Reviewed, UniProtKB/Swiss-Prot A7TSL2 (PMIP_VANPO)

Names and origin

Protein names

Recommended name:
    Mitochondrial intermediate peptidase
      Short name=MIP
    EC=3.4.24.59
Alternative name(s):
    Octapeptidyl aminopeptidase

Gene names

Name:	OCT1
ORF Names:	Kpol_297p8

Organism

Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294) (Kluyveromyces polysporus) [Complete proteome]

Taxonomic identifier

436907 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Vanderwaltozyma

Protein attributes

Sequence length	787 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred 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 component	Mitochondrion
Domain	Transit peptide
Ligand	Metal-binding Zinc
Molecular function	Hydrolase Metalloprotease Protease
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	proteolysis Inferred from electronic annotation. Source: InterPro
Cellular component	mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	metalloendopeptidase activity Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 36	36	Mitochondrion Potential
	Chain	37 – 787	751	Mitochondrial intermediate peptidase		PRO_0000338596
Sites
	Active site	574	1	By similarity
	Metal binding	573	1	Zinc; catalytic By similarity
	Metal binding	577	1	Zinc; catalytic By similarity
	Metal binding	580	1	Zinc; catalytic By similarity

Sequences

	Sequence		Length	Mass (Da)
	A7TSL2-1 [UniParc]. Last modified October 2, 2007. Version 1. Checksum: 478D339F977CF096	FASTA	787	90,031
	10 20 30 40 50 60 MQNKVLRGIL FKNVPLGYSY NRSIRHPTFG NSIIRWASTQ VKTSSDVLQR SFDDHLYWTE 70 80 90 100 110 120 INKQNYSSKE GWGSITKRLK GNKLTTNRSG LFNNEYLTSP EGLKLFSQVS LEKSQKIVDK 130 140 150 160 170 180 LRSDRTPEGL RLYVQNLDLL SDTLCRVIDL CEFIRSSHPD YKFVEAAQDC YEEMFEFMNM 190 200 210 220 230 240 LNTDVNLCFT LKHVLENKEI ASKLSEEELR VGRILLEDFE KSGIYMKPEV REQFITLSQS 250 260 270 280 290 300 ISVIGQEFIS NTDFVKDNNV VVSCNQLDSL GIDPELLSQI EKDIAGKNYK IPTYGYIPFA 310 320 330 340 350 360 LLKSCPSEEI REKIWVAVHN CSNEQIKRLT DLVKLRAVLS QLLGKKSYAE YQLEGKMAKN 370 380 390 400 410 420 PKEVIEFIKT LMDFTKPMAA KELDGIAEKK LTIKSNGSNL SVCDILKTVR PWDRDYYSAI 430 440 450 460 470 480 EREQTSAKNL YGSEEVLKYF TLGNVMQGLS NLFQKIYGIK LELDVPKIGE TWSPEVRKIN 490 500 510 520 530 540 VISEDEGLIG IIYCDLFERS GKTSNAAHFT ICCSRDISPY ETEDSTTQIA IDSKGTRFQL 550 560 570 580 590 600 PIISLVCNFS KTMISETDSV CFLHLPEVET LFHEMGHAMH SMLGRTKLQN ISGTRCATDF 610 620 630 640 650 660 VELPSILMEY FARDPRVLET IGKHYLTKET VKREMLEPHL QDLKYLQHCE TYSQAKMAML 670 680 690 700 710 720 DQTLHGETIS SHLDHLDVVK LYQDLERQLG VLVDDKSNWC GKFGHLFGYS AVYYSYLFDR 730 740 750 760 770 780 AIASKIWGAL FERNPFSRAS GDKYRNSVLQ WGGSRDPWHC IASALDKPEL AKGDDEAIKY IGSTNQL

References

[1]

"Independent sorting-out of thousands of duplicated gene pairs in two yeast species descended from a whole-genome duplication." Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H. Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(2007) [PubMed: 17494770] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	DS480515 Genomic DNA. Translation: EDO14747.1.
RefSeq	XP_001642605.1.
3D structure databases
ModBase	Search...
Protein family/group databases
MEROPS	M03.006.
Genome annotation databases
GeneID	5542774.
KEGG	vpo:Kpol_297p8.
Family and domain databases
InterPro	IPR001567. Pept_M3A_M3B. IPR006025. Pept_M_Zn_BS. [Graphical view]
Pfam	PF01432. Peptidase_M3. 1 hit. [Graphical view]
PROSITE	PS00142. ZINC_PROTEASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PMIP_VANPO

Accession

Primary (citable) accession number: A7TSL2

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 10, 2008
Last sequence update:	October 2, 2007
Last modified:	June 16, 2009
This is version 13 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)