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A2QWM4 (PMIP_ASPNC) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 47. 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
Alternative name(s):
Octapeptidyl aminopeptidase
Gene names
Name:oct1
ORF Names:An11g05710
OrganismAspergillus niger (strain CBS 513.88 / FGSC A1513) [Complete proteome]
Taxonomic identifier425011 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length799 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

Cleaves proteins, imported into the mitochondrion, to their mature size. While most mitochondrial precursor proteins are processed to the mature form in one step by mitochondrial processing peptidase (MPP), the sequential cleavage by MIP of an octapeptide after initial processing by MPP is a required step for a subgroup of nuclear-encoded precursor proteins destined for the matrix or the inner membrane 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.

Subcellular location

Mitochondrion matrix By similarity.

Sequence similarities

Belongs to the peptidase M3 family.

Ontologies

Keywords
   Cellular componentMitochondrion
   DomainTransit peptide
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
Metalloprotease
Protease
   Technical termComplete 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 – ?Mitochondrion Potential
Chain? – 799Mitochondrial intermediate peptidasePRO_0000338572

Sites

Active site5631 By similarity
Metal binding5621Zinc; catalytic By similarity
Metal binding5661Zinc; catalytic By similarity
Metal binding5691Zinc; catalytic By similarity

Sequences

Sequence LengthMass (Da)Tools
A2QWM4 [UniParc].

Last modified March 6, 2007. Version 1.
Checksum: BE7D0384194750AD

FASTA79988,989
        10         20         30         40         50         60 
MGASLLLPLR RRPWTCRTCL LQARRSLETA ASPATHRAAF DYLPSKNDAQ KKSDDDTLRR 

        70         80         90        100        110        120 
VFDSQPFWRE FSQRSAAHLK PTGLVQNQYL TSPDGFRVFA TTTLQKCQAI VAKVLAGTTL 

       130        140        150        160        170        180 
EDYQSMARDL DRLSDLLCRV IDLSDFIRVI HPDPRVQEAA TQAYALMFEY MNVLNTTTGL 

       190        200        210        220        230        240 
NDQLKKAAAN PEVTARWSDE EKIVAQILIK DFSNSAIHMP PHARQRFVNL SNDISQLGNT 

       250        260        270        280        290        300 
FVNAAEPAKS HVTVSANSLR GLDPILVQQI KRWNRTASVP SMGLIPRLAL RSVHDEGVRR 

       310        320        330        340        350        360 
EVYLATRTSS ARQIQRLEQL LAKRAELAQL SGYDSFAHMT LSDKMAKSPE AVSNFLTSLV 

       370        380        390        400        410        420 
GSNRPYVQEE LAQLQSMKGS AGRLQPWDHA YYVHQRVLQY SQSRRSRELS AVPEFFSLGT 

       430        440        450        460        470        480 
VMQGLSRLFD RLYGVRLVPQ ETAAGETWNS DVRRLDVVDE ADRHIAVIYC DLFSRPNKHP 

       490        500        510        520        530        540 
NPAHYTLRCA REISAEEVAE CATTMDASAH PNDGMATAVD RDAKTLRQLP TIALVCDFPE 

       550        560        570        580        590        600 
PPATGTGRPS LLSEHSVRTL FHEMGHALHS ILGQTRLQSI SGTRCATDFA ELPSVLMERF 

       610        620        630        640        650        660 
ATAPEVLALY ARHWETDAPL SESMMQHMEK DRTAHGSIYG AMENESQILM ALVDQAYHSL 

       670        680        690        700        710        720 
PAGQATSIDS TAVFHQVSAE HCTLPDPTDT KPPTSWQGFF GHLHGYGATY YSYIFDRAIA 

       730        740        750        760        770        780 
NKLWEDVFQQ GKAAVDRQAG ERYKNEVLRW GGGRNGWNCV AGVLGSAHPA NADGRLVEGG 

       790 
DEAMREVGRW GLGRDGVSE 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM270239 Genomic DNA. Translation: CAK40728.1.
RefSeqXP_001394557.1. XM_001394520.2.

3D structure databases

ProteinModelPortalA2QWM4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5061.CADANGAP00008739.

Protein family/group databases

MEROPSM03.006.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADANGAT00008906; CADANGAP00008739; CADANGAG00008906.
GeneID4984800.
KEGGang:ANI_1_762094.

Phylogenomic databases

eggNOGCOG0339.
HOGENOMHOG000076521.
KOK01410.
OrthoDBEOG71GB4R.

Family and domain databases

Gene3D1.10.1370.10. 2 hits.
3.40.390.10. 1 hit.
InterProIPR024079. MetalloPept_cat_dom.
IPR024077. Neurolysin/TOP_dom2.
IPR001567. Pept_M3A_M3B.
[Graphical view]
PfamPF01432. Peptidase_M3. 1 hit.
[Graphical view]
PROSITEPS00039. DEAD_ATP_HELICASE. 1 hit.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePMIP_ASPNC
AccessionPrimary (citable) accession number: A2QWM4
Entry history
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: March 6, 2007
Last modified: November 13, 2013
This is version 47 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries