Proline-rich protein LAS17 - Saccharomyces cerevisiae (Baker's yeast)

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Reviewed, UniProtKB/Swiss-Prot Q12446 (LAS17_YEAST)

Last modified June 16, 2009. Version 74. History...

Clusters with 100%, 90%, 50% identity |

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
Proline-rich protein LAS17

Gene names

Name:	LAS17
Ordered Locus Names:	YOR181W

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

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Protein attributes

Sequence length	633 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Subunit structure

Interacts with KRE6, LSB3, LSB5 and YSC84. Ref.3 Ref.4

Miscellaneous

Present with 8580 molecules/cell in log phase SD medium. Ref.5

Sequence similarities

Contains 1 WH1 domain.

Contains 1 WH2 domain.

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Ontologies

Keywords
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	actin cortical patch localization Inferred from genetic interaction. Source: SGD actin polymerization or depolymerization Inferred from direct assay. Source: SGD bipolar cellular bud site selection Traceable author statement. Source: SGD endocytosis Traceable author statement. Source: SGD positive regulation of actin filament bundle formation Inferred from direct assay. Source: SGD response to osmotic stress Traceable author statement. Source: SGD
Cellular component	actin cortical patch Ref.3 Inferred from direct assay. Source: SGD mating projection tip Inferred from direct assay. Source: SGD
Molecular function	cytoskeletal protein binding Inferred from direct assay. Source: SGD identical protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct
itself		1	EBI-10022,EBI-10022
ACT1	P60010	2	EBI-10022,EBI-2169
ARC15	P40518	1	EBI-10022,EBI-2750
ARC18	Q05933	1	EBI-10022,EBI-2764
ARC19	P33204	1	EBI-10022,EBI-2757
ARC35	P53731	1	EBI-10022,EBI-2770
ARC40	P38328	2	EBI-10022,EBI-2777
ARP2	P32381	2	EBI-10022,EBI-2927
BBC1	P47068	2	EBI-10022,EBI-3437
BZZ1	P38822	6	EBI-10022,EBI-3889
CYK2	Q05080	2	EBI-10022,EBI-5412
END3	P39013	1	EBI-10022,EBI-6460
LSB1	P53281	5	EBI-10022,EBI-23329
LSB3	P43603	6	EBI-10022,EBI-22980
LSB5	P25369	4	EBI-10022,EBI-10218
MYO3	P36006	2	EBI-10022,EBI-11670
MYO5	Q04439	4	EBI-10022,EBI-11687
PIN3	Q06449	5	EBI-10022,EBI-35523
RVS167	P39743	6	EBI-10022,EBI-14500
SLA2	P33338	1	EBI-10022,EBI-17323
SSU81	P40073	2	EBI-10022,EBI-18140
SYP1	P25623	1	EBI-10022,EBI-21900
VRP1	P37370	3	EBI-10022,EBI-20502
YSC84	P32793	7	EBI-10022,EBI-24460

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 633

633

Proline-rich protein LAS17

PRO_0000084361

Regions

Domain

16 – 127

112

WH1

Domain

547 – 567

WH2

Compositional bias

185 – 529

345

Pro-rich

Compositional bias

185 – 190

Poly-Pro

Compositional bias

323 – 329

Poly-Pro

Compositional bias

342 – 348

Poly-Pro

Compositional bias

352 – 358

Poly-Pro

Compositional bias

385 – 391

Poly-Pro

Compositional bias

427 – 431

Poly-Pro

Compositional bias

470 – 474

Poly-Pro

Compositional bias

503 – 507

Poly-Pro

Compositional bias

520 – 526

Poly-Pro

Amino acid modifications

Modified residue

586

Phosphoserine Ref.6

Modified residue

588

Phosphoserine Ref.6 Ref.7

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Sequences

Sequence

Length

Mass (Da)

Tools

Q12446-1 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: 4488355563AA2645
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FASTA

633

67,572

        10         20         30         40         50         60 
MGLLNSSDKE IIKRALPKAS NKIIDVTVAR LYIAYPDKNE WQYTGLSGAL ALVDDLVGNT 

