ID   DRI1_YEAST              Reviewed;         719 AA.
AC   P32770; D6VRI4; Q12228;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   27-MAR-2024, entry version 181.
DE   RecName: Full=Putative RNA-binding protein involved in heterochromatin assembly {ECO:0000305};
DE   AltName: Full=Asparagine-rich protein {ECO:0000305};
DE            Short=Protein ARP {ECO:0000305};
GN   Name=NRP1 {ECO:0000312|SGD:S000002326};
GN   Synonyms=ARP {ECO:0000305}, ARP1 {ECO:0000305};
GN   OrderedLocusNames=YDL167C {ECO:0000312|SGD:S000002326};
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].
RC   STRAIN=ATCC 38626 / AH22 / NRRL Y-12843;
RX   PubMed=8483449; DOI=10.1007/bf00279438;
RA   Wehner E.P., Rao E., Brendel M.;
RT   "Molecular structure and genetic regulation of SFA, a gene responsible for
RT   resistance to formaldehyde in Saccharomyces cerevisiae, and
RT   characterization of its protein product.";
RL   Mol. Gen. Genet. 237:351-358(1993).
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   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   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-345, AND IDENTIFICATION BY
RP   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   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-455, 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   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-345 AND SER-455, 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   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-630, 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 play a role in chromatin organization.
CC       {ECO:0000250|UniProtKB:O13801}.
CC   -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000250|UniProtKB:O13801}.
CC       Nucleus {ECO:0000250|UniProtKB:O13801}.
CC   -!- MISCELLANEOUS: Present with 3570 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
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DR   EMBL; X68020; CAA48159.1; -; Genomic_DNA.
DR   EMBL; Z67750; CAA91579.1; -; Genomic_DNA.
DR   EMBL; Z74215; CAA98741.1; -; Genomic_DNA.
DR   EMBL; BK006938; DAA11694.1; -; Genomic_DNA.
DR   PIR; S61046; S61046.
DR   RefSeq; NP_010114.1; NM_001180227.1.
DR   AlphaFoldDB; P32770; -.
DR   BioGRID; 31898; 108.
DR   DIP; DIP-5159N; -.
DR   IntAct; P32770; 13.
DR   STRING; 4932.YDL167C; -.
DR   GlyGen; P32770; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P32770; -.
DR   MaxQB; P32770; -.
DR   PaxDb; 4932-YDL167C; -.
DR   PeptideAtlas; P32770; -.
DR   EnsemblFungi; YDL167C_mRNA; YDL167C; YDL167C.
DR   GeneID; 851387; -.
DR   KEGG; sce:YDL167C; -.
DR   AGR; SGD:S000002326; -.
DR   SGD; S000002326; NRP1.
DR   VEuPathDB; FungiDB:YDL167C; -.
DR   eggNOG; KOG4198; Eukaryota.
DR   GeneTree; ENSGT00940000174896; -.
DR   HOGENOM; CLU_022834_0_0_1; -.
DR   InParanoid; P32770; -.
DR   OMA; FAKNVVC; -.
DR   OrthoDB; 228305at2759; -.
DR   BioCyc; YEAST:G3O-29559-MONOMER; -.
DR   BioGRID-ORCS; 851387; 1 hit in 10 CRISPR screens.
DR   PRO; PR:P32770; -.
DR   Proteomes; UP000002311; Chromosome IV.
DR   RNAct; P32770; Protein.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0010494; C:cytoplasmic stress granule; IDA:SGD.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR   CDD; cd12452; RRM_ARP_like; 1.
DR   Gene3D; 3.30.70.330; -; 1.
DR   Gene3D; 4.10.1060.10; Zinc finger, RanBP2-type; 2.
DR   InterPro; IPR034351; Nrp1_RRM.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR000504; RRM_dom.
DR   InterPro; IPR001876; Znf_RanBP2.
DR   InterPro; IPR036443; Znf_RanBP2_sf.
DR   PANTHER; PTHR23111:SF40; RNA-BINDING PROTEIN INVOLVED IN HETEROCHROMATIN ASSEMBLY-RELATED; 1.
DR   PANTHER; PTHR23111; ZINC FINGER PROTEIN; 1.
DR   Pfam; PF00641; zf-RanBP; 2.
DR   SMART; SM00547; ZnF_RBZ; 2.
DR   SUPFAM; SSF90209; Ran binding protein zinc finger-like; 2.
DR   SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR   PROSITE; PS50102; RRM; 1.
DR   PROSITE; PS01358; ZF_RANBP2_1; 2.
DR   PROSITE; PS50199; ZF_RANBP2_2; 2.
PE   1: Evidence at protein level;
KW   Chromosome; Metal-binding; Nucleus; Phosphoprotein; Reference proteome;
KW   Repeat; RNA-binding; Zinc; Zinc-finger.
FT   CHAIN           1..719
FT                   /note="Putative RNA-binding protein involved in
FT                   heterochromatin assembly"
FT                   /id="PRO_0000081689"
FT   DOMAIN          226..322
FT                   /note="RRM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   ZN_FING         355..384
FT                   /note="RanBP2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT   ZN_FING         581..610
FT                   /note="RanBP2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT   REGION          389..415
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          511..561
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          622..661
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        622..652
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         345
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:15665377,
FT                   ECO:0007744|PubMed:18407956"
FT   MOD_RES         455
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:18407956"
FT   MOD_RES         630
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   CONFLICT        493
FT                   /note="I -> N (in Ref. 1; CAA48159)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   719 AA;  79299 MW;  ADA9BC09FD582669 CRC64;
     MHYVVLELQV AHLPDTPKDQ CRIANIAFQI VNAETLVCHY GTNSLPSIEV NGTTKSLESA
     MVQLDKDIHD VIGNDDFVLV SLYSTWHIRV TLPRQARDDG FILTSYLQHP KVFDLWKEFD
     RWCVNHPEIL GQKKAISNNN CNTKSISINA AKNTKDLDEI VRILEVSIPT EEAGSVPEIY
     SLLKRTTDIL IQLHKKCTSP EDMESVLTKP YDSHTDIRAF LQEKSKILYM NNLPPDTTQS
     ELESWFTQYG VRPVGFWTVK NIVEDTSNVN NNWSLNNSPY VEDQDSISGF VVFQTHEEAT
     EVLALNGRSI LSNLANTKQP RVVEHVLELQ PSSTGVLDKA QEILSPFPQS KNKPRPGDWN
     CPSCGFSNFQ RRTACFRCSF PAPSNSQIHT ANSNNNVNSS RNNLNNRVNS GSSSNISNTA
     ANHPYGAPEF NMIANNTPAA LTYNRAHFPA ITPLSRQNSL NMAPSNSGSP IIIADHFSGN
     NNIAPNYRYN NNINNNNNNI NNMTNNRYNI NNNINGNGNG NGNNSNNNNN HNNNHNNNHH
     NGSINSNSNT NNNNNNNNGN NSNNCNSNIG MGGCGSNMPF RAGDWKCSTC TYHNFAKNVV
     CLRCGGPKSI SGDASETNHY IDSSTFGPAS RTPSNNNISV NTNGGSNAGR TDGNDNKGRD
     ISLMEFMSPP LSMATKSMKE GDGNGSSFNE FKSDKANVNF SNVGDNSAFG NGFNSSIRW
//