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P0CQ19 (PMIP1_CRYNB) 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 1

Short name=MIP 1
EC=3.4.24.59
Alternative name(s):
Octapeptidyl aminopeptidase 1
Gene names
Name:OCT1
Ordered Locus Names:CNBC3550
OrganismCryptococcus neoformans var. neoformans serotype D (strain B-3501A) (Filobasidiella neoformans) [Complete proteome]
Taxonomic identifier283643 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaTremellomycetesTremellalesTremellaceaeFilobasidiellaFilobasidiella/Cryptococcus neoformans species complex

Protein attributes

Sequence length761 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)
   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 – ?Mitochondrion Potential
Chain? – 761Mitochondrial intermediate peptidase 1PRO_0000410219

Regions

Compositional bias24 – 3512Poly-Pro

Sites

Active site5311 By similarity
Metal binding5301Zinc; catalytic By similarity
Metal binding5341Zinc; catalytic By similarity
Metal binding5371Zinc; catalytic By similarity

Sequences

Sequence LengthMass (Da)Tools
P0CQ19 [UniParc].

Last modified June 28, 2011. Version 1.
Checksum: 8AAD7126975FB945

FASTA76183,271
        10         20         30         40         50         60 
MLRLPRITRR ALSSGALAPH FDRPLPPPPP APPAPLCALP PLTAPDALAP LTRRTVRHAD 

        70         80         90        100        110        120 
ALVARIAAAP AHPDPAELRR VVKNLDRLSD VLCGVIDMCE LVRNVHPDPH WVAAAEKTYE 

       130        140        150        160        170        180 
TLCSFMNQLN TSTGLYDALV ATVSHTFPGN PLSPAELRVA QTFLSDFERS GIQLPPGVRA 

       190        200        210        220        230        240 
KFVRHSDNIL SLGRTFLSFA AAGPSADTPI EIPEPEVLLA GLSSKFVASL PRKKRKGPAL 

       250        260        270        280        290        300 
LAPGSWEAQM IGRYADNEEA RRLVYIGSMR EDKDRVYVLE TMLKERAELA HVLGKETWAD 

       310        320        330        340        350        360 
VALSDKMAKT PQNVLQFLTS LATHHRPSAA ADVAALQRLK ALSTVSRTSS QLPTVHAWDR 

       370        380        390        400        410        420 
DHYAEQYAAS LLPNGSLPSI TPYFSVGTAM SGLSHMLSRL YGISFKPVSV AHGEVWHPSV 

       430        440        450        460        470        480 
RRLDVMDEHG KRIGVIYCDL FSRPGKPSAG AAHYTVRCSR RVDDDPSEGD GLPPGWDQHL 

       490        500        510        520        530        540 
GKGMEVQGEA LHGKEGKYQL PIVVLTTDFG TVEESGPALL GWNDLETLFH EMGHAIHSMI 

       550        560        570        580        590        600 
GQTEFHNVSG TRCATDFVEL PSILMEHFIS SPAVLSTFAT HYTTNEPLPI PLIQAHLQLD 

       610        620        630        640        650        660 
QSLKALETHS QILMALLDQK YHSIKHGEQL DSTRVWNELQ SQVGVIPPVR GTAWQTQFGH 

       670        680        690        700        710        720 
LYGYGATYYS YLFDRAIAGK IWSSLFARGR TGPAAANHDP AAAEDILSRE GGEAFKEKVL 

       730        740        750        760 
KWGGGRDPWE MVGDVIGGAE GEQVAKGDEK AMELVGRWMI K 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AAEY01000013 Genomic DNA. Translation: EAL22217.1.
RefSeqXP_776864.1. XM_771771.1.

3D structure databases

ProteinModelPortalP0CQ19.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4935020.
KEGGcnb:CNBC3550.

Phylogenomic databases

HOGENOMHOG000076521.
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 namePMIP1_CRYNB
AccessionPrimary (citable) accession number: P0CQ19
Secondary accession number(s): Q55VY2, Q5KKA9
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