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Q6Y5M7

- PMIP_COPSC

UniProt

Q6Y5M7 - PMIP_COPSC

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Protein

Mitochondrial intermediate peptidase

Gene
OCT1, MIP
Organism
Coprinopsis scobicola (Ink cap fungus)
Status
Reviewed - Annotation score: 3 out of 5 - Protein inferred from homologyi

Functioni

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 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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi556 – 5561Zinc; catalytic By similarity
Active sitei557 – 5571 By similarity
Metal bindingi560 – 5601Zinc; catalytic By similarity
Metal bindingi563 – 5631Zinc; 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

Metal-binding, Zinc

Protein family/group databases

MEROPSiM03.006.

Names & Taxonomyi

Protein namesi
Recommended name:
Mitochondrial intermediate peptidase (EC:3.4.24.59)
Short name:
MIP
Alternative name(s):
Octapeptidyl aminopeptidase
Gene namesi
Name:OCT1
Synonyms:MIP
OrganismiCoprinopsis scobicola (Ink cap fungus)
Taxonomic identifieri71696 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaAgaricomycetesAgaricomycetidaeAgaricalesPsathyrellaceaeCoprinopsis

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 – 3333Mitochondrion Reviewed predictionAdd
BLAST
Chaini34 – 772739Mitochondrial intermediate peptidasePRO_0000343201Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliQ6Y5M7.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi485 – 4884Poly-Asp

Sequence similaritiesi

Belongs to the peptidase M3 family.

Keywords - Domaini

Transit peptide

Family and domain databases

Gene3Di1.10.1370.10. 2 hits.
3.40.390.10. 2 hits.
InterProiIPR024079. MetalloPept_cat_dom.
IPR024077. Neurolysin/TOP_dom2.
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.

Q6Y5M7-1 [UniParc]FASTAAdd to Basket

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MLARPSTTVL ARRPFFRFRG CLNEPRPTKA RCLATAATHH QIPSTVDDKA    50
LVDLFDQPSL SKVRSHFHST GLFGHPSLTH PRSLVSLAES TLVRAQLLTQ 100
RILDAKESED ELAHVVKNLD RLSDMLCGVI DLAELVRNAH PDRLWVEAGN 150
HAYETLCEFM NVLNTHTGLN DTLKTVLSNP TLVKSLDPEA YQTALIFSRD 200
FEKSGIDLPP ATRNKFVSLS SDILILGRQF LENASTPRPP TSVKASELAG 250
LKDKGMGVRL QLQAQFTNRD LQVYPGSLQA QMIMRAAPNE EPRRKLYLAA 300
NSSTPEQIHV LETLLKKRAE LAQLVGRDSF AHMTLDDKMA KKPEHVTNFL 350
DALIDHTRPF ARNALRTLAQ RKQAHHNLPA LPVIQAWDRD FYCPPDPPAP 400
PIPLPPLTIG TVFMGLSRLF RHLYGVSLRP AQAASGEVWH PDVQKLEVVD 450
EQQGIIGWIY ADLFPRRGKA SGAAHYTVRC SRRTDDDDEA NDGMFEGTEL 500
QIQESQQFEA VKRHRLPNQE GVYQLPLVVL LTEFARPSLS KGAAVLEWHE 550
VQTLFHEMGH AMHSMLGRTE YQNVSGTRCA TDFVELPSIL MEHFLNSPAV 600
LSLFDADNTT SLRQIGNHHN DPCHAIDTYS QIMLAVVDQV YHSPSVLNSS 650
FDSTNEFANL VNKRGLIPYV PGTSFQTQFG HLFGYGATYY SYLFDRAIAS 700
RVWSKVFSRD PLNRELGEQY KQEVLRWGGA RDPWEMVSTL LDQPELAAGD 750
AEAMREVGRW RIEDEVGNSG RH 772
Length:772
Mass (Da):86,698
Last modified:July 5, 2004 - v1
Checksum:i3ACB37CE292B2ED0
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY179561 Genomic DNA. Translation: AAO61500.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY179561 Genomic DNA. Translation: AAO61500.1 .

3D structure databases

ProteinModelPortali Q6Y5M7.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi M03.006.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 1.10.1370.10. 2 hits.
3.40.390.10. 2 hits.
InterProi IPR024079. MetalloPept_cat_dom.
IPR024077. Neurolysin/TOP_dom2.
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. "Evolution of the gene encoding mitochondrial intermediate peptidase and its cosegregation with the A mating-type locus of mushroom fungi."
    James T.Y., Kuees U., Rehner S.A., Vilgalys R.
    Fungal Genet. Biol. 41:381-390(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: Cb.M8.

Entry informationi

Entry nameiPMIP_COPSC
AccessioniPrimary (citable) accession number: Q6Y5M7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 2008
Last sequence update: July 5, 2004
Last modified: May 14, 2014
This is version 38 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

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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