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A1CTP5 (PMIP_ASPCL) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 43. 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:ACLA_083770
OrganismAspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1) [Complete proteome]
Taxonomic identifier344612 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length801 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 – 4141Mitochondrion Potential
Chain42 – 801760Mitochondrial intermediate peptidase
PRO_0000338569

Sites

Active site5661 By similarity
Metal binding5651Zinc; catalytic By similarity
Metal binding5691Zinc; catalytic By similarity
Metal binding5721Zinc; catalytic By similarity

Sequences

Sequence LengthMass (Da)Tools
A1CTP5 [UniParc].

Last modified January 23, 2007. Version 1.
Checksum: 38B5273FF01FD833

FASTA80189,815
        10         20         30         40         50         60 
MKPQLLTPLR RRPWTCRQCL QRLQRLQQQT RRSFETAASP APGHTQVDYI PADASQSKKV 

        70         80         90        100        110        120 
DDETIRRVFD SQHFWREFSQ RRSTQSKPTG LVQNQYLTSP DGFRTFANVS LQKCQAIVSK 

       130        140        150        160        170        180 
VLAASTLEEY RTMARDLDRL SDLLCRVIDL SDFIRVIHPD PRVQEAATQA YALMFEYMNV 

       190        200        210        220        230        240 
LNTTTGLNDQ LKKAVANPEV ASHWTEEEKI VAQILIKDFS NSAILMPPQE RQRFVNLSND 

       250        260        270        280        290        300 
ISQLGSSFVN SPEPAKSQVV VNANSLRGLD PMLVQQIKRW NRTASVPTTG MIPRLALRSV 

       310        320        330        340        350        360 
HDESVRREVY LASRTSSARQ LHRLEELLLK RAELAKLSGY SSFGHMTLSD KMAKSPEAVS 

       370        380        390        400        410        420 
NFLTSLVDSN RTLVREELLQ LRNMKGSPLQ PWDHAYYVHK RVMQYSQSRR SRELSAVPEF 

       430        440        450        460        470        480 
FSLGTVMQGL SRLFDRLYGV RLVPQEAAPG ETWNPDVRRL DVVDEADRHI AVIYCDLFSR 

       490        500        510        520        530        540 
PNKHPNPAHF TLRCSREISA TEVAECASLD QSSHPNDGMA TAVDPTTKTL RQLPTIALVC 

       550        560        570        580        590        600 
DFAEPAAHGG RPSLLSEHSV RTLFHEMGHA LHSILGQTRL QSISGTRCAT DFAELPSVLM 

       610        620        630        640        650        660 
EHFATAPSVL SLYARHWETD EPLSERMIQS MERDRTAHGS IYGAVENEAQ ILMALVDQEY 

       670        680        690        700        710        720 
HSRPADGGRI DSTALYHEVA QRHSSLPDPA ETAPPTSWQG FFGHLYGYGA TYYSYIFDRA 

       730        740        750        760        770        780 
IANKLWADVF GAGRAAVDRA AGERYKTEVL RWGGGRNGWQ CVAGVLGPSN ASNADGRLVE 

       790        800 
GGDEAMREVG RWGLGRDGVS G 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DS027060 Genomic DNA. Translation: EAW06682.1.
RefSeqXP_001268108.1. XM_001268107.1.

3D structure databases

ProteinModelPortalA1CTP5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5057.CADACLAP00007518.

Protein family/group databases

MEROPSM03.006.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADACLAT00007709; CADACLAP00007518; CADACLAG00007709.
GeneID4700295.
KEGGact:ACLA_083770.

Phylogenomic databases

eggNOGCOG0339.
HOGENOMHOG000076521.
KOK01410.
OMANEMICIA.
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. 1 hit.
[Graphical view]
PROSITEPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePMIP_ASPCL
AccessionPrimary (citable) accession number: A1CTP5
Entry history
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: January 23, 2007
Last modified: November 13, 2013
This is version 43 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