Q06449 (PIN3_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
[PSI+] inducibility protein 3

Alternative name(s):
LAS seventeen-binding protein 2
Short name=LAS17-binding protein 2

Gene names

Name:	PIN3
Synonyms:	LSB2
Ordered Locus Names:	YPR154W

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	215 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Overproduction promotes the de novo induction of the [PSI+] prion form of SUP35. The prion-inducing effect depends on the association with the actin cytoskeleton. Also implicated in prion maintenance during heat stress. Ref.11
Subunit structure	Interacts with LAS17, RSP5 and SUP35. Ref.4 Ref.10 Ref.11
Subcellular location	Cytoplasm. Nucleus. Cytoplasm › cytoskeleton › actin patch. Note: When overexpressed, localizes to punctate structures which are reminiscent of cortical actin patches. Transiently colocalizes with SUP35 aggregates during prionogenesis. Ref.6 Ref.11
Induction	By heat shock. Can thereby reach physiological protein levels high enough to promote prion-formation. Ref.11
Domain	The PY motif is recognized directly by the WW domains of RSP5.
Post-translational modification	Ubiquitinated by RSP5. Ubiquitination reduces the protein abundance and its prion-inducing ability. Ref.10 Ref.11
Miscellaneous	Present with 2190 molecules/cell in log phase SD medium. Although this protein promotes prion formation and it has a Asn/Gln-rich prion-like domain, it does not seem to have a prion form by itself.
Sequence similarities	Belongs to the LSB1 family. Contains 1 SH3 domain.

Ontologies

Keywords
Cellular component	Cytoplasm Cytoskeleton Nucleus
Domain	SH3 domain
PTM	Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	actin cytoskeleton organization Inferred from physical interaction Ref.4. Source: SGD
Cellular_component	actin cortical patch Inferred from electronic annotation. Source: UniProtKB-SubCell cytoplasm Inferred from direct assay Ref.6. Source: SGD nucleus Inferred from direct assay Ref.6. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
APP1	P53933	3	EBI-35523,EBI-28798
LAS17	Q12446	10	EBI-35523,EBI-10022

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 215

215

[PSI+] inducibility protein 3

PRO_0000268696

Regions

Domain

54 – 113

60

SH3

Motif

124 – 127

4

PY motif

Compositional bias

122 – 125

4

Poly-Pro

Compositional bias

126 – 181

56

Asn/Gln-rich

Amino acid modifications

Modified residue

52

1

Phosphoserine Ref.9

Cross-link

80

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.8

Experimental info

Mutagenesis

80

1

K → R: Abolishes formation of ubiquitinated protein forms. Ref.11

Mutagenesis

91

1

W → S: Abolishes interaction with LAS17, but not with SUP35. Blocks colocalization with actin, aggregation, and prion-inducing ability. Ref.11

Mutagenesis

124 – 125

2

PP → AA: Abolishes RSP5 binding site and consequently ubiquitination.

Mutagenesis

174 – 175

2

QQ → AA: Reduces, but does not abolish the ability to promote [PSI+] induction.

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

215

Helix Strand Turn

Details...

