Reviewed, UniProtKB/Swiss-Prot P53379 (MKC7_YEAST)

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

4932 [NCBI]

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 proteins C-terminally to the most C-terminal basic residue. Can process the alpha-mating factor precursor. Required for cell wall integrity. Ref.1 Ref.3 Ref.5
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. Note: GPI-anchored plasma membrane protein (GPI-PMP). Ref.1 Ref.3
Miscellaneous	Present with 538 molecules/cell in log phase SD medium. Ref.4
Sequence similarities	Belongs to the peptidase A1 family.
Biophysicochemical properties	pH dependence: Optimum pH is 4-7. Optimum pH is substrate-dependent.

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 Direct protein sequencing
Gene Ontology (GO)
Biological process	proteolysis Ref.1 Inferred from mutant phenotype. Source: SGD
Cellular component	anchored to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell fungal-type cell wall Inferred from direct assay. Source: SGD plasma membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	aspartic-type endopeptidase activity Ref.3 Inferred from direct assay. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 22	22	Potential
	Propeptide	23 – 65	43	Potential		PRO_0000025835
	Chain	66 – 575	510	Aspartic proteinase MKC7		PRO_0000025836
	Propeptide	576 – 596	21	Removed in mature form Potential		PRO_0000025837
Regions
	Compositional bias	532 – 536	5	Poly-Ser
	Compositional bias	567 – 570	4	Poly-Ser
Sites
	Active site	99	1	By similarity
	Active site	360	1	By similarity
Amino acid modifications
	Lipidation	575	1	GPI-anchor amidated asparagine Potential
	Glycosylation	180	1	N-linked (GlcNAc...) Potential
	Glycosylation	190	1	N-linked (GlcNAc...) Potential
	Glycosylation	219	1	N-linked (GlcNAc...) Potential
	Glycosylation	229	1	N-linked (GlcNAc...) Potential
	Glycosylation	232	1	N-linked (GlcNAc...) Potential
	Glycosylation	286	1	N-linked (GlcNAc...) Potential
	Glycosylation	346	1	N-linked (GlcNAc...) Potential
	Glycosylation	471	1	N-linked (GlcNAc...) Potential
	Glycosylation	517	1	N-linked (GlcNAc...) Potential
Experimental info
	Sequence conflict	546	1	T → A in AAC49112. Ref.1
	Sequence conflict	571	1	T → P in AAC49112. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P53379-1 [UniParc]. Last modified December 21, 2004. Version 2. Checksum: A3C395A370B392BF	FASTA	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], FUNCTION, SUBCELLULAR LOCATION.
[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. , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P. Nature 387:75-78(1997) [PubMed: 9169867] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	"Purification and characterization of the yeast glycosylphosphatidylinositol-anchored, monobasic-specific aspartyl protease yapsin 2 (Mkc7p)." Komano H., Rockwell N., Wang G.T., Krafft G.A., Fuller R.S. J. Biol. Chem. 274:24431-24437(1999) [PubMed: 10446224] [Abstract] Cited for: PROTEIN SEQUENCE OF 269-275, FUNCTION, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES.
[4]	"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].
[5]	"Yapsins are a family of aspartyl proteases required for cell wall integrity in Saccharomyces cerevisiae." Krysan D.J., Ting E.L., Abeijon C., Kroos L., Fuller R.S. Eukaryot. Cell 4:1364-1374(2005) [PubMed: 16087741] [Abstract] Cited for: FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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
SMR	P53379. Positions 71-472.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-4585N.
IntAct	P53379. 9 interactions.
STRING	P53379.
Protein family/group databases
MEROPS	A01.031.
Genome annotation databases
Ensembl	YDR144C; YDR144C; YDR144C; Saccharomyces cerevisiae. [Genome view]
GeneID	851722.
KEGG	sce:YDR144C.
NMPDR	fig|4932.3.peg.1177.
Organism-specific databases
CYGD	YDR144c.
SGD	S000002551. MKC7.
Phylogenomic databases
eggNOG	fuNOG05617.
HOGENOM	HBG398805.
OMA	NGGSIDC.
OrthoDB	EOG9MKPZC.
PhylomeDB	P53379.
Enzyme and pathway databases
BRENDA	3.4.23.41. 250.
Gene expression databases
ArrayExpress	P53379.
Genevestigator	P53379.
GermOnline	YDR144C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR001461. Peptidase_A1. IPR021109. Peptidase_aspartic. IPR001969. Peptidase_aspartic_AS. IPR009007. Peptidase_aspartic_catalytic. [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]
ProtoNet	Search...
Other Resources
NextBio	969430.

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:	February 9, 2010
This is version 95 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)