PRP42_YEAST
ID PRP42_YEAST Reviewed; 544 AA.
AC Q03776; D6VSL6;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=U1 small nuclear ribonucleoprotein component PRP42;
DE Short=U1 snRNP protein PRP42;
DE AltName: Full=65 kDa snRNP protein;
DE AltName: Full=Pre-mRNA-processing factor 42;
GN Name=PRP42; Synonyms=MUD16, SNU65; OrderedLocusNames=YDR235W;
GN ORFNames=YD8419.02;
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.
RC STRAIN=ATCC 204511 / S288c / AB972;
RX PubMed=9418882; DOI=10.1128/mcb.18.1.353;
RA McLean M.R., Rymond B.C.;
RT "Yeast pre-mRNA splicing requires a pair of U1 snRNP-associated
RT tetratricopeptide repeat proteins.";
RL Mol. Cell. Biol. 18:353-360(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(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 IDENTIFICATION IN U1 SNRNP COMPLEX.
RX PubMed=9630245;
RA Gottschalk A., Tang J., Puig O., Salgado J., Neubauer G., Colot H.V.,
RA Mann M., Seraphin B., Rosbash M., Luehrmann R., Fabrizio P.;
RT "A comprehensive biochemical and genetic analysis of the yeast U1 snRNP
RT reveals five novel proteins.";
RL RNA 4:374-393(1998).
RN [5]
RP IDENTIFICATION IN U1 SNRNP COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=10504710; DOI=10.1038/13732;
RA Rigaut G., Shevchenko A., Rutz B., Wilm M., Mann M., Seraphin B.;
RT "A generic protein purification method for protein complex characterization
RT and proteome exploration.";
RL Nat. Biotechnol. 17:1030-1032(1999).
RN [6]
RP IDENTIFICATION IN U1.U2.U4/U6.U5 PENTA-SNRNP COMPLEX, AND IDENTIFICATION BY
RP 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 [7]
RP FUNCTION.
RX PubMed=12897147; DOI=10.1128/mcb.23.16.5768-5779.2003;
RA Kotovic K.M., Lockshon D., Boric L., Neugebauer K.M.;
RT "Cotranscriptional recruitment of the U1 snRNP to intron-containing genes
RT in yeast.";
RL Mol. Cell. Biol. 23:5768-5779(2003).
RN [8]
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 [9]
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: Essential component of the U1 snRNP particle, which
CC recognizes and binds the 5'-splice site of pre-mRNA. Together with
CC other non-snRNP factors, U1 snRNP forms the spliceosomal commitment
CC complex, that targets pre-mRNA to the splicing pathway. U1 snRNP is
CC cotranscriptionally recruited to intron-containing genes. Required for
CC U1 snRNP biogenesis. {ECO:0000269|PubMed:12897147,
CC ECO:0000269|PubMed:9418882}.
CC -!- SUBUNIT: Component of the 18S U1 snRNP particle, a subcomplex of the
CC spliceosome. {ECO:0000269|PubMed:10504710, ECO:0000269|PubMed:11804584,
CC ECO:0000269|PubMed:9630245}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 1730 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; AF020682; AAB81948.1; -; Genomic_DNA.
DR EMBL; Z49701; CAA89721.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12076.1; -; Genomic_DNA.
DR PIR; S54531; S54531.
DR RefSeq; NP_010521.1; NM_001180543.1.
DR PDB; 5ZWN; EM; 3.30 A; T=1-544.
DR PDB; 6G90; EM; 4.00 A; E=1-544.
DR PDB; 6N7P; EM; 3.60 A; D=1-544.
DR PDB; 6N7R; EM; 3.20 A; D=1-544.
DR PDB; 6N7X; EM; 3.60 A; D=1-544.
DR PDB; 7OQC; EM; 4.10 A; E=1-544.
DR PDB; 7OQE; EM; 5.90 A; E=1-544.
DR PDBsum; 5ZWN; -.
DR PDBsum; 6G90; -.
DR PDBsum; 6N7P; -.
DR PDBsum; 6N7R; -.
DR PDBsum; 6N7X; -.
DR PDBsum; 7OQC; -.
