LHP1_YEAST
ID LHP1_YEAST Reviewed; 275 AA.
AC P33399; D6VRU5;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 2.
DT 03-AUG-2022, entry version 197.
DE RecName: Full=La protein homolog;
DE AltName: Full=La autoantigen homolog;
DE AltName: Full=La ribonucleoprotein;
GN Name=LHP1; Synonyms=LAH1, YLA1; OrderedLocusNames=YDL051W;
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 CHARACTERIZATION.
RC STRAIN=YPH501;
RX PubMed=8035818; DOI=10.1128/mcb.14.8.5412-5424.1994;
RA Yoo C.J., Wolin S.L.;
RT "La proteins from Drosophila melanogaster and Saccharomyces cerevisiae: a
RT yeast homolog of the La autoantigen is dispensable for growth.";
RL Mol. Cell. Biol. 14:5412-5424(1994).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 101-275, AND CHARACTERIZATION.
RX PubMed=7799435; DOI=10.1006/jmbi.1994.0008;
RA Lin-Marq N., Clarkson S.G.;
RT "A yeast RNA binding protein that resembles the human autoantigen La.";
RL J. Mol. Biol. 245:81-85(1995).
RN [6]
RP NUCLEOTIDE SEQUENCE OF 1-252.
RX PubMed=8408076; DOI=10.1016/s0021-9258(20)80661-9;
RA Nagiec M.M., Wells G.B., Lester R.L., Dickson R.C.;
RT "A suppressor gene that enables Saccharomyces cerevisiae to grow without
RT making sphingolipids encodes a protein that resembles an Escherichia coli
RT fatty acyltransferase.";
RL J. Biol. Chem. 268:22156-22163(1993).
RN [7]
RP FUNCTION.
RX PubMed=9150139; DOI=10.1016/s0092-8674(00)80220-2;
RA Yoo C.J., Wolin S.L.;
RT "The yeast La protein is required for the 3' endonucleolytic cleavage that
RT matures tRNA precursors.";
RL Cell 89:393-402(1997).
RN [8]
RP INTERACTION WITH SXM1, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=9412461; DOI=10.1083/jcb.139.7.1655;
RA Rosenblum J.S., Pemberton L.F., Blobel G.;
RT "A nuclear import pathway for a protein involved in tRNA maturation.";
RL J. Cell Biol. 139:1655-1661(1997).
RN [9]
RP FUNCTION, AND U6 RNA-BINDING.
RX PubMed=9857199; DOI=10.1093/emboj/17.24.7442;
RA Pannone B.K., Xue D., Wolin S.L.;
RT "A role for the yeast La protein in U6 snRNP assembly: evidence that the La
RT protein is a molecular chaperone for RNA polymerase III transcripts.";
RL EMBO J. 17:7442-7453(1998).
RN [10]
RP FUNCTION.
RX PubMed=9851972; DOI=10.1101/gad.12.23.3650;
RA Anderson J., Phan L., Cuesta R., Carlson B.A., Pak M., Asano K.,
RA Bjoerk G.R., Tamame M., Hinnebusch A.G.;
RT "The essential Gcd10p-Gcd14p nuclear complex is required for 1-
RT methyladenosine modification and maturation of initiator methionyl-tRNA.";
RL Genes Dev. 12:3650-3662(1998).
RN [11]
RP INTERACTION WITH SXM1, AND SUBCELLULAR LOCATION.
RX PubMed=9817748; DOI=10.1083/jcb.143.4.887;
RA Rosenblum J.S., Pemberton L.F., Bonifaci N., Blobel G.;
RT "Nuclear import and the evolution of a multifunctional RNA-binding
RT protein.";
RL J. Cell Biol. 143:887-899(1998).
RN [12]
RP FUNCTION, AND RNA-BINDING.
RX PubMed=10385518; DOI=10.1083/jcb.145.7.1369;
RA Dechampesme A.M., Koroleva O., Leger-Silvestre I., Gas N., Camier S.;
RT "Assembly of 5S ribosomal RNA is required at a specific step of the pre-
RT rRNA processing pathway.";
RL J. Cell Biol. 145:1369-1380(1999).
RN [13]
RP SUBCELLULAR LOCATION.
RX PubMed=10564276; DOI=10.1091/mbc.10.11.3849;
RA Sobel S.G., Wolin S.L.;
RT "Two yeast La motif-containing proteins are RNA-binding proteins that
RT associate with polyribosomes.";
RL Mol. Biol. Cell 10:3849-3862(1999).
RN [14]
RP FUNCTION.
RX PubMed=10330157; DOI=10.1128/mcb.19.6.4167;
RA Calvo O., Cuesta R., Anderson J., Gutierrez N., Garcia-Barrio M.T.,
RA Hinnebusch A.G., Tamame M.;
RT "GCD14p, a repressor of GCN4 translation, cooperates with Gcd10p and Lhp1p
RT in the maturation of initiator methionyl-tRNA in Saccharomyces
RT cerevisiae.";
RL Mol. Cell. Biol. 19:4167-4181(1999).
RN [15]
RP FUNCTION, AND RNA-BINDING.
RX PubMed=10747032; DOI=10.1093/emboj/19.7.1650;
RA Xue D., Rubinson D.A., Pannone B.K., Yoo C.J., Wolin S.L.;
RT "U snRNP assembly in yeast involves the La protein.";
RL EMBO J. 19:1650-1660(2000).
RN [16]
RP FUNCTION, AND RNA-BINDING.
RX PubMed=10891482; DOI=10.1128/mcb.20.15.5415-5424.2000;
RA Kufel J., Allmang C., Chanfreau G., Petfalski E., Lafontaine D.L.,
RA Tollervey D.;
RT "Precursors to the U3 small nucleolar RNA lack small nucleolar RNP proteins
RT but are stabilized by La binding.";
RL Mol. Cell. Biol. 20:5415-5424(2000).
RN [17]
RP FUNCTION.
RX PubMed=11333229; DOI=10.1093/genetics/158.1.187;
RA Pannone B.K., Kim S.D., Noe D.A., Wolin S.L.;
RT "Multiple functional interactions between components of the Lsm2-Lsm8
RT complex, U6 snRNA, and the yeast La protein.";
RL Genetics 158:187-196(2001).
RN [18]
RP PHOSPHORYLATION AT SER-15; SER-19 AND SER-235, IDENTIFICATION BY MASS
RP SPECTROMETRY, FUNCTION, AND MUTAGENESIS OF SER-15; SER-19 AND SER-235.
RX PubMed=11720288;
RA Long K.S., Cedervall T., Walch-Solimena C., Noe D.A., Huddleston M.J.,
RA Annan R.S., Wolin S.L.;
RT "Phosphorylation of the Saccharomyces cerevisiae La protein does not appear
RT to be required for its functions in tRNA maturation and nascent RNA
RT stabilization.";
RL RNA 7:1589-1602(2001).
RN [19]
RP FUNCTION, AND RNA-BINDING.
RX PubMed=12077351; DOI=10.1128/mcb.22.14.5248-5256.2002;
RA Kufel J., Allmang C., Verdone L., Beggs J.D., Tollervey D.;
RT "Lsm proteins are required for normal processing of pre-tRNAs and their
RT efficient association with La-homologous protein Lhp1p.";
RL Mol. Cell. Biol. 22:5248-5256(2002).
RN [20]
RP FUNCTION.
RX PubMed=14657028; DOI=10.1093/emboj/cdg625;
RA Chakshusmathi G., Kim S.D., Rubinson D.A., Wolin S.L.;
RT "A La protein requirement for efficient pre-tRNA folding.";
RL EMBO J. 22:6562-6572(2003).
RN [21]
RP FUNCTION.
RX PubMed=12828645; DOI=10.1046/j.1365-2958.2003.03568.x;
RA Aye M., Sandmeyer S.B.;
RT "Ty3 requires yeast La homologous protein for wild-type frequencies of
RT transposition.";
RL Mol. Microbiol. 49:501-515(2003).
RN [22]
RP FUNCTION.
RX PubMed=14627812; DOI=10.1093/nar/gkg904;
RA Kufel J., Allmang C., Verdone L., Beggs J., Tollervey D.;
RT "A complex pathway for 3' processing of the yeast U3 snoRNA.";
RL Nucleic Acids Res. 31:6788-6797(2003).
