P32525 (ECM25_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein ECM25

Alternative name(s):
Extracellular matrix protein 25

Gene names

Name:	ECM25
Ordered Locus Names:	YJL201W
ORF Names:	J0325

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	599 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	May be involved in cell wall organization and biogenesis.
Subcellular location	Cytoplasm Ref.8.
Miscellaneous	Present with 1750 molecules/cell in log phase SD medium. Ref.9
Sequence similarities	Contains 1 Rho-GAP domain.

Ontologies

Keywords
Biological process	Cell wall biogenesis/degradation
Cellular component	Cytoplasm
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	filamentous growth Inferred from mutant phenotype. Source: SGD fungal-type cell wall organization Inferred from mutant phenotype Ref.6. Source: SGD signal transduction Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from direct assay Ref.8. Source: SGD
Molecular function	protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
SLA1	P32790	3	EBI-26215,EBI-17313

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 599	599	Protein ECM25		PRO_0000086918
Regions
	Domain	181 – 359	179	Rho-GAP
	Compositional bias	363 – 493	131	Ser-rich
Amino acid modifications
	Modified residue	402	1	Phosphoserine Ref.7
	Modified residue	408	1	Phosphoserine Ref.11 Ref.12
	Modified residue	411	1	Phosphoserine Ref.10 Ref.11 Ref.12
	Modified residue	413	1	Phosphothreonine Ref.12
	Modified residue	436	1	Phosphoserine Ref.12
	Modified residue	458	1	Phosphothreonine Ref.12
	Modified residue	461	1	Phosphoserine Ref.12
	Modified residue	471	1	Phosphoserine Ref.12
	Modified residue	492	1	Phosphoserine Ref.12
	Modified residue	493	1	Phosphoserine Ref.12
	Modified residue	494	1	Phosphothreonine Ref.12

Sequences

	Sequence		Length	Mass (Da)
	P32525 [UniParc]. Last modified February 1, 1995. Version 2. Checksum: 0A23F564E04597DE	FASTA	599	68,464
	10 20 30 40 50 60 MIDINVNNIF FRSYSVDPNS GHAIYVFDST YLPASDEIGD KQVYDLLINA LMDRLVMKLP 70 80 90 100 110 120 QAPYSLVIFS SGFSQRKISW VYGIKMFAKL PKETKFYLQK IFIVHESFFV RSVYQVISNA 130 140 150 160 170 180 MNFNFLDSKD SQHDFPSLVH VLDLTSLSEL IDITRLRISL NVYLYDYQIR EHINVPEEYY 190 200 210 220 230 240 NRLTPLAIRQ YRQLVFDKIF KKLQNDALLC ELIFQKPGNY KKVNIFLDII KRNNYIDLSQ 250 260 270 280 290 300 WDIYSLASVW LNYFIKNKAK PLIPIELIPL PIVDDLKFTS ETFRKIIKFN QYQDLFMVII 310 320 330 340 350 360 PFFNRIIAHG ESTKHDSRTL SKALTPALCK EKLSMMTNDR LAIGSRYIKN LLDFFPEIAK 370 380 390 400 410 420 EISSPPSSVS SSSTIPVLPK PRKSSPTRYS ELGCLTLPRS RSPSPQRSVT SPTYTPVALQ 430 440 450 460 470 480 NTPVLKPKSS SRNVSSPSFN AKPPLPIKAV TRPQLSLTSN SNTDLALASS STDTLSSPTK 490 500 510 520 530 540 TPSADSLPLS NSSTDLTISD NIKEMVKDEP AKDKNSVETD IFVQQFESLT LVQNAKIKKF 550 560 570 580 590 DKELQEKKKK NETTSKTADK FSQKGYSDIK ASNKVSRLAA LYEERLQGLQ VMNEMKQRW