DR PDBsum; 7OQE; -.
DR AlphaFoldDB; Q03776; -.
DR SMR; Q03776; -.
DR BioGRID; 32286; 83.
DR ComplexPortal; CPX-23; U1 small nuclear ribonucleoprotein complex.
DR DIP; DIP-2836N; -.
DR IntAct; Q03776; 19.
DR MINT; Q03776; -.
DR STRING; 4932.YDR235W; -.
DR MaxQB; Q03776; -.
DR PaxDb; Q03776; -.
DR PRIDE; Q03776; -.
DR EnsemblFungi; YDR235W_mRNA; YDR235W; YDR235W.
DR GeneID; 851821; -.
DR KEGG; sce:YDR235W; -.
DR SGD; S000002643; PRP42.
DR VEuPathDB; FungiDB:YDR235W; -.
DR eggNOG; KOG1258; Eukaryota.
DR HOGENOM; CLU_037892_0_0_1; -.
DR InParanoid; Q03776; -.
DR OMA; IELWISY; -.
DR BioCyc; YEAST:G3O-29811-MON; -.
DR PRO; PR:Q03776; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q03776; protein.
DR GO; GO:0000243; C:commitment complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IC:ComplexPortal.
DR GO; GO:0005681; C:spliceosomal complex; IC:ComplexPortal.
DR GO; GO:0005685; C:U1 snRNP; IDA:SGD.
DR GO; GO:0071004; C:U2-type prespliceosome; IDA:SGD.
DR GO; GO:0003723; F:RNA binding; IDA:SGD.
DR GO; GO:0000395; P:mRNA 5'-splice site recognition; IBA:GO_Central.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IMP:SGD.
DR Gene3D; 1.25.40.10; -; 2.
DR InterPro; IPR003107; HAT.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR SMART; SM00386; HAT; 3.
DR SUPFAM; SSF48452; SSF48452; 1.
PE 1: Evidence at protein level;
KW 3D-structure; mRNA processing; mRNA splicing; Nucleus; Reference proteome;
KW Repeat; Ribonucleoprotein; RNA-binding; Spliceosome.
FT CHAIN 1..544
FT /note="U1 small nuclear ribonucleoprotein component PRP42"
FT /id="PRO_0000262751"
FT REPEAT 7..39
FT /note="HAT 1"
FT REPEAT 51..83
FT /note="HAT 2"
FT REPEAT 85..118
FT /note="HAT 3"
FT REPEAT 121..156
FT /note="HAT 4"
FT REPEAT 163..195
FT /note="HAT 5"
FT REPEAT 255..288
FT /note="HAT 6"
FT REPEAT 290..322
FT /note="HAT 7"
FT REPEAT 366..397
FT /note="HAT 8"
FT REPEAT 456..488
FT /note="HAT 9"
FT MOTIF 230..235
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT HELIX 3..8
FT /evidence="ECO:0007829|PDB:6N7R"
FT HELIX 11..22
FT /evidence="ECO:0007829|PDB:6N7R"
FT HELIX 24..26
FT /evidence="ECO:0007829|PDB:5ZWN"
FT HELIX 28..39
FT /evidence="ECO:0007829|PDB:6N7R"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:6N7R"
FT HELIX 50..66
FT /evidence="ECO:0007829|PDB:6N7R"
FT HELIX 71..83
FT /evidence="ECO:0007829|PDB:6N7R"
FT HELIX 87..100
FT /evidence="ECO:0007829|PDB:6N7R"
FT TURN 101..103
FT /evidence="ECO:0007829|PDB:6N7R"
FT HELIX 106..119
FT /evidence="ECO:0007829|PDB:6N7R"
FT HELIX 123..137
FT /evidence="ECO:0007829|PDB:6N7R"
FT TURN 141..143
FT /evidence="ECO:0007829|PDB:6N7R"
FT HELIX 144..157
FT /evidence="ECO:0007829|PDB:6N7R"
FT STRAND 159..161
FT /evidence="ECO:0007829|PDB:6N7R"
FT HELIX 162..171
FT /evidence="ECO:0007829|PDB:6N7R"
FT HELIX 179..191
FT /evidence="ECO:0007829|PDB:6N7R"
FT HELIX 199..202
FT /evidence="ECO:0007829|PDB:6N7R"
FT HELIX 205..210
FT /evidence="ECO:0007829|PDB:6N7R"
FT HELIX 223..254
FT /evidence="ECO:0007829|PDB:6N7R"
FT TURN 255..258
FT /evidence="ECO:0007829|PDB:6N7R"
FT HELIX 273..289
FT /evidence="ECO:0007829|PDB:6N7R"
FT HELIX 292..302
FT /evidence="ECO:0007829|PDB:6N7R"
FT TURN 303..308
FT /evidence="ECO:0007829|PDB:6N7R"
FT HELIX 311..322
FT /evidence="ECO:0007829|PDB:6N7R"
FT HELIX 327..340
FT /evidence="ECO:0007829|PDB:6N7R"
FT HELIX 345..357
FT /evidence="ECO:0007829|PDB:6N7R"
FT HELIX 361..374
FT /evidence="ECO:0007829|PDB:6N7R"
FT TURN 375..377
FT /evidence="ECO:0007829|PDB:5ZWN"
FT HELIX 379..381
FT /evidence="ECO:0007829|PDB:6N7R"
FT HELIX 385..402
FT /evidence="ECO:0007829|PDB:6N7R"
FT HELIX 408..410
FT /evidence="ECO:0007829|PDB:6N7R"
FT HELIX 418..428
FT /evidence="ECO:0007829|PDB:6N7R"
FT TURN 429..432
FT /evidence="ECO:0007829|PDB:6N7R"
FT STRAND 433..435
FT /evidence="ECO:0007829|PDB:6N7R"
FT HELIX 437..444
FT /evidence="ECO:0007829|PDB:6N7R"
FT HELIX 450..459
FT /evidence="ECO:0007829|PDB:6N7R"
FT HELIX 461..467
FT /evidence="ECO:0007829|PDB:6N7R"
FT HELIX 470..473
FT /evidence="ECO:0007829|PDB:6N7R"
FT HELIX 476..487
FT /evidence="ECO:0007829|PDB:6N7R"
FT STRAND 490..492
FT /evidence="ECO:0007829|PDB:6N7R"
FT HELIX 494..503
FT /evidence="ECO:0007829|PDB:6N7R"
FT HELIX 505..508
FT /evidence="ECO:0007829|PDB:6N7R"
FT TURN 511..513
FT /evidence="ECO:0007829|PDB:5ZWN"
FT HELIX 514..528
FT /evidence="ECO:0007829|PDB:6N7R"
FT HELIX 533..539
FT /evidence="ECO:0007829|PDB:6N7R"
SQ SEQUENCE 544 AA; 65145 MW; 7F6790FFD0ECEB80 CRC64;
MDKYTALIHD ENFSTLTLNV SRYPKSLAYW EKLLNYIVKA SAPICKSTEP QLLKLIRCTY
SSMLNEFPYL ENYYIDFALL EYKLGNVSMS HKIFQRGLQA FNQRSLLLWT SYLKFCNNVI
SHQKQLFKKY ETAEEYVGLH FFSGEFWDLY LEQISSRCTS SKKYWNVLRK ILEIPLHSFS
KFYALWLQRI DDIMDLKQLS QLTSKDELLK KLKIDINYSG RKGPYLQDAK KKLKKITKEM
YMVVQYQVLE IYSIFESKIY INYYTSPETL VSSDEIETWI KYLDYTITLQ TDSLTHLNFQ
RALLPLAHYD LVWIKYSKWL INSKNDLLGA KNVLLMGLKF SLKKTEIIKL LYSVICKLNE
YVLLRNLLEK IESSYSDNVE NVDDFEIFWD YLQFKTFCQN SLYSSRYSDS QSNGLLNKEL
FDKVWKRLSC KEKKSGQEIL LNNLVQFYSK DTVEFVEKNI FQKIIEFGWE YYLQNGMFWN
CYCRLIYFDT SRSYLDKRQY IVRKIWPQID KKFAQSVLPS LTEFCESYFP EEMDTLEEMF
TEEP
