ID   PIH1_YEAST              Reviewed;         344 AA.
AC   P38768; D3DKY1;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   27-MAR-2024, entry version 162.
DE   RecName: Full=Protein interacting with Hsp90 1;
DE   AltName: Full=Nucleolar protein 17;
GN   Name=PIH1; Synonyms=NOP17; OrderedLocusNames=YHR034C;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8091229; DOI=10.1126/science.8091229;
RA   Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA   Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA   Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA   Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA   St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA   Waterston R., Wilson R., Vaudin M.;
RT   "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT   VIII.";
RL   Science 265:2077-2082(1994).
RN   [2]
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   [3]
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   [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   INTERACTION WITH HSP90, IDENTIFICATION IN THE R2PT COMPLEX, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=15766533; DOI=10.1016/j.cell.2004.12.024;
RA   Zhao R., Davey M.G., Hsu Y.-C., Kaplanek P., Tong A., Parsons A.B.,
RA   Krogan N.J., Cagney G., Mai D., Greenblatt J.F., Boone C., Emili A.,
RA   Houry W.A.;
RT   "Navigating the chaperone network: an integrative map of physical and
RT   genetic interactions mediated by the hsp90 chaperone.";
RL   Cell 120:715-727(2005).
RN   [6]
RP   INTERACTION WITH NOP53.
RX   PubMed=16128814; DOI=10.1111/j.1742-4658.2005.04861.x;
RA   Granato D.C., Gonzales F.A., Luz J.S., Cassiola F., Machado-Santelli G.M.,
RA   Oliveira C.C.;
RT   "Nop53p, an essential nucleolar protein that interacts with Nop17p and
RT   Nip7p, is required for pre-rRNA processing in Saccharomyces cerevisiae.";
RL   FEBS J. 272:4450-4463(2005).
RN   [7]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH RRP43 AND NOP58.
RX   PubMed=15670595; DOI=10.1016/j.jmb.2004.11.071;
RA   Gonzales F.A., Zanchin N.I., Luz J.S., Oliveira C.C.;
RT   "Characterization of Saccharomyces cerevisiae Nop17p, a novel Nop58p-
RT   interacting protein that is involved in pre-rRNA processing.";
RL   J. Mol. Biol. 346:437-455(2005).
CC   -!- FUNCTION: Involved in pre-rRNA processing and required for the NOP58-
CC       snoRNA interaction. {ECO:0000269|PubMed:15670595}.
CC   -!- SUBUNIT: Component of the R2TP complex composed at least of RVB1, RVB2,
CC       TAH1 and PIH1. Interacts also with HSP90, RRP43, NOP53 and NOP58.
CC       {ECO:0000269|PubMed:15670595, ECO:0000269|PubMed:15766533,
CC       ECO:0000269|PubMed:16128814}.
CC   -!- INTERACTION:
CC       P38768; P02829: HSP82; NbExp=4; IntAct=EBI-24499, EBI-8659;
CC       P38768; Q12499: NOP58; NbExp=3; IntAct=EBI-24499, EBI-12126;
CC       P38768; Q12498: PRM4; NbExp=3; IntAct=EBI-24499, EBI-32462;
CC       P38768; P25359: RRP43; NbExp=2; IntAct=EBI-24499, EBI-1773;
CC       P38768; Q03940: RVB1; NbExp=10; IntAct=EBI-24499, EBI-30712;
CC       P38768; Q12464: RVB2; NbExp=7; IntAct=EBI-24499, EBI-31814;
CC       P38768; P25638: TAH1; NbExp=17; IntAct=EBI-24499, EBI-21956;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC   -!- MISCELLANEOUS: Present with 2610 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the PIH1 family. {ECO:0000305}.
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DR   EMBL; U00062; AAB68914.1; -; Genomic_DNA.
DR   EMBL; BK006934; DAA06725.1; -; Genomic_DNA.
DR   PIR; S46745; S46745.
DR   RefSeq; NP_011899.1; NM_001179164.1.
DR   PDB; 2MNJ; NMR; -; B=257-344.
DR   PDB; 4CGU; X-ray; 2.11 A; B=187-344.
DR   PDB; 4CHH; X-ray; 2.03 A; A/B=1-185.
DR   PDBsum; 2MNJ; -.
DR   PDBsum; 4CGU; -.
DR   PDBsum; 4CHH; -.
DR   AlphaFoldDB; P38768; -.
DR   BMRB; P38768; -.
DR   SMR; P38768; -.
DR   BioGRID; 36465; 268.
DR   ComplexPortal; CPX-1814; R2TP co-chaperone complex.
DR   DIP; DIP-807N; -.
DR   IntAct; P38768; 17.
DR   MINT; P38768; -.
DR   STRING; 4932.YHR034C; -.
DR   MaxQB; P38768; -.
DR   PaxDb; 4932-YHR034C; -.
DR   PeptideAtlas; P38768; -.
DR   EnsemblFungi; YHR034C_mRNA; YHR034C; YHR034C.
DR   GeneID; 856429; -.
DR   KEGG; sce:YHR034C; -.
DR   AGR; SGD:S000001076; -.
DR   SGD; S000001076; PIH1.
DR   VEuPathDB; FungiDB:YHR034C; -.
DR   eggNOG; KOG4356; Eukaryota.
DR   HOGENOM; CLU_072113_0_0_1; -.
DR   InParanoid; P38768; -.
DR   OMA; EWCLESC; -.
DR   OrthoDB; 2725608at2759; -.
DR   BioCyc; YEAST:G3O-31094-MONOMER; -.
DR   BioGRID-ORCS; 856429; 0 hits in 10 CRISPR screens.
DR   PRO; PR:P38768; -.
DR   Proteomes; UP000002311; Chromosome VIII.
DR   RNAct; P38768; Protein.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0005634; C:nucleus; HDA:SGD.
DR   GO; GO:0097255; C:R2TP complex; IDA:SGD.
DR   GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR   GO; GO:0000492; P:box C/D snoRNP assembly; IMP:SGD.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0006457; P:protein folding; IMP:SGD.
DR   GO; GO:0050821; P:protein stabilization; NAS:ComplexPortal.
DR   GO; GO:0008361; P:regulation of cell size; HMP:SGD.
DR   GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR   GO; GO:0006364; P:rRNA processing; IMP:SGD.
DR   Gene3D; 2.60.40.4160; -; 1.
DR   IDEAL; IID50209; -.
DR   InterPro; IPR041441; Pih1_CS_Ascomycota.
DR   InterPro; IPR012981; PIH1_N.
DR   PANTHER; PTHR22997:SF0; PIH1 DOMAIN-CONTAINING PROTEIN 1; 1.
DR   PANTHER; PTHR22997; UNCHARACTERIZED; 1.
DR   Pfam; PF08190; PIH1; 1.
DR   Pfam; PF18482; Pih1_fungal_CS; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; mRNA processing; mRNA splicing; Nucleus;
KW   Reference proteome.
FT   CHAIN           1..344
FT                   /note="Protein interacting with Hsp90 1"
FT                   /id="PRO_0000058440"
FT   REGION          195..222
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        195..209
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   STRAND          29..32
FT                   /evidence="ECO:0007829|PDB:4CHH"
FT   STRAND          35..47
FT                   /evidence="ECO:0007829|PDB:4CHH"
FT   STRAND          49..51
FT                   /evidence="ECO:0007829|PDB:4CHH"
FT   STRAND          58..66
FT                   /evidence="ECO:0007829|PDB:4CHH"
FT   HELIX           78..86
FT                   /evidence="ECO:0007829|PDB:4CHH"
FT   STRAND          100..103
FT                   /evidence="ECO:0007829|PDB:4CHH"
FT   STRAND          109..118
FT                   /evidence="ECO:0007829|PDB:4CHH"
FT   HELIX           119..127
FT                   /evidence="ECO:0007829|PDB:4CHH"
FT   HELIX           129..147
FT                   /evidence="ECO:0007829|PDB:4CHH"
FT   STRAND          149..151
FT                   /evidence="ECO:0007829|PDB:4CHH"
FT   STRAND          153..155
FT                   /evidence="ECO:0007829|PDB:4CHH"
FT   STRAND          160..162
FT                   /evidence="ECO:0007829|PDB:4CHH"
FT   STRAND          164..167
FT                   /evidence="ECO:0007829|PDB:4CHH"
FT   STRAND          171..174
FT                   /evidence="ECO:0007829|PDB:4CHH"
FT   HELIX           175..177
FT                   /evidence="ECO:0007829|PDB:4CHH"
FT   HELIX           180..182
FT                   /evidence="ECO:0007829|PDB:4CHH"
FT   STRAND          262..264
FT                   /evidence="ECO:0007829|PDB:2MNJ"
FT   STRAND          267..273
FT                   /evidence="ECO:0007829|PDB:4CGU"
FT   STRAND          275..278
FT                   /evidence="ECO:0007829|PDB:4CGU"
FT   STRAND          280..287
FT                   /evidence="ECO:0007829|PDB:4CGU"
FT   STRAND          289..291
FT                   /evidence="ECO:0007829|PDB:2MNJ"
FT   STRAND          300..302
FT                   /evidence="ECO:0007829|PDB:4CGU"
FT   TURN            303..306
FT                   /evidence="ECO:0007829|PDB:4CGU"
FT   STRAND          307..309
FT                   /evidence="ECO:0007829|PDB:4CGU"
FT   STRAND          311..313
FT                   /evidence="ECO:0007829|PDB:4CGU"
FT   STRAND          315..317
FT                   /evidence="ECO:0007829|PDB:4CGU"
FT   TURN            326..328
FT                   /evidence="ECO:0007829|PDB:4CGU"
FT   STRAND          330..334
FT                   /evidence="ECO:0007829|PDB:4CGU"
FT   TURN            335..338
FT                   /evidence="ECO:0007829|PDB:4CGU"
FT   STRAND          339..344
FT                   /evidence="ECO:0007829|PDB:4CGU"
SQ   SEQUENCE   344 AA;  39519 MW;  02C06D0A113B1B3B CRC64;
     MADFLLRPIK QRHRNEDKYV SVDAADGSVS KIEPIADFVI KTKLLSANGP EKLQDGRKVF
     INVCHSPLVP KPEVDFNARI VFPLIIQNEW EIPIITSCYR MDHDKKGQEC YVWDCCINSD
     CSRWICDDIQ LREILVEWCL ESCEIRDSVV LCRDRIAFPK MKKKGAELPA LEVLNDELHQ
     DYKAKMHKII EEEAGDPMSI LRGRNDDGDD NNDPDDGTLP PLFPIENKIS GAKIEEIDKN
     EIAHRNLKQA PAPAPAPHEQ QEDVPEYEVK MKRFKGAAYK LRILIENKAP NSKPDRFSPS
     YNFAENILYI NGKLSIPLPR DIVVNAADIK IFHIRKERTL YIYI
//