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UniProtKB - P32950 (CARP2_CANPA)
Protein
Candidapepsin-2
Gene
SAPP2
Organism
Candida parapsilosis (Yeast)
Status
Functioni
Catalytic activityi
- Preferential cleavage at the carboxyl of hydrophobic amino acids, but fails to cleave 15-Leu-|-Tyr-16, 16-Tyr-|-Leu-17 and 24-Phe-|-Phe-25 of insulin B chain. Activates trypsinogen, and degrades keratin. EC:3.4.23.24
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Active sitei | 93 | PROSITE-ProRule annotation | 1 | |
Active sitei | 273 | PROSITE-ProRule annotation | 1 |
GO - Molecular functioni
- aspartic-type endopeptidase activity Source: UniProtKB-KW
Keywordsi
Molecular function | Aspartyl protease, Hydrolase, Protease |
Enzyme and pathway databases
BRENDAi | 3.4.23.24, 1133 |
Protein family/group databases
MEROPSi | A01.076 |
Names & Taxonomyi
Protein namesi | |
Gene namesi | Name:SAPP2 Synonyms:ACPL |
Organismi | Candida parapsilosis (Yeast) |
Taxonomic identifieri | 5480 [NCBI] |
Taxonomic lineagei | Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Debaryomycetaceae › Candida/Lodderomyces clade › Candida |
Organism-specific databases
VEuPathDBi | FungiDB:CPAR2_102580 |
Subcellular locationi
Extracellular region or secreted
Extracellular region or secreted
- extracellular region Source: UniProtKB-SubCell
Keywords - Cellular componenti
SecretedPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Signal peptidei | 1 – 25 | Or 18, or 21Sequence analysisAdd BLAST | 25 | |
PropeptideiPRO_0000025871 | 26 – 61 | Activation peptide1 PublicationAdd BLAST | 36 | |
ChainiPRO_0000025872 | 62 – 412 | Candidapepsin-2Add BLAST | 351 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Glycosylationi | 53 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 108 ↔ 113 | By similarity | ||
Disulfide bondi | 311 ↔ 345 | By similarity |
Post-translational modificationi
O-glycosylated.Curated
Keywords - PTMi
Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, ZymogenFamily & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 75 – 383 | Peptidase A1PROSITE-ProRule annotationAdd BLAST | 309 |
Sequence similaritiesi
Belongs to the peptidase A1 family.Curated
Keywords - Domaini
SignalFamily and domain databases
CDDi | cd05474, SAP_like, 1 hit |
Gene3Di | 2.40.70.10, 2 hits |
InterProi | View protein in InterPro IPR001461, Aspartic_peptidase_A1 IPR001969, Aspartic_peptidase_AS IPR033121, PEPTIDASE_A1 IPR021109, Peptidase_aspartic_dom_sf IPR033876, SAP-like |
PANTHERi | PTHR47965, PTHR47965, 1 hit |
Pfami | View protein in Pfam PF00026, Asp, 1 hit |
PRINTSi | PR00792, PEPSIN |
SUPFAMi | SSF50630, SSF50630, 1 hit |
PROSITEi | View protein in PROSITE PS00141, ASP_PROTEASE, 2 hits PS51767, PEPTIDASE_A1, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
P32950-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MTTIAIFTKN VLLAIAFALF AQGAAIPDPA KRDDNPGFVA LDFEVTRKPL
60 70 80 90 100
DVNATSELSK RSSPSSPLYF EGPSYGIRVS VGSNKQEQQV VLDTGSSDFW
110 120 130 140 150
VVDSSASCQK GNCKQYGTFD PHSSTSFKSL GSSFRSIGYG DKSSSIGTWG
160 170 180 190 200
QDTIYLGGTS ITNQRFADVT STSVNQGILG VGRVETESAN PPYDNVPITL
210 220 230 240 250
KKQGKIKTNA YSLYLNSPGA ATGTIIFGGV DNAKYSGKLI EEPLVSDRYL
260 270 280 290 300
AVNLKSLNYN GDNSNAGFGV VVDSGTTISY LPDSIVNDLA NKVGAYLEPV
310 320 330 340 350
GLGNELYFID CNANPQGSAS FTFDNGAKIT VPLSEFVLQS TANACVWGLQ
360 370 380 390 400
SSDRQNVPPI LGDNFLRHAY AFQLDKETVL SRSGEVHFCL KCFSNLETSI
410
VWKAFFYNRY IQ
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | Z11918 Genomic DNA Translation: CAA77976.1 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | Z11918 Genomic DNA Translation: CAA77976.1 |
3D structure databases
SMRi | P32950 |
ModBasei | Search... |
Protein family/group databases
MEROPSi | A01.076 |
Organism-specific databases
VEuPathDBi | FungiDB:CPAR2_102580 |
Enzyme and pathway databases
BRENDAi | 3.4.23.24, 1133 |
Family and domain databases
CDDi | cd05474, SAP_like, 1 hit |
Gene3Di | 2.40.70.10, 2 hits |
InterProi | View protein in InterPro IPR001461, Aspartic_peptidase_A1 IPR001969, Aspartic_peptidase_AS IPR033121, PEPTIDASE_A1 IPR021109, Peptidase_aspartic_dom_sf IPR033876, SAP-like |
PANTHERi | PTHR47965, PTHR47965, 1 hit |
Pfami | View protein in Pfam PF00026, Asp, 1 hit |
PRINTSi | PR00792, PEPSIN |
SUPFAMi | SSF50630, SSF50630, 1 hit |
PROSITEi | View protein in PROSITE PS00141, ASP_PROTEASE, 2 hits PS51767, PEPTIDASE_A1, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | CARP2_CANPA | |
Accessioni | P32950Primary (citable) accession number: P32950 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | October 1, 1993 |
Last sequence update: | October 1, 1993 | |
Last modified: | September 29, 2021 | |
This is version 98 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Fungal Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Direct protein sequencingDocuments
- Peptidase families
Classification of peptidase families and list of entries - SIMILARITY comments
Index of protein domains and families