ID G8YMF4_PICSO Unreviewed; 618 AA.
AC G8YMF4;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 24-JAN-2024, entry version 59.
DE RecName: Full=candidapepsin {ECO:0000256|ARBA:ARBA00013207};
DE EC=3.4.23.24 {ECO:0000256|ARBA:ARBA00013207};
GN Name=Piso0_001317 {ECO:0000313|EMBL:CCE88550.1};
GN ORFNames=GNLVRS01_PISO0F03833g {ECO:0000313|EMBL:CCE88550.1};
OS Pichia sorbitophila (strain ATCC MYA-4447 / BCRC 22081 / CBS 7064 / NBRC
OS 10061 / NRRL Y-12695) (Hybrid yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Millerozyma.
OX NCBI_TaxID=559304 {ECO:0000313|EMBL:CCE88550.1, ECO:0000313|Proteomes:UP000005222};
RN [1] {ECO:0000313|Proteomes:UP000005222}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4447 / BCRC 22081 / CBS 7064 / NBRC 10061 / NRRL
RC Y-12695 {ECO:0000313|Proteomes:UP000005222};
RX DOI=10.1534/g3.111.000745;
RA Leh Louis V., Despons L., Friedrich A., Martin T., Durrens P.,
RA Casaregola S., Neuveglise C., Fairhead C., Marck C., Cruz J.A.,
RA Straub M.L., Kugler V., Sacerdot C., Uzunov Z., Thierry A., Weiss S.,
RA Bleykasten C., De Montigny J., Jacques N., Jung P., Lemaire M., Mallet S.,
RA Morel G., Richard G.F., Sarkar A., Savel G., Schacherer J., Seret M.L.,
RA Talla E., Samson G., Jubin C., Poulain J., Vacherie B., Barbe V.,
RA Pelletier E., Sherman D.J., Westhof E., Weissenbach J., Baret P.V.,
RA Wincker P., Gaillardin C., Dujon B., Souciet J.L.;
RT "Pichia sorbitophila, an interspecies yeast hybrid reveals early steps of
RT genome resolution following polyploidization.";
RL G3 (Bethesda) 2:299-311(2012).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential cleavage at the carboxyl of hydrophobic amino
CC acids, but fails to cleave 15-Leu-|-Tyr-16, 16-Tyr-|-Leu-17 and 24-
CC Phe-|-Phe-25 of insulin B chain. Activates trypsinogen, and degrades
CC keratin.; EC=3.4.23.24; Evidence={ECO:0000256|ARBA:ARBA00001675};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR EMBL; FO082054; CCE88550.1; -; Genomic_DNA.
DR AlphaFoldDB; G8YMF4; -.
DR STRING; 559304.G8YMF4; -.
DR MEROPS; A01.067; -.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_013253_9_1_1; -.
DR InParanoid; G8YMF4; -.
DR OMA; TEFYISY; -.
DR Proteomes; UP000005222; Chromosome F.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd05474; SAP_like; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 3.
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; PTHR47966:SF65; ASPARTIC-TYPE ENDOPEPTIDASE; 1.
DR PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR Pfam; PF00026; Asp; 2.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; Acid proteases; 2.
DR PROSITE; PS00141; ASP_PROTEASE; 2.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Aspartyl protease {ECO:0000256|ARBA:ARBA00022750,
KW ECO:0000256|RuleBase:RU000454};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|RuleBase:RU000454};
KW Protease {ECO:0000256|RuleBase:RU000454};
KW Reference proteome {ECO:0000313|Proteomes:UP000005222};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..618
FT /note="candidapepsin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003519128"
FT DOMAIN 72..517
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT REGION 139..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..158
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 90
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 414
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ SEQUENCE 618 AA; 65050 MW; 9457846495AC3B11 CRC64;
MRVSWVFLAA ALSGAVSSQE DHPLKINFNV VRGNDHSDIS KRDNRGAFFA PSLGKRDDDG
VSVSLKNEKT FYLAQLKIGS NSQQVGVLVD TGSSDLWIVS KDVKCAESRY SSQKRDASYL
GEQADDLDKR DRFLQGKGDF APQKQASSNP APTKTQNVKH MDQVGAASSV TASAAAEDVA
NKDGFSFSTI VVSDISGFSM PSFSMPSFSF NAPSNAAGGG GAAGGGAGGG PQQTGGCTAY
GSFETSKSDS FHKNSSAPPF AIQYADGSDA VGQWGYDDVE IGGSKVKGLS FAVVNETGSE
MGVLGIGLPG LETTYTGQRA GDPYKYENLP LKMKSQGLIK KSAYSLYLSE EDAKSGTVLF
GAVDTAKFDG NLQTLKVLDT GLGYDEPIRL QIRLDSIKVE DTPLYDAGVA AVLDSGSTLS
YFPSILAKRM GKMLGGKYSS NLGAYQIKCP SSSSANVTFD FGGAKISVPL SELVLSYGKQ
CYLGILESKS PYVLLGDNFL RRAYVVYDLD DNEISLAQVK YTSDENIQAI SSSVPKASKA
PGYSSVNLPS SFGGSNPTKV VSYNGGSATG SYMSFSNSPA SHTSSSGGKT SDAAPFSSFK
IILKLFVTIC LFGSIALL
//