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A5E4V6 (PMIP_LODEL) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 39. 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:LELG_04645
OrganismLodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus) [Complete proteome]
Taxonomic identifier379508 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeLodderomyces

Protein attributes

Sequence length811 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 – 2525Mitochondrion Potential
Chain26 – 811786Mitochondrial intermediate peptidase
PRO_0000338586

Regions

Compositional bias55 – 584Poly-Asn
Compositional bias431 – 44414Poly-Thr
Compositional bias447 – 4526Poly-Thr

Sites

Active site5941 By similarity
Metal binding5931Zinc; catalytic By similarity
Metal binding5971Zinc; catalytic By similarity
Metal binding6001Zinc; catalytic By similarity

Sequences

Sequence LengthMass (Da)Tools
A5E4V6 [UniParc].

Last modified June 12, 2007. Version 1.
Checksum: E9995C8F9BF12958

FASTA81191,934
        10         20         30         40         50         60 
MRSGSRLSNY LVRLSGRVSF TQKRSLTNVK LPSNVNYERL KAAFDSDEHT LNGKNNNNEG 

        70         80         90        100        110        120 
KLFSKTALFQ GQKDGSASTG LFKNSYLTSP QGLVQFSKKS KLQAQTLVDE MTRDVLTHQG 

       130        140        150        160        170        180 
KLDYIKKLDQ LSDILCRTID VAEFIRVVHD DQKWVDAAQQ THEIIFEYMN QLNTNVELYA 

       190        200        210        220        230        240 
NLVKILEDKD LISQLSDEEI KVGEYLRQDF ERSGIHMDPQ SRDQFVSLTQ EISIMGSHFN 

       250        260        270        280        290        300 
NESSSLKSDW ISITSNEFSA IEDRFIQSEV MRASALYPGK KESGTYYIPL ASAIPYRIMI 

       310        320        330        340        350        360 
QCGSGNLRKK MWIGLHEASD EQVQVLNHFV AYRALLAKML GYDSYAHYQL EHKMAKKPEN 

       370        380        390        400        410        420 
VLSFLTNLQE NLKNSQVLKE LRALSALQQG YSLLSDEELI RQIKPWDRDF LLKSFEAKKL 

       430        440        450        460        470        480 
SSTENGEKAS TDTSTSTTTS TTTTDSTTTT ATFSNSTDSV AIKRLCEYFS IGTVIAGLSK 

       490        500        510        520        530        540 
LFSALYNISF VVEPTVKGEV WNEKRVRKLN VLNNSNGETM GYLYLDFCSP KVFPSHFTVV 

       550        560        570        580        590        600 
CLRQLNKAES VSEHGDMVQL SKDYQLPVVA LVCNFTSGNP TLLSLDQVDT IFHEMGHAMH 

       610        620        630        640        650        660 
SMIGRTQLHN LSGTRCATDF VEIPSVLMES FSKDPRVLSE IGCHYRTGEP VPINLLEQAQ 

       670        680        690        700        710        720 
SQRSALEACE TFVQSKMAML DQELHSKEIV ELLRQGLEAI NSTEIYHQVE RDLEIFADEW 

       730        740        750        760        770        780 
STWHGKFPHL FSYGAVYYSY LLDRAIANVL WQKLFAKDPW SRDAGIKYKE EILKWGGTKD 

       790        800        810 
PWACLADALQ MEELRKGDAH AMQIIGENSK L 

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CH981530 Genomic DNA. Translation: EDK46464.1.
RefSeqXP_001523832.1. XM_001523782.1.

3D structure databases

ProteinModelPortalA5E4V6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING36914.A5E4V6.

Protein family/group databases

MEROPSM03.006.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5231285.
KEGGlel:LELG_04645.

Phylogenomic databases

eggNOGCOG0339.
KOK01410.
OMALQVFYSA.
OrthoDBEOG71GB4R.

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. 2 hits.
[Graphical view]
PROSITEPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePMIP_LODEL
AccessionPrimary (citable) accession number: A5E4V6
Entry history
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: June 12, 2007
Last modified: November 13, 2013
This is version 39 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