Beta strand

58 – 61

4

Beta strand

80 – 86

7

Beta strand

88 – 96

9

Beta strand

99 – 104

6

Helix

105 – 107

3

Beta strand

108 – 110

3

Sequences

	Sequence		Length	Mass (Da)
	Q06449 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 37C95425B02FB284	FASTA	215	23,539
	10 20 30 40 50 60 MSASLINRSL TNIRTELDFL KGSNVISNDV YDQINKSLPA KWDPANAPRN ASPASLEYVE 70 80 90 100 110 120 ALYQFDPQQD GDLGLKPGDK VQLLEKLSPE WYKGSCNGRT GIFPANYVKP AFSGSNGPSN 130 140 150 160 170 180 LPPPPQYKAQ ELQQIPTQNS AASSYQQQPF PPPSTNYYQQ PQQQPQQAPP PQQQQQQQQH 190 200 210 QSSHSHLKSF GSKLGNAAIF GAGASIGSDI VNNIF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI." Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M. , Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J. Nature 387:103-105(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[2]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[3]	"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J. Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[4]	"The Saccharomyces cerevisiae homologue of human Wiskott-Aldrich syndrome protein Las17p interacts with the Arp2/3 complex." Madania A., Dumoulin P., Grava S., Kitamoto H., Scharer-Brodbeck C., Soulard A., Moreau V., Winsor B. Mol. Biol. Cell 10:3521-3538(1999) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH LAS17.
[5]	"Prions affect the appearance of other prions: the story of [PIN(+)]." Derkatch I.L., Bradley M.E., Hong J.Y., Liebman S.W. Cell 106:171-182(2001) [PubMed] [Europe PMC] [Abstract] Cited for: PRION FORMATION.
[6]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[7]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[8]	"A proteomics approach to understanding protein ubiquitination." Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D., Marsischky G., Roelofs J., Finley D., Gygi S.P. Nat. Biotechnol. 21:921-926(2003) [PubMed] [Europe PMC] [Abstract] Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-80, MASS SPECTROMETRY. Strain: SUB592.
[9]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52, MASS SPECTROMETRY.
[10]	"Yeast Rsp5 ubiquitin ligase affects the actin cytoskeleton in vivo and in vitro." Kaminska J., Spiess M., Stawiecka-Mirota M., Monkaityte R., Haguenauer-Tsapis R., Urban-Grimal D., Winsor B., Zoladek T. Eur. J. Cell Biol. 90:1016-1028(2011) [PubMed] [Europe PMC] [Abstract] Cited for: UBIQUITINATION BY RSP5, INTERACTION WITH RSP5.
[11]	"Prion induction by the short-lived, stress-induced protein Lsb2 is regulated by ubiquitination and association with the actin cytoskeleton." Chernova T.A., Romanyuk A.V., Karpova T.S., Shanks J.R., Ali M., Moffatt N., Howie R.L., O'Dell A., McNally J.G., Liebman S.W., Chernoff Y.O., Wilkinson K.D. Mol. Cell 43:242-252(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, UBIQUITINATION BY RSP5, MUTAGENESIS OF LYS-80; TRP-91; 124-PRO-PRO-125 AND 174-GLN-GLN-175, SUBCELLULAR LOCATION, INDUCTION, INTERACTION WITH LAS17 AND SUP35.
[12]	"Structural genomics of yeast SH3 domains." Kursula P., Kursula I., Lehmann F., Zou P., Song Y.H., Wilmanns M. Submitted (JUN-2005) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 57-112.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U28371 Genomic DNA. Translation: AAB68051.1.
AY692989 Genomic DNA. Translation: AAT93008.1.
BK006949 Genomic DNA. Translation: DAA11566.1.

PIR

S61138.

RefSeq

NP_015480.1. NM_001184251.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1YNZ	X-ray	2.20	A	57-112	[»]
1ZX6	X-ray	1.60	A	57-112	[»]

ProteinModelPortal

Q06449.

SMR

Q06449. Positions 57-112.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-6257N.

IntAct

Q06449. 20 interactions.

MINT

MINT-374980.

STRING

4932.YPR154W.

Proteomic databases

PaxDb

Q06449.

PeptideAtlas

Q06449.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YPR154W; YPR154W; YPR154W.

GeneID

856277.

KEGG

sce:YPR154W.

Organism-specific databases

CYGD

YPR154w.

SGD

S000006358. PIN3.

Phylogenomic databases

eggNOG

NOG298780.

GeneTree

ENSGT00510000054224.

HOGENOM

HOG000195703.

OMA

SPEWYKG.

OrthoDB

EOG4N606F.

Gene expression databases

Genevestigator

Q06449.

GermOnline

YPR154W. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR000108. p67phox.
IPR001452. SH3_domain.
[Graphical view]

Pfam

PF00018. SH3_1. 1 hit.
[Graphical view]

PRINTS

PR00499. P67PHOX.
PR00452. SH3DOMAIN.

SMART

SM00326. SH3. 1 hit.
[Graphical view]

SUPFAM

SSF50044. SH3. 1 hit.

PROSITE

PS50002. SH3. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q06449.

NextBio

981592.

Entry information

Entry name

PIN3_YEAST

Accession

Primary (citable) accession number: Q06449
Secondary accession number(s): D6W4F0

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 12, 2006
Last sequence update:	November 1, 1996
Last modified:	April 3, 2013
This is version 98 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program