Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P06026

- CARP_RHICH

UniProt

P06026 - CARP_RHICH

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Rhizopuspepsin

Gene
N/A
Organism
Rhizopus chinensis (Bread mold)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

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
Complete GO annotation...

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

        10         20         30         40         50
MKFTLISSCI AIAALAVAVD AAPGEKKISI PLAKNPNYKP SAKNAIQKAI
60 70 80 90 100
AKYNKHKINT STGGIVPDAG VGTVPMTDYG NDVEYYGQVT IGTPGKKFNL
110 120 130 140 150
DFDTGSSDLW IASTLCTNCG SRQTKYDPKQ SSTYQADGRT WSISYGDGSS
160 170 180 190 200
ASGILAKDNV NLGGLLIKGQ TIELAKREAA SFANGPNDGL LGLGFDTITT
210 220 230 240 250
VRGVKTPMDN LISQGLISRP IFGVYLGKAS NGGGGEYIFG GYDSTKFKGS
260 270 280 290 300
LTTVPIDNSR GWWGITVDRA TVGTSTVASS FDGILDTGTT LLILPNNVAA
310 320 330 340 350
SVARAYGASD NGDGTYTISC DTSRFKPLVF SINGASFQVS PDSLVFEEYQ
360 370 380 390
GQCIAGFGYG NFDFAIIGDT FLKNNYVVFN QGVPEVQIAP VAQ
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