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UniProtKB - P43096 (CARP7_CANAX)
Protein
Candidapepsin-7
Gene
SAP7
Organism
Candida albicans (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 | 244 | PROSITE-ProRule annotation | 1 | |
Active sitei | 464 | PROSITE-ProRule annotation | 1 |
GO - Molecular functioni
- aspartic-type endopeptidase activity Source: UniProtKB-KW
Keywordsi
Molecular function | Aspartyl protease, Hydrolase, Protease |
Protein family/group databases
MEROPSi | A01.065 |
Names & Taxonomyi
Protein namesi | Recommended name: Candidapepsin-7 (EC:3.4.23.24)Alternative name(s): ACP 7 Aspartate protease 7 Secreted aspartic protease 7 |
Gene namesi | Name:SAP7 |
Organismi | Candida albicans (Yeast) |
Taxonomic identifieri | 5476 [NCBI] |
Taxonomic lineagei | Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Debaryomycetaceae › Candida/Lodderomyces clade › Candida |
Organism-specific databases
VEuPathDBi | FungiDB:C1_04870W_A FungiDB:CAWG_00909 |
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 – 16 | Sequence analysisAdd BLAST | 16 | |
PropeptideiPRO_0000025860 | 17 – 211 | Activation peptideSequence analysisAdd BLAST | 195 | |
ChainiPRO_0000025861 | 212 – 588 | Candidapepsin-7Add BLAST | 377 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Glycosylationi | 150 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 260 ↔ 269 | By similarity | ||
Glycosylationi | 286 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 308 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 327 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 423 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 445 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 486 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 500 ↔ 540 | By similarity |
Post-translational modificationi
O-glycosylated.By similarity
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 | 226 – 574 | Peptidase A1PROSITE-ProRule annotationAdd BLAST | 349 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 83 – 124 | DisorderedSequence analysisAdd BLAST | 42 | |
Regioni | 144 – 209 | DisorderedSequence analysisAdd BLAST | 66 |
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, 1 hit PS51767, PEPTIDASE_A1, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
P43096-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MQRVLELLLL SSTALAVIGD GFIALPVHKL QAGEGSAHFP NRLPIFDVVN
60 70 80 90 100
GVAKSVEDDV NQIIQPIFGN GIFSGGSIQG THSGNGHSVK YEVSLPSSSA
110 120 130 140 150
QKGSNGPSST DNKDTDPSKT GFSLDDLMNS ISTDFWNLIG LNKPPTSSDN
160 170 180 190 200
GSKDADFTPS AVSQVEQPTS KSVESTAPGS ASSASSSSSS EAASSSQPSE
210 220 230 240 250
DSQPSSSANK KTGAFFLSLD NTQTLYTATL KVGSPAQEVQ VMIDTGSSDL
260 270 280 290 300
WFISSGNSQC KVNGGSIDCD KYGVFDKSKS SSWHDNKTDY SISYYDGDKA
310 320 330 340 350
SGTMGQDNIT FADGFSIENA NFAVIDNTTS SIGVFGVGYP ELEAVKSKYT
360 370 380 390 400
NLPFAMKEQN LIAKVAYSLY LDSRDAVQGY ILFGGIDHAF YTGDLKAFDI
410 420 430 440 450
VQCNDKYVYS QIPLTSVASS LNNYTNAYGL PAGSNHPKVG AVIYNGTDSF
460 470 480 490 500
NGGVDLKDTL TLLDTGTTYS YLSKDQVESI VGLYGNVTYN DAGKAYEVPC
510 520 530 540 550
WVGNPGNYLE FNFKNEQYIK VPTSEFVISV GTYASGAELC VFGILPGTHS
560 570 580
ILGDNFMRSV YAVFDLEDHV ISIAQAAYND NHAVVPIE
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | Z30193 Genomic DNA Translation: CAA82925.1 |
PIRi | S49058, S42074 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | Z30193 Genomic DNA Translation: CAA82925.1 |
PIRi | S49058, S42074 |
3D structure databases
SMRi | P43096 |
ModBasei | Search... |
Protein family/group databases
MEROPSi | A01.065 |
Organism-specific databases
VEuPathDBi | FungiDB:C1_04870W_A FungiDB:CAWG_00909 |
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, 1 hit PS51767, PEPTIDASE_A1, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | CARP7_CANAX | |
Accessioni | P43096Primary (citable) accession number: P43096 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | November 1, 1995 |
Last sequence update: | November 1, 1995 | |
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
Documents
- Peptidase families
Classification of peptidase families and list of entries - SIMILARITY comments
Index of protein domains and families