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P06026

- CARP_RHICH

UniProt

P06026 - CARP_RHICH

Protein

Rhizopuspepsin

Gene
N/A
Organism
Rhizopus chinensis (Bread mold)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 94 (01 Oct 2014)
      Sequence version 2 (01 Oct 1996)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    Hydrolysis of proteins with broad specificity similar to that of pepsin A, preferring hydrophobic residues at P1 and P1'. Clots milk and activates trypsinogen. Does not cleave 4-Gln-|-His-5, but does cleave 10-His-|-Leu-11 and 12-Val-|-Glu-13 in B chain of insulin.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei103 – 1031PROSITE-ProRule annotation
    Active sitei286 – 2861PROSITE-ProRule annotation

    GO - Molecular functioni

    1. aspartic-type endopeptidase activity Source: UniProtKB-KW

    Keywords - Molecular functioni

    Aspartyl protease, Hydrolase, Protease

    Protein family/group databases

    MEROPSiA01.012.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Rhizopuspepsin (EC:3.4.23.21)
    OrganismiRhizopus chinensis (Bread mold)
    Taxonomic identifieri4843 [NCBI]
    Taxonomic lineageiEukaryotaFungiFungi incertae sedisEarly diverging fungal lineagesMucoromycotinaMucoralesMucorineaeRhizopodaceaeRhizopus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2121Sequence AnalysisAdd
    BLAST
    Propeptidei22 – 6847Activation peptide1 PublicationPRO_0000025881Add
    BLAST
    Chaini69 – 393325RhizopuspepsinPRO_0000025882Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi116 ↔ 119
    Disulfide bondi320 ↔ 353

    Keywords - PTMi

    Disulfide bond, Zymogen

    Interactioni

    Structurei

    Secondary structure

    1
    393
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi73 – 797
    Turni80 – 834
    Beta strandi84 – 918
    Turni92 – 954
    Beta strandi96 – 1038
    Beta strandi110 – 1134
    Beta strandi121 – 1233
    Helixi128 – 1303
    Beta strandi135 – 14410
    Beta strandi150 – 16213
    Beta strandi165 – 17814
    Helixi180 – 1834
    Beta strandi188 – 1925
    Helixi196 – 1983
    Helixi207 – 2137
    Beta strandi218 – 2269
    Helixi229 – 2313
    Beta strandi235 – 2395
    Helixi244 – 2463
    Beta strandi252 – 2554
    Beta strandi264 – 2674
    Beta strandi269 – 2724
    Beta strandi275 – 2784
    Beta strandi281 – 2855
    Beta strandi290 – 2956
    Helixi296 – 30510
    Beta strandi312 – 3143
    Beta strandi316 – 3183
    Helixi322 – 3243
    Beta strandi328 – 3325
    Beta strandi335 – 3395
    Helixi341 – 3444
    Beta strandi345 – 3495
    Beta strandi352 – 36716
    Helixi369 – 3724
    Beta strandi375 – 3806
    Turni381 – 3844
    Beta strandi385 – 3917

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1UH7X-ray2.10A69-392[»]
    1UH8X-ray2.30A69-392[»]
    1UH9X-ray2.00A69-392[»]
    2APRX-ray1.80A69-392[»]
    3APRX-ray1.80E69-392[»]
    4APRX-ray2.50E69-392[»]
    5APRX-ray2.10E69-392[»]
    6APRX-ray2.50E69-392[»]
    ProteinModelPortaliP06026.
    SMRiP06026. Positions 69-393.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP06026.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase A1 family.Curated

