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Q0CI79 (PMIP_ASPTN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 43. 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:ATEG_06605
OrganismAspergillus terreus (strain NIH 2624 / FGSC A1156) [Complete proteome]
Taxonomic identifier341663 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length802 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.

Sequence caution

The sequence EAU33149.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence EAU33149.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

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 – 2424Mitochondrion Potential
Chain25 – 802778Mitochondrial intermediate peptidase
PRO_0000338574

Sites

Active site5661 By similarity
Metal binding5651Zinc; catalytic By similarity
Metal binding5691Zinc; catalytic By similarity
Metal binding5721Zinc; catalytic By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0CI79 [UniParc].

Last modified June 10, 2008. Version 2.
Checksum: 3E92F4BA281CEB5F

FASTA80289,472
        10         20         30         40         50         60 
MGGPKLLMPL RPRPWTCRTC LQRLHSARRS LKTAASPSPQ STSFEYNRSA HNTQKSTTDD 

        70         80         90        100        110        120 
ETLRRVFDSP SFWKEFSQRS SLHTKPTGLV QNQYLTSPEG FRTFANVSLH KCQAIVHKVL 

       130        140        150        160        170        180 
AASTLEEYRD MARDLDRLSD LLCRVIDLSD FIRVIHPDPQ VQEAATQAYA LMFDYMNVLN 

       190        200        210        220        230        240 
TTTGLNDQLK KAAANPDVTS HWSAEEKIVA QILIKDFSNS AIHMPPNERQ RFVNLSNEIS 

       250        260        270        280        290        300 
QLGSNFVNAA EPAKSHVVVG TNSLRGLDPL LVQQIKRWNR TASVPTMGMI PRLVLRSVHD 

       310        320        330        340        350        360 
EGVRKDVYLA TRTSSSRQIK RLEQLLAKRA ELAQLSGYAS FGHMTLSDKM AKSPEAVSNF 

       370        380        390        400        410        420 
LTSLVGSNRQ FVHEELAQLQ GMKGSSPLQA WDHAYYVHQR VMQYSQSRRS RELSIVPEFF 

       430        440        450        460        470        480 
SLGTVMQGLS RLFNRLYGVR LVPQETAPGE TWNPDVRRLD VVDEAERHIA VIYCDLFSRP 

       490        500        510        520        530        540 
NKHPNPAHFT LRCSREISNQ EVAECASMDQ SAHPNDGMAT AVDPQSKTLR QLPTIALVCD 

       550        560        570        580        590        600 
FPDPPATSAG RPSLLSEHSV RTLFHEMGHA LHSILGQTRL QSISGTRCAT DFAELPSVLM 

       610        620        630        640        650        660 
ERFATAPEVL SMYARHWQTD QPLSENMMRS MEQDRTAHGS IYGAVENEAQ ILMALVDQAY 

       670        680        690        700        710        720 
HSVPAEAAGK IDSTAIYHQV SQAHSSLPEP SDTQPPTSWQ GFFGHLYGYG ATYYSYIFDR 

       730        740        750        760        770        780 
AIANKLWEDV FQSGQASVDR NAGERYKNEV LRWGGGRNGW DCVAGVLGSG NPSNADGRLV 

       790        800 
EGGDDAMREV GRWGLGRDGV SG 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CH476602 Genomic DNA. Translation: EAU33149.1. Sequence problems.
RefSeqXP_001215783.1. XM_001215783.1.

3D structure databases

ProteinModelPortalQ0CI79.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING33178.CADATEAP00008513.

Protein family/group databases

MEROPSM03.006.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4322361.

Phylogenomic databases

eggNOGCOG0339.
HOGENOMHOG000076521.
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_ASPTN
AccessionPrimary (citable) accession number: Q0CI79
Entry history
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: June 10, 2008
Last modified: May 14, 2014
This is version 43 of the entry and version 2 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