Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q5RF14 (MIPEP_PONAB) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 54. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Mitochondrial intermediate peptidase

Short name=MIP
EC=3.4.24.59
Gene names
Name:MIPEP
OrganismPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) [Reference proteome]
Taxonomic identifier9601 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo

Protein attributes

Sequence length713 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Cleaves proteins, imported into the mitochondrion, to their mature size By similarity.

Catalytic activity

Release of an N-terminal octapeptide as second stage of processing of some proteins imported into the mitochondrion.

Cofactor

Binds 1 zinc ion By similarity.

Enzyme regulation

Activity is divalent cation-dependent. It is stimulated by manganese, magnesium or calcium ions and reversibly inhibited by zinc, cobalt and iron By similarity.

Subunit structure

Monomer By similarity.

Subcellular location

Mitochondrion matrix By similarity.

Sequence similarities

Belongs to the peptidase M3 family.

Ontologies

Keywords
   Cellular componentMitochondrion
   DomainTransit peptide
   LigandCalcium
Cobalt
Iron
Magnesium
Manganese
Metal-binding
Zinc
   Molecular functionHydrolase
Metalloprotease
Protease
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processproteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentmitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

metalloendopeptidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3535Mitochondrion By similarity
Chain36 – 713678Mitochondrial intermediate peptidase
PRO_0000319049

Sites

Active site4961 By similarity
Metal binding4951Zinc; catalytic By similarity
Metal binding4991Zinc; catalytic By similarity
Metal binding5021Zinc; catalytic By similarity

Amino acid modifications

Modified residue1261N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5RF14 [UniParc].

Last modified December 21, 2004. Version 1.
Checksum: 32FB7C32F5BD1FF9

FASTA71380,478
        10         20         30         40         50         60 
MLCVGRLGGL GARAAALPPR RAGRGILEAG IRARRVSTSW SPVGAAFNVK PQGSRLDLFG 

        70         80         90        100        110        120 
ERRGLFGVPE LSAPEGFHAA QEKALRKAEL LVGRACSTPP GPQTVLIFDE LSDSLCRVAD 

       130        140        150        160        170        180 
LADFVKIAHP EPAFREAAEE ACRSIGTMVE KLNTNVDLYQ SLRKLLADKK LVDSLDPETR 

       190        200        210        220        230        240 
RVAELFMFDF EISGIHLDKE KRKRAVDLNV KILDLSSTFL MGANFPNKIE KHLLPEHIRR 

       250        260        270        280        290        300 
NFTSAGDHII IDGLHAESPD DLVREAAYKI FLYPNAGQLK CLEELLSSRD LLAKLVGYST 

       310        320        330        340        350        360 
FSHRALQGTI AKNPETVMQF LEKLSDKLSE RTLKDFEMIR GMKMKLNPQN SEVMPWDPPY 

       370        380        390        400        410        420 
YSGVIRAERY NIEPSLYCPF FSLGACMEGL NILLNRLLGI SLYAEQPAKG EVWSEDVRKL 

       430        440        450        460        470        480 
AVVHESEGLL GYIYCDFFQR ADKPHQDCHF TIRGGRLKED GDYQLPVVVL MLNLPRSSRS 

       490        500        510        520        530        540 
SPTLLTPGMM ENLFHEMGHA MHSMLGRTRY QHVTGTRCPT DFAEVPSILM EYFANDYRVV 

       550        560        570        580        590        600 
NQFARHYQTG QPLPKNMVSR LCESKKVCAA ADMQLQVFYA TLDQIYHGKH PLRNSTTDIL 

       610        620        630        640        650        660 
KETQEKFYGL PYVPDTAWQL RFSHLVGYGA KYYSYLMSRA VASMVWKECF LQDPFNRAAG 

       670        680        690        700        710 
ERYRREMLAH GGGREPMLMV EGMLQKCPSV DDFVSALVSD LDLDFETFLM DSE 

« Hide

References

[1]The German cDNA consortium
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR857347 mRNA. Translation: CAH89643.1.
RefSeqNP_001124737.1. NM_001131265.1.

3D structure databases

ProteinModelPortalQ5RF14.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSM03.A05.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100171586.
KEGGpon:100171586.

Organism-specific databases

CTD4285.

Phylogenomic databases

HOGENOMHOG000230535.
HOVERGENHBG008215.
InParanoidQ5RF14.
KOK01410.

Family and domain databases

Gene3D1.10.1370.10. 2 hits.
1.20.1050.40. 1 hit.
3.40.390.10. 1 hit.
InterProIPR024079. MetalloPept_cat_dom.
IPR024077. Neurolysin/TOP_dom2.
IPR024080. Neurolysin/TOP_N.
IPR001567. Pept_M3A_M3B.
[Graphical view]
PfamPF01432. Peptidase_M3. 1 hit.
[Graphical view]
PROSITEPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMIPEP_PONAB
AccessionPrimary (citable) accession number: Q5RF14
Entry history
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: December 21, 2004
Last modified: October 16, 2013
This is version 54 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries