SAP1_MALGO
ID SAP1_MALGO Reviewed; 395 AA.
AC A8PZM4;
DT 07-NOV-2018, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Secreted aspartyl protease 1 {ECO:0000303|PubMed:29246799};
DE EC=3.4.23.- {ECO:0000269|PubMed:29246799};
DE Flags: Precursor;
GN Name=SAP1 {ECO:0000303|PubMed:29246799}; ORFNames=MGL_1932;
OS Malassezia globosa (strain ATCC MYA-4612 / CBS 7966) (Dandruff-associated
OS fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Malasseziomycetes; Malasseziales; Malasseziaceae; Malassezia.
OX NCBI_TaxID=425265;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4612 / CBS 7966;
RX PubMed=18000048; DOI=10.1073/pnas.0706756104;
RA Xu J., Saunders C.W., Hu P., Grant R.A., Boekhout T., Kuramae E.E.,
RA Kronstad J.W., DeAngelis Y.M., Reeder N.L., Johnstone K.R., Leland M.,
RA Fieno A.M., Begley W.M., Sun Y., Lacey M.P., Chaudhary T., Keough T.,
RA Chu L., Sears R., Yuan B., Dawson T.L. Jr.;
RT "Dandruff-associated Malassezia genomes reveal convergent and divergent
RT virulence traits shared with plant and human fungal pathogens.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:18730-18735(2007).
RN [2]
RP PROTEIN SEQUENCE OF 89-395, IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION,
RP INDUCTION, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND ACTIVITY REGULATION.
RX PubMed=29246799; DOI=10.1016/j.jid.2017.11.034;
RA Li H., Goh B.N., Teh W.K., Jiang Z., Goh J.P.Z., Goh A., Wu G., Hoon S.S.,
RA Raida M., Camattari A., Yang L., O'Donoghue A.J., Dawson T.L. Jr.;
RT "Skin commensal Malassezia globosa secreted protease attenuates
RT Staphylococcus aureus biofilm formation.";
RL J. Invest. Dermatol. 138:1137-1145(2018).
CC -!- FUNCTION: Dominant secreted aspartyl protease that has a clear
CC preference for aromatic residues in the P1' position directly adjacent
CC to the cleavage site and, in particular, Trp. In addition, it generally
CC cleaves peptides containing Lys, Arg, Phe, Tyr, or Nle (norleucine) in
CC the P1 position, Nle and Glu at P2, and Arg and Val at P2'. Has
CC important roles in facilitating the interaction of the yeast with the
CC external environment (PubMed:29246799). Is able to rapidly hydrolyze
CC Staphylococcus aureus protein A, an important S.aureus virulence factor
CC involved in immune evasion and biofilm formation. Shows anti-biofilm
CC properties and thus plays a role in inter-kingdom interactions,
CC beneficial for host skin health (PubMed:29246799).
CC {ECO:0000269|PubMed:29246799}.
CC -!- ACTIVITY REGULATION: Inhibited by pepstatin A.
CC {ECO:0000269|PubMed:29246799}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.4 uM for peptide RPKPVE-Nva-WRK {ECO:0000269|PubMed:29246799};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:29246799}.
CC -!- INDUCTION: Highly expressed during exponential growth in rich media
CC (PubMed:29246799). Also part of the 3 most highly expressed
CC extracellular proteases in minimal media (PubMed:29246799). Expressed
CC on human skin (PubMed:29246799). {ECO:0000269|PubMed:29246799}.
CC -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
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DR EMBL; AAYY01000006; EDP43719.1; -; Genomic_DNA.
DR RefSeq; XP_001730933.1; XM_001730881.1.
DR AlphaFoldDB; A8PZM4; -.
DR SMR; A8PZM4; -.
DR EnsemblFungi; EDP43719; EDP43719; MGL_1932.
DR GeneID; 5855240; -.
DR KEGG; mgl:MGL_1932; -.
DR VEuPathDB; FungiDB:MGL_1932; -.
DR InParanoid; A8PZM4; -.
DR OMA; VDNITPP; -.
DR OrthoDB; 753343at2759; -.
DR Proteomes; UP000008837; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd05471; pepsin_like; 1.
DR Gene3D; 2.40.70.10; -; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR034164; Pepsin-like_dom.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR PANTHER; PTHR47966; PTHR47966; 1.
DR Pfam; PF00026; Asp; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; SSF50630; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 1: Evidence at protein level;
KW Aspartyl protease; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Hydrolase; Protease; Reference proteome; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..88
FT /note="Removed in mature form"
FT /evidence="ECO:0000269|PubMed:29246799"
FT /id="PRO_0000445601"
FT CHAIN 89..395
FT /note="Secreted aspartyl protease 1"
FT /id="PRO_5002727153"
FT DOMAIN 105..391
FT /note="Peptidase A1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT ACT_SITE 121
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT ACT_SITE 283
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT CARBOHYD 41
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 321..352
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
SQ SEQUENCE 395 AA; 43273 MW; 288119C61EEFEFA9 CRC64;
MQLSIQAIIG FVVAAGLAVA SELPSPMTVN LERRKMLVTK NDTVDFKAVR KQANALNYKY
DKLLRNFRKN TGRDHPLLHL LLDLIDKRDG KGDVDLDDIG EGQLWAGDVQ FGQSKFKIDF
DTGSADTLVN PFVYFPHRSK SSRKTHHTFS TAYGDGTTAS GFIYTDDLKI GGYKAKDVAI
GLSVTKFIND EDNQGIAGMS FPAVQSFPKK FDPFFVALVK QKVVPEPVFQ FTLKRGSGST
LHLGGIDNSR FQGELSYVDV NPEDGFWISE GKVNGKKIDA CIDTGSSIIF GPIDEVREVI
TKMDGVTPFT AGGALHGAFD CSKPPKLDFE FAGQKFNLGE NQVSFGKYQG QCVLSIMGQK
NLPMNAWVVG DSFLQTASVV FDMGKNRMGF APSSN
