PIN3_YEAST
ID PIN3_YEAST Reviewed; 215 AA.
AC Q06449; D6W4F0;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=[PSI+] inducibility protein 3;
DE AltName: Full=LAS seventeen-binding protein 2;
DE Short=LAS17-binding protein 2;
GN Name=PIN3; Synonyms=LSB2; OrderedLocusNames=YPR154W;
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=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
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 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 [4]
RP INTERACTION WITH LAS17.
RX PubMed=10512884; DOI=10.1091/mbc.10.10.3521;
RA Madania A., Dumoulin P., Grava S., Kitamoto H., Scharer-Brodbeck C.,
RA Soulard A., Moreau V., Winsor B.;
RT "The Saccharomyces cerevisiae homologue of human Wiskott-Aldrich syndrome
RT protein Las17p interacts with the Arp2/3 complex.";
RL Mol. Biol. Cell 10:3521-3538(1999).
RN [5]
RP PRION FORMATION.
RX PubMed=11511345; DOI=10.1016/s0092-8674(01)00427-5;
RA Derkatch I.L., Bradley M.E., Hong J.Y., Liebman S.W.;
RT "Prions affect the appearance of other prions: the story of [PIN(+)].";
RL Cell 106:171-182(2001).
RN [6]
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 [7]
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 [8]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-80, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=SUB592;
RX PubMed=12872131; DOI=10.1038/nbt849;
RA Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D., Marsischky G.,
RA Roelofs J., Finley D., Gygi S.P.;
RT "A proteomics approach to understanding protein ubiquitination.";
RL Nat. Biotechnol. 21:921-926(2003).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52 AND SER-55, 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 [10]
RP UBIQUITINATION BY RSP5, AND INTERACTION WITH RSP5.
RX PubMed=22000681; DOI=10.1016/j.ejcb.2011.08.002;
RA Kaminska J., Spiess M., Stawiecka-Mirota M., Monkaityte R.,
RA Haguenauer-Tsapis R., Urban-Grimal D., Winsor B., Zoladek T.;
RT "Yeast Rsp5 ubiquitin ligase affects the actin cytoskeleton in vivo and in
RT vitro.";
RL Eur. J. Cell Biol. 90:1016-1028(2011).
RN [11]
RP FUNCTION, UBIQUITINATION BY RSP5, MUTAGENESIS OF LYS-80; TRP-91;
RP 124-PRO-PRO-125 AND 174-GLN-GLN-175, SUBCELLULAR LOCATION, INDUCTION, AND
RP INTERACTION WITH LAS17 AND SUP35.
RX PubMed=21777813; DOI=10.1016/j.molcel.2011.07.001;
RA Chernova T.A., Romanyuk A.V., Karpova T.S., Shanks J.R., Ali M.,
RA Moffatt N., Howie R.L., O'Dell A., McNally J.G., Liebman S.W.,
RA Chernoff Y.O., Wilkinson K.D.;
RT "Prion induction by the short-lived, stress-induced protein Lsb2 is
RT regulated by ubiquitination and association with the actin cytoskeleton.";
RL Mol. Cell 43:242-252(2011).
RN [12]
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 [13]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-80, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 57-112.
RA Kursula P., Kursula I., Lehmann F., Zou P., Song Y.H., Wilmanns M.;
RT "Structural genomics of yeast SH3 domains.";
RL Submitted (JUN-2005) to the PDB data bank.
CC -!- FUNCTION: Overproduction promotes the de novo induction of the [PSI+]
CC prion form of SUP35. The prion-inducing effect depends on the
CC association with the actin cytoskeleton. Also implicated in prion
CC maintenance during heat stress. {ECO:0000269|PubMed:21777813}.
CC -!- SUBUNIT: Interacts with LAS17, RSP5 and SUP35.
CC {ECO:0000269|PubMed:10512884, ECO:0000269|PubMed:21777813,
CC ECO:0000269|PubMed:22000681}.
CC -!- INTERACTION:
CC Q06449; P53933: APP1; NbExp=4; IntAct=EBI-35523, EBI-28798;
CC Q06449; Q12446: LAS17; NbExp=4; IntAct=EBI-35523, EBI-10022;
CC Q06449; P47075: VTC4; NbExp=2; IntAct=EBI-35523, EBI-25789;
CC Q06449; P40483: YIL108W; NbExp=3; IntAct=EBI-35523, EBI-25176;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:14562095}. Cytoplasm, cytoskeleton, actin patch
CC {ECO:0000269|PubMed:21777813}. Note=When overexpressed, localizes to
CC punctate structures which are reminiscent of cortical actin patches
CC (PubMed:21777813). Transiently colocalizes with SUP35 aggregates during
CC prionogenesis (PubMed:21777813). {ECO:0000269|PubMed:21777813}.
CC -!- INDUCTION: By heat shock. Can thereby reach physiological protein
CC levels high enough to promote prion-formation.
CC {ECO:0000269|PubMed:21777813}.
