HRP1_YEAST
ID HRP1_YEAST Reviewed; 534 AA.
AC Q99383; D6W1U5; Q02741;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Nuclear polyadenylated RNA-binding protein 4 {ECO:0000305};
DE AltName: Full=Cleavage factor IB;
DE Short=CFIB;
DE AltName: Full=Heterogeneous nuclear ribonucleoprotein 1 {ECO:0000303|PubMed:8770588};
GN Name=HRP1 {ECO:0000303|PubMed:8770588}; Synonyms=NAB4, NAB5;
GN OrderedLocusNames=YOL123W;
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].
RA Oberdorf A.M., Anderson J.T., Devore D.R., Swanson M.S.;
RL Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8770588; DOI=10.1093/genetics/142.1.103;
RA Henry M., Borland C.Z., Bossie M., Silver P.A.;
RT "Potential RNA binding proteins in Saccharomyces cerevisiae identified as
RT suppressors of temperature-sensitive mutations in NPL3.";
RL Genetics 142:103-115(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8896268;
RX DOI=10.1002/(sici)1097-0061(199609)12:10b<1041::aid-yea989>3.0.co;2-i;
RA Lafuente M.J., Gamo F.-J., Gancedo C.;
RT "DNA sequence analysis of a 10 624 bp fragment of the left arm of
RT chromosome XV from Saccharomyces cerevisiae reveals a RNA binding protein,
RT a mitochondrial protein, two ribosomal proteins and two new open reading
RT frames.";
RL Yeast 12:1041-1045(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [5]
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 [6]
RP PROTEIN SEQUENCE OF 182-189 AND 245-257, FUNCTION, RNA-BINDING, AND
RP SUBCELLULAR LOCATION.
RX PubMed=9334319; DOI=10.1101/gad.11.19.2545;
RA Kessler M.M., Henry M.F., Shen E., Zhao J., Gross S., Silver P.A.,
RA Moore C.L.;
RT "Hrp1, a sequence-specific RNA-binding protein that shuttles between the
RT nucleus and the cytoplasm, is required for mRNA 3'-end formation in
RT yeast.";
RL Genes Dev. 11:2545-2556(1997).
RN [7]
RP FUNCTION.
RX PubMed=9857200; DOI=10.1093/emboj/17.24.7454;
RA Minvielle-Sebastia L., Beyer K., Krecic A.M., Hector R.E., Swanson M.S.,
RA Keller W.;
RT "Control of cleavage site selection during mRNA 3' end formation by a yeast
RT hnRNP.";
RL EMBO J. 17:7454-7468(1998).
RN [8]
RP SUBCELLULAR LOCATION, AND METHYLATION BY HMT1.
RX PubMed=9499403; DOI=10.1101/gad.12.5.679;
RA Shen E.C., Henry M.F., Weiss V.H., Valentini S.R., Silver P.A., Lee M.S.;
RT "Arginine methylation facilitates the nuclear export of hnRNP proteins.";
RL Genes Dev. 12:679-691(1998).
RN [9]
RP RNA-BINDING.
RX PubMed=9776761; DOI=10.1093/nar/26.21.4965;
RA Chen S., Hyman L.E.;
RT "A specific RNA-protein interaction at yeast polyadenylation efficiency
RT elements.";
RL Nucleic Acids Res. 26:4965-4974(1998).
RN [10]
RP METHYLATION BY HMT1.
RX PubMed=10024178; DOI=10.1017/s1355838299981633;
RA Valentini S.R., Weiss V.H., Silver P.A.;
RT "Arginine methylation and binding of Hrp1p to the efficiency element for
RT mRNA 3'-end formation.";
RL RNA 5:272-280(1999).
RN [11]
RP FUNCTION IN NMD, AND INTERACTION WITH NAM7.
RX PubMed=10882134; DOI=10.1016/s1097-2765(00)80443-8;
RA Gonzalez C.I., Ruiz-Echevarria M.J., Vasudevan S., Henry M.F., Peltz S.W.;
RT "The yeast hnRNP-like protein Hrp1/Nab4 marks a transcript for nonsense-
RT mediated mRNA decay.";
RL Mol. Cell 5:489-499(2000).
RN [12]
RP FUNCTION IN PRE-MRNA 3'-END FORMATION.
RX PubMed=11344258; DOI=10.1073/pnas.101046598;
RA Gross S., Moore C.;
RT "Five subunits are required for reconstitution of the cleavage and
RT polyadenylation activities of Saccharomyces cerevisiae cleavage factor I.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:6080-6085(2001).
RN [13]
RP SUBCELLULAR LOCATION.
RX PubMed=12192043; DOI=10.1128/mcb.22.18.6441-6457.2002;
RA Hammell C.M., Gross S., Zenklusen D., Heath C.V., Stutz F., Moore C.,
RA Cole C.N.;
RT "Coupling of termination, 3' processing, and mRNA export.";
RL Mol. Cell. Biol. 22:6441-6457(2002).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND SER-3, AND
RP IDENTIFICATION BY 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 [15]
RP SUBCELLULAR LOCATION.
