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Q5RF14

- MIPEP_PONAB

UniProt

Q5RF14 - MIPEP_PONAB

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Protein
Mitochondrial intermediate peptidase
Gene
MIPEP
Organism
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at transcript leveli

Functioni

Cleaves proteins, imported into the mitochondrion, to their mature size By similarity.

Catalytic activityi

Release of an N-terminal octapeptide as second stage of processing of some proteins imported into the mitochondrion.

Cofactori

Binds 1 zinc ion By similarity.

Enzyme regulationi

Activity is divalent cation-dependent. It is stimulated by manganese, magnesium or calcium ions and reversibly inhibited by zinc, cobalt and iron By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi495 – 4951Zinc; catalytic By similarity
Active sitei496 – 4961 By similarity
Metal bindingi499 – 4991Zinc; catalytic By similarity
Metal bindingi502 – 5021Zinc; catalytic By similarity

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. metalloendopeptidase activity Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Calcium, Cobalt, Iron, Magnesium, Manganese, Metal-binding, Zinc

Protein family/group databases

MEROPSiM03.A05.

Names & Taxonomyi

Protein namesi
Recommended name:
Mitochondrial intermediate peptidase (EC:3.4.24.59)
Short name:
MIP
Gene namesi
Name:MIPEP
OrganismiPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Taxonomic identifieri9601 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo
ProteomesiUP000001595: Unplaced

Subcellular locationi

Mitochondrion matrix By similarity

GO - Cellular componenti

  1. mitochondrial matrix Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3535Mitochondrion By similarity
Add
BLAST
Chaini36 – 713678Mitochondrial intermediate peptidase
PRO_0000319049Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei126 – 1261N6-acetyllysine By similarity

Keywords - PTMi

Acetylation

Interactioni

Subunit structurei

Monomer By similarity.

Structurei

3D structure databases

ProteinModelPortaliQ5RF14.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M3 family.

Keywords - Domaini

Transit peptide

Phylogenomic databases

HOGENOMiHOG000230535.
HOVERGENiHBG008215.
InParanoidiQ5RF14.
KOiK01410.

Family and domain databases

Gene3Di1.10.1370.10. 2 hits.
1.20.1050.40. 1 hit.
3.40.390.10. 1 hit.
InterProiIPR024079. MetalloPept_cat_dom.
IPR024077. Neurolysin/TOP_dom2.
IPR024080. Neurolysin/TOP_N.
IPR001567. Pept_M3A_M3B.
[Graphical view]
PfamiPF01432. Peptidase_M3. 1 hit.
[Graphical view]
PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q5RF14-1 [UniParc]FASTAAdd to Basket

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MLCVGRLGGL GARAAALPPR RAGRGILEAG IRARRVSTSW SPVGAAFNVK    50
PQGSRLDLFG ERRGLFGVPE LSAPEGFHAA QEKALRKAEL LVGRACSTPP 100
GPQTVLIFDE LSDSLCRVAD LADFVKIAHP EPAFREAAEE ACRSIGTMVE 150
KLNTNVDLYQ SLRKLLADKK LVDSLDPETR RVAELFMFDF EISGIHLDKE 200
KRKRAVDLNV KILDLSSTFL MGANFPNKIE KHLLPEHIRR NFTSAGDHII 250
IDGLHAESPD DLVREAAYKI FLYPNAGQLK CLEELLSSRD LLAKLVGYST 300
FSHRALQGTI AKNPETVMQF LEKLSDKLSE RTLKDFEMIR GMKMKLNPQN 350
SEVMPWDPPY YSGVIRAERY NIEPSLYCPF FSLGACMEGL NILLNRLLGI 400
SLYAEQPAKG EVWSEDVRKL AVVHESEGLL GYIYCDFFQR ADKPHQDCHF 450
TIRGGRLKED GDYQLPVVVL MLNLPRSSRS SPTLLTPGMM ENLFHEMGHA 500
MHSMLGRTRY QHVTGTRCPT DFAEVPSILM EYFANDYRVV NQFARHYQTG 550
QPLPKNMVSR LCESKKVCAA ADMQLQVFYA TLDQIYHGKH PLRNSTTDIL 600
KETQEKFYGL PYVPDTAWQL RFSHLVGYGA KYYSYLMSRA VASMVWKECF 650
LQDPFNRAAG ERYRREMLAH GGGREPMLMV EGMLQKCPSV DDFVSALVSD 700
LDLDFETFLM DSE 713
Length:713
Mass (Da):80,478
Last modified:December 21, 2004 - v1
Checksum:i32FB7C32F5BD1FF9
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CR857347 mRNA. Translation: CAH89643.1.
RefSeqiNP_001124737.1. NM_001131265.1.

Genome annotation databases

GeneIDi100171586.
KEGGipon:100171586.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CR857347 mRNA. Translation: CAH89643.1 .
RefSeqi NP_001124737.1. NM_001131265.1.

3D structure databases

ProteinModelPortali Q5RF14.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi M03.A05.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 100171586.
KEGGi pon:100171586.

Organism-specific databases

CTDi 4285.

Phylogenomic databases

HOGENOMi HOG000230535.
HOVERGENi HBG008215.
InParanoidi Q5RF14.
KOi K01410.

Family and domain databases

Gene3Di 1.10.1370.10. 2 hits.
1.20.1050.40. 1 hit.
3.40.390.10. 1 hit.
InterProi IPR024079. MetalloPept_cat_dom.
IPR024077. Neurolysin/TOP_dom2.
IPR024080. Neurolysin/TOP_N.
IPR001567. Pept_M3A_M3B.
[Graphical view ]
Pfami PF01432. Peptidase_M3. 1 hit.
[Graphical view ]
PROSITEi PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. The German cDNA consortium
    Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Kidney.

Entry informationi

Entry nameiMIPEP_PONAB
AccessioniPrimary (citable) accession number: Q5RF14
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: December 21, 2004
Last modified: May 14, 2014
This is version 55 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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