38.
DR   VEuPathDB; FungiDB:YGR075C; -.
DR   eggNOG; ENOG502RXT7; Eukaryota.
DR   HOGENOM; CLU_1147968_0_0_1; -.
DR   InParanoid; Q00723; -.
DR   OMA; FKCLLMK; -.
DR   BioCyc; YEAST:G3O-30787-MON; -.
DR   PRO; PR:Q00723; -.
DR   Proteomes; UP000002311; Chromosome VII.
DR   RNAct; Q00723; protein.
DR   GO; GO:0005634; C:nucleus; IC:ComplexPortal.
DR   GO; GO:0071011; C:precatalytic spliceosome; IBA:GO_Central.
DR   GO; GO:0005681; C:spliceosomal complex; IC:ComplexPortal.
DR   GO; GO:0046540; C:U4/U6 x U5 tri-snRNP complex; IDA:SGD.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; IC:ComplexPortal.
DR   GO; GO:0000388; P:spliceosome conformational change to release U4 (or U4atac) and U1 (or U11); IMP:SGD.
DR   InterPro; IPR005037; PRP38.
DR   PANTHER; PTHR23142; PTHR23142; 1.
DR   Pfam; PF03371; PRP38; 1.
PE   1: Evidence at protein level;
KW   3D-structure; mRNA processing; mRNA splicing; Nucleus; Reference proteome;
KW   Ribonucleoprotein; Spliceosome.
FT   CHAIN           1..242
FT                   /note="Pre-mRNA-splicing factor 38"
FT                   /id="PRO_0000058590"
FT   REGION          217..242
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        224..242
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MUTAGEN         87
FT                   /note="C->Y: In PRP83-2; temperature-sensitive; blocks
FT                   splicing of RPS17A after a 2 hour shift to the restrictive
FT                   temperature of 37 degrees Celsius; spliceosome assembly
FT                   arrested at the complex I stage."
FT                   /evidence="ECO:0000269|PubMed:9582287"
SQ   SEQUENCE   242 AA;  27967 MW;  62EB225947AF4349 CRC64;
     MAVNEFQVES NISPKQLNNQ SVSLVIPRLT RDKIHNSMYY KVNLSNESLR GNTMVELLKV
     MIGAFGTIKG QNGHLHMMVL GGIEFKCILM KLIEIRPNFQ QLNFLLNVKN ENGFDSKYII
     ALLLVYARLQ YYYLNGNNKN DDDENDLIKL FKVQLYKYSQ HYFKLKSFPL QVDCFAHSYN
     EELCIIHIDE LVDWLATQDH IWGIPLGKCQ WNKIYNSDEE SSSSESESNG DSEDDNDTSS
     ES
 
 
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