CC -!- DOMAIN: The PY motif is recognized directly by the WW domains of RSP5.
CC -!- PTM: Ubiquitinated by RSP5. Ubiquitination reduces the protein
CC abundance and its prion-inducing ability. {ECO:0000269|PubMed:21777813,
CC ECO:0000269|PubMed:22000681}.
CC -!- MISCELLANEOUS: Present with 2190 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- MISCELLANEOUS: Although this protein promotes prion formation and it
CC has a Asn/Gln-rich prion-like domain, it does not seem to have a prion
CC form by itself.
CC -!- SIMILARITY: Belongs to the LSB1 family. {ECO:0000305}.
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DR EMBL; U28371; AAB68051.1; -; Genomic_DNA.
DR EMBL; AY692989; AAT93008.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11566.1; -; Genomic_DNA.
DR PIR; S61138; S61138.
DR RefSeq; NP_015480.1; NM_001184251.1.
DR PDB; 1YNZ; X-ray; 2.20 A; A=57-112.
DR PDB; 1ZX6; X-ray; 1.60 A; A=57-112.
DR PDBsum; 1YNZ; -.
DR PDBsum; 1ZX6; -.
DR AlphaFoldDB; Q06449; -.
DR SMR; Q06449; -.
DR BioGRID; 36321; 118.
DR DIP; DIP-6257N; -.
DR IntAct; Q06449; 45.
DR MINT; Q06449; -.
DR STRING; 4932.YPR154W; -.
DR MoonDB; Q06449; Predicted.
DR iPTMnet; Q06449; -.
DR MaxQB; Q06449; -.
DR PaxDb; Q06449; -.
DR PRIDE; Q06449; -.
DR EnsemblFungi; YPR154W_mRNA; YPR154W; YPR154W.
DR GeneID; 856277; -.
DR KEGG; sce:YPR154W; -.
DR SGD; S000006358; PIN3.
DR VEuPathDB; FungiDB:YPR154W; -.
DR eggNOG; KOG3601; Eukaryota.
DR GeneTree; ENSGT00950000182882; -.
DR HOGENOM; CLU_064525_2_0_1; -.
DR InParanoid; Q06449; -.
DR OMA; THIASQT; -.
DR BioCyc; YEAST:G3O-34285-MON; -.
DR EvolutionaryTrace; Q06449; -.
DR PRO; PR:Q06449; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q06449; protein.
DR GO; GO:0030479; C:actin cortical patch; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0034316; P:negative regulation of Arp2/3 complex-mediated actin nucleation; IDA:SGD.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR Pfam; PF00018; SH3_1; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Cytoskeleton; Isopeptide bond;
KW Nucleus; Phosphoprotein; Reference proteome; SH3 domain; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..215
FT /note="[PSI+] inducibility protein 3"
FT /id="PRO_0000268696"
FT DOMAIN 54..113
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 114..189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 124..127
FT /note="PY motif"
FT COMPBIAS 126..153
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 154..168
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..189
FT /note="Polar 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 52
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 55
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CROSSLNK 80
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT MUTAGEN 80
FT /note="K->R: Abolishes formation of ubiquitinated protein
FT forms."
FT /evidence="ECO:0000269|PubMed:21777813"
FT MUTAGEN 91
FT /note="W->S: Abolishes interaction with LAS17, but not with
FT SUP35. Blocks colocalization with actin, aggregation, and
FT prion-inducing ability."
FT /evidence="ECO:0000269|PubMed:21777813"
FT MUTAGEN 124..125
FT /note="PP->AA: Abolishes RSP5 binding site and consequently
FT ubiquitination."
FT /evidence="ECO:0000269|PubMed:21777813"
FT MUTAGEN 174..175
FT /note="QQ->AA: Reduces, but does not abolish the ability to
FT promote [PSI+] induction."
FT /evidence="ECO:0000269|PubMed:21777813"
FT STRAND 58..61
FT /evidence="ECO:0007829|PDB:1ZX6"
FT STRAND 80..86
FT /evidence="ECO:0007829|PDB:1ZX6"
FT STRAND 88..96
FT /evidence="ECO:0007829|PDB:1ZX6"
FT STRAND 99..104
FT /evidence="ECO:0007829|PDB:1ZX6"
FT HELIX 105..107
FT /evidence="ECO:0007829|PDB:1ZX6"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:1ZX6"
SQ SEQUENCE 215 AA; 23539 MW; 37C95425B02FB284 CRC64;
MSASLINRSL TNIRTELDFL KGSNVISNDV YDQINKSLPA KWDPANAPRN ASPASLEYVE
ALYQFDPQQD GDLGLKPGDK VQLLEKLSPE WYKGSCNGRT GIFPANYVKP AFSGSNGPSN
LPPPPQYKAQ ELQQIPTQNS AASSYQQQPF PPPSTNYYQQ PQQQPQQAPP PQQQQQQQQH
QSSHSHLKSF GSKLGNAAIF GAGASIGSDI VNNIF
