Reviewed, UniProtKB/Swiss-Prot P53259 (PCP1_YEAST)

Names and origin

Protein names

Recommended name:
    Rhomboid protein 1, mitochondrial
    EC=3.4.21.105
Alternative name(s):
    Processing of cytochrome c peroxidase protein 1
    Mitochondrial distribution and morphology protein 37

Gene names

Name:	PCP1
Synonyms:	MDM37, RBD1, UGO2
Ordered Locus Names:	YGR101W

Organism

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

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	346 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Mitochondrial rhomboid serine protease processing the mitochondrial membrane fusion regulator MGM1, and the cytochrome c peroxidase (CCP1). Required for TIM11 stability, ATP synthase complex assembly, mitochondrial morphology, cytochrome c (CYC1) storage and mitochondrial genome maintenance. Ref.2 Ref.3 Ref.4 Ref.5 Ref.6 Ref.8
Catalytic activity	Cleaves type-1 transmembrane domains using a catalytic dyad composed of serine and histidine that are contributed by different transmembrane domains.
Subcellular location	Mitochondrion inner membrane; Multi-pass membrane protein Ref.4 Ref.6 Ref.7.
Sequence similarities	Belongs to the peptidase S54 family.

Ontologies

Keywords
Cellular component	Membrane Mitochondrion Mitochondrion inner membrane
Domain	Transit peptide Transmembrane
Molecular function	Hydrolase Protease Serine protease
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	protein import into mitochondrial intermembrane space Ref.2 Traceable author statement. Source: SGD signal peptide processing Ref.2 Inferred from mutant phenotype. Source: SGD
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrial inner membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	protein binding Inferred from physical interaction. Source: IntAct serine-type peptidase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
	P23180	1	EBI-23242,EBI-24332
ECM4	P36156	1	EBI-23242,EBI-2042717

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 73	73	Mitochondrion Potential
	Chain	74 – 346	273	Rhomboid protein 1, mitochondrial		PRO_0000027392
Regions
	Transmembrane	109 – 129	21	Potential
	Transmembrane	145 – 165	21	Potential
	Transmembrane	203 – 223	21	Potential
	Transmembrane	246 – 266	21	Potential
	Transmembrane	275 – 295	21	Potential
	Transmembrane	308 – 328	21	Potential
Sites
	Active site	256	1	Nucleophile
	Active site	313	1
Experimental info
	Mutagenesis	202	1	N → A: Abolishes protease activity. Ref.4
	Mutagenesis	252	1	S → A or I: Does not abolish protease activity. Ref.2 Ref.4
	Mutagenesis	254 – 256	3	GAS → AAI: Abolishes protease activity. Ref.2 Ref.4 Ref.6
	Mutagenesis	256	1	S → A, I or G: Abolishes protease activity. Ref.2 Ref.4 Ref.6
	Mutagenesis	313	1	H → A: Abolishes protease activity. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	P53259-1 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 692AC44C043C9A28	FASTA	346	38,815
	10 20 30 40 50 60 MSGVSSVMLG LRPATRIFFR SNISVSPSRT FVSYIGRSQS TSILKNAPNL EDNVTNLQKI 70 80 90 100 110 120 IPKRFFSQTS ILKSRWKPIF NEETTNRYVR LNRFQQYQQQ RSGGNPLGSM TILGLSLMAG 130 140 150 160 170 180 IYFGSPYLFE HVPPFTYFKT HPKNLVYALL GINVAVFGLW QLPKCWRFLQ KYMLLQKDYV 190 200 210 220 230 240 TSKISIIGSA FSHQEFWHLG MNMLALWSFG TSLATMLGAS NFFSLYMNSA IAGSLFSLWY 250 260 270 280 290 300 PKLARLAIVG PSLGASGALF GVLGCFSYLF PHAKILLFVF PVPGGAWVAF LASVAWNAAG 310 320 330 340 CALRWGSFDY AAHLGGSMMG VLYGWYISKA VEKQRQRRLQ AAGRWF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII." Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E. , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K. Nature 387:81-84(1997) [PubMed: 9169869] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[2]	"A novel two-step mechanism for removal of a mitochondrial signal sequence involves the mAAA complex and the putative rhomboid protease Pcp1." Esser K., Tursun B., Ingenhoven M., Michaelis G., Pratje E. J. Mol. Biol. 323:835-843(2002) [PubMed: 12417197] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF SER-252; 254-GLY--SER-256 AND SER-256.
[3]	"Genetic basis of mitochondrial function and morphology in Saccharomyces cerevisiae." Dimmer K.S., Fritz S., Fuchs F., Messerschmitt M., Weinbach N., Neupert W., Westermann B. Mol. Biol. Cell 13:847-853(2002) [PubMed: 11907266] [Abstract] Cited for: FUNCTION.
[4]	"Cells lacking Pcp1p/Ugo2p, a rhomboid-like protease required for Mgm1p processing, lose mtDNA and mitochondrial structure in a Dnm1p-dependent manner, but remain competent for mitochondrial fusion." Sesaki H., Southard S.M., Hobbs A.E.A., Jensen R.E. Biochem. Biophys. Res. Commun. 308:276-283(2003) [PubMed: 12901865] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF ASN-202; SER-252; SER-256 AND HIS-313.
[5]	"Processing of Mgm1 by the rhomboid-type protease Pcp1 is required for maintenance of mitochondrial morphology and of mitochondrial DNA." Herlan M., Vogel F., Bornhoevd C., Neupert W., Reichert A.S. J. Biol. Chem. 278:27781-27788(2003) [PubMed: 12707284] [Abstract] Cited for: FUNCTION.
[6]	"Mitochondrial membrane remodelling regulated by a conserved rhomboid protease." McQuibban G.A., Saurya S., Freeman M. Nature 423:537-541(2003) [PubMed: 12774122] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-256.
[7]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed: 14562095] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[8]	"A novel role of Mgm1p, a dynamin-related GTPase, in ATP synthase assembly and cristae formation/maintenance." Amutha B., Gordon D.M., Gu Y., Pain D. Biochem. J. 381:19-23(2004) [PubMed: 15125685] [Abstract] Cited for: FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	Z72886 Genomic DNA. Translation: CAA97104.1.
PIR	S64406.
RefSeq	NP_011615.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-5524N.
IntAct	P53259. 4 interactions.
STRING	P53259.
Protein family/group databases
MEROPS	S54.007.
Genome annotation databases
Ensembl	YGR101W; YGR101W; YGR101W; Saccharomyces cerevisiae. [Genome view]
GeneID	852993.
KEGG	sce:YGR101W.
NMPDR	fig|4932.3.peg.2732.
Organism-specific databases
CYGD	YGR101w.
SGD	S000003333. PCP1.
Phylogenomic databases
HOGENOM	HBG396582.
OMA	THREEYL.
OrthoDB	EOG9RNCRK.
Enzyme and pathway databases
BRENDA	3.4.21.105. 250.
Gene expression databases
ArrayExpress	P53259.
Genevestigator	P53259.
GermOnline	YGR101W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR002610. Peptidase_S54_rhomboid. [Graphical view]
PANTHER	PTHR22936. Peptidase_S54_rhomboid. 1 hit.
Pfam	PF01694. Rhomboid. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	972824.

Entry information

Entry name

PCP1_YEAST

Accession

Primary (citable) accession number: P53259

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	December 15, 2009
This is version 70 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)