Reviewed, UniProtKB/Swiss-Prot Q6FW88 (PMIP_CANGA)

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
Ordered Locus Names:	CAGL0D02112g

Organism

Candida glabrata (Yeast) (Torulopsis glabrata) [Complete proteome]

Taxonomic identifier

5478 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Nakaseomyces › mitosporic Nakaseomyces

Protein attributes

Sequence length	761 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 – 37	37	Mitochondrion Potential
	Chain	38 – 761	724	Mitochondrial intermediate peptidase		PRO_0000338577
Sites
	Active site	548	1	By similarity
	Metal binding	547	1	Zinc; catalytic By similarity
	Metal binding	551	1	Zinc; catalytic By similarity
	Metal binding	554	1	Zinc; catalytic By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6FW88-1 [UniParc]. Last modified July 19, 2004. Version 1. Checksum: 89CA8567A26EC72E	FASTA	761	87,333
	10 20 30 40 50 60 MLIQKILLNK EISRLPRILS ILNYTGLRWL SGSSGRNTTE LQRIFDDSKY WQSLSENTTQ 70 80 90 100 110 120 YTKETGLFKN PYLTSTDGLR QFSHDSLHKA HKLAEILRNS VSKEEKVHYI MNLDQLSDTL 130 140 150 160 170 180 CRVIDLCEFL RSAHPDQSYV EAAQMCHEEM FEFMNVLNTD VVLCNKLKEV LEDPEILKVL 190 200 210 220 230 240 SEEERKVGEI LLDDFEKSGI YMKAGIREQF IELSQQISVI GQEFINNTDY VAKEFIKVKR 250 260 270 280 290 300 DEMDKSGISP LLTARLNRDL TGKYYKIPTY GQIPLQILKS CPDEDIRKEV WAALHNCPKA 310 320 330 340 350 360 QIQRLNQLVR LRVILSNLLG KQSYSDYQLD NKMAGSPENV KGFIKTLMNV TKPLAARELE 370 380 390 400 410 420 FIARDKLNAP DSRHMSDNEI LSIVKPWDKN YFSSKYDSDN EMAMIRDEQL RYYFSLGNVI 430 440 450 460 470 480 NGLSELFKRI YGITLQPSRT ENGETWSPDV RRLDVISEEE GLVGVIYCDL FERVGKISNP 490 500 510 520 530 540 AHFTVCCSRQ VYPDENDFTT IQTGQNSDGT VFQLPVISLV CNFSTVALPN GNRTCFLHMN 550 560 570 580 590 600 EIETLFHEMG HAMHSMLGRT RLQNISGTRC ATDFVELPSI LMEHFARDIR VLRTIGSHYE 610 620 630 640 650 660 TSEPAPEALL NDYLDKTQFL QHCETYSQAK MAMLDQKLHG SFSLSDIERI DSAKIYQKLE 670 680 690 700 710 720 TRLQVLADDE SNWCGRFGHL FGYGATYYSY LFDRAIASKV WDSLFKDDPF NRTGGEKFKE 730 740 750 760 RVLKWGGLKN PWSCIADVLE KPDLAKGGAE AMTYIGDSED L

References

[1]

"Genome evolution in yeasts." Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S. , Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., Wincker P., Souciet J.-L. Nature 430:35-44(2004) [PubMed: 15229592] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 2001 / CBS 138 / IFO 0622 / NRRL Y-65.

Cross-references

Sequence databases
EMBLGenBankDDBJ	CR380950 Genomic DNA. Translation: CAG58417.1.
RefSeq	XP_445506.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q6FW88.
Protein family/group databases
MEROPS	M03.006.
Genome annotation databases
GeneID	2887167.
GenomeReviews	Gene locus CAGL0D02112g in contig CR380950_GR.
KEGG	cgr:CAGL0D02112g.
Phylogenomic databases
HOGENOM	Q6FW88.
OMA	AMGERYR.
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_CANGA

Accession

Primary (citable) accession number: Q6FW88

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 10, 2008
Last sequence update:	July 19, 2004
Last modified:	November 3, 2009
This is version 38 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)