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Protein

Mucorpepsin

Gene
N/A
Organism
Rhizomucor miehei
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei107 – 1071PROSITE-ProRule annotation
Active sitei306 – 3061PROSITE-ProRule annotation

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Aspartyl protease, Hydrolase, Protease

Protein family/group databases

MEROPSiA01.013.

Names & Taxonomyi

Protein namesi
Recommended name:
Mucorpepsin (EC:3.4.23.23)
Alternative name(s):
Mucor rennin
OrganismiRhizomucor miehei
Taxonomic identifieri4839 [NCBI]
Taxonomic lineageiEukaryotaFungiFungi incertae sedisMucoromycotinaMucoralesLichtheimiaceaeRhizomucor

Pathology & Biotechi

Protein family/group databases

Allergomei3880. Rhi m AP.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222Add
BLAST
Propeptidei23 – 6947Activation peptide1 PublicationPRO_0000025893Add
BLAST
Chaini70 – 430361Mucorpepsin1 PublicationPRO_0000025894Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi120 ↔ 1261 Publication
Glycosylationi148 – 1481N-linked (GlcNAc...)1 Publication
Glycosylationi257 – 2571N-linked (GlcNAc...)1 Publication
Disulfide bondi341 ↔ 3851 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Structurei

Secondary structure

1
430
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi76 – 827Combined sources
Turni84 – 863Combined sources
Beta strandi89 – 957Combined sources
Turni96 – 994Combined sources
Beta strandi100 – 1078Combined sources
Beta strandi114 – 1174Combined sources
Helixi122 – 1243Combined sources
Helixi134 – 1363Combined sources
Beta strandi141 – 1499Combined sources
Beta strandi156 – 16914Combined sources
Beta strandi171 – 18313Combined sources
Helixi186 – 1883Combined sources
Beta strandi194 – 1963Combined sources
Beta strandi200 – 2034Combined sources
Helixi207 – 2093Combined sources
Helixi211 – 2166Combined sources
Helixi223 – 2297Combined sources
Beta strandi232 – 24110Combined sources
Beta strandi244 – 25411Combined sources
Helixi258 – 2603Combined sources
Beta strandi261 – 2633Combined sources
Beta strandi266 – 2694Combined sources
Beta strandi281 – 2899Combined sources
Beta strandi292 – 30615Combined sources
Beta strandi311 – 3133Combined sources
Turni316 – 3194Combined sources
Helixi322 – 3265Combined sources
Beta strandi331 – 3333Combined sources
Beta strandi334 – 3363Combined sources
Beta strandi338 – 3403Combined sources
Turni341 – 3455Combined sources
Beta strandi350 – 3578Combined sources
Beta strandi364 – 3718Combined sources
Helixi372 – 3743Combined sources
Beta strandi375 – 39218Combined sources
Beta strandi394 – 3963Combined sources
Beta strandi398 – 4003Combined sources
Helixi401 – 4044Combined sources
Beta strandi407 – 4126Combined sources
Turni413 – 4164Combined sources
Beta strandi417 – 4237Combined sources
Helixi425 – 4273Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2ASIX-ray2.15A70-430[»]
2RMPX-ray2.70A70-430[»]
ProteinModelPortaliP00799.
SMRiP00799. Positions 73-430.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00799.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini89 – 421333Peptidase A1PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase A1 family.Curated
Contains 1 peptidase A1 domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Family and domain databases