RX PubMed=18981231; DOI=10.1083/jcb.200807043;
RA Buchan J.R., Muhlrad D., Parker R.;
RT "P bodies promote stress granule assembly in Saccharomyces cerevisiae.";
RL J. Cell Biol. 183:441-455(2008).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-3; SER-206; THR-458
RP AND SER-462, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-3 AND SER-462, AND
RP IDENTIFICATION BY 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).
RN [18]
RP SUBCELLULAR LOCATION.
RX PubMed=23222640; DOI=10.1038/nsmb.2468;
RA Mitchell S.F., Jain S., She M., Parker R.;
RT "Global analysis of yeast mRNPs.";
RL Nat. Struct. Mol. Biol. 20:127-133(2013).
RN [19]
RP METHYLATION AT ARG-519, AND PHOSPHORYLATION AT SER-2; SER-3; SER-51;
RP SER-87; SER-460 AND SER-462.
RX PubMed=33856219; DOI=10.1021/acs.jproteome.0c00927;
RA Hamey J.J., Nguyen A., Wilkins M.R.;
RT "Discovery of arginine methylation, phosphorylation, and their co-
RT occurrence in condensate-associated proteins in Saccharomyces cerevisiae.";
RL J. Proteome Res. 20:2420-2434(2021).
CC -!- FUNCTION: RNA-binding protein, which is involved in the
CC polyadenylation-dependent pre-mRNA 3'-end formation and cooperates with
CC the cleavage factor CFIA complex and the cleavage and polyadenylation
CC factor (CPF) complex. May be involved in regulation of poly(A) site
CC selection. Is involved in nonsense-mediated mRNA decay. Seems to bind
CC to an RNA downstream sequence element (DSE) located 3' of a nonsense
CC codon and may mark the transcript for decay.
CC {ECO:0000269|PubMed:10882134, ECO:0000269|PubMed:11344258,
CC ECO:0000269|PubMed:9334319, ECO:0000269|PubMed:9857200}.
CC -!- SUBUNIT: Interacts with NAM7. {ECO:0000269|PubMed:10882134}.
CC -!- INTERACTION:
CC Q99383; P38217: KAP104; NbExp=4; IntAct=EBI-11783, EBI-9152;
CC Q99383; P25298: RNA14; NbExp=2; IntAct=EBI-11783, EBI-15632;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9334319,
CC ECO:0000269|PubMed:9499403}. Nucleus {ECO:0000269|PubMed:23222640,
CC ECO:0000269|PubMed:9334319, ECO:0000269|PubMed:9499403}. Cytoplasm,
CC Stress granule {ECO:0000269|PubMed:18981231}.
CC -!- PTM: Methylated by HMT1 (PubMed:9499403, PubMed:10024178). The
CC methylation is required for nuclear export (PubMed:9499403).
CC {ECO:0000269|PubMed:10024178, ECO:0000269|PubMed:9499403}.
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DR EMBL; U35737; AAA79097.1; -; Genomic_DNA.
DR EMBL; U38535; AAB18142.1; -; Genomic_DNA.
DR EMBL; X95258; CAA64546.1; -; Genomic_DNA.
DR EMBL; Z74865; CAA99142.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10661.1; -; Genomic_DNA.
DR PIR; S66820; S66820.
DR RefSeq; NP_014518.1; NM_001183377.1.
DR PDB; 2CJK; NMR; -; A=156-322.
DR PDB; 2KM8; NMR; -; C=156-322.
DR PDBsum; 2CJK; -.
DR PDBsum; 2KM8; -.
DR AlphaFoldDB; Q99383; -.
DR BMRB; Q99383; -.
DR SMR; Q99383; -.
DR BioGRID; 34252; 331.
DR ComplexPortal; CPX-1896; mRNA cleavage factor complex CFI.
DR DIP; DIP-1371N; -.
DR IntAct; Q99383; 34.
DR MINT; Q99383; -.
DR STRING; 4932.YOL123W; -.
DR iPTMnet; Q99383; -.
DR MaxQB; Q99383; -.
DR PaxDb; Q99383; -.
DR PRIDE; Q99383; -.
DR EnsemblFungi; YOL123W_mRNA; YOL123W; YOL123W.
DR GeneID; 853997; -.
DR KEGG; sce:YOL123W; -.
DR SGD; S000005483; HRP1.
DR VEuPathDB; FungiDB:YOL123W; -.
DR eggNOG; KOG4205; Eukaryota.
DR GeneTree; ENSGT00940000175437; -.
DR HOGENOM; CLU_012062_0_2_1; -.
DR InParanoid; Q99383; -.
DR OMA; MQQQTGV; -.
DR BioCyc; YEAST:G3O-33519-MON; -.
DR EvolutionaryTrace; Q99383; -.
