LOC1_YEAST
ID LOC1_YEAST Reviewed; 204 AA.
AC P43586; D6VTN1;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=60S ribosomal subunit assembly/export protein LOC1;
DE AltName: Full=Localization of ASH1 mRNA protein 1;
GN Name=LOC1; OrderedLocusNames=YFR001W;
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 204511 / S288c / AB972;
RX PubMed=8789262;
RX DOI=10.1002/(sici)1097-0061(199601)12:1<77::aid-yea887>3.0.co;2-5;
RA Naitou M., Ozawa M., Sasanuma S., Kobayashi M., Hagiwara H., Shibata T.,
RA Hanaoka F., Watanabe K., Ono A., Yamazaki M., Tashiro H., Eki T.,
RA Murakami Y.;
RT "Sequencing of a 23 kb fragment from Saccharomyces cerevisiae chromosome
RT VI.";
RL Yeast 12:77-84(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7670463; DOI=10.1038/ng0795-261;
RA Murakami Y., Naitou M., Hagiwara H., Shibata T., Ozawa M., Sasanuma S.,
RA Sasanuma M., Tsuchiya Y., Soeda E., Yokoyama K., Yamazaki M., Tashiro H.,
RA Eki T.;
RT "Analysis of the nucleotide sequence of chromosome VI from Saccharomyces
RT cerevisiae.";
RL Nat. Genet. 10:261-268(1995).
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 FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11309412; DOI=10.1083/jcb.153.2.307;
RA Long R.M., Gu W., Meng X., Gonsalvez G.B., Singer R.H., Chartrand P.;
RT "An exclusively nuclear RNA-binding protein affects asymmetric localization
RT of ASH1 mRNA and Ash1p in yeast.";
RL J. Cell Biol. 153:307-318(2001).
RN [6]
RP INTERACTION WITH NOP7, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=11583614; DOI=10.1016/s1097-2765(01)00344-6;
RA Harnpicharnchai P., Jakovljevic J., Horsey E., Miles T., Roman J., Rout M.,
RA Meagher D., Imai B., Guo Y., Brame C.J., Shabanowitz J., Hunt D.F.,
RA Woolford J.L. Jr.;
RT "Composition and functional characterization of yeast 66S ribosome assembly
RT intermediates.";
RL Mol. Cell 8:505-515(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 INTERACTION WITH RRP1, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15100437; DOI=10.1261/rna.5255804;
RA Horsey E.W., Jakovljevic J., Miles T.D., Harnpicharnchai P.,
RA Woolford J.L. Jr.;
RT "Role of the yeast Rrp1 protein in the dynamics of pre-ribosome
RT maturation.";
RL RNA 10:813-827(2004).
RN [10]
RP INTERACTION WITH RRP15, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15769876; DOI=10.1261/rna.7200205;
RA De Marchis M.L., Giorgi A., Schinina M.E., Bozzoni I., Fatica A.;
RT "Rrp15p, a novel component of pre-ribosomal particles required for 60S
RT ribosome subunit maturation.";
RL RNA 11:495-502(2005).
RN [11]
RP FUNCTION.
RX PubMed=16871394; DOI=10.1007/s00438-006-0151-7;
RA Urbinati C.R., Gonsalvez G.B., Aris J.P., Long R.M.;
RT "Loc1p is required for efficient assembly and nuclear export of the 60S
RT ribosomal subunit.";
RL Mol. Genet. Genomics 276:369-377(2006).
RN [12]
RP INTERACTION WITH SHE2.
RX PubMed=19244342; DOI=10.1091/mbc.e08-11-1151;
RA Shen Z., Paquin N., Forget A., Chartrand P.;
RT "Nuclear shuttling of She2p couples ASH1 mRNA localization to its
RT translational repression by recruiting Loc1p and Puf6p.";
RL Mol. Biol. Cell 20:2265-2275(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24, 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: Required for efficient assembly and nuclear export of the 60S
CC ribosomal subunit. Involved in asymmetric localization of ASH1 mRNA.
CC {ECO:0000269|PubMed:11309412, ECO:0000269|PubMed:16871394}.
CC -!- SUBUNIT: Component of the 66S pre-ribosomal particle. Interacts with
CC NOP7, RRP1, RRP15 and SHE2. {ECO:0000269|PubMed:11583614,
CC ECO:0000269|PubMed:15100437, ECO:0000269|PubMed:15769876,
CC ECO:0000269|PubMed:19244342}.