RN [23]
RP RNA-BINDING.
RX PubMed=14704279; DOI=10.1073/pnas.0307425100;
RA Inada M., Guthrie C.;
RT "Identification of Lhp1p-associated RNAs by microarray analysis in
RT Saccharomyces cerevisiae reveals association with coding and noncoding
RT RNAs.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:434-439(2004).
RN [24]
RP FUNCTION.
RX PubMed=15579677; DOI=10.1534/genetics.104.028126;
RA Aye M., Irwin B., Beliakova-Bethell N., Chen E., Garrus J., Sandmeyer S.;
RT "Host factors that affect Ty3 retrotransposition in Saccharomyces
RT cerevisiae.";
RL Genetics 168:1159-1176(2004).
RN [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, 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 [26]
RP FUNCTION.
RX PubMed=16581807; DOI=10.1261/rna.2307206;
RA Copela L.A., Chakshusmathi G., Sherrer R.L., Wolin S.L.;
RT "The La protein functions redundantly with tRNA modification enzymes to
RT ensure tRNA structural stability.";
RL RNA 12:644-654(2006).
RN [27]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, 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 [28]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15; SER-19; SER-230; SER-233
RP AND SER-235, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [29]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15 AND SER-19, 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 [30]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, 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).
RN [31]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [32]
RP METHYLATION AT ARG-104.
RX PubMed=23865587; DOI=10.1021/pr400556c;
RA Low J.K., Hart-Smith G., Erce M.A., Wilkins M.R.;
RT "Analysis of the proteome of Saccharomyces cerevisiae for methylarginine.";
RL J. Proteome Res. 12:3884-3899(2013).
CC -!- FUNCTION: Molecular chaperone that binds nascent RNA polymerase III
CC transcripts, stabilizing these RNAs against exonucleases. Required for
CC the 3' endonucleolytic cleavage that matures tRNA precursors and for
CC efficient folding of certain pre-tRNAs. Cooperates with GCD14 in the
CC maturation of a subset of RNA polymerase III transcripts. Functions
CC also in the assembly of certain RNA polymerase II-transcribed RNAs into
CC RNPs. Binds and stabilizes newly synthesized U6 snRNA as well as
CC precursors of U3 snRNA from degradation. Facilitates efficient Sm
CC protein binding, thus assisting formation of the U4/U6 snRNP. Required
CC for Ty3 normal transposition frequency. {ECO:0000269|PubMed:10330157,
CC ECO:0000269|PubMed:10385518, ECO:0000269|PubMed:10747032,
CC ECO:0000269|PubMed:10891482, ECO:0000269|PubMed:11333229,
CC ECO:0000269|PubMed:11720288, ECO:0000269|PubMed:12077351,
CC ECO:0000269|PubMed:12828645, ECO:0000269|PubMed:14627812,
CC ECO:0000269|PubMed:14657028, ECO:0000269|PubMed:15579677,
CC ECO:0000269|PubMed:16581807, ECO:0000269|PubMed:9150139,
CC ECO:0000269|PubMed:9412461, ECO:0000269|PubMed:9851972,
CC ECO:0000269|PubMed:9857199}.
CC -!- SUBUNIT: Interacts with SXM1. {ECO:0000269|PubMed:9412461,
CC ECO:0000269|PubMed:9817748}.
CC -!- INTERACTION:
CC P33399; P33203: PRP40; NbExp=2; IntAct=EBI-10046, EBI-701;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10564276,
CC ECO:0000269|PubMed:9412461, ECO:0000269|PubMed:9817748}. Note=Imported
CC into nucleus by the nuclear transport factor SXM1.
CC -!- PTM: Phosphorylation is not required for the roles tRNA and snRNP
CC biogenesis. {ECO:0000269|PubMed:11720288}.
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DR EMBL; L33023; AAA21777.1; -; Genomic_DNA.
DR EMBL; Z74099; CAA98612.1; -; Genomic_DNA.
DR EMBL; AY558373; AAS56699.1; -; Genomic_DNA.
DR EMBL; L13282; AAA16515.1; -; Unassigned_DNA.
DR EMBL; X80801; CAA56782.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11805.1; -; Genomic_DNA.
