Reviewed, UniProtKB/Swiss-Prot A5DI46 (PMIP_PICGU)

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:	PGUG_02947

Organism

Pichia guilliermondii (Yeast) (Candida guilliermondii) [Complete proteome]

Taxonomic identifier

4929 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	786 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 – 29	29	Mitochondrion Potential
	Chain	30 – 786	757	Mitochondrial intermediate peptidase		PRO_0000338592
Sites
	Active site	568	1	By similarity
	Metal binding	567	1	Zinc; catalytic By similarity
	Metal binding	571	1	Zinc; catalytic By similarity
	Metal binding	574	1	Zinc; catalytic By similarity

Sequences

	Sequence		Length	Mass (Da)
	A5DI46-1 [UniParc]. Last modified February 10, 2009. Version 2. Checksum: 784FAB0D1430E2E3	FASTA	786	90,517
	10 20 30 40 50 60 MSSILLRSYR HHAKVWTRPS SKSSFIRSLA SRSNPTSSFE HVRRVFDDDK YYQDFNNGTL 70 80 90 100 110 120 SRKIFSGPRT GLFKNEKLTT PQGLIDFSGQ CLTEAQTLVD TMIREAETSD QGKIHYIRRL 130 140 150 160 170 180 DQLSDILCRV IDVAEFIRVA HPNSKWTHAA QQTHELMFEY MNQLNTNVQL HTILGNILAD 190 200 210 220 230 240 KSITSKLSSE EIMVGEYLKQ DFERSGIYME PHTRENFVAL TQEISVLGSH FNNGIHELKD 250 260 270 280 290 300 YWCEISQQEY EAIDNADLKR EIRRFQQKSP RSSRNSVYIP LAGSLPYSIL QRCSMESVRR 310 320 330 340 350 360 KVWIALHNAS EEQISTLNLF LKYRATLSKM LGYESFAHYQ LEHKMAKNPE NVLTFLENLQ 370 380 390 400 410 420 RKMVDGENSG LISELESLYA MSNHWKPGAS KSDIIHAIQP WDRDYLLHKL QEEKKETQLD 430 440 450 460 470 480 DNISEYLSVG TIMSGLSQLF HSIYSIELLP EPSASGETWA SQVRKIKVFD NETQSTLGFL 490 500 510 520 530 540 YLDFWSPNVL PSHFTIVCSR QLNKDLGEKV EVMKPLVQLD ETESHQLPVI SLVCNFHQGN 550 560 570 580 590 600 SFIGRFAGLE TSKPTLLTLD QVDTIFHEMG HAMHSMIGRT KLQNLSGTRC STDFVELPSV 610 620 630 640 650 660 LMESFSKDPR VLGRIARHYS TNELLPHDIL AKHQHYRNVL ENSETYMQSK MAMLDQVLHG 670 680 690 700 710 720 KSIVKQLEMA RDDIDSTTMY HSLEKELKVF SDQWSTWHGK FPHLFSYGAV YFSYLFDRAI 730 740 750 760 770 780 AEKIWKSLFQ NDPWSREAGT TYKEAILKWG GTRDPWHCLA DALSNQELSK GDEKAMRIIG GETKDL

References

[1]

"Evolution of pathogenicity and sexual reproduction in eight Candida genomes." Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S., Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I., Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C., Fitzpatrick D.A., de Groot P.W.J. , Harris D., Hoyer L.L., Hube B., Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D., Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T., Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C., Birren B.W., Kellis M., Cuomo C.A. Nature 459:657-662(2009) [PubMed: 19465905] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 6260 / CBS 566 / IFO 10279 / JCM 1539 / NRRL Y-324.

Cross-references

Sequence databases
EMBLGenBankDDBJ	CH408157 Genomic DNA. Translation: EDK38849.2.
3D structure databases
ModBase	Search...
Protein family/group databases
MEROPS	M03.006.
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_PICGU

Accession

Primary (citable) accession number: A5DI46

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 10, 2008
Last sequence update:	February 10, 2009
Last modified:	October 13, 2009
This is version 17 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)