CC -!- INTERACTION:
CC P43586; Q08235: BRX1; NbExp=3; IntAct=EBI-22906, EBI-3775;
CC P43586; Q12389: DBP10; NbExp=5; IntAct=EBI-22906, EBI-5644;
CC P43586; P32892: DRS1; NbExp=4; IntAct=EBI-22906, EBI-6170;
CC P43586; P36049: EBP2; NbExp=6; IntAct=EBI-22906, EBI-6289;
CC P43586; P38911: FPR3; NbExp=3; IntAct=EBI-22906, EBI-6951;
CC P43586; Q06205: FPR4; NbExp=3; IntAct=EBI-22906, EBI-6956;
CC P43586; Q03532: HAS1; NbExp=5; IntAct=EBI-22906, EBI-8170;
CC P43586; P43586: LOC1; NbExp=3; IntAct=EBI-22906, EBI-22906;
CC P43586; Q12176: MAK21; NbExp=3; IntAct=EBI-22906, EBI-10944;
CC P43586; P38112: MAK5; NbExp=3; IntAct=EBI-22906, EBI-10394;
CC P43586; P39744: NOC2; NbExp=6; IntAct=EBI-22906, EBI-29259;
CC P43586; Q02892: NOG1; NbExp=4; IntAct=EBI-22906, EBI-12105;
CC P43586; Q08208: NOP12; NbExp=3; IntAct=EBI-22906, EBI-35895;
CC P43586; P37838: NOP4; NbExp=4; IntAct=EBI-22906, EBI-12122;
CC P43586; Q12080: NOP53; NbExp=3; IntAct=EBI-22906, EBI-29395;
CC P43586; P40010: NUG1; NbExp=4; IntAct=EBI-22906, EBI-22449;
CC P43586; P53131: PRP43; NbExp=3; IntAct=EBI-22906, EBI-505;
CC P43586; Q12754: RRP12; NbExp=3; IntAct=EBI-22906, EBI-30678;
CC P43586; P36080: RRP14; NbExp=3; IntAct=EBI-22906, EBI-26762;
CC P43586; P25582: SPB1; NbExp=4; IntAct=EBI-22906, EBI-17814;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:11309412,
CC ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 3650 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the LOC1 family. {ECO:0000305}.
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DR EMBL; D50617; BAA09240.1; -; Genomic_DNA.
DR EMBL; AY557809; AAS56135.1; -; Genomic_DNA.
DR EMBL; BK006940; DAA12441.1; -; Genomic_DNA.
DR PIR; S56256; S56256.
DR RefSeq; NP_116656.1; NM_001179966.1.
DR AlphaFoldDB; P43586; -.
DR SMR; P43586; -.
DR BioGRID; 31149; 161.
DR DIP; DIP-6615N; -.
DR IntAct; P43586; 72.
DR MINT; P43586; -.
DR STRING; 4932.YFR001W; -.
DR iPTMnet; P43586; -.
DR MaxQB; P43586; -.
DR PaxDb; P43586; -.
DR PRIDE; P43586; -.
DR EnsemblFungi; YFR001W_mRNA; YFR001W; YFR001W.
DR GeneID; 850551; -.
DR KEGG; sce:YFR001W; -.
DR SGD; S000001897; LOC1.
DR VEuPathDB; FungiDB:YFR001W; -.
DR eggNOG; ENOG502RY6R; Eukaryota.
DR HOGENOM; CLU_096593_1_0_1; -.
DR InParanoid; P43586; -.
DR OMA; RESMNTI; -.
DR BioCyc; YEAST:G3O-30454-MON; -.
DR PRO; PR:P43586; -.
DR Proteomes; UP000002311; Chromosome VI.
DR RNAct; P43586; protein.
DR GO; GO:0101031; C:chaperone complex; IMP:SGD.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005730; C:nucleolus; IDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0030687; C:preribosome, large subunit precursor; IDA:SGD.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0003729; F:mRNA binding; IDA:SGD.
DR GO; GO:0000480; P:endonucleolytic cleavage in 5'-ETS of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR GO; GO:0000447; P:endonucleolytic cleavage in ITS1 to separate SSU-rRNA from 5.8S rRNA and LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR GO; GO:0000472; P:endonucleolytic cleavage to generate mature 5'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR GO; GO:0008298; P:intracellular mRNA localization; IMP:SGD.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0017148; P:negative regulation of translation; IDA:SGD.
DR GO; GO:0050821; P:protein stabilization; IMP:SGD.
DR GO; GO:0042273; P:ribosomal large subunit biogenesis; IMP:SGD.
DR GO; GO:0000055; P:ribosomal large subunit export from nucleus; IMP:SGD.
DR InterPro; IPR037650; Loc1.
DR PANTHER; PTHR28028; PTHR28028; 1.
PE 1: Evidence at protein level;
KW Coiled coil; mRNA transport; Nucleus; Phosphoprotein; Reference proteome;
KW Ribosome biogenesis; Transport.
FT CHAIN 1..204
FT /note="60S ribosomal subunit assembly/export protein LOC1"
FT /id="PRO_0000202680"
FT REGION 1..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 155..204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 120..166
FT /evidence="ECO:0000255"
FT COMPBIAS 22..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..56
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 155..198
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 204 AA; 23590 MW; 69970294E9C980F9 CRC64;
MAPKKPSKRQ NLRREVAPEV FQDSQARNQL ANVPHLTEKS AQRKPSKTKV KKEQSLARLY
GAKKDKKGKY SEKDLNIPTL NRAIVPGVKI RRGKKGKKFI ADNDTLTLNR LITTIGDKYD
DIAESKLEKA RRLEEIRELK RKEIERKEAL KQDKLEEKKD EIKKKSSVAR TIRRKNKRDM
LKSEAKASES KTEGRKVKKV SFAQ
