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Reviewed, UniProtKB/Swiss-Prot P09177 (CARP_RHIPU)

Last modified July 22, 2008. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Mucorpepsin
    EC=3.4.23.23
Alternative name(s):
    Mucor rennin
OrganismRhizomucor pusillus
Taxonomic identifier4840 [NCBI]
Taxonomic lineageEukaryotaFungiFungi incertae sedisBasal fungal lineagesMucoromycotinaMucoralesMucoraceaeRhizomucor

Protein attributes

Sequence length427 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

This enzyme, capable of clotting milk is frequently used for cheese production.

Catalytic activity

Hydrolysis of proteins, favoring hydrophobic residues at P1 and P1'. Clots milk. Does not accept Lys at P1, and hence does not activate trypsinogen.

Sequence similarities

Belongs to the peptidase A1 family.

Ontologies

Keywords

   DomainSignal
   Molecular functionAspartyl protease
Hydrolase
Protease
   PTMGlycoprotein
Zymogen
   Technical term3D-structure
Direct protein sequencing

Gene Ontology (GO)

None. [Check GOA]

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical view

Molecule processing

Signal peptide1 – 2222
Propeptide23 – 6644Activation peptide
Chain67 – 427361Mucorpepsin

Sites

Active site1041
Active site3031

Amino acid modifications

Glycosylation2541N-linked (GlcNAc...)
Disulfide bond117 ↔ 123
Disulfide bond338 ↔ 382

Experimental info

Sequence conflict4271N → D AA sequence Ref.2

Secondary structure

...................................................................... 427
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P09177-1 [UniParc].

Last modified January 1, 1990. Version 2.
Checksum: DB560157A5D99BCF

FASTA42745,646
        10         20         30         40         50         60 
MLFSKISSAI LLTAASFALT SARPVSKQSD ADDKLLALPL TSVNRKYSQT KHGQQAAEKL 

        70         80         90        100        110        120 
GGIKAFAEGD GSVDTPGLYD FDLEEYAIPV SIGTPGQDFY LLFDTGSSDT WVPHKGCDNS 

       130        140        150        160        170        180 
EGCVGKRFFD PSSSSTFKET DYNLNITYGT GGANGIYFRD SITVGGATVK QQTLAYVDNV 

       190        200        210        220        230        240 
SGPTAEQSPD SELFLDGMFG AAYPDNTAME AEYGDTYNTV HVNLYKQGLI SSPVFSVYMN 

       250        260        270        280        290        300 
TNDGGGQVVF GGANNTLLGG DIQYTDVLKS RGGYFFWDAP VTGVKIDGAD AVSFDGAQAF 

       310        320        330        340        350        360 
TIDTGTNFFI APSSFAEKVV KAALPDATES QQGYTVPCSK YQDSKTTFSL VLQKSGSSSD 

       370        380        390        400        410        420 
TIDVSVPISK MLLPVDKSGE TCMFIVLPDG GNQFIVGNLF LRFFVNVYDF GKNRIGFAPL 


ASGYENN 

« Hide

References

[1]"Cloning and sequencing of a gene for Mucor rennin, an aspartate protease from Mucor pusillus."
Tonouchi N., Shoun H., Uozumi T., Beppu T.
Nucleic Acids Res. 14:7557-7568(1986) [PubMed: 3534790] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
Strain: IFO 4578(+).
[2]"Protein chemical characterization of Mucor pusillus aspartic proteinase. Amino acid sequence homology with the other aspartic proteinases, disulfide bond arrangement and site of carbohydrate attachment."
Baudys M., Foundling S., Pavlik M., Blundell T.L., Kostka V.
FEBS Lett. 235:271-274(1988) [PubMed: 3042459] [Abstract]
Cited for: PROTEIN SEQUENCE OF 67-427.
[3]"Secretion by yeast of the zymogen form of Mucor rennin, an aspartic proteinase of Mucor pusillus, and its conversion to the mature form."
Hiramatsu R., Aikawa J., Horinouchi S., Beppu T.
J. Biol. Chem. 264:16862-16866(1989) [PubMed: 2506185] [Abstract]
Cited for: SEQUENCE REVISION TO 22, PROTEOLYTIC PROCESSING.
[4]"X-ray analyses of aspartic proteinases. V. Structure and refinement at 2.0-A resolution of the aspartic proteinase from Mucor pusillus."
Newman M., Watson F., Roychowdhury P., Jones H., Badassi M., Cleasby A., Wood S.P., Tickle I.J., Blundell T.L.
J. Mol. Biol. 230:260-283(1993) [PubMed: 8450540] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).

Cross-references

Sequence databases

X06219 Genomic DNA. Translation: CAA29568.1. Sequence problems.
PIRA25767.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1MPPX-ray2.00A67-426[»]
SMRP09177. Positions 71-427.
ModBaseSearch...

Protein family/group databases

MEROPSA01.013.

Family and domain databases

InterProIPR001969. Pept_Asp_AS.
IPR009007. Pept_Aspartc_cat.
IPR001461. Peptidase_A1.
[Graphical view]
Gene3DG3DSA:2.40.70.10. Pept_Aspartc_cat. 1 hit.
PANTHERPTHR13683. Peptidase_A1. 1 hit.
PfamPF00026. Asp. 1 hit.
[Graphical view]
PRINTSPR00792. PEPSIN.
PROSITEPS00141. ASP_PROTEASE. 2 hits.
[Graphical view]
ProDomP09177.
[Graphical view] [Entries sharing at least one domain]
BLOCKSSearch...

Other Resources

LinkHubP09177.
ProtoNetSearch...

Entry information

Entry nameCARP_RHIPU
AccessionPrimary (citable) accession number: P09177
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 1, 1990
Last modified: July 22, 2008
This is version 69 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents