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

Q2UN31 (PMIP_ASPOR) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 52. 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:AO090001000525
OrganismAspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold) [Complete proteome]
Taxonomic identifier510516 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length800 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)
   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 – 2323Mitochondrion Potential
Chain24 – 800777Mitochondrial intermediate peptidase
PRO_0000338573

Sites

Active site5641 By similarity
Metal binding5631Zinc; catalytic By similarity
Metal binding5671Zinc; catalytic By similarity
Metal binding5701Zinc; catalytic By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2UN31 [UniParc].

Last modified January 24, 2006. Version 1.
Checksum: 474F93077541B66F

FASTA80089,243
        10         20         30         40         50         60 
MAGHMLMPLR RRPWTCRACL QRLQQPRRSL ETAASPSSQS DVYDYAPTNH STQKKSNDET 

        70         80         90        100        110        120 
LRRVFDSQPF WREFSQRSAT QSKPTGLVQN QYLTNPDGFR AFANVSLQRC QAIVAKVLAA 

       130        140        150        160        170        180 
STLEEYRDMA RDLDRLSDLL CRVIDLSDFI RVIHPDPRVQ EAATQAYALM FEYMNVLNTT 

       190        200        210        220        230        240 
TGLNDQLKKA ASNPDVTSYW SEEEKIVAQI LIKDFSNSAI HMPPNERQRF VNLSNDISQL 

       250        260        270        280        290        300 
GSNFVNSAEP AKSQVVVGAN SLRGLDPILV QQIRRWNRTA SVPTTGMIPR LALRSVHDEG 

       310        320        330        340        350        360 
VRREVYLATR TSSSRQLHRL EELLSKRAEL AQLSGHASFG HMTLSDKMAK SPEAVSNFLT 

       370        380        390        400        410        420 
ALVGSNREYV QEELSKLQAM KGGSPLQPWD HAYYVHQRVL QYSQSRRSRE LSAVPEFFSL 

       430        440        450        460        470        480 
GTVMQGLSRL FDRLYGVRLV PQETAAGETW NPDVRRLDVV DEAERHIAVI YCDLFSRPNK 

       490        500        510        520        530        540 
HPNPAHFTLR CAREISSEEV AECATMDHSA HPNDGMATAV DPQSKTLRQL PTIALVCDFA 

       550        560        570        580        590        600 
EPPATGAGRP SLLSEHSVRT LFHEMGHALH SILGQTRLQS ISGTRCATDF AELPSVLMER 

       610        620        630        640        650        660 
FATEPAVLSM YARHWQTDQP LSESMMLSME KDRLAHGSIY GAVENEAQIL MALVDQAYHS 

       670        680        690        700        710        720 
IPADKAGQID STAIYHQVSS AHSTLPDPTD SRPPTSWQGF FGHLYGYGAT YYSYIFDRAI 

       730        740        750        760        770        780 
ANKIWEDVFQ AGKAAVDREA GERYKNEVLR WGGGRNGWDC VAGVLGSANA ANANGRLAEG 

       790        800 
GDEAMREVGR WGLGRDGVSG 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP007154 Genomic DNA. Translation: BAE57034.1.
RefSeqXP_001819036.1. XM_001818984.1.

3D structure databases

ProteinModelPortalQ2UN31.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5062.CADAORAP00000468.

Protein family/group databases

MEROPSM03.006.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADAORAT00000479; CADAORAP00000468; CADAORAG00000479.
GeneID5991007.
KEGGaor:AOR_1_1462164.

Phylogenomic databases

eggNOGCOG0339.
HOGENOMHOG000076521.
KOK01410.
OMAHATHGDG.
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]
PROSITEPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePMIP_ASPOR
AccessionPrimary (citable) accession number: Q2UN31
Entry history
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: January 24, 2006
Last modified: May 14, 2014
This is version 52 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