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P0CQ20 (PMIP2_CRYNJ) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 14. 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 2

Short name=MIP 2
EC=3.4.24.59
Alternative name(s):
Octapeptidyl aminopeptidase 2
Gene names
Name:OCT2
Ordered Locus Names:CNB02140
OrganismCryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC MYA-565) (Filobasidiella neoformans) [Reference proteome]
Taxonomic identifier214684 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaTremellomycetesTremellalesTremellaceaeFilobasidiellaFilobasidiella/Cryptococcus neoformans species complex

Protein attributes

Sequence length823 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 AAW41837.1 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
Reference 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 – 3333Mitochondrion Potential
Chain34 – 823790Mitochondrial intermediate peptidase 2
PRO_0000338582

Regions

Compositional bias528 – 5358Poly-Asp

Sites

Active site5961 By similarity
Metal binding5951Zinc; catalytic By similarity
Metal binding5991Zinc; catalytic By similarity
Metal binding6021Zinc; catalytic By similarity

Sequences

Sequence LengthMass (Da)Tools
P0CQ20 [UniParc].

Last modified June 28, 2011. Version 1.
Checksum: 4C30FAD763938997

FASTA82392,172
        10         20         30         40         50         60 
MRRLQQSLRR RSARRCPFIL IPHRLLTTSY ASYKPAPQAT LEIEDTNSPT FLLKTSPIQL 

        70         80         90        100        110        120 
PARATSDDSA IKAHFDLPHS IFGDMVGVRR EHVKGLFHYD SLTQPESLMR LTDRTLIQAS 

       130        140        150        160        170        180 
AIVQRIVVAP QDPTGRELRL VVKNLDRLSD ILCGVIDMCE LIRNVHPHQD WVNQSDRTHQ 

       190        200        210        220        230        240 
ILCSFMNELN ATRGLYESLA KAIAHPFNDP LTTSELRVAR IFLTDFERSG IHLPPSVRER 

       250        260        270        280        290        300 
FVKHSDALLF LGRSFLSSAS SGPSTVPHIE IPDPHRLLTG LGRQFVDSLP RTGRNGQAVI 

       310        320        330        340        350        360 
EPGSWEAQMI LRYAREGRAR ELVYVGGMRA DKKRISVLEA MLKERAELAS VLGKNNWAEV 

       370        380        390        400        410        420 
VLVDKMTKTP ENVMRFLTSL AQHHQPVARA EVDMLRRMKA TALTGNYFDP RNSRTRHLPL 

       430        440        450        460        470        480 
FHAWDRDYYS DKYLTSLIPT GSPPSISPYL STGTVMSGLS RIFSRLYGIS FKPAVVSPGE 

       490        500        510        520        530        540 
VWHPSVRRLD VVHEEEGLIG VIYCDFFSRI GKSSGAAHYT VRCSRRVDDD DIDGDGLPED 

       550        560        570        580        590        600 
WDKPYGPGLE ADKESLSGKP GKYQLPIIAL SMDVGTVNEG RPALLNWQEL ETLFHEMGHA 

       610        620        630        640        650        660 
IHSMIGRTEY HNVSGTRCAT DFVELPSILM EHFVSSPEVL STLAFHHATG EPLPIPVIEA 

       670        680        690        700        710        720 
HLALNQSLSA LETHGQIAMA LLDQKYHTLR HGQDSFDSTA IWFQLQQEIG VIQPVPGTAW 

       730        740        750        760        770        780 
QMQFGHLYGY GATYYSYLFD RAIAGKIWST LFHRSGTSQA YDRKAEGILS REGGELLKEK 

       790        800        810        820 
VLKWGGGRDP WEMVGDVIGG VEGDELSKGD ERALALVGSW SVV 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017342 Genomic DNA. Translation: AAW41837.1. Different initiation.
RefSeqXP_569144.1. XM_569144.1.

3D structure databases

ProteinModelPortalP0CQ20.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiAAW41837; AAW41837; CNB02140.
GeneID3255573.
KEGGcne:CNB02140.

Phylogenomic databases

KOK01410.
OrthoDBEOG71GB4R.

Family and domain databases

Gene3D1.10.1370.10. 2 hits.
1.20.1050.40. 1 hit.
3.40.390.10. 2 hits.
InterProIPR024079. MetalloPept_cat_dom.
IPR024077. Neurolysin/TOP_dom2.
IPR024080. Neurolysin/TOP_N.
IPR001567. Pept_M3A_M3B.
[Graphical view]
PfamPF01432. Peptidase_M3. 1 hit.
[Graphical view]
PROSITEPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePMIP2_CRYNJ
AccessionPrimary (citable) accession number: P0CQ20
Secondary accession number(s): Q55XK7, Q5KMC8
Entry history
Integrated into UniProtKB/Swiss-Prot: June 28, 2011
Last sequence update: June 28, 2011
Last modified: May 14, 2014
This is version 14 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