A6ZZI7 (PMIP_YEAS7) Reviewed, UniProtKB/Swiss-Prot

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:	SCY_3247

Organism

Saccharomyces cerevisiae (strain YJM789) (Baker's yeast) [Complete proteome]

Taxonomic identifier

307796 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	772 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. Cleaves precursor proteins of respiratory components, including subunits of the electron transport chain and tricarboxylic acid cycle enzymes, and components of the mitochondrial genetic machinery, including ribosomal proteins, translation factors, and proteins required for mitochondrial DNA metabolism.
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.
Enzyme regulation	Stimulated by Fe2+ By similarity.
Subcellular location	Mitochondrion matrix.
Miscellaneous	Present with 2690 molecules/cell in log phase SD medium.
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: UniProtKB-KW
Cellular_component	mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW metalloendopeptidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 37	37	Mitochondrion Potential
	Chain	38 – 772	735	Mitochondrial intermediate peptidase		PRO_0000340084
Sites
	Active site	559	1	By similarity
	Metal binding	558	1	Zinc; catalytic By similarity
	Metal binding	562	1	Zinc; catalytic By similarity
	Metal binding	565	1	Zinc; catalytic By similarity

Sequences

	Sequence		Length	Mass (Da)
	A6ZZI7 [UniParc]. Last modified September 11, 2007. Version 1. Checksum: 4A5E12AEE44397D0	FASTA	772	88,190
	10 20 30 40 50 60 MLRTIILKAG SNASIPSLSR QNKLLRFFAT AGAVSRTSPG SIKKIFDDNS YWRNINGQDA 70 80 90 100 110 120 NNSKISQYLF KKNKTGLFKN PYLTSPDGLR KFSQVSLQQA QELLDKMRND FSESGKLTYI 130 140 150 160 170 180 MNLDRLSDTL CRVIDLCEFI RSTHPDDAFV RAAQDCHEQM FEFMNVLNTD VSLCNMLKSV 190 200 210 220 230 240 LNNPEVSSKL SAEELKVGKI LLDDFEKSGI YMNPDVREKF IQLSQEISLV GQEFINHTDY 250 260 270 280 290 300 PGSNSVKIPC KDLDNSKVST FLLKQLNKDV KGQNYKVPTF GYAAYALLKS CENEMVRKKL 310 320 330 340 350 360 WTALHSCSDK QVKRLSHLIK LRAILANLMH KTSYAEYQLE GKMAKNPKDV QDFILTLMNN 370 380 390 400 410 420 TIEKTANELK FIAELKAKDL KKPLTTNTDE ILKLVRPWDR DYYTGKYFQL NPSNSPSAKE 430 440 450 460 470 480 ISYYFTLGNV IQGLSDLFQQ IYGIRLEPAI TDEGETWSPD VRRLNVISEE EGIIGIIYCD 490 500 510 520 530 540 LFERNGKTSN PAHFTVCCSR QIYPSETDFS TIQVGENPDG TYFQLPVISL VCNFSPILIA 550 560 570 580 590 600 SKKSLCFLQL SEVETLFHEM GHAMHSMLGR THMQNISGTR CATDFVELPS ILMEHFAKDI 610 620 630 640 650 660 RILTKIGKHY GTGETIQADM LQRFMKSTNF LQNCETYSQA KMAMLDQSFH DEKIISDIDN 670 680 690 700 710 720 FDVVENYQAL ERRLKVLVDD QSNWCGRFGH LFGYGATYYS YLFDRTIASK IWYALFEDDP 730 740 750 760 770 YSRKNGDKFK KHLLKWGGLK DPWKCIADVL ECPMLEKGGS DAMEFIAQSH KS

References

[1]

"Genome sequencing and comparative analysis of Saccharomyces cerevisiae strain YJM789." Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z., Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X., Jia P., Luedi P., Oefner P.J., David L. , Dietrich F.S., Li Y., Davis R.W., Steinmetz L.M. Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: YJM789.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AAFW02000151 Genomic DNA. Translation: EDN60035.1.
3D structure databases
ProteinModelPortal	A6ZZI7.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
Gene3D	1.10.1370.10. 2 hits. 1.20.1050.40. 1 hit. 3.40.390.10. 1 hit.
InterPro	IPR024079. MetalloPept_cat_dom. IPR024077. Neurolysin/TOP_dom2. IPR024080. Neurolysin/TOP_N. IPR001567. Pept_M3A_M3B. [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_YEAS7

Accession

Primary (citable) accession number: A6ZZI7

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 10, 2008
Last sequence update:	September 11, 2007
Last modified:	March 6, 2013
This is version 29 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program