ASPR1_PHARH
ID ASPR1_PHARH Reviewed; 405 AA.
AC O60020;
DT 15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 25-MAY-2022, entry version 82.
DE RecName: Full=Aspartic protease {ECO:0000303|PubMed:10091328, ECO:0000312|EMBL:AAC17105.1};
DE EC=3.4.23.-;
DE Flags: Precursor;
GN Name=pr1 {ECO:0000303|PubMed:10091328, ECO:0000312|EMBL:AAC17105.1};
OS Phaffia rhodozyma (Yeast) (Xanthophyllomyces dendrorhous).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Cystofilobasidiales; Mrakiaceae; Phaffia.
OX NCBI_TaxID=264483;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAC17105.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 82-92, FUNCTION, ACTIVITY
RP REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 96594 / BCRC 22365 / CBS 6938 / JCM 9684 / VKM Y-2793
RC {ECO:0000269|PubMed:10091328};
RX PubMed=10091328; DOI=10.1007/s002530051384;
RA Bang M.L., Villadsen I., Sandal T.;
RT "Cloning and characterization of an endo-beta-1,3(4)glucanase and an
RT aspartic protease from Phaffia rhodozyma CBS 6938.";
RL Appl. Microbiol. Biotechnol. 51:215-222(1999).
CC -!- FUNCTION: Possesses acidic protease activity. Hydrolyzes casein and
CC azoalbumin in vitro. {ECO:0000269|PubMed:10091328}.
CC -!- ACTIVITY REGULATION: Inhibited by pepstatin A.
CC {ECO:0000269|PubMed:10091328}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 4-6. {ECO:0000269|PubMed:10091328};
CC Temperature dependence:
CC Optimum temperature is approximately 40 degrees Celsius.
CC {ECO:0000269|PubMed:10091328};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10091328}.
CC -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000255}.
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DR EMBL; AF064871; AAC17105.1; -; mRNA.
DR AlphaFoldDB; O60020; -.
DR SMR; O60020; -.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IDA:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
DR CDD; cd05471; pepsin_like; 1.
DR Gene3D; 2.40.70.10; -; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
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; PS00141; ASP_PROTEASE; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 1: Evidence at protein level;
KW Aspartyl protease; Cleavage on pair of basic residues;
KW Direct protein sequencing; Disulfide bond; Hydrolase; Protease; Secreted;
KW Signal; Zymogen.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT PROPEP 22..81
FT /note="Removed in mature form"
FT /evidence="ECO:0000269|PubMed:10091328"
FT /id="PRO_0000390379"
FT CHAIN 82..405
FT /note="Aspartic protease"
FT /evidence="ECO:0000269|PubMed:10091328"
FT /id="PRO_0000390380"
FT DOMAIN 97..402
FT /note="Peptidase A1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT ACT_SITE 113
FT /evidence="ECO:0000250|UniProtKB:P00790,
FT ECO:0000255|PROSITE-ProRule:PRU10094"
FT ACT_SITE 290
FT /evidence="ECO:0000250|UniProtKB:P00790,
FT ECO:0000255|PROSITE-ProRule:PRU10094"
FT DISULFID 126..131
FT /evidence="ECO:0000250|UniProtKB:P00790"
FT DISULFID 332..366
FT /evidence="ECO:0000250|UniProtKB:P00790"
SQ SEQUENCE 405 AA; 41370 MW; B722F5A28B6D7272 CRC64;
MISDTVIAIL AVALVGSTVQ AAPVDATATS TSGIIAVPIS KSAAQLAREA DPVVSLDWLK
KTKAQAQYKH KQANARLHSK RATGASVLTD QGSESLWTGP ITIGGQSFTV DWDTGSSDLW
VPSSACSSAA CNAHHKYTLT STGKKQSGTF SISYGDGSSA SGPVYKDNVV ASGLQATSQV
FGAVTSESSS FSSDPSDGIS GLGWPALAQL SGTSYFWSLI NQGTVTSPVF SFRLATTNSE
LYLGGINSAH YTGAITYTPV TQKAYWTIAL GGVSVNGAAI NPSVSSAIID TGTTLVYGPT
AGVAALYAKI PGSASMADTY GSDYQGYYTF PCSAVPTVAL TFGGSSFSVP TSAFNLGTVS
SGSKQCVGGI VGQGDGSWLV GDVFLQGVYS IYDVGNARVG FAKTV
