NEW1_YEAST
ID NEW1_YEAST Reviewed; 1196 AA.
AC Q08972; D6W3E4; Q05402; Q7LHP2;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=[NU+] prion formation protein 1;
GN Name=NEW1; OrderedLocusNames=YPL226W; ORFNames=P1445;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [2]
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 [3]
RP DOMAINS, AND PREDICTION OF FUNCTION.
RX PubMed=9020838; DOI=10.1038/ng0297-137;
RA Decottignies A., Goffeau A.;
RT "Complete inventory of the yeast ABC proteins.";
RL Nat. Genet. 15:137-145(1997).
RN [4]
RP IDENTIFICATION AS A PRION-FORMING PROTEIN.
RX PubMed=10660050; DOI=10.1016/s0092-8674(00)81565-2;
RA Santoso A., Chien P., Osherovich L.Z., Weissman J.S.;
RT "Molecular basis of a yeast prion species barrier.";
RL Cell 100:277-288(2000).
RN [5]
RP PRION FORMATION.
RX PubMed=11511345; DOI=10.1016/s0092-8674(01)00427-5;
RA Derkatch I.L., Bradley M.E., Hong J.Y., Liebman S.W.;
RT "Prions affect the appearance of other prions: the story of [PIN(+)].";
RL Cell 106:171-182(2001).
RN [6]
RP DOMAIN, AND PRION FORMATION.
RX PubMed=11511346; DOI=10.1016/s0092-8674(01)00440-8;
RA Osherovich L.Z., Weissman J.S.;
RT "Multiple Gln/Asn-rich prion domains confer susceptibility to induction of
RT the yeast [PSI(+)] prion.";
RL Cell 106:183-194(2001).
RN [7]
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 [8]
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 [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=YAL6B;
RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA Jensen O.N.;
RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT pathway.";
RL Mol. Cell. Proteomics 4:310-327(2005).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1191, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-443 AND THR-1191, AND
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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1191, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: May be involved in the mRNA export process (By similarity).
CC Forms the [NU+] prion and induces [PSI+] prion formation.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000250}.
CC -!- DOMAIN: The N-terminal 153 residues are responsible for the prion
CC properties of NEW1. {ECO:0000269|PubMed:11511346,
CC ECO:0000269|PubMed:9020838}.
CC -!- MISCELLANEOUS: Present with 37600 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCF family.
CC EF3 subfamily. {ECO:0000305}.
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DR EMBL; X94561; CAA64261.1; -; Genomic_DNA.
DR EMBL; Z73582; CAA97941.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11210.1; -; Genomic_DNA.
DR PIR; S65245; S65245.
DR RefSeq; NP_015098.1; NM_001184040.1.
DR PDB; 6S47; EM; 3.28 A; Bi=141-1112.
DR PDBsum; 6S47; -.
DR AlphaFoldDB; Q08972; -.
DR SMR; Q08972; -.
DR BioGRID; 35959; 610.
DR DIP; DIP-6323N; -.
DR IntAct; Q08972; 30.
DR MINT; Q08972; -.
DR STRING; 4932.YPL226W; -.
DR iPTMnet; Q08972; -.
DR MaxQB; Q08972; -.
DR PaxDb; Q08972; -.
DR PRIDE; Q08972; -.
DR EnsemblFungi; YPL226W_mRNA; YPL226W; YPL226W.
DR GeneID; 855875; -.
DR KEGG; sce:YPL226W; -.
DR SGD; S000006147; NEW1.
DR VEuPathDB; FungiDB:YPL226W; -.
DR eggNOG; KOG0062; Eukaryota.
DR eggNOG; KOG1242; Eukaryota.
DR HOGENOM; CLU_002848_0_1_1; -.
DR InParanoid; Q08972; -.
DR OMA; VQKFDDH; -.
DR BioCyc; YEAST:G3O-34115-MON; -.
DR PRO; PR:Q08972; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q08972; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005844; C:polysome; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; HDA:SGD.
DR GO; GO:0043022; F:ribosome binding; IDA:SGD.
DR GO; GO:0008079; F:translation termination factor activity; IMP:SGD.
