NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 270-280 AND 400-419.
STRAIN=cv. Desiree;
TISSUE=Green leaf;
PubMed=1324169 [NCBI, ExPASy, EBI, Israel, Japan]
Braun H.P., Emmermann M., Kruft V., Schmitz U.K.;
"The general mitochondrial processing peptidase from potato is an integral part of cytochrome c reductase of the respiratory chain.";
EMBO J. 11:3219-3227(1992).

Comments

FUNCTION: Cleaves presequences (transit peptides) from mitochondrial protein precursors (By similarity).
FUNCTION: This is a component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is part of the mitochondrial respiratory chain. Mediate formation of the complex between cytochromes c and c1.
CATALYTIC ACTIVITY: Release of N-terminal transit peptides from precursor proteins imported into the mitochondrion, typically with Arg in position P2.
CATALYTIC ACTIVITY: QH₂ + 2 ferricytochrome c = Q + 2 ferrocytochrome c + 2 H⁺.
SUBUNIT: Heterodimer of alpha and beta subunits.
SUBCELLULAR LOCATION: Mitochondrion inner membrane.
SIMILARITY: Belongs to the peptidase M16 family [view classification].
CAUTION: Does not seem to have a protease activity as it lack the zinc-binding site.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X66284; CAA46990.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S23558; S23558.

3D structure databases

HSSP

P11914; 1HR6. [HSSP ENTRY / PDB]

ModBase

P29677.

Protein-protein interaction databases

IntAct

P29677; -.

Protein family/group databases

MEROPS

M16.971; -.

Ontologies

GO:0005746;	Cellular component: mitochondrial respiratory chain (inferred from electronic annotation from UniProtKB-KW).
GO:0004222;	Molecular function: metalloendopeptidase activity (inferred from electronic annotation from InterPro).
GO:0008121;	Molecular function: ubiquinol-cytochrome-c reductase activity (inferred from electronic annotation from EC).
GO:0008270;	Molecular function: zinc ion binding (inferred from electronic annotation from InterPro).
GO:0022900;	Biological process: electron transport chain (inferred from electronic annotation from UniProtKB-KW).
GO:0006508;	Biological process: proteolysis (inferred from electronic annotation from InterPro).
GO:0006810;	Biological process: transport (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR011237; Pept_M16_core.
IPR011765; Pept_M16_N.
IPR001431; Pept_M16_Zn_BS.
IPR007863; Peptidase_M16_C.
Graphical view of domain structure.

Gene3D

G3DSA:3.30.830.10; Pept_M16_core; 2.

Pfam

PF00675; Peptidase_M16; 1.
PF05193; Peptidase_M16_C; 1.
Pfam graphical view of domain structure.

PROSITE

PS00143; INSULINASE; 1.

Other

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Direct protein sequencing; Electron transport; Hydrolase; Membrane; Metalloprotease; Mitochondrion; Mitochondrion inner membrane; Oxidoreductase; Protease; Respiratory chain; Transit peptide; Transport.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 ?`		`Mitochondrion.`
`CHAIN`	`? 504`		`Mitochondrial-processing peptidase subunit alpha.`	`PRO_0000026776`

Sequence information

Length: 504 AA [This is the length of the unprocessed precursor]

Molecular weight: 54677 Da [This is the MW of the unprocessed precursor]

CRC64: FD3053688571D987 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MYRCASSRLS SLKARQGNRV LTRFSSSAAV ATKPSGGLFS WITGDTSSSV TPLDFPLNDV 

        70         80         90        100        110        120 
KLSPPLPDYV EPAKTQITTL ANGLKVASEA SVNPAASIGL YVDCGSIYET PASYGATHLL 

       130        140        150        160        170        180 
ERMAFKSTLN RSHLRIVREI EAIGGNVTAS ASREHMIYTY DALKTYVPQM VEMLADCVRN 

       190        200        210        220        230        240 
PAFLDWEVKE QLEKVKAEIS EYSKNPQHLL LEAVHSAGYA GPYGNSLMAT EATINRLNST 

       250        260        270        280        290        300 
VLEEFVAENY TAPRMVLAAS GVEHEEFLKV AEPLLSDLPK VATIEEPKPV YVGGDYRCQA 

       310        320        330        340        350        360 
DAEMTHFALA FEVPGGWMSE KESMTLTVLQ MLMGGGGSFS AGGPGKGMYS RLYLRVLNQY 

       370        380        390        400        410        420 
PQIHAFSAFS SIYNNTGLFG IQGTTSSDFG PQAVDVAVKE LIAVANPSEV DQVQLNRAKQ 

       430        440        450        460        470        480 
ATKSAILMNL ESRMVASEDI GRQLLTYGER NPVEHFLKAI DAVSAKDIAS VVQKLISSPL 

       490        500 
TMASYGDVLS LPSYDAVSSR FRSK

P29677 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools