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Protein

Candidapepsin-2

Gene

SAPP2

Organism
Candida parapsilosis (Yeast)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

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.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei93PROSITE-ProRule annotation1
Active sitei273PROSITE-ProRule annotation1

GO - Molecular functioni

Keywordsi

Molecular functionAspartyl protease, Hydrolase, Protease

Enzyme and pathway databases

BRENDAi3.4.23.24. 1133.

Protein family/group databases

MEROPSiA01.076.

Names & Taxonomyi

Protein namesi
Recommended name:
Candidapepsin-2 (EC:3.4.23.24)
Alternative name(s):
ACP 2
Aspartate protease 2
Gene namesi
Name:SAPP2
Synonyms:ACPL
OrganismiCandida parapsilosis (Yeast)
Taxonomic identifieri5480 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeCandida/Lodderomyces cladeCandida

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 25Or 18, or 21Sequence analysisAdd BLAST25
PropeptideiPRO_000002587126 – 61Activation peptide1 PublicationAdd BLAST36
ChainiPRO_000002587262 – 412Candidapepsin-2Add BLAST351

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi53N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi108 ↔ 113By similarity
Disulfide bondi311 ↔ 345By similarity

Post-translational modificationi

O-glycosylated.Curated

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Zymogen

Structurei

3D structure databases

ProteinModelPortaliP32950.
SMRiP32950.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini75 – 383Peptidase A1PROSITE-ProRule annotationAdd BLAST309

Sequence similaritiesi

Belongs to the peptidase A1 family.Curated

Keywords - Domaini

Signal

Family and domain databases

CDDicd05474. SAP_like. 1 hit.
Gene3Di2.40.70.10. 2 hits.
InterProiView protein in InterPro
IPR001461. Aspartic_peptidase_A1.
IPR001969. Aspartic_peptidase_AS.
IPR033121. PEPTIDASE_A1.
IPR021109. Peptidase_aspartic_dom.
IPR033876. SAP-like.
PANTHERiPTHR13683. PTHR13683. 1 hit.
PfamiView protein in Pfam
PF00026. Asp. 1 hit.
PRINTSiPR00792. PEPSIN.
SUPFAMiSSF50630. SSF50630. 1 hit.
PROSITEiView protein in PROSITE
PS00141. ASP_PROTEASE. 2 hits.
PS51767. PEPTIDASE_A1. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P32950-1 [UniParc]FASTAAdd to basket

« Hide

        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
Length:412
Mass (Da):44,443
Last modified:October 1, 1993 - v1
Checksum:i6D4DE8B954ADC8B3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z11918 Genomic DNA. Translation: CAA77976.1.

Similar proteinsi

Entry informationi

Entry nameiCARP2_CANPA
AccessioniPrimary (citable) accession number: P32950
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: May 10, 2017
This is version 91 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families