MKC7_YEAST
ID MKC7_YEAST Reviewed; 596 AA.
AC P53379; D6VSC7;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 2.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Aspartic proteinase MKC7;
DE EC=3.4.23.41;
DE AltName: Full=Yapsin-2;
DE Flags: Precursor;
GN Name=MKC7; Synonyms=YPS2; OrderedLocusNames=YDR144C;
GN ORFNames=YD2943.03C, YD8358.01C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=7479877; DOI=10.1073/pnas.92.23.10752;
RA Komano H., Fuller R.S.;
RT "Shared functions in vivo of a glycosyl-phosphatidylinositol-linked
RT aspartyl protease, Mkc7, and the proprotein processing protease Kex2 in
RT yeast.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:10752-10756(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP PROTEIN SEQUENCE OF 269-275, FUNCTION, SUBCELLULAR LOCATION, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=10446224; DOI=10.1074/jbc.274.34.24431;
RA Komano H., Rockwell N., Wang G.T., Krafft G.A., Fuller R.S.;
RT "Purification and characterization of the yeast
RT glycosylphosphatidylinositol-anchored, monobasic-specific aspartyl protease
RT yapsin 2 (Mkc7p).";
RL J. Biol. Chem. 274:24431-24437(1999).
RN [5]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [6]
RP FUNCTION.
RX PubMed=16087741; DOI=10.1128/ec.4.8.1364-1374.2005;
RA Krysan D.J., Ting E.L., Abeijon C., Kroos L., Fuller R.S.;
RT "Yapsins are a family of aspartyl proteases required for cell wall
RT integrity in Saccharomyces cerevisiae.";
RL Eukaryot. Cell 4:1364-1374(2005).
CC -!- FUNCTION: Cleaves proteins C-terminally to the most C-terminal basic
CC residue. Can process the alpha-mating factor precursor. Required for
CC cell wall integrity. {ECO:0000269|PubMed:10446224,
CC ECO:0000269|PubMed:16087741, ECO:0000269|PubMed:7479877}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolyzes various precursor proteins with Arg or Lys in P1,
CC and commonly Arg or Lys also in P2. The P3 amino acid is usually non-
CC polar, but otherwise additional basic amino acids are favorable in
CC both non-prime and prime positions.; EC=3.4.23.41;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 4-7. Optimum pH is substrate-dependent.
CC {ECO:0000269|PubMed:10446224};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10446224,
CC ECO:0000269|PubMed:7479877}; Lipid-anchor, GPI-anchor
CC {ECO:0000269|PubMed:10446224, ECO:0000269|PubMed:7479877}. Note=GPI-
CC anchored plasma membrane protein (GPI-PMP).
CC -!- MISCELLANEOUS: Present with 538 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
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DR EMBL; U14733; AAC49112.1; -; Genomic_DNA.
DR EMBL; Z50046; CAA90367.1; -; Genomic_DNA.
DR EMBL; Z54139; CAA90813.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11987.1; -; Genomic_DNA.
DR PIR; S57971; S57971.
DR RefSeq; NP_010428.3; NM_001180451.3.
DR AlphaFoldDB; P53379; -.
DR SMR; P53379; -.
DR BioGRID; 32198; 107.
DR DIP; DIP-4585N; -.
DR IntAct; P53379; 1.
DR MINT; P53379; -.
DR STRING; 4932.YDR144C; -.
DR MEROPS; A01.031; -.
DR iPTMnet; P53379; -.
DR MaxQB; P53379; -.
DR PaxDb; P53379; -.
DR PRIDE; P53379; -.
DR EnsemblFungi; YDR144C_mRNA; YDR144C; YDR144C.
DR GeneID; 851722; -.
DR KEGG; sce:YDR144C; -.
DR SGD; S000002551; MKC7.
DR VEuPathDB; FungiDB:YDR144C; -.
DR eggNOG; KOG1339; Eukaryota.
DR GeneTree; ENSGT00940000166661; -.
DR HOGENOM; CLU_013253_9_1_1; -.
DR InParanoid; P53379; -.
DR OMA; IWGYDDV; -.
DR BioCyc; YEAST:G3O-29741-MON; -.
DR PRO; PR:P53379; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P53379; protein.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR GO; GO:0009277; C:fungal-type cell wall; IDA:SGD.
DR GO; GO:0000324; C:fungal-type vacuole; HDA:SGD.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IDA:SGD.
DR GO; GO:0031505; P:fungal-type cell wall organization; IGI:SGD.
DR GO; GO:0006508; P:proteolysis; IMP:SGD.
DR GO; GO:0001402; P:signal transduction involved in filamentous growth; IMP:SGD.
DR CDD; cd05474; SAP_like; 1.
DR Gene3D; 2.40.70.10; -; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR InterPro; IPR033876; SAP-like.
DR PANTHER; PTHR47965; PTHR47965; 1.
DR Pfam; PF00026; Asp; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; SSF50630; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 2.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 1: Evidence at protein level;
KW Aspartyl protease; Cell membrane; Direct protein sequencing; Glycoprotein;
KW GPI-anchor; Hydrolase; Lipoprotein; Membrane; Protease; Reference proteome;
KW Signal; Zymogen.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..65
FT /evidence="ECO:0000255"
FT /id="PRO_0000025835"
FT CHAIN 66..575
FT /note="Aspartic proteinase MKC7"
FT /id="PRO_0000025836"
FT PROPEP 576..596
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000025837"
FT DOMAIN 81..468
FT /note="Peptidase A1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT REGION 530..578
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 530..577
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 99
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT ACT_SITE 360
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT LIPID 575
FT /note="GPI-anchor amidated asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 180
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 190
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 219
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 229
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 232
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 286
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 346
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 471
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 517
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 546
FT /note="T -> A (in Ref. 1; AAC49112)"
FT /evidence="ECO:0000305"
FT CONFLICT 571
FT /note="T -> P (in Ref. 1; AAC49112)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 596 AA; 64269 MW; A3C395A370B392BF CRC64;
MKLSVLTFVV DALLVCSSIV DAGVTDFPSL PSNEVYVKMN FQKKYGSSFE NALDDTKGRT
RLMTRDDDYE LVELTNQNSF YSVELDIGTP PQKVTVLVDT GSSDLWVTGS DNPYCSTKKK
DTTGSSFKQV NKDALASVVE SVFTEISYDT TIVTSEATAT FDSTASTSQL IDCATYGTFN
TSKSSTFNSN NTEFSIAYGD TTFASGTWGH DQLSLNDLNI TGLSFAVANE TNSTVGVLGI
GLPGLESTYS GVSLSSVQKS YTYNNFPMVL KNSGVIKSTA YSLFANDSDS KHGTILFGAV
DHGKYAGDLY TIPIINTLQH RGYKDPIQFQ VTLQGLGTSK GDKEDNLTTL TTTKIPVLLD
SGTTISYMPT ELVKMLADQV GATYSSAYGY YIMDCIKEME EESSIIFDFG GFYLSNWLSD
FQLVTDSRSN ICILGIAPQS DPTIILGDNF LANTYVVYDL DNMEISMAQA NFSDDGEYIE
IIESAVPSAL KAPGYSSTWS TYESIVSGGN MFSTAANSSI SYFASTSHSA TSSSSSKGQK
TQTSTTALSI SKSTSSTSST GMLSPTSSSS TRKENGGHNL NPPFFARFIT AIFHHI
