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P37932 (PMIP_SCHCO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 84. 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
Synonyms:MEP, MIP
OrganismSchizophyllum commune (Split gill fungus)
Taxonomic identifier5334 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaAgaricomycetesAgaricomycetidaeAgaricalesSchizophyllaceaeSchizophyllum

Protein attributes

Sequence length775 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 Ref.1.

Sequence similarities

Belongs to the peptidase M3 family.

Sequence caution

The sequence AAB01366.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Cellular componentMitochondrion
   DomainTransit peptide
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
Metalloprotease
Protease
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 – 2828Mitochondrion Potential
Chain29 – 775747Mitochondrial intermediate peptidase
PRO_0000028581

Sites

Active site5591 By similarity
Metal binding5581Zinc; catalytic By similarity
Metal binding5621Zinc; catalytic By similarity
Metal binding5651Zinc; catalytic By similarity

Natural variations

Natural variant5721E → G in strain: UVM 9-4.
Natural variant6511Q → E in strain: UVM 9-1 and CBS 340.81 / UVM 4-40.
Natural variant6591K → E in strain: UVM 9-1 and CBS 340.81 / UVM 4-40.
Natural variant7291R → Q in strain: UVM 9-1.

Experimental info

Sequence conflict4861T → D Ref.2
Sequence conflict621 – 6222HD → QH in AAB01366. Ref.2
Sequence conflict621 – 6222HD → QH in AAB01368. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P37932 [UniParc].

Last modified October 1, 1996. Version 2.
Checksum: 875772B6D9560C55

FASTA77586,915
        10         20         30         40         50         60 
MIARPARDVL SSATKKQFRF RGCLAARHEP YHTSTSRAGQ VAILPATTDD KTLVSVFDSP 

        70         80         90        100        110        120 
RSNAKLSAFA TTGLFNHSTV THPRALNSIA QGTLIRAHVL TNRILRAKES REELFKVVKN 

       130        140        150        160        170        180 
LDRLSDMLCS VIDLCELVRN SHPDRAWVEA ANDAYEGLCQ TMNELNTHVG LYDVLKIVLS 

       190        200        210        220        230        240 
DPEIVKSLSP EAYRTAMIFW NDFEKSAINL PAKEREEFVA LSSEIISLGR MFLEETTAAR 

       250        260        270        280        290        300 
PPAKIPPSDL AGLKDKGMGV RLQLQAQFTQ RDLHVYPGSL QAQMIMRSAP AEEARRRVYI 

       310        320        330        340        350        360 
ASHSSTPEQI ELLERMLSTR ARLARLVGRE SFAAMALDDK MAKNPTNVAR FLDSLMDRSR 

       370        380        390        400        410        420 
PYARRALRNL SMRKQEHLHT PPFPTIQAWD RDYYCPPEPP APPIPLPRLT FGTVLMGLSR 

       430        440        450        460        470        480 
LFRHLYGIHL RPVKPIAGEV WHSDVHKLEV VDEERGVIGL IYADVFARRG KASGAAHYTV 

       490        500        510        520        530        540 
RCSRRTDDDD VQGDNDELTR MYPDLIKQSE EFEAVGRGPI PGLPGTYQQP LVVLLCEFAR 

       550        560        570        580        590        600 
PSLGAAVLEW HEVMTLFHEM GHAMHSMIGR TEYQNVSGTR CPTDFVELPS ILMEHFLNSR 

       610        620        630        640        650        660 
QVLSLFHADS TSSSSQPIGN HDEDPCHSID TYAQIMLAAL DQIYHSPAAL QPGFDSTRKL 

       670        680        690        700        710        720 
ARLHDEKGLI PYVPGTSFQT QFGHLFGYGA TYYSYLFDRA IASRVWKDVF SSSPLSRETG 

       730        740        750        760        770 
ERYKQEVLRY GGGKDPWEMV SALLKAPELA SGDAEAMATV GRWKIEDEVG LPGRH 

« Hide

References

[1]"Mammalian mitochondrial intermediate peptidase: structure/function analysis of a new homologue from Schizophyllum commune and relationship to thimet oligopeptidases."
Isaya G., Sakati W.R., Rollins R.A., Shen G.P., Hanson L.C., Ullrich R.C., Novotny C.P.
Genomics 28:450-461(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION.
Strain: 1-71.
[2]"The A alpha mating locus of Schizophyllum commune encodes two dissimilar multiallelic homeodomain proteins."
Stankis M.M., Specht C.A., Yang H., Giasson L., Ullrich R.C., Novotny C.P.
Proc. Natl. Acad. Sci. U.S.A. 89:7169-7173(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 486-775.
Strain: ATCC 44201 / CBS 340.81 / UVM 4-40 / 4-40, UVM 9-1 and UVM 9-4.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L43072 Genomic DNA. Translation: AAA93531.1.
M97179 Genomic DNA. Translation: AAB01366.1. Different initiation.
M97180 Genomic DNA. Translation: AAB01368.1.
M97181 Genomic DNA. Translation: AAB01371.1.
PIRE37271.
F37271.

3D structure databases

ProteinModelPortalP37932.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSM03.006.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D1.10.1370.10. 2 hits.
3.40.390.10. 2 hits.
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_SCHCO
AccessionPrimary (citable) accession number: P37932
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1996
Last modified: May 14, 2014
This is version 84 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