CARP2_CANAX
ID CARP2_CANAX Reviewed; 398 AA.
AC P0CS83; P28871; P43097; Q59MV8; Q8NKF0; Q8NKF1;
DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT 22-FEB-2012, sequence version 1.
DT 03-AUG-2022, entry version 44.
DE RecName: Full=Candidapepsin-2;
DE EC=3.4.23.24;
DE AltName: Full=ACP 2;
DE AltName: Full=Aspartate protease 2;
DE AltName: Full=Secreted aspartic protease 2;
DE Flags: Precursor;
GN Name=SAP2; Synonyms=PRA11, PRA2;
OS Candida albicans (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=5476;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF N-TERMINUS, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=ATCC 10261 / CBS 2718 / NBRC 1061 / FMJ 1011;
RX PubMed=1447155; DOI=10.1128/jb.174.23.7848-7853.1992;
RA Wright R.J., Carne A., Hieber A.D., Lamont I.L., Emerson G.W.,
RA Sullivan P.A.;
RT "A second gene for a secreted aspartate proteinase in Candida albicans.";
RL J. Bacteriol. 174:7848-7853(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=TIMM 2726 / 114 / Serotype A;
RX PubMed=1491622; DOI=10.1111/j.1348-0421.1992.tb02124.x;
RA Mukai H., Takeda O., Asada K., Kato I., Murayama S.Y., Yamaguchi H.;
RT "cDNA cloning of an aspartic proteinase secreted by Candida albicans.";
RL Microbiol. Immunol. 36:1207-1216(1992).
RN [3]
RP PROTEIN SEQUENCE OF 57-71.
RC STRAIN=3153A, and SS;
RX PubMed=8407785; DOI=10.1128/jb.175.19.6126-6133.1993;
RA White T.C., Miyasaki S.H., Agabian N.;
RT "Three distinct secreted aspartyl proteinases in Candida albicans.";
RL J. Bacteriol. 175:6126-6133(1993).
RN [4]
RP CHARACTERIZATION.
RC STRAIN=ATCC 10231 / CBS 6431 / CIP 48.72 / DSM 1386 / NBRC 1594;
RX PubMed=9043112; DOI=10.1099/00221287-143-2-349;
RA Smolenski G., Sullivan P.A., Cutfield S.M., Cutfield J.F.;
RT "Analysis of secreted aspartic proteinases from Candida albicans:
RT purification and characterization of individual Sap1, Sap2 and Sap3
RT isoenzymes.";
RL Microbiology 143:349-356(1997).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 57-398.
RC STRAIN=ATCC 10261 / CBS 2718 / NBRC 1061 / FMJ 1011;
RX PubMed=8591036; DOI=10.1016/s0969-2126(01)00261-1;
RA Cutfield S.M., Dodson E.J., Anderson B.F., Moody P.C.E., Marshall C.J.,
RA Sullivan P.A., Cutfield J.F.;
RT "The crystal structure of a major secreted aspartic proteinase from Candida
RT albicans in complexes with two inhibitors.";
RL Structure 3:1261-1271(1995).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 57-398 IN COMPLEX WITH A70450,
RP PROTEIN SEQUENCE OF N-TERMINUS, SUBCELLULAR LOCATION, AND SUBUNIT.
RC STRAIN=Val-1;
RX PubMed=8845753; DOI=10.1002/pro.5560050408;
RA Abad-Zapatero C., Goldman R., Muchmore S.W., Hutchins C., Stewart K.,
RA Navaza J., Payne C.D., Ray T.L.;
RT "Structure of a secreted aspartic protease from C. albicans complexed with
RT a potent inhibitor: implications for the design of antifungal agents.";
RL Protein Sci. 5:640-652(1996).
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;
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:8845753}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1447155,
CC ECO:0000269|PubMed:8845753}.
CC -!- PTM: O-glycosylated.
CC -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M83663; AAA34332.1; -; Genomic_DNA.
DR EMBL; X62289; CAA44178.1; -; mRNA.
DR PIR; A45280; A45280.
DR PDB; 1EAG; X-ray; 2.10 A; A=57-398.
DR PDB; 1ZAP; X-ray; 2.50 A; A=57-398.
DR PDB; 3PVK; X-ray; 1.27 A; A=57-398.
DR PDB; 3Q70; X-ray; 1.40 A; A=57-398.
DR PDBsum; 1EAG; -.
DR PDBsum; 1ZAP; -.
DR PDBsum; 3PVK; -.
DR PDBsum; 3Q70; -.
DR AlphaFoldDB; P0CS83; -.
DR SMR; P0CS83; -.
DR BindingDB; P0CS83; -.
DR ChEMBL; CHEMBL6021; -.
DR MEROPS; A01.060; -.
DR VEuPathDB; FungiDB:CAWG_02075; -.
DR VEuPathDB; FungiDB:CR_07800W_A; -.
DR BRENDA; 3.4.23.24; 1096.
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; 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 3D-structure; Aspartyl protease; Cleavage on pair of basic residues;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Hydrolase;
KW Protease; Secreted; Signal; Zymogen.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT PROPEP 19..56
FT /note="Activation peptide"
FT /evidence="ECO:0000269|PubMed:1447155,
FT ECO:0000269|PubMed:8407785, ECO:0000269|PubMed:8845753"
FT /id="PRO_0000025850"
FT CHAIN 57..398
FT /note="Candidapepsin-2"
FT /id="PRO_0000025851"
FT DOMAIN 70..384
FT /note="Peptidase A1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT ACT_SITE 88
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT ACT_SITE 274
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT BINDING 88..90
FT /ligand="pepstatin A"
FT /ligand_id="ChEBI:CHEBI:190525"
FT /ligand_note="inhibitor"
FT /evidence="ECO:0000250|UniProtKB:P0CY29"
FT BINDING 141..142
FT /ligand="pepstatin A"
FT /ligand_id="ChEBI:CHEBI:190525"
FT /ligand_note="inhibitor"
FT /evidence="ECO:0000250|UniProtKB:P0CY29"
FT BINDING 274..278
FT /ligand="pepstatin A"
FT /ligand_id="ChEBI:CHEBI:190525"
FT /ligand_note="inhibitor"
FT /evidence="ECO:0000250|UniProtKB:P0CY29"
FT CARBOHYD 313
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 321
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 103..115
FT /evidence="ECO:0000250"
FT DISULFID 312..350
FT /evidence="ECO:0000250"
FT VARIANT 9
FT /note="A -> G (in strain: TIMM 2726)"
FT CONFLICT 43
FT /note="F -> S (in Ref. 2; CAA44178)"
FT /evidence="ECO:0000305"
FT CONFLICT 214..236
FT /note="YLNSPDAATGQIIFGGVDNAKYS -> ILILQMSPRDKSFSVGLIMLNIV
FT (in Ref. 2; CAA44178)"
FT /evidence="ECO:0000305"
FT CONFLICT 370..396
FT /note="AYIVYDLDDNEISLAQVKYTSASSISA -> LILFMIWMIMKFLWLKSNILL
FT FQYFS (in Ref. 2; CAA44178)"
FT /evidence="ECO:0000305"
FT STRAND 59..65
FT /evidence="ECO:0007829|PDB:3PVK"
FT STRAND 67..76
FT /evidence="ECO:0007829|PDB:3PVK"
FT TURN 77..80
FT /evidence="ECO:0007829|PDB:3PVK"
FT STRAND 81..88
FT /evidence="ECO:0007829|PDB:3PVK"
FT STRAND 94..103
FT /evidence="ECO:0007829|PDB:3PVK"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:3PVK"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:3PVK"
FT STRAND 130..139
FT /evidence="ECO:0007829|PDB:3PVK"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:3PVK"
FT STRAND 145..157
FT /evidence="ECO:0007829|PDB:3PVK"
FT STRAND 160..177
FT /evidence="ECO:0007829|PDB:3PVK"
FT STRAND 179..181
FT /evidence="ECO:0007829|PDB:3PVK"
FT HELIX 185..187
FT /evidence="ECO:0007829|PDB:3PVK"
FT HELIX 196..202
FT /evidence="ECO:0007829|PDB:3PVK"
FT STRAND 205..214
FT /evidence="ECO:0007829|PDB:3PVK"
FT STRAND 221..227
FT /evidence="ECO:0007829|PDB:3PVK"
FT STRAND 229..231
FT /evidence="ECO:0007829|PDB:3PVK"
FT STRAND 234..237
FT /evidence="ECO:0007829|PDB:3PVK"
FT STRAND 240..243
FT /evidence="ECO:0007829|PDB:3PVK"
FT STRAND 247..249
FT /evidence="ECO:0007829|PDB:3PVK"
FT STRAND 251..259
FT /evidence="ECO:0007829|PDB:3PVK"
FT STRAND 262..273
FT /evidence="ECO:0007829|PDB:3PVK"
FT STRAND 278..282
FT /evidence="ECO:0007829|PDB:3PVK"
FT HELIX 284..293
FT /evidence="ECO:0007829|PDB:3PVK"
FT STRAND 297..300
FT /evidence="ECO:0007829|PDB:3PVK"
FT STRAND 302..305
FT /evidence="ECO:0007829|PDB:1ZAP"
FT STRAND 306..310
FT /evidence="ECO:0007829|PDB:3PVK"
FT STRAND 316..323
FT /evidence="ECO:0007829|PDB:3PVK"
FT STRAND 327..331
FT /evidence="ECO:0007829|PDB:3PVK"
FT HELIX 332..335
FT /evidence="ECO:0007829|PDB:3PVK"
FT STRAND 336..338
FT /evidence="ECO:0007829|PDB:1EAG"
FT TURN 339..343
FT /evidence="ECO:0007829|PDB:1ZAP"
FT STRAND 350..356
FT /evidence="ECO:0007829|PDB:3PVK"
FT HELIX 364..367
FT /evidence="ECO:0007829|PDB:3PVK"
FT STRAND 370..375
FT /evidence="ECO:0007829|PDB:3PVK"
FT TURN 376..379
FT /evidence="ECO:0007829|PDB:3PVK"
FT STRAND 380..386
FT /evidence="ECO:0007829|PDB:3PVK"
FT STRAND 394..396
FT /evidence="ECO:0007829|PDB:3PVK"
SQ SEQUENCE 398 AA; 42330 MW; 53F2AF0F3DB04DB0 CRC64;
MFLKNIFIAL AIALLVDATP TTTKRSAGFV ALDFSVVKTP KAFPVTNGQE GKTSKRQAVP
VTLHNEQVTY AADITVGSNN QKLNVIVDTG SSDLWVPDVN VDCQVTYSDQ TADFCKQKGT
YDPSGSSASQ DLNTPFKIGY GDGSSSQGTL YKDTVGFGGV SIKNQVLADV DSTSIDQGIL
GVGYKTNEAG GSYDNVPVTL KKQGVIAKNA YSLYLNSPDA ATGQIIFGGV DNAKYSGSLI
ALPVTSDREL RISLGSVEVS GKTINTDNVD VLLDSGTTIT YLQQDLADQI IKAFNGKLTQ
DSNGNSFYEV DCNLSGDVVF NFSKNAKISV PASEFAASLQ GDDGQPYDKC QLLFDVNDAN
ILGDNFLRSA YIVYDLDDNE ISLAQVKYTS ASSISALT