    Keywords - Domaini

    Signal

    Family and domain databases

    Gene3Di2.40.70.10. 2 hits.
    InterProiIPR001461. Aspartic_peptidase.
    IPR001969. Aspartic_peptidase_AS.
    IPR021109. Peptidase_aspartic_dom.
    [Graphical view]
    PANTHERiPTHR13683. PTHR13683. 1 hit.
    PfamiPF00026. Asp. 1 hit.
    [Graphical view]
    PRINTSiPR00792. PEPSIN.
    SUPFAMiSSF50630. SSF50630. 1 hit.
    PROSITEiPS00141. ASP_PROTEASE. 2 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P06026-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKFTLISSCI AIAALAVAVD AAPGEKKISI PLAKNPNYKP SAKNAIQKAI    50
    AKYNKHKINT STGGIVPDAG VGTVPMTDYG NDVEYYGQVT IGTPGKKFNL 100
    DFDTGSSDLW IASTLCTNCG SRQTKYDPKQ SSTYQADGRT WSISYGDGSS 150
    ASGILAKDNV NLGGLLIKGQ TIELAKREAA SFANGPNDGL LGLGFDTITT 200
    VRGVKTPMDN LISQGLISRP IFGVYLGKAS NGGGGEYIFG GYDSTKFKGS 250
    LTTVPIDNSR GWWGITVDRA TVGTSTVASS FDGILDTGTT LLILPNNVAA 300
    SVARAYGASD NGDGTYTISC DTSRFKPLVF SINGASFQVS PDSLVFEEYQ 350
    GQCIAGFGYG NFDFAIIGDT FLKNNYVVFN QGVPEVQIAP VAQ 393
    Length:393
    Mass (Da):41,327
    Last modified:October 1, 1996 - v2
    Checksum:i479BBDB3D001D25C
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti83 – 831V → I.
    Natural varianti129 – 1291K → N.
    Natural varianti184 – 1841N → S.
    Natural varianti230 – 2301S → K.
    Natural varianti298 – 2981V → I.
    Natural varianti309 – 3091S → Y.
    Natural varianti361 – 3611N → D.
    Natural varianti393 – 3931Q → E.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L33859 Genomic DNA. Translation: AAB59306.1.
    L33858 Genomic DNA. Translation: AAB59305.1.
    J02651 mRNA. Translation: AAA33879.1.
    PIRiA26681.
    A41415.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L33859 Genomic DNA. Translation: AAB59306.1 .
    L33858 Genomic DNA. Translation: AAB59305.1 .
    J02651 mRNA. Translation: AAA33879.1 .
    PIRi A26681.
    A41415.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1UH7 X-ray 2.10 A 69-392 [» ]
    1UH8 X-ray 2.30 A 69-392 [» ]
    1UH9 X-ray 2.00 A 69-392 [» ]
    2APR X-ray 1.80 A 69-392 [» ]
    3APR X-ray 1.80 E 69-392 [» ]
    4APR X-ray 2.50 E 69-392 [» ]
    5APR X-ray 2.10 E 69-392 [» ]
    6APR X-ray 2.50 E 69-392 [» ]
    ProteinModelPortali P06026.
    SMRi P06026. Positions 69-393.
    ModBasei Search...
    MobiDBi Search...

    Chemistry

    BindingDBi P06026.
    ChEMBLi CHEMBL4253.

    Protein family/group databases

    MEROPSi A01.012.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P06026.

    Family and domain databases

    Gene3Di 2.40.70.10. 2 hits.
    InterProi IPR001461. Aspartic_peptidase.
    IPR001969. Aspartic_peptidase_AS.
    IPR021109. Peptidase_aspartic_dom.
    [Graphical view ]
    PANTHERi PTHR13683. PTHR13683. 1 hit.
    Pfami PF00026. Asp. 1 hit.
    [Graphical view ]
    PRINTSi PR00792. PEPSIN.
    SUPFAMi SSF50630. SSF50630. 1 hit.
    PROSITEi PS00141. ASP_PROTEASE. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Gregoli P.A., Delaney R.
      Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE.
    2. "Amino acid sequence of rhizopuspepsin isozyme pI 5."
      Delaney R., Wong R.N.S., Meng G.-Z., Wu N.-H., Tang J.
      J. Biol. Chem. 262:1461-1467(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 42-393.
    3. "The amino acid sequence of rhizopuspepsin, an aspartic proteinase from Rhizopus chinensis."
      Takahashi K.
      J. Biol. Chem. 262:1468-1478(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 69-393.
    4. "Homology among acid proteases: comparison of crystal structures at 3-A resolution of acid proteases from Rhizopus chinensis and Endothia parasitica."
      Subramanian E., Swan I.D.A., Liu M., Davies D.R., Jenkins J.A., Tickle I.J., Blundell T.L.
      Proc. Natl. Acad. Sci. U.S.A. 74:556-559(1977) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 69-392.
    5. "Structure and refinement at 1.8-A resolution of the aspartic proteinase from Rhizopus chinensis."
      Suguna K., Bott R.R., Padlan E.A., Subramanian E., Sheriff S., Cohen G.H., Davies D.R.
      J. Mol. Biol. 196:877-900(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 69-392.

    Entry informationi

    Entry nameiCARP_RHICH
    AccessioniPrimary (citable) accession number: P06026
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 13, 1987
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 94 of the entry and version 2 of the sequence. [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

    External Data

    Dasty 3