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The sequence of a 36 kb segment on the left arm of yeast chromosome X identifies 24 open reading frames including NUC1, PRP21 (SPP91), CDC6, CRY2, the gene for S24, a homologue to the aconitase gene ACO1 and two homologues to chromosome III genes." Purnelle B., Coster F., Goffeau A. Yeast 10:1235-1249(1994) [PubMed: 7754713] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[2]	"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X." Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C., Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D., Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J., Heumann K. , Hilger F., Hollenberg C.P., Huang M.-E., Jacq C., Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E., Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T., Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R., Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N., To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H., von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L. EMBO J. 15:2031-2049(1996) [PubMed: 8641269] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"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: 17322287] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[5]	"The Saccharomyces cerevisiae PRP21 gene product is an integral component of the prespliceosome." Arenas J.E., Abelson J.N. Proc. Natl. Acad. Sci. U.S.A. 90:6771-6775(1993) [PubMed: 8341697] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-323.
[6]	"Large scale identification of genes involved in cell surface biosynthesis and architecture in Saccharomyces cerevisiae." Lussier M., White A.-M., Sheraton J., di Paolo T., Treadwell J., Southard S.B., Horenstein C.I., Chen-Weiner J., Ram A.F.J., Kapteyn J.C., Roemer T.W., Vo D.H., Bondoc D.C., Hall J., Zhong W.-W., Sdicu A.-M., Davies J., Klis F.M., Robbins P.W., Bussey H. Genetics 147:435-450(1997) [PubMed: 9335584] [Abstract] Cited for: IDENTIFICATION.
[7]	"Phosphoproteome analysis by mass spectrometry and its application to Saccharomyces cerevisiae." Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M., Shabanowitz J., Hunt D.F., White F.M. Nat. Biotechnol. 20:301-305(2002) [PubMed: 11875433] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-402, MASS SPECTROMETRY. Strain: 2124.
[8]	"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: 14562095] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[9]	"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].
[10]	"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway." Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N. Mol. Cell. Proteomics 4:310-327(2005) [PubMed: 15665377] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-411, MASS SPECTROMETRY. Strain: YAL6B.
[11]	"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-408 AND SER-411, MASS SPECTROMETRY.
[12]	"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-408; SER-411; THR-413; SER-436; THR-458; SER-461; SER-471; SER-492; SER-493 AND THR-494, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X77688 Genomic DNA. Translation: CAA54756.1. Z49476 Genomic DNA. Translation: CAA89496.1. AY692747 Genomic DNA. Translation: AAT92766.1. L07744 Genomic DNA. Translation: AAB09602.1. BK006943 Genomic DNA. Translation: DAA08608.1.
PIR	S46630.
RefSeq	NP_012334.1. NM_001181634.1.
3D structure databases
ProteinModelPortal	P32525.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-2926N.
IntAct	P32525. 4 interactions.
MINT	MINT-646629.
STRING	P32525.
Proteomic databases
PeptideAtlas	P32525.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YJL201W; YJL201W; YJL201W.
GeneID	853229.
KEGG	sce:YJL201W.
NMPDR	fig|4932.3.peg.3297.
Organism-specific databases
CYGD	YJL201w.
SGD	S000003737. ECM25.
Phylogenomic databases
eggNOG	fuNOG08153.
HOGENOM	HBG202224.
OMA	RISLNVY.
OrthoDB	EOG4HMNJP.
Gene expression databases
ArrayExpress	P32525.
Genevestigator	P32525.
GermOnline	YJL201W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR008936. Rho_GTPase_activation_prot. IPR000198. RhoGAP_dom. [Graphical view]
Gene3D	G3DSA:1.10.555.10. RhoGAP. 1 hit.
Pfam	PF00620. RhoGAP. 1 hit. [Graphical view]
SMART	SM00324. RhoGAP. 1 hit. [Graphical view]
SUPFAM	SSF48350. Rho_GAP. 1 hit.
PROSITE	PS50238. RHOGAP. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	973440.

Entry information

Entry name

ECM25_YEAST

Accession

Primary (citable) accession number: P32525
Secondary accession number(s): D6VVZ2

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	February 1, 1995
Last modified:	December 14, 2011
This is version 104 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program