Reviewed, UniProtKB/Swiss-Prot A5E4V6 (PMIP_LODEL)

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:	LELG_04645

Organism

Lodderomyces elongisporus (Yeast) (Saccharomyces elongisporus) [Complete proteome]

Taxonomic identifier

36914 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	811 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 – 25	25	Mitochondrion Potential
	Chain	26 – 811	786	Mitochondrial intermediate peptidase		PRO_0000338586
Regions
	Compositional bias	55 – 58	4	Poly-Asn
	Compositional bias	431 – 444	14	Poly-Thr
	Compositional bias	447 – 452	6	Poly-Thr
Sites
	Active site	594	1	By similarity
	Metal binding	593	1	Zinc; catalytic By similarity
	Metal binding	597	1	Zinc; catalytic By similarity
	Metal binding	600	1	Zinc; catalytic By similarity

Sequences

	Sequence		Length	Mass (Da)
	A5E4V6-1 [UniParc]. Last modified June 12, 2007. Version 1. Checksum: E9995C8F9BF12958	FASTA	811	91,934
	10 20 30 40 50 60 MRSGSRLSNY LVRLSGRVSF TQKRSLTNVK LPSNVNYERL KAAFDSDEHT LNGKNNNNEG 70 80 90 100 110 120 KLFSKTALFQ GQKDGSASTG LFKNSYLTSP QGLVQFSKKS KLQAQTLVDE MTRDVLTHQG 130 140 150 160 170 180 KLDYIKKLDQ LSDILCRTID VAEFIRVVHD DQKWVDAAQQ THEIIFEYMN QLNTNVELYA 190 200 210 220 230 240 NLVKILEDKD LISQLSDEEI KVGEYLRQDF ERSGIHMDPQ SRDQFVSLTQ EISIMGSHFN 250 260 270 280 290 300 NESSSLKSDW ISITSNEFSA IEDRFIQSEV MRASALYPGK KESGTYYIPL ASAIPYRIMI 310 320 330 340 350 360 QCGSGNLRKK MWIGLHEASD EQVQVLNHFV AYRALLAKML GYDSYAHYQL EHKMAKKPEN 370 380 390 400 410 420 VLSFLTNLQE NLKNSQVLKE LRALSALQQG YSLLSDEELI RQIKPWDRDF LLKSFEAKKL 430 440 450 460 470 480 SSTENGEKAS TDTSTSTTTS TTTTDSTTTT ATFSNSTDSV AIKRLCEYFS IGTVIAGLSK 490 500 510 520 530 540 LFSALYNISF VVEPTVKGEV WNEKRVRKLN VLNNSNGETM GYLYLDFCSP KVFPSHFTVV 550 560 570 580 590 600 CLRQLNKAES VSEHGDMVQL SKDYQLPVVA LVCNFTSGNP TLLSLDQVDT IFHEMGHAMH 610 620 630 640 650 660 SMIGRTQLHN LSGTRCATDF VEIPSVLMES FSKDPRVLSE IGCHYRTGEP VPINLLEQAQ 670 680 690 700 710 720 SQRSALEACE TFVQSKMAML DQELHSKEIV ELLRQGLEAI NSTEIYHQVE RDLEIFADEW 730 740 750 760 770 780 STWHGKFPHL FSYGAVYYSY LLDRAIANVL WQKLFAKDPW SRDAGIKYKE EILKWGGTKD 790 800 810 PWACLADALQ MEELRKGDAH AMQIIGENSK L

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 11503 / CBS 2605 / IFO 1676 / JCM 1781 / NRRL YB-4239.

Cross-references

Sequence databases
EMBLGenBankDDBJ	CH981530 Genomic DNA. Translation: EDK46464.1.
RefSeq	XP_001523832.1.
3D structure databases
ModBase	Search...
Protein family/group databases
MEROPS	M03.006.
Genome annotation databases
GeneID	5231285.
Phylogenomic databases
OMA	VTEMNIE.
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_LODEL

Accession

Primary (citable) accession number: A5E4V6

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 10, 2008
Last sequence update:	June 12, 2007
Last modified:	November 3, 2009
This is version 16 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)