DR GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; ISS:SGD.
DR GO; GO:0006449; P:regulation of translational termination; IMP:SGD.
DR GO; GO:0042274; P:ribosomal small subunit biogenesis; IMP:SGD.
DR Gene3D; 1.25.10.10; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR023780; Chromo_domain.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00005; ABC_tran; 2.
DR Pfam; PF00385; Chromo; 1.
DR SMART; SM00382; AAA; 2.
DR SMART; SM00298; CHROMO; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
DR PROSITE; PS50013; CHROMO_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amyloid; ATP-binding; Cytoplasm; mRNA transport;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Prion; Reference proteome;
KW Repeat; Transport.
FT CHAIN 1..1196
FT /note="[NU+] prion formation protein 1"
FT /id="PRO_0000268690"
FT DOMAIN 570..786
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 812..1129
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 942..1003
FT /note="Chromo"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00053"
FT REGION 1..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 103..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1137..1166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1177..1196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 604..611
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 846..853
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT MOD_RES 443
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 1191
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
SQ SEQUENCE 1196 AA; 134331 MW; 3C8C52A3F54C2902 CRC64;
MPPKKFKDLN SFLDDQPKDP NLVASPFGGY FKNPAADAGS NNASKKSSYQ QQRNWKQGGN
YQQGGYQSYN SNYNNYNNYN NYNNYNNYNN YNKYNGQGYQ KSTYKQSAVT PNQSGTPTPS
ASTTSLTSLN EKLSNLELTP ISQFLSKIPE CQSITDCKNQ IKLIIEEFGK EGNSTGEKIE
EWKIVDVLSK FIKPKNPSLV RESAMLIISN IAQFFSGKPP QEAYLLPFFN VALDCISDKE
NTVKRAAQHA IDSLLNCFPM EALTCFVLPT ILDYLSSGAK WQAKMAALSV VDRIREDSAN
DLLELTFKDA VPVLTDVATD FKPELAKQGY KTLLDYVSIL DNLDLSPRYK LIVDTLQDPS
KVPESVKSLS SVTFVAEVTE PSLSLLVPIL NRSLNLSSSS QEQLRQTVIV VENLTRLVNN
RNEIESFIPL LLPGIQKVVD TASLPEVREL AEKALNVLKE DDEADKENKF SGRLTLEEGR
DFLLDHLKDI KADDSCFVKP YMNDETVIKY MSKILTVDSN VNDWKRLEDF LTAVFGGSDS
QREFVKQDFI HNLRALFYQE KERADEDEGI EIVNTDFSLA YGSRMLLNKT NLRLLKGHRY
GLCGRNGAGK STLMRAIANG QLDGFPDKDT LRTCFVEHKL QGEEGDLDLV SFIALDEELQ
STSREEIAAA LESVGFDEER RAQTVGSLSG GWKMKLELAR AMLQKADILL LDEPTNHLDV
SNVKWLEEYL LEHTDITSLI VSHDSGFLDT VCTDIIHYEN KKLAYYKGNL AAFVEQKPEA
KSYYTLTDSN AQMRFPPPGI LTGVKSNTRA VAKMTDVTFS YPGAQKPSLS HVSCSLSLSS
RVACLGPNGA GKSTLIKLLT GELVPNEGKV EKHPNLRIGY IAQHALQHVN EHKEKTANQY
LQWRYQFGDD REVLLKESRK ISEDEKEMMT KEIDIDDGRG KRAIEAIVGR QKLKKSFQYE
VKWKYWKPKY NSWVPKDVLV EHGFEKLVQK FDDHEASREG LGYRELIPSV ITKHFEDVGL
DSEIANHTPL GSLSGGQLVK VVIAGAMWNN PHLLVLDEPT NYLDRDSLGA LAVAIRDWSG
GVVMISHNNE FVGALCPEQW IVENGKMVQK GSAQVDQSKF EDGGNADAVG LKASNLAKPS
VDDDDSPANI KVKQRKKRLT RNEKKLQAER RRLRYIEWLS SPKGTPKPVD TDDEED