Gene3Di2.40.70.10. 2 hits.
InterProiIPR001461. Aspartic_peptidase_A1.
IPR001969. Aspartic_peptidase_AS.
IPR033121. PEPTIDASE_A1.
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.
PS51767. PEPTIDASE_A1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P00799-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLFSQITSAI LLTAASLSLT TARPVSKQSE SKDKLLALPL TSVSRKFSQT
60 70 80 90 100
KFGQQQLAEK LAGLKPFSEA AADGSVDTPG YYDFDLEEYA IPVSIGTPGQ
110 120 130 140 150
DFLLLFDTGS SDTWVPHKGC TKSEGCVGSR FFDPSASSTF KATNYNLNIT
160 170 180 190 200
YGTGGANGLY FEDSIAIGDI TVTKQILAYV DNVRGPTAEQ SPNADIFLDG
210 220 230 240 250
LFGAAYPDNT AMEAEYGSTY NTVHVNLYKQ GLISSPLFSV YMNTNSGTGE
260 270 280 290 300
VVFGGVNNTL LGGDIAYTDV MSRYGGYYFW DAPVTGITVD GSAAVRFSRP
310 320 330 340 350
QAFTIDTGTN FFIMPSSAAS KIVKAALPDA TETQQGWVVP CASYQNSKST
360 370 380 390 400
ISIVMQKSGS SSDTIEISVP VSKMLLPVDQ SNETCMFIIL PDGGNQYIVG
410 420 430
NLFLRFFVNV YDFGNNRIGF APLASAYENE
Length:430
Mass (Da):46,168
Last modified:January 1, 1988 - v1
Checksum:i1431DB2435B71CEF
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti136 – 1361A → T AA sequence (Ref. 3) Curated
Sequence conflicti157 – 1571N → D AA sequence (Ref. 3) Curated
Sequence conflicti163 – 1697Missing AA sequence (Ref. 3) Curated
Sequence conflicti252 – 2521Missing AA sequence (Ref. 3) Curated
Sequence conflicti376 – 3761Missing AA sequence (Ref. 3) Curated
Sequence conflicti392 – 3921D → N AA sequence (Ref. 3) Curated
Sequence conflicti399 – 3991V → Y AA sequence (Ref. 3) Curated
Sequence conflicti411 – 4111Missing AA sequence (Ref. 3) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti262 – 2621G → S.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M18411 mRNA. Translation: AAA33423.1.
M15267 Genomic DNA. Translation: AAA33421.1.
PIRiA29039. CMUMF.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M18411 mRNA. Translation: AAA33423.1.
M15267 Genomic DNA. Translation: AAA33421.1.
PIRiA29039. CMUMF.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2ASIX-ray2.15A70-430[»]
2RMPX-ray2.70A70-430[»]
ProteinModelPortaliP00799.
SMRiP00799. Positions 73-430.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

Allergomei3880. Rhi m AP.
MEROPSiA01.013.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP00799.

Family and domain databases

Gene3Di2.40.70.10. 2 hits.
InterProiIPR001461. Aspartic_peptidase_A1.
IPR001969. Aspartic_peptidase_AS.
IPR033121. PEPTIDASE_A1.
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.
PS51767. PEPTIDASE_A1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Primary structure of Mucor miehei aspartyl protease: evidence for a zymogen intermediate."
    Gray G.L., Hayenga K., Cullen D., Wilson L.J., Norton S.
    Gene 48:41-53(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Primary structure of a precursor to the aspartic proteinase from Rhizomucor miehei shows that the enzyme is synthesized as a zymogen."
    Boel E., Bech A.-M., Randrup K., Draeger B., Fiil N.P., Foltmann B.
    Proteins 1:363-369(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Partial primary structure of Mucor miehei protease."
    Bech A.-M., Foltmann B.
    Neth. Milk Dairy J. 35:275-280(1981)
    Cited for: PROTEIN SEQUENCE OF 70-430.
  4. Foltmann B.
    Submitted (NOV-1982) to the PIR data bank
    Cited for: SEQUENCE REVISION.
  5. "Crystallization and preliminary X-ray structure solution of Rhizomucor miehei aspartic proteinase."
    Jia Z., Vandonselaar M., Schneider P., Quail J.W.
    Acta Crystallogr. D 51:243-244(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
  6. "Crystal structure of the aspartic proteinase from Rhizomucor miehei at 2.15-A resolution."
    Yang J., Teplyakov A., Quail J.W.
    J. Mol. Biol. 268:449-459(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS).

Entry informationi

Entry nameiCARP_RHIMI
AccessioniPrimary (citable) accession number: P00799
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 1, 1988
Last modified: April 13, 2016
This is version 93 of the entry and version 1 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.