SUB3_PSED2
ID SUB3_PSED2 Reviewed; 404 AA.
AC L8GD75;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2013, sequence version 1.
DT 03-AUG-2022, entry version 37.
DE RecName: Full=Subtilisin-like protease 3 {ECO:0000250|UniProtKB:L8G6I7};
DE EC=3.4.21.- {ECO:0000250|UniProtKB:L8FSM5};
DE AltName: Full=Destructin-3 {ECO:0000303|PubMed:25944934};
DE AltName: Full=Serine protease 3 {ECO:0000303|PubMed:25785714};
DE Short=PdSP3 {ECO:0000303|PubMed:25785714};
DE Flags: Precursor;
GN Name=SP3 {ECO:0000303|PubMed:25785714}; ORFNames=GMDG_04447;
OS Pseudogymnoascus destructans (strain ATCC MYA-4855 / 20631-21) (Bat
OS white-nose syndrome fungus) (Geomyces destructans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=658429;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4855 / 20631-21;
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C.A., Blehert D.S., Lorch J.M., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E.,
RA Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D.,
RA Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The genome sequence of Geomyces destructans 20631-21.";
RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP GENE NAME.
RX PubMed=25785714; DOI=10.1371/journal.pone.0120508;
RA Pannkuk E.L., Risch T.S., Savary B.J.;
RT "Isolation and identification of an extracellular subtilisin-like serine
RT protease secreted by the bat pathogen Pseudogymnoascus destructans.";
RL PLoS ONE 10:E0120508-E0120508(2015).
RN [3]
RP SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=25944934; DOI=10.1073/pnas.1507082112;
RA O'Donoghue A.J., Knudsen G.M., Beekman C., Perry J.A., Johnson A.D.,
RA DeRisi J.L., Craik C.S., Bennett R.J.;
RT "Destructin-1 is a collagen-degrading endopeptidase secreted by
RT Pseudogymnoascus destructans, the causative agent of white-nose syndrome.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:7478-7483(2015).
RN [4]
RP ERRATUM OF PUBMED:25944934.
RX PubMed=26015578; DOI=10.1073/pnas.1509071112;
RA O'Donoghue A.J., Knudsen G.M., Beekman C., Perry J.A., Johnson A.D.,
RA DeRisi J.L., Craik C.S., Bennett R.J.;
RL Proc. Natl. Acad. Sci. U.S.A. 112:E3152-E3152(2015).
CC -!- FUNCTION: Secreted subtilisin-like serine endopeptidase
CC (PubMed:25944934). Mediates the degradation of collagen, the major
CC structural protein in the mammalian host. Degrades the nonhelical
CC regions of collagen that function in the cross-linking of the helical
CC components (By similarity). May function as virulence factor involved
CC in epidermal wing necrosis observed in white nose syndrome (WNS) in
CC bats (By similarity). {ECO:0000250|UniProtKB:L8FSM5,
CC ECO:0000250|UniProtKB:L8G6I7, ECO:0000269|PubMed:25944934}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:25944934}.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
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DR EMBL; GL573249; ELR10046.1; -; Genomic_DNA.
DR RefSeq; XP_012742868.1; XM_012887414.1.
DR AlphaFoldDB; L8GD75; -.
DR SMR; L8GD75; -.
DR STRING; 658429.L8GD75; -.
DR EnsemblFungi; ELR10046; ELR10046; GMDG_04447.
DR VEuPathDB; FungiDB:GMDG_04447; -.
DR HOGENOM; CLU_011263_1_4_1; -.
DR InParanoid; L8GD75; -.
DR OrthoDB; 308083at2759; -.
DR Proteomes; UP000011064; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04077; Peptidases_S8_PCSK9_ProteinaseK_like; 1.
DR Gene3D; 3.30.70.80; -; 1.
DR Gene3D; 3.40.50.200; -; 1.
DR InterPro; IPR034193; PCSK9_ProteinaseK-like.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023827; Peptidase_S8_Asp-AS.
DR InterPro; IPR022398; Peptidase_S8_His-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR010259; S8pro/Inhibitor_I9.
DR InterPro; IPR037045; S8pro/Inhibitor_I9_sf.
DR Pfam; PF05922; Inhibitor_I9; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52743; SSF52743; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00136; SUBTILASE_ASP; 1.
DR PROSITE; PS00137; SUBTILASE_HIS; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Hydrolase; Protease; Reference proteome; Secreted;
KW Serine protease; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..114
FT /evidence="ECO:0000250|UniProtKB:L8FSM5"
FT /id="PRO_0000434140"
FT CHAIN 115..404
FT /note="Subtilisin-like protease 3"
FT /id="PRO_0000434141"
FT DOMAIN 38..112
FT /note="Inhibitor I9"
FT /evidence="ECO:0000255"
FT DOMAIN 123..404
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 158
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 190
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 347
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT SITE 114..115
FT /note="Cleavage; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:L8FSM5"
FT CARBOHYD 133
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 243
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 251
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 286
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 307
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 340
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 366
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 404 AA; 42540 MW; 1048D9BA43C29A5A CRC64;
MLFSKSLVAL VACFLPLIVS ATELKLRNAA ATNVAADSYI VVYKDIDDST FESEMFNVHS
FLSKRDSTFR GLGHKYKMPK FKGYQIESDM DTVNRISQSP HVAYVDKDVK VSAYDLSVRI
GAPWGLDRIS HRNGTSPGLE EYTYDSSAGG GTTIYIIDTG VYIEHVEFEG RATFGANFIP
GSPDTDEDGH GTHVAGIAAG ANFGVASKAK IIAVRVLDAN GDGKGSNVLA GMQWAADDAG
KKNQTAKSVI NMSLGADYSE AFNKATEAII AKGIVVVAAA GNEDANASGV SPASTVDAIT
VGATDRNDSR AAFSNWGVAL DVFAPGVDIL SAWIGGKDAN KTISGTSMAC PHVAGLAAYF
IGLEKNGTST PSKIATKIKG VATKNVVLHP KNSRDNLAYN DDGY
