YPS3_YEAST
ID YPS3_YEAST Reviewed; 508 AA.
AC Q12303; D6VYB9;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Aspartic proteinase yapsin-3;
DE EC=3.4.23.-;
DE Flags: Precursor;
GN Name=YPS3; OrderedLocusNames=YLR121C; ORFNames=L2964, L9233.10;
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].
RC STRAIN=ATCC 90840 / EAY235 / FY23;
RX PubMed=9090053;
RX DOI=10.1002/(sici)1097-0061(19970315)13:3<241::aid-yea61>3.0.co;2-#;
RA Verhasselt P., Volckaert G.;
RT "Sequence analysis of a 37.6 kbp cosmid clone from the right arm of
RT Saccharomyces cerevisiae chromosome XII, carrying YAP3, HOG1, SNR6, tRNA-
RT Arg3 and 23 new open reading frames, among which several homologies to
RT proteins involved in cell division control and to mammalian growth factors
RT and other animal proteins are found.";
RL Yeast 13:241-250(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(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 48-68, FUNCTION, SUBCELLULAR LOCATION, AND PROTEOLYTIC
RP PROCESSING.
RX PubMed=10191273; DOI=10.1042/bj3390407;
RA Olsen V., Cawley N.X., Brandt J., Egel-Mitani M., Loh Y.P.;
RT "Identification and characterization of Saccharomyces cerevisiae yapsin 3,
RT a new member of the yapsin family of aspartic proteases encoded by the YPS3
RT gene.";
RL Biochem. J. 339:407-411(1999).
RN [5]
RP INDUCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11016834; DOI=10.1007/s004380000285;
RA Terashima H., Yabuki N., Arisawa M., Hamada K., Kitada K.;
RT "Up-regulation of genes encoding glycosylphosphatidylinositol (GPI)-
RT attached proteins in response to cell wall damage caused by disruption of
RT FKS1 in Saccharomyces cerevisiae.";
RL Mol. Gen. Genet. 264:64-74(2000).
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 mono- and paired-basic
CC residues. Required for cell wall integrity.
CC {ECO:0000269|PubMed:10191273, ECO:0000269|PubMed:16087741}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10191273,
CC ECO:0000269|PubMed:11016834}; Lipid-anchor, GPI-anchor
CC {ECO:0000269|PubMed:10191273, ECO:0000269|PubMed:11016834}. Note=GPI-
CC anchored plasma membrane protein (GPI-PMP).
CC -!- INDUCTION: Positively regulated in response to cell wall perturbation.
CC {ECO:0000269|PubMed:11016834}.
CC -!- PTM: Can also be processed to start at Phe-54.
CC {ECO:0000269|PubMed:10191273}.
CC -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
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DR EMBL; X89514; CAA61700.1; -; Genomic_DNA.
DR EMBL; Z73293; CAA97689.1; -; Genomic_DNA.
DR EMBL; U53877; AAB82368.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09435.1; -; Genomic_DNA.
DR PIR; S64958; S64958.
DR RefSeq; NP_013222.1; NM_001182008.1.
DR AlphaFoldDB; Q12303; -.
DR SMR; Q12303; -.
DR BioGRID; 31393; 37.
DR DIP; DIP-4569N; -.
DR IntAct; Q12303; 1.
DR MINT; Q12303; -.
DR STRING; 4932.YLR121C; -.
DR MEROPS; A01.035; -.
DR MaxQB; Q12303; -.
DR PaxDb; Q12303; -.
DR PRIDE; Q12303; -.
DR EnsemblFungi; YLR121C_mRNA; YLR121C; YLR121C.
DR GeneID; 850812; -.
DR KEGG; sce:YLR121C; -.
DR SGD; S000004111; YPS3.
DR VEuPathDB; FungiDB:YLR121C; -.
DR eggNOG; KOG1339; Eukaryota.
DR GeneTree; ENSGT00940000166661; -.
DR HOGENOM; CLU_013253_9_1_1; -.
DR InParanoid; Q12303; -.
DR OMA; TKKYKGD; -.
DR BioCyc; YEAST:G3O-32266-MON; -.
DR PRO; PR:Q12303; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q12303; protein.
DR GO; GO:0046658; C:anchored component of plasma membrane; IDA:SGD.
DR GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR GO; GO:0009277; C:fungal-type cell wall; IBA:GO_Central.
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; IBA:GO_Central.
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; Cleavage on pair of basic residues;
KW Direct protein sequencing; Glycoprotein; GPI-anchor; Hydrolase;
KW Lipoprotein; Membrane; Protease; Reference proteome; Signal; Zymogen.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..47
FT /evidence="ECO:0000269|PubMed:10191273"
FT /id="PRO_0000025841"
FT CHAIN 48..483
FT /note="Aspartic proteinase yapsin-3"
FT /id="PRO_0000025842"
FT PROPEP 484..508
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000025843"
FT DOMAIN 63..394
FT /note="Peptidase A1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT REGION 448..476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 81
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT ACT_SITE 288
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT LIPID 483
FT /note="GPI-anchor amidated asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 75
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 120
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 160
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 163
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 275
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 309
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 328
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 367
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 422
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 445
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 462
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 508 AA; 54570 MW; 552E4B236FF12ABA CRC64;
MKLQLAAVAT LAVLTSPAFG RVLPDGKYVK IPFTKKKNGD NGELSKRSNG HEKFVLANEQ
SFYSVELAIG TPSQNLTVLL DTGSADLWVP GKGNPYCGSV MDCDQYGVFD KTKSSTFKAN
KSSPFYAAYG DGTYAEGAFG QDKLKYNELD LSGLSFAVAN ESNSTFGVLG IGLSTLEVTY
SGKVAIMDKR SYEYDNFPLF LKHSGAIDAT AYSLFLNDES QSSGSILFGA VDHSKYEGQL
YTIPLVNLYK SQGYQHPVAF DVTLQGLGLQ TDKRNITLTT TKLPALLDSG TTLTYLPSQA
VALLAKSLNA SYSKTLGYYE YTCPSSDNKT SVAFDFGGFR INAPLSDFTM QTSVGTCVLA
IIPQAGNATA ILGDSFLRNA YVVYDLDNYE ISLAQAKYGT GKENVEVIKS TVPSAIRAPS
YNNTWSNYAS ATSGGNIFTT VRTFNGTSTA TTTRSTTTKK TNSTTTAKST HKSKRALQRA
ATNSASSIRS TLGLLLVPSL LILSVFFS
