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   02-SEP-2026, entry version 196.
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%3c77::aid-yea887%3e3.0.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=4; IntAct=EBI-22906, EBI-3775;
CC       P43586; Q12389: DBP10; NbExp=6; IntAct=EBI-22906, EBI-5644;
CC       P43586; P32892: DRS1; NbExp=5; IntAct=EBI-22906, EBI-6170;
CC       P43586; P36049: EBP2; NbExp=7; IntAct=EBI-22906, EBI-6289;
CC       P43586; P38911: FPR3; NbExp=4; IntAct=EBI-22906, EBI-6951;
CC       P43586; Q06205: FPR4; NbExp=4; IntAct=EBI-22906, EBI-6956;
CC       P43586; Q03532: HAS1; NbExp=6; 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=7; IntAct=EBI-22906, EBI-29259;
CC       P43586; Q02892: NOG1; NbExp=5; IntAct=EBI-22906, EBI-12105;
CC       P43586; Q08208: NOP12; NbExp=4; IntAct=EBI-22906, EBI-35895;
CC       P43586; P40007: NOP16; NbExp=3; IntAct=EBI-22906, EBI-22439;
CC       P43586; P37838: NOP4; NbExp=5; IntAct=EBI-22906, EBI-12122;
CC       P43586; Q12080: NOP53; NbExp=3; IntAct=EBI-22906, EBI-29395;
CC       P43586; P40010: NUG1; NbExp=5; 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=4; IntAct=EBI-22906, EBI-26762;
CC       P43586; P25582: SPB1; NbExp=5; 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   PDB; 7NAC; EM; 3.04 A; 7=1-204.
DR   PDB; 7R6K; EM; 3.17 A; 7=1-204.
DR   PDB; 7R7A; EM; 3.04 A; 7=1-204.
DR   PDB; 7R7C; EM; 3.71 A; 7=1-204.
DR   PDB; 8V83; EM; 2.53 A; 7=1-204.
DR   PDB; 8V84; EM; 2.70 A; 7=1-204.
DR   PDB; 8V87; EM; 2.66 A; 7=1-204.
DR   AlphaFoldDB; P43586; -.
DR   EMDB; EMD-24269; -.
DR   EMDB; EMD-24280; -.
DR   EMDB; EMD-24296; -.
DR   EMDB; EMD-24297; -.
DR   EMDB; EMD-43017; -.
DR   EMDB; EMD-43021; -.
DR   EMDB; EMD-43027; -.
DR   SMR; P43586; -.
DR   BioGRID; 31149; 192.
DR   DIP; DIP-6615N; -.
DR   FunCoup; P43586; 462.
DR   IntAct; P43586; 97.
DR   MINT; P43586; -.
DR   STRING; 4932.YFR001W; -.
DR   iPTMnet; P43586; -.
DR   PaxDb; 4932-YFR001W; -.
DR   PeptideAtlas; P43586; -.
DR   EnsemblFungi; YFR001W_mRNA; YFR001W; YFR001W.
DR   GeneID; 850551; -.
DR   KEGG; sce:YFR001W; -.
DR   AGR; SGD:S000001897; -.
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   OrthoDB; 1743802at2759; -.
DR   BioCyc; YEAST:G3O-30454-MONOMER; -.
DR   BioGRID-ORCS; 850551; 0 hits in 10 CRISPR screens.
DR   PRO; PR:P43586; -.
DR   Proteomes; UP000002311; Chromosome VI.
DR   RNAct; P43586; protein.
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:0101031; C:protein folding chaperone complex; IMP:SGD.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0140693; F:molecular condensate scaffold activity; IDA:DisProt.
DR   GO; GO:0003729; F:mRNA binding; IDA:SGD.
DR   GO; GO:0043022; F:ribosome binding; IDA:SGD.
DR   GO; GO:0140691; F:RNA folding chaperone; IDA:DisProt.
DR   GO; GO:0033592; F:RNA strand annealing activity; IDA:DisProt.
DR   GO; GO:0019843; F:rRNA binding; IPI:DisProt.
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:0017148; P:negative regulation of translation; IDA: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   DisProt; DP04308; -.
DR   InterPro; IPR037650; Loc1.
DR   InterPro; IPR060655; LOC1_helical.
DR   PANTHER; PTHR28028; 60S RIBOSOMAL SUBUNIT ASSEMBLY/EXPORT PROTEIN LOC1; 1.
DR   PANTHER; PTHR28028:SF1; 60S RIBOSOMAL SUBUNIT ASSEMBLY_EXPORT PROTEIN LOC1; 1.
DR   Pfam; PF28225; LOC1_helical; 1.
DR   PDBsum; 7NAC; -.
DR   PDBsum; 7R6K; -.
DR   PDBsum; 7R7A; -.
DR   PDBsum; 7R7C; -.
DR   PDBsum; 8V83; -.
DR   PDBsum; 8V84; -.
DR   PDBsum; 8V87; -.
PE   1: Evidence at protein level;
KW   3D-structure; Coiled coil; mRNA transport; Nucleus; Phosphoprotein;
KW   Reference proteome; 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        1..11
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        22..31
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        155..164
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        165..177
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        178..195
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"
FT   STRAND          12..15
FT                   /evidence="ECO:0007829|PDB:8V87"
FT   HELIX           24..29
FT                   /evidence="ECO:0007829|PDB:8V87"
FT   HELIX           38..40
FT                   /evidence="ECO:0007829|PDB:8V87"
FT   HELIX           43..46
FT                   /evidence="ECO:0007829|PDB:8V87"
FT   HELIX           47..60
FT                   /evidence="ECO:0007829|PDB:8V87"
FT   TURN            72..74
FT                   /evidence="ECO:0007829|PDB:8V87"
FT   HELIX           78..80
FT                   /evidence="ECO:0007829|PDB:7R7A"
FT   STRAND          83..85
FT                   /evidence="ECO:0007829|PDB:8V87"
FT   HELIX           106..114
FT                   /evidence="ECO:0007829|PDB:8V83"
FT   TURN            118..120
FT                   /evidence="ECO:0007829|PDB:8V87"
FT   HELIX           126..147
FT                   /evidence="ECO:0007829|PDB:8V87"
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
//