DR PIR; B48600; B48600.
DR RefSeq; NP_010232.1; NM_001180110.1.
DR AlphaFoldDB; P33399; -.
DR SMR; P33399; -.
DR BioGRID; 32008; 164.
DR DIP; DIP-6444N; -.
DR IntAct; P33399; 21.
DR MINT; P33399; -.
DR STRING; 4932.YDL051W; -.
DR iPTMnet; P33399; -.
DR MaxQB; P33399; -.
DR PaxDb; P33399; -.
DR PRIDE; P33399; -.
DR EnsemblFungi; YDL051W_mRNA; YDL051W; YDL051W.
DR GeneID; 851509; -.
DR KEGG; sce:YDL051W; -.
DR SGD; S000002209; LHP1.
DR VEuPathDB; FungiDB:YDL051W; -.
DR eggNOG; KOG0118; Eukaryota.
DR GeneTree; ENSGT00830000128380; -.
DR HOGENOM; CLU_043291_0_0_1; -.
DR InParanoid; P33399; -.
DR OMA; MNFPHED; -.
DR BioCyc; YEAST:G3O-29469-MON; -.
DR PRO; PR:P33399; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P33399; protein.
DR GO; GO:0005730; C:nucleolus; IDA:SGD.
DR GO; GO:0005654; C:nucleoplasm; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0030532; C:small nuclear ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:0097322; F:7SK snRNA binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IDA:SGD.
DR GO; GO:0000049; F:tRNA binding; IDA:SGD.
DR GO; GO:0017070; F:U6 snRNA binding; IDA:UniProtKB.
DR GO; GO:0000494; P:box C/D RNA 3'-end processing; IBA:GO_Central.
DR GO; GO:0048024; P:regulation of mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0008033; P:tRNA processing; IMP:SGD.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR045180; La_dom_prot.
DR InterPro; IPR006630; La_HTH.
DR InterPro; IPR002344; Lupus_La.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR22792; PTHR22792; 1.
DR Pfam; PF05383; La; 1.
DR Pfam; PF00076; RRM_1; 1.
DR PRINTS; PR00302; LUPUSLA.
DR SMART; SM00715; LA; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50961; HTH_LA; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW Acetylation; Methylation; Nucleus; Phosphoprotein; Reference proteome;
KW RNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..275
FT /note="La protein homolog"
FT /id="PRO_0000207608"
FT DOMAIN 23..112
FT /note="HTH La-type RNA-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00332"
FT DOMAIN 123..216
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 222..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 240..256
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 234..249
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..275
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:11720288,
FT ECO:0007744|PubMed:17287358, ECO:0007744|PubMed:18407956"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:11720288,
FT ECO:0007744|PubMed:15665377, ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 104
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000269|PubMed:23865587"
FT MOD_RES 230
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 233
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 235
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:11720288,
FT ECO:0007744|PubMed:17287358"
FT MUTAGEN 15
FT /note="S->A: Prevents phosphorylation; when associated with
FT A-19 and A-235."
FT /evidence="ECO:0000269|PubMed:11720288"
FT MUTAGEN 19
FT /note="S->A: Prevents phosphorylation; when associated with
FT A-15 and A-235."
FT /evidence="ECO:0000269|PubMed:11720288"
FT MUTAGEN 235
FT /note="S->A: Prevents phosphorylation; when associated with
FT A-15 and A-19."
FT /evidence="ECO:0000269|PubMed:11720288"
SQ SEQUENCE 275 AA; 32104 MW; 43CDB2E6C740978D CRC64;
MSEKPQQEEQ EKPQSRRNSF AVIEFTPEVL DRCLKQVEFY FSEFNFPYDR FLRTTAEKND
GWVPISTIAT FNRMKKYRPV DKVIEALRSS EILEVSADGE NVKRRVPLDL TAARNARIEQ
NQRTLAVMNF PHEDVEASQI PELQENLEAF FKKLGEINQV RLRRDHRNKK FNGTVLVEFK
TIPECEAFLK SYSNDDESNE ILSYEGKKLS VLTKKQFDLQ REASKSKNFS GRSRSFNGHK
KKNLPKFPKN KKKNGKEESK EDSSAIADDD EEHKE