DR PRO; PR:Q99383; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q99383; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0010494; C:cytoplasmic stress granule; IDA:SGD.
DR GO; GO:0005849; C:mRNA cleavage factor complex; IPI:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0003729; F:mRNA binding; IDA:SGD.
DR GO; GO:0003723; F:RNA binding; IDA:SGD.
DR GO; GO:0006378; P:mRNA polyadenylation; IDA:SGD.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IEA:UniProtKB-KW.
DR GO; GO:0098789; P:pre-mRNA cleavage required for polyadenylation; IDA:SGD.
DR GO; GO:0072423; P:response to DNA damage checkpoint signaling; IMP:SGD.
DR CDD; cd12577; RRM1_Hrp1p; 1.
DR CDD; cd12330; RRM2_Hrp1p; 1.
DR Gene3D; 3.30.70.330; -; 2.
DR InterPro; IPR034156; Hrp1_RRM1.
DR InterPro; IPR034155; Hrp1_RRM2.
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; 2.
DR SUPFAM; SSF54928; SSF54928; 2.
DR PROSITE; PS50102; RRM; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Methylation;
KW mRNA processing; Nonsense-mediated mRNA decay; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; RNA-binding.
FT CHAIN 1..534
FT /note="Nuclear polyadenylated RNA-binding protein 4"
FT /id="PRO_0000081658"
FT DOMAIN 159..241
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 243..320
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 316..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 415..534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..31
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..81
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..97
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..145
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 324..354
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 419..483
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 484..509
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:33856219,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 3
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:33856219,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 51
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:33856219"
FT MOD_RES 87
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:33856219"
FT MOD_RES 206
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 458
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 460
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:33856219"
FT MOD_RES 462
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:33856219,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 519
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000269|PubMed:33856219"
FT HELIX 157..159
FT /evidence="ECO:0007829|PDB:2CJK"
FT STRAND 160..163
FT /evidence="ECO:0007829|PDB:2CJK"
FT HELIX 172..179
FT /evidence="ECO:0007829|PDB:2CJK"
FT TURN 180..182
FT /evidence="ECO:0007829|PDB:2CJK"
FT STRAND 185..189
FT /evidence="ECO:0007829|PDB:2CJK"
FT TURN 194..196
FT /evidence="ECO:0007829|PDB:2CJK"
FT STRAND 203..209
FT /evidence="ECO:0007829|PDB:2CJK"
FT HELIX 211..218
FT /evidence="ECO:0007829|PDB:2CJK"
FT STRAND 223..226
FT /evidence="ECO:0007829|PDB:2KM8"
FT HELIX 236..241
FT /evidence="ECO:0007829|PDB:2CJK"
FT STRAND 243..250
FT /evidence="ECO:0007829|PDB:2CJK"
FT HELIX 256..264
FT /evidence="ECO:0007829|PDB:2CJK"
FT STRAND 265..267
FT /evidence="ECO:0007829|PDB:2KM8"
FT STRAND 270..273
FT /evidence="ECO:0007829|PDB:2CJK"
FT STRAND 277..281
FT /evidence="ECO:0007829|PDB:2CJK"
FT STRAND 284..293
FT /evidence="ECO:0007829|PDB:2CJK"
FT HELIX 294..302
FT /evidence="ECO:0007829|PDB:2CJK"
FT STRAND 304..306
FT /evidence="ECO:0007829|PDB:2CJK"
FT STRAND 308..311
FT /evidence="ECO:0007829|PDB:2CJK"
FT STRAND 313..317
FT /evidence="ECO:0007829|PDB:2CJK"
SQ SEQUENCE 534 AA; 59650 MW; 1B231069437B093D CRC64;
MSSDEEDFND IYGDDKPTTT EEVKKEEEQN KAGSGTSQLD QLAALQALSS SLNKLNNPNS
NNSSSNNSNQ DTSSSKQDGT ANDKEGSNED TKNEKKQESA TSANANANAS SAGPSGLPWE
QLQQTMSQFQ QPSSQSPPQQ QVTQTKEERS KADLSKESCK MFIGGLNWDT TEDNLREYFG
KYGTVTDLKI MKDPATGRSR GFGFLSFEKP SSVDEVVKTQ HILDGKVIDP KRAIPRDEQD
KTGKIFVGGI GPDVRPKEFE EFFSQWGTII DAQLMLDKDT GQSRGFGFVT YDSADAVDRV
CQNKFIDFKD RKIEIKRAEP RHMQQKSSNN GGNNGGNNMN RRGGNFGNQG DFNQMYQNPM
MGGYNPMMNP QAMTDYYQKM QEYYQQMQKQ TGMDYTQMYQ QQMQQMAMMM PGFAMPPNAM
TLNQPQQDSN ATQGSPAPSD SDNNKSNDVQ TIGNTSNTDS GSPPLNLPNG PKGPSQYNDD
HNSGYGYNRD RGDRDRNDRD RDYNHRSGGN HRRNGRGGRG GYNRRNNGYH PYNR
