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Protein

Candidapepsin-1

Gene

SAPP1

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 sitei94PROSITE-ProRule annotation1
Active sitei282PROSITE-ProRule annotation1

GO - Molecular functioni

Keywordsi

Molecular functionAspartyl protease, Hydrolase, Protease

Enzyme and pathway databases

BRENDAi3.4.23.24. 1133.

Protein family/group databases

MEROPSiA01.038.

Names & Taxonomyi

Protein namesi
Recommended name:
Candidapepsin-1 (EC:3.4.23.24)
Alternative name(s):
ACP 1
Aspartate protease 1
Gene namesi
Name:SAPP1
Synonyms:ACPR
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_000002586926 – 62Activation peptide1 PublicationAdd BLAST37
ChainiPRO_000002587063 – 402Candidapepsin-1Add BLAST340

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi52N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi109 ↔ 115By similarity
Disulfide bondi320 ↔ 354By similarity

Post-translational modificationi

O-glycosylated.Curated

Keywords - PTMi

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

Structurei

Secondary structure

1402
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi65 – 71Combined sources7
Beta strandi73 – 82Combined sources10
Turni83 – 86Combined sources4
Beta strandi87 – 94Combined sources8
Beta strandi100 – 109Combined sources10
Turni115 – 118Combined sources4
Helixi123 – 125Combined sources3
Beta strandi130 – 139Combined sources10
Beta strandi145 – 157Combined sources13
Beta strandi160 – 177Combined sources18
Beta strandi179 – 181Combined sources3
Helixi185 – 187Combined sources3
Helixi205 – 211Combined sources7
Beta strandi216 – 223Combined sources8
Beta strandi230 – 236Combined sources7
Beta strandi238 – 240Combined sources3
Beta strandi243 – 246Combined sources4
Beta strandi249 – 253Combined sources5
Beta strandi256 – 258Combined sources3
Beta strandi260 – 270Combined sources11
Beta strandi272 – 281Combined sources10
Beta strandi286 – 290Combined sources5
Helixi292 – 302Combined sources11
Beta strandi305 – 310Combined sources6
Beta strandi313 – 318Combined sources6
Beta strandi326 – 332Combined sources7
Beta strandi337 – 341Combined sources5
Helixi342 – 345Combined sources4
Beta strandi346 – 348Combined sources3
Beta strandi350 – 352Combined sources3
Beta strandi354 – 360Combined sources7
Helixi368 – 371Combined sources4
Beta strandi377 – 380Combined sources4
Turni381 – 384Combined sources4
Beta strandi385 – 391Combined sources7
Beta strandi399 – 401Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3FV3X-ray1.85A/B/C/D/E/F/G/H63-402[»]
3TNEX-ray2.40A/B63-402[»]
ProteinModelPortaliP32951.
SMRiP32951.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP32951.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini76 – 389Peptidase A1PROSITE-ProRule annotationAdd BLAST314

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.

P32951-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVAIVTLTRQ VLLTIALALF AQGAAIPEEA AKRDDNPGFV ALDFDVLRKP
60 70 80 90 100
LNLTEALLRE KRDSISLSLI NEGPSYASKV SVGSNKQQQT VIIDTGSSDF
110 120 130 140 150
WVVDSNAQCG KGVDCKSSGT FTPSSSSSYK NLGAAFTIRY GDGSTSQGTW
160 170 180 190 200
GKDTVTINGV SITGQQIADV TQTSVDQGIL GIGYTSNEAV YDTSGRQTTP
210 220 230 240 250
NYDNVPVTLK KQGKIRTNAY SLYLNSPSAE TGTIIFGGVD NAKYSGKLVA
260 270 280 290 300
EQVTSSQPLT ISLASVNLKG SSFSFGDGAL LDSGTTLTYF PSDFAAQLAD
310 320 330 340 350
KAGARLVQVA RDQYLYFIDC NTDTSGTTVF NFGNGAKITV PNTEYVYQNG
360 370 380 390 400
DGTCLWGIQP SDDTILGDNF LRHAYYLLYN LDANTISIAQ VKYTTDSSIS

AV
Length:402
Mass (Da):42,833
Last modified:October 1, 1993 - v1
Checksum:i38B06222F52BC1EA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z11919 Genomic DNA. Translation: CAA77977.1.
PIRiB47701.

Similar proteinsi

Entry informationi

Entry nameiCARP1_CANPA
AccessioniPrimary (citable) accession number: P32951
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: May 10, 2017
This is version 99 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

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families