Aspartic proteinase MKC7 precursor - Saccharomyces cerevisiae (Baker's yeast)

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Reviewed, UniProtKB/Swiss-Prot P53379 (MKC7_YEAST)

Last modified July 22, 2008. Version 78. History...

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

Names and origin

Protein names

Recommended name:
    Aspartic proteinase MKC7
    EC=3.4.23.41
Alternative name(s):
    Yapsin-2

Gene names

Name:	MKC7
Synonyms:	YPS2
Ordered Locus Names:	YDR144C
ORF Names:	YD8358.01C, YD2943.03C

Organism

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

Taxonomic identifier

Taxonomic lineage

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

Protein attributes

Sequence length	596 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Cleaves at paired basic residues. Can process the alpha-mating factor precursor.
Catalytic activity	Hydrolyzes various precursor proteins with Arg or Lys in P1, and commonly Arg or Lys also in P2. The P3 amino acid is usually non-polar, but otherwise additional basic amino acids are favorable in both non-prime and prime positions.
Subcellular location	Cell membrane; Lipid-anchor › GPI-anchor.
Miscellaneous	Present with 538 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the peptidase A1 family.

Ontologies

Keywords
Cellular component	Cell membrane Membrane
Domain	Signal
Molecular function	Aspartyl protease Hydrolase Protease
PTM	GPI-anchor Glycoprotein Lipoprotein Zymogen
Technical term	Complete proteome
Gene Ontology (GO)
Uncategorized	aspartic-type signal peptidase activity Inferred from direct assay. Source: SGD
Biological process	proteolysis Ref.1 Inferred from mutant phenotype. Source: SGD
Cellular component	fungal-type cell wall Inferred from direct assay. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Molecule processing

Signal peptide

22

Potential

Propeptide

43

Potential

Chain

510

Aspartic proteinase MKC7

Propeptide

21

Removed in mature form Potential

Regions

Compositional bias

5

Poly-Ser

Compositional bias

4

Poly-Ser

Sites

Active site

1

By similarity

Active site

1

By similarity

Amino acid modifications

Lipidation

1

GPI-anchor amidated asparagine Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict

1

T → A in AAC49112. Ref.1

Sequence conflict

1

T → P in AAC49112. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

P53379-1 [UniParc].

Last modified December 21, 2004. Version 2.
Checksum: A3C395A370B392BF
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596

64,269

        10         20         30         40         50         60 
MKLSVLTFVV DALLVCSSIV DAGVTDFPSL PSNEVYVKMN FQKKYGSSFE NALDDTKGRT 

        70         80         90        100        110        120 
RLMTRDDDYE LVELTNQNSF YSVELDIGTP PQKVTVLVDT GSSDLWVTGS DNPYCSTKKK 

       130        140        150        160        170        180 
DTTGSSFKQV NKDALASVVE SVFTEISYDT TIVTSEATAT FDSTASTSQL IDCATYGTFN 

       190        200        210        220        230        240 
TSKSSTFNSN NTEFSIAYGD TTFASGTWGH DQLSLNDLNI TGLSFAVANE TNSTVGVLGI 

       250        260        270        280        290        300 
GLPGLESTYS GVSLSSVQKS YTYNNFPMVL KNSGVIKSTA YSLFANDSDS KHGTILFGAV 

       310        320        330        340        350        360 
DHGKYAGDLY TIPIINTLQH RGYKDPIQFQ VTLQGLGTSK GDKEDNLTTL TTTKIPVLLD 

       370        380        390        400        410        420 
SGTTISYMPT ELVKMLADQV GATYSSAYGY YIMDCIKEME EESSIIFDFG GFYLSNWLSD 

       430        440        450        460        470        480 
FQLVTDSRSN ICILGIAPQS DPTIILGDNF LANTYVVYDL DNMEISMAQA NFSDDGEYIE 

       490        500        510        520        530        540 
IIESAVPSAL KAPGYSSTWS TYESIVSGGN MFSTAANSSI SYFASTSHSA TSSSSSKGQK 

       550        560        570        580        590 
TQTSTTALSI SKSTSSTSST GMLSPTSSSS TRKENGGHNL NPPFFARFIT AIFHHI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Shared functions in vivo of a glycosyl-phosphatidylinositol-linked aspartyl protease, Mkc7, and the proprotein processing protease Kex2 in yeast." Komano H., Fuller R.S. Proc. Natl. Acad. Sci. U.S.A. 92:10752-10756(1995) [PubMed: 7479877] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV." Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T. Zaccaria P. Nature 387:75-78(1997) [PubMed: 9169867] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	"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].
+	Additional computationally mapped references.

Cross-references

Sequence databases
	U14733 Genomic DNA. Translation: AAC49112.1. Z50046 Genomic DNA. Translation: CAA90367.1. Z54139 Genomic DNA. Translation: CAA90813.1.
PIR	S57971.
RefSeq	NP_010428.1.
3D structure databases
HSSP	HSSP built from PDB template 2REN based on UniProtKB P00797.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:4585N.
Protein family/group databases
MEROPS	A01.031.
Genome annotation databases
Ensembl	YDR144C. Saccharomyces cerevisiae. [Contig view]
GeneID	851722.
GenomeReviews	Gene locus YDR144C in contig Z71256_GR.
KEGG	sce:YDR144C.
NMPDR	fig\|4932.3.peg.1177.
Organism-specific databases
CYGD	YDR144c.
SGD	S000002551. MKC7.
Yeast-GFP	Search...
Phylogenomic databases
HOGENOM	P53379.
Gene expression databases
ArrayExpress	P53379.
GermOnline	YDR144C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR001969. Pept_Asp_AS. IPR009007. Pept_Aspartc_cat. IPR001461. Peptidase_A1. [Graphical view]
Gene3D	G3DSA:2.40.70.10. Pept_Aspartc_cat. 1 hit.
PANTHER	PTHR13683. Peptidase_A1. 1 hit.
Pfam	PF00026. Asp. 1 hit. [Graphical view]
PRINTS	PR00792. PEPSIN.
PROSITE	PS00141. ASP_PROTEASE. 2 hits. [Graphical view]
ProDom	P53379. [Graphical view] [Entries sharing at least one domain]
BLOCKS	Search...
Other Resources
LinkHub	P53379.
ProtoNet	Search...

Entry information

Entry name

MKC7_YEAST

Accession

Primary (citable) accession number: P53379

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	December 21, 2004
Last modified:	July 22, 2008
This is version 78 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

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

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