        70         80         90        100        110        120 
FFLKLVDING HRGVIWDQEL YVNFEYYQDR TFFHTFEMEE CFAGLLFVDI NEASHFLKRV 

       130        140        150        160        170        180 
QKRERYANRK TLLNKNAVAL TKKVREEQKS QVVHGPRGES LIDNQRKRYN YEDVDTIPTT 

       190        200        210        220        230        240 
KHKAPPPPPP TAETFDSDQT SSFSDINSTT ASAPTTPAPA LPPASPEVRK EETHPKHSLP 

       250        260        270        280        290        300 
PLPNQFAPLP DPPQHNSPPQ NNAPSQPQSN PFPFPIPEIP STQSATNPFP FPVPQQQFNQ 

       310        320        330        340        350        360 
APSMGIPQQN RPLPQLPNRN NRPVPPPPPM RTTTEGSGVR LPAPPPPPRR GPAPPPPPHR 

       370        380        390        400        410        420 
HVTSNTLNSA GGNSLLPQAT GRRGPAPPPP PRASRPTPNV TMQQNPQQYN NSNRPFGYQT 

       430        440        450        460        470        480 
NSNMSSPPPP PVTTFNTLTP QMTAATGQPA VPLPQNTQAP SQATNVPVAP PPPPASLGQS 

       490        500        510        520        530        540 
QIPQSAPSAP IPPTLPSTTS AAPPPPPAFL TQQPQSGGAP APPPPPQMPA TSTSGGGSFA 

       550        560        570        580        590        600 
ETTGDAGRDA LLASIRGAGG IGALRKVDKS QLDKPSVLLQ EARGESASPP AAAGNGGTPG 

       610        620        630 
GPPASLADAL AAALNKRKTK VGAHDDMDNG DDW

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Yeast mutants sensitive to local anesthetics." Toh-e A. Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XV." Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D. Kleine K. Nature 387:98-102(1997) [PubMed: 9169874] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[3]	"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: 10512884] [Abstract] Cited for: INTERACTION WITH LSB3; LSB5 AND YSC84.
[4]	"Actin patch assembly proteins Las17p and Sla1p restrict cell wall growth to daughter cells and interact with cis-Golgi protein Kre6p." Li H., Page N., Bussey H. Yeast 19:1097-1112(2002) [PubMed: 12237851] [Abstract] Cited for: INTERACTION WITH KRE6.
[5]	"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: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[6]	"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: 17563356] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-586 AND SER-588, MASS SPECTROMETRY.
[7]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-588, MASS SPECTROMETRY.
+	Additional computationally mapped references.

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Cross-references

Sequence databases

D78487 Genomic DNA. Translation: BAA11386.1.
Z75089 Genomic DNA. Translation: CAA99390.1.

PIR

S62057.

RefSeq

NP_014824.1.

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1ZUK	X-ray	1.90	C	350-360	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:963N.

IntAct

Q12446. 53 interactions.

Genome annotation databases

Ensembl

YOR181W. Saccharomyces cerevisiae. [Contig view]

GeneID

854353.

GenomeReviews

Gene locus YOR181W in contig Y13140_GR.

KEGG

sce:YOR181W.

NMPDR

fig|4932.3.peg.5932.

Organism-specific databases

CYGD

YOR181w.

SGD

S000005707. LAS17.

Yeast-GFP

Search...

Phylogenomic databases

HOGENOM

Q12446.

OMA

Q12446. LYIAYPD.

Gene expression databases

ArrayExpress

Q12446.

GermOnline

YOR181W. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR000697. EVH1.
IPR011993. PH_type.
IPR003124. WH2_actin_bd.
[Graphical view]

Gene3D

G3DSA:2.30.29.30. PH_type. 1 hit.

Pfam

PF00568. WH1. 1 hit.
PF02205. WH2. 1 hit.
[Graphical view]

SMART

SM00461. WH1. 1 hit.
SM00246. WH2. 1 hit.
[Graphical view]

PROSITE

PS50229. WH1. 1 hit.
PS51082. WH2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

976446.

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Entry information

Entry name

LAS17_YEAST

Accession

Primary (citable) accession number: Q12446

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1997
Last modified:	June 16, 2009
This is version 74 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)

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Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents