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

Q1E8M9 (PMIP_COCIM) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 48. 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:CIMG_01084
OrganismCoccidioides immitis (strain RS) (Valley fever fungus) [Reference proteome]
Taxonomic identifier246410 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeOnygenalesmitosporic OnygenalesCoccidioides

Protein attributes

Sequence length795 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
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 – 2222Mitochondrion Potential
Chain23 – 795773Mitochondrial intermediate peptidase
PRO_0000338579

Sites

Active site5621 By similarity
Metal binding5611Zinc; catalytic By similarity
Metal binding5651Zinc; catalytic By similarity
Metal binding5681Zinc; catalytic By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1E8M9 [UniParc].

Last modified July 11, 2006. Version 1.
Checksum: 168DA75ECA56482F

FASTA79589,923
        10         20         30         40         50         60 
MLKTLNRRSW TCRQCIRILR RNAETRRYFQ GASAASPLCQ HTVSSSTSDK ARDDQTLRLI 

        70         80         90        100        110        120 
FDSEPFWREF SQPKSSTSKR TGLLQNQYLT GPDGFLQFAQ VSLQKCQKIV AKVIAASTLE 

       130        140        150        160        170        180 
DYRGMVRDLD RLSDLLCRVI DMAEFMKLNH PSPQIQDAAT QAYALMFEYM NVLNTTPELD 

       190        200        210        220        230        240 
AQLKRASADL NVTSHWSPEE KVAARVLLKD FSQSAIHLPP KDRQKFVALS NEISQLGPMF 

       250        260        270        280        290        300 
VTNRQPETDH VTVDKNKLRG MDPSLIQQLQ RWRKVAVPMF GDIPRIALYS VHDEETRKEI 

       310        320        330        340        350        360 
YVTSRTSSKV QIRRLETLLQ KRAELAKLAG FPSYAHMTLS DKMAKTPEAV VNFLEALNAS 

       370        380        390        400        410        420 
NRGQVQDELS QLLALKQADV PSATQLQPWD HAYYVHQYSA RHSRVRRSRE STLLPAFFSI 

       430        440        450        460        470        480 
GTVIQGLSRL FTRLYGIRLV PTETLPGEIW NPDVRRLDVV DESDRRLAVI YCDLFTRPYK 

       490        500        510        520        530        540 
SPNPTHFTLR GSREISQAEI AECADLSSSL HPNDGMATTI KPETNKLYQL PTVALICDFD 

       550        560        570        580        590        600 
QSESRSTPSL LNEHNLETLF HEMGHAVHSV LARTDLQTIS GTRCATDFVE LPSVIMENFA 

       610        620        630        640        650        660 
TAPEVLALYA RHWETNEPLP EHMVKSMELN RQSRVSMHGG MDNEVQILMA LLDQAYHSSR 

       670        680        690        700        710        720 
PLEPNFDSTR IYHDVYSTHS SLPDPPGSRT SWQGYFAHLV GYGATYYSYL FDRAIANKVW 

       730        740        750        760        770        780 
SDVFKGGELS TNRDAGERFK NEVLRWGGGR DGWNCVAGLL GNNPANDNGK LAEGGEEAMR 

       790 
EVGRWGLGLM GTSEL 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
GG704911 Genomic DNA. Translation: EAS35809.2.
RefSeqXP_001247313.1. XM_001247312.1.
XP_001247392.1. XM_001247391.1.

3D structure databases

ProteinModelPortalQ1E8M9.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSM03.006.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4566657.
4567355.
KEGGcim:CIMG_01084.
cim:CIMG_01163.

Phylogenomic databases

KOK01410.
K14816.
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_COCIM
AccessionPrimary (citable) accession number: Q1E8M9
Secondary accession number(s): J3KIK8
Entry history
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: July 11, 2006
Last modified: November 13, 2013
This is version 48 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