NAM8_YEAST
ID NAM8_YEAST Reviewed; 523 AA.
AC Q00539; D3DL37;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 2.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Protein NAM8 {ECO:0000303|PubMed:2651895};
DE AltName: Full=Nuclear accommodation of mitochondria protein 8 {ECO:0000303|PubMed:2651895};
DE AltName: Full=U1 snRNP component NAM8 {ECO:0000303|PubMed:9630245};
GN Name=NAM8 {ECO:0000303|PubMed:2651895};
GN Synonyms=MRE2 {ECO:0000303|PubMed:7625279},
GN MUD15 {ECO:0000303|PubMed:9630245}; OrderedLocusNames=YHR086W;
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=R23/50;
RX PubMed=1603056; DOI=10.1007/bf00587571;
RA Ekwall K., Kermorgant M., Dujardin G., Groudinsky O., Slonimski P.P.;
RT "The NAM8 gene in Saccharomyces cerevisiae encodes a protein with putative
RT RNA binding motifs and acts as a suppressor of mitochondrial splicing
RT deficiencies when overexpressed.";
RL Mol. Gen. Genet. 233:136-144(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Leem S.-H., Hayashi A., Ajimura M., Ogawa H.;
RT "A yeast MRE2 gene that is essential for meiotic recombination encodes a
RT novel ribonucleoprotein.";
RL Submitted (JUN-1992) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8091229; DOI=10.1126/science.8091229;
RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA Waterston R., Wilson R., Vaudin M.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT VIII.";
RL Science 265:2077-2082(1994).
RN [4]
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 [5]
RP IDENTIFICATION.
RX PubMed=2651895; DOI=10.1007/bf00427051;
RA Asher B.E., Groudinsky O., Dujardin G., Altamura N., Kermorgant M.,
RA Slonimski P.P.;
RT "Novel class of nuclear genes involved in both mRNA splicing and protein
RT synthesis in Saccharomyces cerevisiae mitochondria.";
RL Mol. Gen. Genet. 215:517-528(1989).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=7625279; DOI=10.1016/0065-227x(95)99383-z;
RA Ogawa H., Johzuka K., Nakagawa T., Leem S.H., Hagihara A.H.;
RT "Functions of the yeast meiotic recombination genes, MRE11 and MRE2.";
RL Adv. Biophys. 31:67-76(1995).
RN [7]
RP FUNCTION.
RX PubMed=9112441; DOI=10.1046/j.1365-2443.1997.d01-283.x;
RA Nakagawa T., Ogawa H.;
RT "Involvement of the MRE2 gene of yeast in formation of meiosis-specific
RT double-strand breaks and crossover recombination through RNA splicing.";
RL Genes Cells 2:65-79(1997).
RN [8]
RP IDENTIFICATION WITHIN THE 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 [9]
RP FUNCTION.
RX PubMed=10072385; DOI=10.1101/gad.13.5.569;
RA Puig O., Gottschalk A., Fabrizio P., Seraphin B.;
RT "Interaction of the U1 snRNP with nonconserved intronic sequences affects
RT 5' splice site selection.";
RL Genes Dev. 13:569-580(1999).
RN [10]
RP FUNCTION.
RX PubMed=10983980; DOI=10.1016/s1097-2765(00)00033-2;
RA Spingola M., Ares M. Jr.;
RT "A yeast intronic splicing enhancer and Nam8p are required for Mer1p-
RT activated splicing.";
RL Mol. Cell 6:329-338(2000).
RN [11]
RP FUNCTION, AND DOMAIN.
RX PubMed=21208980; DOI=10.1093/nar/gkq1328;
RA Qiu Z.R., Schwer B., Shuman S.;
RT "Determinants of Nam8-dependent splicing of meiotic pre-mRNAs.";
RL Nucleic Acids Res. 39:3427-3445(2011).
RN [12]
RP FUNCTION, AND DOMAIN.
RX PubMed=21788335; DOI=10.1261/rna.2792011;
RA Qiu Z.R., Schwer B., Shuman S.;
RT "Defining the Mer1 and Nam8 meiotic splicing regulons by cDNA rescue.";
RL RNA 17:1648-1654(2011).
RN [13]
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).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [15] {ECO:0007744|PDB:6N7X}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.60 ANGSTROMS) OF THE U1 SNRNP COMPLEX,
RP AND IDENTIFICATION WITHIN THE U1 SNRNP COMPLEX.
RX PubMed=29051543; DOI=10.1038/s41467-017-01241-9;
RA Li X., Liu S., Jiang J., Zhang L., Espinosa S., Hill R.C., Hansen K.C.,
RA Zhou Z.H., Zhao R.;
RT "CryoEM structure of Saccharomyces cerevisiae U1 snRNP offers insight into
RT alternative splicing.";
RL Nat. Commun. 8:1035-1035(2017).
RN [16] {ECO:0007744|PDB:6G90}
RP STRUCTURE BY ELECTRON MICROSCOPY (4.00 ANGSTROMS) OF THE PRE-SPLICEOSOME
RP COMPLEX, AND IDENTIFICATION WITHIN THE U1 SNRNP COMPLEX.
RX PubMed=29995849; DOI=10.1038/s41586-018-0323-8;
RA Plaschka C., Lin P.C., Charenton C., Nagai K.;
RT "Prespliceosome structure provides insights into spliceosome assembly and
RT regulation.";
RL Nature 559:419-422(2018).
RN [17] {ECO:0007744|PDB:5ZWN}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.30 ANGSTROMS) OF THE SPLICEOSOME, AND
RP IDENTIFICATION WITHIN THE U1 SNRNP COMPLEX.
RX PubMed=29794219; DOI=10.1126/science.aau0325;
RA Bai R., Wan R., Yan C., Lei J., Shi Y.;
RT "Structures of the fully assembled Saccharomyces cerevisiae spliceosome
RT before activation.";
RL Science 360:1423-1429(2018).
RN [18] {ECO:0007744|PDB:6N7P, ECO:0007744|PDB:6N7R}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.20 ANGSTROMS) OF THE SPLICEOSOMAL E
RP COMPLEX, IDENTIFICATION WITHIN THE U1 SNRNP COMPLEX, AND DOMAIN.
RX PubMed=31485080; DOI=10.1038/s41586-019-1523-6;
RA Li X., Liu S., Zhang L., Issaian A., Hill R.C., Espinosa S., Shi S.,
RA Cui Y., Kappel K., Das R., Hansen K.C., Zhou Z.H., Zhao R.;
RT "A unified mechanism for intron and exon definition and back-splicing.";
RL Nature 573:375-380(2019).
RN [19] {ECO:0007744|PDB:7OQC, ECO:0007744|PDB:7OQE}
RP STRUCTURE BY ELECTRON MICROSCOPY (4.10 ANGSTROMS) OF THE U1 SNRNP COMPLEX,
RP AND IDENTIFICATION WITHIN THE U1 SNRNP COMPLEX.
RX PubMed=34349264; DOI=10.1038/s41586-021-03789-5;
RA Zhang Z., Rigo N., Dybkov O., Fourmann J.B., Will C.L., Kumar V.,
RA Urlaub H., Stark H., Luehrmann R.;
RT "Structural insights into how Prp5 proofreads the pre-mRNA branch site.";
RL Nature 596:296-300(2021).
CC -!- FUNCTION: Component of the U1 small nuclear ribonucleoprotein complex
CC (U1 snRNP) involved in the initiation of meiotic recombination
CC (PubMed:1603056, PubMed:7625279). Involved in the formation of DSBs at
CC recombination hot-spots through meiosis-specific splicing of REC107
CC pre-mRNA (PubMed:7625279, PubMed:9112441, PubMed:21788335).
CC Collaborates with MER1 to promote splicing of essential meiotic mRNAs
CC REC10, AMA1, MER3, HFM1, SPO22 and PCH2 (PubMed:10983980,
CC PubMed:21208980, PubMed:21788335). NAM8 interacts with the pre-mRNA
CC downstream of the 5' splice site, in a region of non-conserved sequence
CC and is required for efficient splicing of uncapped RNA precursor
CC (PubMed:10072385). {ECO:0000269|PubMed:10072385,
CC ECO:0000269|PubMed:10983980, ECO:0000269|PubMed:1603056,
CC ECO:0000269|PubMed:21208980, ECO:0000269|PubMed:21788335,
CC ECO:0000269|PubMed:7625279, ECO:0000269|PubMed:9112441}.
CC -!- SUBUNIT: Component of the U1 small nuclear ribonucleoprotein complex
CC (U1 snRNP). {ECO:0000269|PubMed:29051543, ECO:0000269|PubMed:29794219,
CC ECO:0000269|PubMed:29995849, ECO:0000269|PubMed:31485080,
CC ECO:0000269|PubMed:34349264, ECO:0000269|PubMed:9630245}.
CC -!- DOMAIN: The RNA binding domains RRM2 and RRM3 are required for NAM8
CC meiotic function (PubMed:21788335, PubMed:21208980). Within the U1
CC snRNP complex, the RRM2 domain of NAM8 is positioned to bind to the
CC intronic region immediately down-stream of nucleotide +13
CC (PubMed:31485080). {ECO:0000269|PubMed:21208980,
CC ECO:0000269|PubMed:21788335, ECO:0000269|PubMed:31485080}.
CC -!- DISRUPTION PHENOTYPE: Affects the meiotic recombination and the
CC formation of viable spores. {ECO:0000269|PubMed:7625279}.
CC -!- MISCELLANEOUS: Present with 1480 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; X64763; CAA46011.1; -; Genomic_DNA.
DR EMBL; D11461; BAA02016.1; -; Genomic_DNA.
DR EMBL; U00060; AAB68928.1; -; Genomic_DNA.
DR EMBL; BK006934; DAA06781.1; -; Genomic_DNA.
DR PIR; S46720; S46720.
DR RefSeq; NP_011954.1; NM_001179216.1.
DR PDB; 5ZWN; EM; 3.30 A; V=1-523.
DR PDB; 6G90; EM; 4.00 A; F=1-523.
DR PDB; 6N7P; EM; 3.60 A; F=1-523.
DR PDB; 6N7R; EM; 3.20 A; F=1-523.
DR PDB; 6N7X; EM; 3.60 A; F=1-523.
DR PDB; 7OQC; EM; 4.10 A; F=1-523.
DR PDB; 7OQE; EM; 5.90 A; F=1-523.
DR PDBsum; 5ZWN; -.
DR PDBsum; 6G90; -.
DR PDBsum; 6N7P; -.
DR PDBsum; 6N7R; -.
DR PDBsum; 6N7X; -.
DR PDBsum; 7OQC; -.
DR PDBsum; 7OQE; -.
DR AlphaFoldDB; Q00539; -.
DR SMR; Q00539; -.
DR BioGRID; 36521; 188.
DR ComplexPortal; CPX-23; U1 small nuclear ribonucleoprotein complex.
DR DIP; DIP-2749N; -.
DR IntAct; Q00539; 36.
DR MINT; Q00539; -.
DR STRING; 4932.YHR086W; -.
DR iPTMnet; Q00539; -.
DR MaxQB; Q00539; -.
DR PaxDb; Q00539; -.
DR PRIDE; Q00539; -.
DR EnsemblFungi; YHR086W_mRNA; YHR086W; YHR086W.
DR GeneID; 856486; -.
DR KEGG; sce:YHR086W; -.
DR SGD; S000001128; NAM8.
DR VEuPathDB; FungiDB:YHR086W; -.
DR eggNOG; KOG0118; Eukaryota.
DR HOGENOM; CLU_016304_7_0_1; -.
DR InParanoid; Q00539; -.
DR OMA; YVKIPAN; -.
DR BioCyc; YEAST:G3O-31133-MON; -.
DR PRO; PR:Q00539; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; Q00539; protein.
DR GO; GO:0000243; C:commitment complex; IPI:SGD.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
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:0003729; F:mRNA binding; IPI:SGD.
DR GO; GO:0000395; P:mRNA 5'-splice site recognition; IC:ComplexPortal.
DR GO; GO:0006376; P:mRNA splice site selection; IMP:SGD.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IPI:SGD.
DR GO; GO:0048026; P:positive regulation of mRNA splicing, via spliceosome; IMP:SGD.
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 Pfam; PF00076; RRM_1; 2.
DR SMART; SM00360; RRM; 3.
DR SUPFAM; SSF54928; SSF54928; 2.
DR PROSITE; PS50102; RRM; 3.
PE 1: Evidence at protein level;
KW 3D-structure; mRNA processing; mRNA splicing; Reference proteome; Repeat;
KW RNA-binding; Spliceosome.
FT CHAIN 1..523
FT /note="Protein NAM8"
FT /id="PRO_0000081659"
FT DOMAIN 54..145
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 163..242
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 313..385
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 239..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 180
FT /note="F -> L (in Ref. 1; CAA46011)"
FT /evidence="ECO:0000305"
FT CONFLICT 208..209
FT /note="GF -> VL (in Ref. 1; CAA46011)"
FT /evidence="ECO:0000305"
FT STRAND 293..295
FT /evidence="ECO:0007829|PDB:6N7R"
FT STRAND 306..308
FT /evidence="ECO:0007829|PDB:6N7R"
FT STRAND 314..318
FT /evidence="ECO:0007829|PDB:6N7R"
FT HELIX 326..333
FT /evidence="ECO:0007829|PDB:6N7R"
FT HELIX 334..336
FT /evidence="ECO:0007829|PDB:6N7R"
FT STRAND 339..343
FT /evidence="ECO:0007829|PDB:6N7R"
FT STRAND 348..357
FT /evidence="ECO:0007829|PDB:6N7R"
FT HELIX 358..367
FT /evidence="ECO:0007829|PDB:6N7R"
FT STRAND 368..370
FT /evidence="ECO:0007829|PDB:6N7R"
FT STRAND 373..375
FT /evidence="ECO:0007829|PDB:5ZWN"
FT STRAND 379..382
FT /evidence="ECO:0007829|PDB:6N7R"
FT HELIX 387..397
FT /evidence="ECO:0007829|PDB:6N7R"
FT STRAND 415..417
FT /evidence="ECO:0007829|PDB:6N7R"
FT STRAND 439..441
FT /evidence="ECO:0007829|PDB:5ZWN"
FT STRAND 444..446
FT /evidence="ECO:0007829|PDB:6N7R"
FT STRAND 493..495
FT /evidence="ECO:0007829|PDB:5ZWN"
FT HELIX 501..518
FT /evidence="ECO:0007829|PDB:6N7R"
SQ SEQUENCE 523 AA; 56972 MW; 64F198EEFB32A909 CRC64;
MSYKQTTYYP SRGNLVRNDS SPYTNTISSE TNNSSTSVLS LQGASNVSLG TTGNQLYMGD
LDPTWDKNTV RQIWASLGEA NINVRMMWNN TLNNGSRSSM GPKNNQGYCF VDFPSSTHAA
NALLKNGMLI PNFPNKKLKL NWATSSYSNS NNSLNNVKSG NNCSIFVGDL APNVTESQLF
ELFINRYAST SHAKIVHDQV TGMSKGYGFV KFTNSDEQQL ALSEMQGVFL NGRAIKVGPT
SGQQQHVSGN NDYNRSSSSL NNENVDSRFL SKGQSFLSNG NNNMGFKRNH MSQFIYPVQQ
QPSLNHFTDP NNTTVFIGGL SSLVTEDELR AYFQPFGTIV YVKIPVGKCC GFVQYVDRLS
AEAAIAGMQG FPIANSRVRL SWGRSAKQTA LLQQAMLSNS LQVQQQQPGL QQPNYGYIPS
STCEAPVLPD NNVSSTMLPG CQILNYSNPY ANANGLGSNN FSFYSNNNAT NTQATSLLAD
TSSMDLSGTG GQQVIMQGSE AVVNSTNAML NRLEQGSNGF MFA
