UniProtKB - P80884 (ANAN_ANACO)
Protein
Ananain
Gene
AN1
Organism
Ananas comosus (Pineapple) (Ananas ananas)
Status
Functioni
Cysteine protease. Displays a high level of diversity in substrate specificity at the P1-P1' cleavage site. A hydrophilic P1 residue is preferred, with Gln or Arg strongly preferred. Favors an Ile/Leu residue at the P2 position of substrates, with an overall higher preference for Leu. The optimal tripeptide for cleavage is Pro-Leu-Gln, with cleavage occurring after the Gln residue. Another optimal tripeptide is Val-Leu-Arg, which may imply that a hydrophobic residue at the P3 position of substrates is preferred.1 Publication
Catalytic activityi
- Hydrolysis of proteins with broad specificity for peptide bonds. Best reported small molecule substrate Bz-Phe-Val-Arg-|-NHMec, but broader specificity than fruit bromelain.1 Publication EC:3.4.22.31
Activity regulationi
Strongly inhibited by chicken egg-white cystatin (Probable). Inhibited by iodoacetamide and the active-site-directed inhibitor trans-epoxysuccinyl-L-leucylamido-(4-guanidino)butane (E-64) (PubMed:31306685).Curated1 Publication
Kineticsi
kcat is 13.9 s(-1) for Z-Phe-Val-Arg-AMC. kcat is 1.58 s(-1) for Z-Phe-Arg-AMC. kcat is 0.16 s(-1) for Z-Arg-Arg-AMC. kcat is 9.80 s(-1) for Pro-Leu-Gln. kcat is 7.13 s(-1) for Val-Leu-Arg. kcat is 5.62 s(-1) for Pro-Leu-Arg. kcat is 4.96 s(-1) for Ala-Leu-Arg. kcat is 6.29 s(-1) for Val-Leu-Lys. kcat is 6.08 s(-1) for Pro-Leu-Lys. kcat is 3.58 s(-1) for Ala-Leu-Lys. kcat is 0.36 s(-1) for Pro-Leu-Asn.1 Publication
- KM=10.5 µM for synthetic 7-amino-4-methylcoumarin (AMC) substrate Z-Phe-Val-Arg-AMC (at pH 5.0 and 37 degrees Celsius)1 Publication
- KM=18.0 µM for synthetic 7-amino-4-methylcoumarin (AMC) substrate Z-Phe-Arg-AMC (at pH 5.0 and 37 degrees Celsius)1 Publication
- KM=198 µM for synthetic 7-amino-4-methylcoumarin (AMC) substrate Z-Arg-Arg-AMC (at pH 5.0 and 37 degrees Celsius)1 Publication
- KM=5.92 µM for tripeptidyl substrate Pro-Leu-Gln (at pH 7.4 and 37 degrees Celsius)1 Publication
- KM=4.29 µM for tripeptidyl substrate Val-Leu-Arg (at pH 7.4 and 37 degrees Celsius)1 Publication
- KM=3.94 µM for tripeptidyl substrate Pro-Leu-Arg (at pH 7.4 and 37 degrees Celsius)1 Publication
- KM=4.15 µM for tripeptidyl substrate Ala-Leu-Arg (at pH 7.4 and 37 degrees Celsius)1 Publication
- KM=5.36 µM for tripeptidyl substrate Val-Leu-Lys (at pH 7.4 and 37 degrees Celsius)1 Publication
- KM=6.94 µM for tripeptidyl substrate Pro-Leu-Lys (at pH 7.4 and 37 degrees Celsius)1 Publication
- KM=5.85 µM for tripeptidyl substrate Ala-Leu-Lys (at pH 7.4 and 37 degrees Celsius)1 Publication
- KM=4.50 µM for tripeptidyl substrate Pro-Leu-Asn (at pH 7.4 and 37 degrees Celsius)1 Publication
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Active sitei | 147 | PROSITE-ProRule annotation1 Publication | 1 | |
Active sitei | 279 | PROSITE-ProRule annotation1 Publication | 1 | |
Active sitei | 300 | PROSITE-ProRule annotation | 1 |
GO - Molecular functioni
- cysteine-type peptidase activity Source: UniProtKB-KW
Keywordsi
Molecular function | Hydrolase, Protease, Thiol protease |
Protein family/group databases
MEROPSi | I29.003 |
Names & Taxonomyi
Protein namesi | |
Gene namesi | Name:AN11 PublicationImported |
Organismi | Ananas comosus (Pineapple) (Ananas ananas) |
Taxonomic identifieri | 4615 [NCBI] |
Taxonomic lineagei | Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliopsida › Liliopsida › Poales › Bromeliaceae › Bromelioideae › Ananas |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Signal peptidei | 1 – 24 | Sequence analysisAdd BLAST | 24 | |
PropeptideiPRO_0000026400 | 25 – 122 | Sequence analysis1 PublicationAdd BLAST | 98 | |
ChainiPRO_0000026401 | 123 – 345 | Ananain1 PublicationAdd BLAST | 223 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Disulfide bondi | 144 ↔ 184 | Combined sources1 Publication | ||
Disulfide bondi | 178 ↔ 217 | Combined sources1 Publication | ||
Disulfide bondi | 273 ↔ 325 | Combined sources1 Publication |
Keywords - PTMi
Disulfide bond, ZymogenExpressioni
Tissue specificityi
Stem (at protein level).1 Publication
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P80884 |
ModBasei | Search... |
PDBe-KBi | Search... |
Family & Domainsi
Sequence similaritiesi
Belongs to the peptidase C1 family.PROSITE-ProRule annotation
Keywords - Domaini
SignalFamily and domain databases
CDDi | cd02248, Peptidase_C1A, 1 hit |
InterProi | View protein in InterPro IPR038765, Papain-like_cys_pep_sf IPR025661, Pept_asp_AS IPR000169, Pept_cys_AS IPR025660, Pept_his_AS IPR000668, Peptidase_C1A_C IPR039417, Peptidase_C1A_papain-like IPR013201, Prot_inhib_I29 |
Pfami | View protein in Pfam PF08246, Inhibitor_I29, 1 hit PF00112, Peptidase_C1, 1 hit |
PRINTSi | PR00705, PAPAIN |
SMARTi | View protein in SMART SM00848, Inhibitor_I29, 1 hit SM00645, Pept_C1, 1 hit |
SUPFAMi | SSF54001, SSF54001, 1 hit |
PROSITEi | View protein in PROSITE PS00640, THIOL_PROTEASE_ASN, 1 hit PS00139, THIOL_PROTEASE_CYS, 1 hit PS00639, THIOL_PROTEASE_HIS, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
P80884-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MTSKVQLVFL FLFLCVMWAS PSAASCDEPS DPMMKQFEEW MAEYGRVYKD
60 70 80 90 100
NDEKMLRFQI FKNNVNHIET FNNRNGNSYT LGINQFTDMT NNEFVAQYTG
110 120 130 140 150
LSLPLNIKRE PVVSFDDVDI SSVPQSIDWR DSGAVTSVKN QGRCGSCWAF
160 170 180 190 200
ASIATVESIY KIKRGNLVSL SEQQVLDCAV SYGCKGGWIN KAYSFIISNK
210 220 230 240 250
GVASAAIYPY KAAKGTCKTN GVPNSAYITR YTYVQRNNER NMMYAVSNQP
260 270 280 290 300
IAAALDASGN FQHYKRGVFT GPCGTRLNHA IVIIGYGQDS SGKKFWIVRN
310 320 330 340
SWGAGWGEGG YIRLARDVSS SFGLCGIAMD PLYPTLQSGP SVEVI
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 291 | S → A AA sequence (PubMed:9355753).Curated | 1 | |
Sequence conflicti | 324 | L → I AA sequence (PubMed:9355753).Curated | 1 |
Mass spectrometryi
Molecular mass is 23478 Da. Determined by ESI. 1 Publication
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AJ002477 mRNA Translation: CAA05487.1 |
PIRi | T07839 |
RefSeqi | XP_020089326.1, XM_020233737.1 |
Genome annotation databases
GeneIDi | 109710925 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AJ002477 mRNA Translation: CAA05487.1 |
PIRi | T07839 |
RefSeqi | XP_020089326.1, XM_020233737.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
6MIS | X-ray | 1.98 | A/B | 123-337 | [»] | |
6OKJ | X-ray | 1.73 | A/B | 123-337 | [»] | |
SMRi | P80884 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein family/group databases
Allergomei | 694, Ana c 2 |
MEROPSi | I29.003 |
Genome annotation databases
GeneIDi | 109710925 |
Family and domain databases
CDDi | cd02248, Peptidase_C1A, 1 hit |
InterProi | View protein in InterPro IPR038765, Papain-like_cys_pep_sf IPR025661, Pept_asp_AS IPR000169, Pept_cys_AS IPR025660, Pept_his_AS IPR000668, Peptidase_C1A_C IPR039417, Peptidase_C1A_papain-like IPR013201, Prot_inhib_I29 |
Pfami | View protein in Pfam PF08246, Inhibitor_I29, 1 hit PF00112, Peptidase_C1, 1 hit |
PRINTSi | PR00705, PAPAIN |
SMARTi | View protein in SMART SM00848, Inhibitor_I29, 1 hit SM00645, Pept_C1, 1 hit |
SUPFAMi | SSF54001, SSF54001, 1 hit |
PROSITEi | View protein in PROSITE PS00640, THIOL_PROTEASE_ASN, 1 hit PS00139, THIOL_PROTEASE_CYS, 1 hit PS00639, THIOL_PROTEASE_HIS, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | ANAN_ANACO | |
Accessioni | P80884Primary (citable) accession number: P80884 Secondary accession number(s): O22293 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | November 1, 1997 |
Last sequence update: | April 27, 2001 | |
Last modified: | December 2, 2020 | |
This is version 87 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Plant Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencingDocuments
- Peptidase families
Classification of peptidase families and list of entries - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families