DRI1_YEAST
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 03-AUG-2022, entry version 174.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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; 87.
DR DIP; DIP-5159N; -.
DR IntAct; P32770; 13.
DR STRING; 4932.YDL167C; -.
DR iPTMnet; P32770; -.
DR MaxQB; P32770; -.
DR PaxDb; P32770; -.
DR PRIDE; P32770; -.
DR EnsemblFungi; YDL167C_mRNA; YDL167C; YDL167C.
DR GeneID; 851387; -.
DR KEGG; sce:YDL167C; -.
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 BioCyc; YEAST:G3O-29559-MON; -.
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 GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR CDD; cd12452; RRM_ARP_like; 1.
DR Gene3D; 3.30.70.330; -; 1.
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 Pfam; PF00641; zf-RanBP; 2.
DR SMART; SM00547; ZnF_RBZ; 2.
DR SUPFAM; SSF54928; SSF54928; 1.
DR SUPFAM; SSF90209; SSF90209; 2.
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
