PCP1_YEAST
ID PCP1_YEAST Reviewed; 346 AA.
AC P53259; D6VUN3;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Rhomboid protein 1, mitochondrial;
DE EC=3.4.21.105;
DE AltName: Full=Mitochondrial distribution and morphology protein 37;
DE AltName: Full=Processing of cytochrome c peroxidase protein 1;
DE Flags: Precursor;
GN Name=PCP1; Synonyms=MDM37, RBD1, UGO2; OrderedLocusNames=YGR101W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP FUNCTION, AND MUTAGENESIS OF SER-252; 254-GLY--SER-256 AND SER-256.
RX PubMed=12417197; DOI=10.1016/s0022-2836(02)01000-8;
RA Esser K., Tursun B., Ingenhoven M., Michaelis G., Pratje E.;
RT "A novel two-step mechanism for removal of a mitochondrial signal sequence
RT involves the mAAA complex and the putative rhomboid protease Pcp1.";
RL J. Mol. Biol. 323:835-843(2002).
RN [4]
RP FUNCTION.
RX PubMed=11907266; DOI=10.1091/mbc.01-12-0588;
RA Dimmer K.S., Fritz S., Fuchs F., Messerschmitt M., Weinbach N., Neupert W.,
RA Westermann B.;
RT "Genetic basis of mitochondrial function and morphology in Saccharomyces
RT cerevisiae.";
RL Mol. Biol. Cell 13:847-853(2002).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ASN-202; SER-252;
RP SER-256 AND HIS-313.
RX PubMed=12901865; DOI=10.1016/s0006-291x(03)01348-2;
RA Sesaki H., Southard S.M., Hobbs A.E.A., Jensen R.E.;
RT "Cells lacking Pcp1p/Ugo2p, a rhomboid-like protease required for Mgm1p
RT processing, lose mtDNA and mitochondrial structure in a Dnm1p-dependent
RT manner, but remain competent for mitochondrial fusion.";
RL Biochem. Biophys. Res. Commun. 308:276-283(2003).
RN [6]
RP FUNCTION.
RX PubMed=12707284; DOI=10.1074/jbc.m211311200;
RA Herlan M., Vogel F., Bornhoevd C., Neupert W., Reichert A.S.;
RT "Processing of Mgm1 by the rhomboid-type protease Pcp1 is required for
RT maintenance of mitochondrial morphology and of mitochondrial DNA.";
RL J. Biol. Chem. 278:27781-27788(2003).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF SER-256.
RX PubMed=12774122; DOI=10.1038/nature01633;
RA McQuibban G.A., Saurya S., Freeman M.;
RT "Mitochondrial membrane remodelling regulated by a conserved rhomboid
RT protease.";
RL Nature 423:537-541(2003).
RN [8]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [9]
RP FUNCTION.
RX PubMed=15125685; DOI=10.1042/bj20040566;
RA Amutha B., Gordon D.M., Gu Y., Pain D.;
RT "A novel role of Mgm1p, a dynamin-related GTPase, in ATP synthase assembly
RT and cristae formation/maintenance.";
RL Biochem. J. 381:19-23(2004).
CC -!- FUNCTION: Mitochondrial rhomboid serine protease processing the
CC mitochondrial membrane fusion regulator MGM1, and the cytochrome c
CC peroxidase (CCP1). Required for TIM11 stability, ATP synthase complex
CC assembly, mitochondrial morphology, cytochrome c (CYC1) storage and
CC mitochondrial genome maintenance. {ECO:0000269|PubMed:11907266,
CC ECO:0000269|PubMed:12417197, ECO:0000269|PubMed:12707284,
CC ECO:0000269|PubMed:12774122, ECO:0000269|PubMed:12901865,
CC ECO:0000269|PubMed:15125685}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cleaves type-1 transmembrane domains using a catalytic dyad
CC composed of serine and histidine that are contributed by different
CC transmembrane domains.; EC=3.4.21.105;
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:12774122, ECO:0000269|PubMed:12901865,
CC ECO:0000269|PubMed:14562095}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:12774122, ECO:0000269|PubMed:12901865,
CC ECO:0000269|PubMed:14562095}.
CC -!- SIMILARITY: Belongs to the peptidase S54 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Z72886; CAA97104.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08194.1; -; Genomic_DNA.
DR PIR; S64406; S64406.
DR RefSeq; NP_011615.1; NM_001181230.1.
DR AlphaFoldDB; P53259; -.
DR SMR; P53259; -.
DR BioGRID; 33344; 147.
DR DIP; DIP-5524N; -.
DR STRING; 4932.YGR101W; -.
DR MEROPS; S54.007; -.
DR PaxDb; P53259; -.
DR PRIDE; P53259; -.
DR EnsemblFungi; YGR101W_mRNA; YGR101W; YGR101W.
DR GeneID; 852993; -.
DR KEGG; sce:YGR101W; -.
DR SGD; S000003333; PCP1.
DR VEuPathDB; FungiDB:YGR101W; -.
DR eggNOG; KOG2980; Eukaryota.
DR GeneTree; ENSGT00390000013063; -.
DR HOGENOM; CLU_034022_2_1_1; -.
DR InParanoid; P53259; -.
DR OMA; KWSLIGS; -.
DR BioCyc; YEAST:G3O-30811-MON; -.
DR BRENDA; 3.4.21.105; 984.
DR PRO; PR:P53259; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53259; protein.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:SGD.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IMP:SGD.
DR GO; GO:0010821; P:regulation of mitochondrion organization; IMP:SGD.
DR GO; GO:0006465; P:signal peptide processing; IMP:SGD.
DR Gene3D; 1.20.1540.10; -; 1.
DR InterPro; IPR022764; Peptidase_S54_rhomboid_dom.
DR InterPro; IPR035952; Rhomboid-like_sf.
DR Pfam; PF01694; Rhomboid; 1.
DR SUPFAM; SSF144091; SSF144091; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Membrane; Mitochondrion; Mitochondrion inner membrane; Protease;
KW Reference proteome; Serine protease; Transit peptide; Transmembrane;
KW Transmembrane helix.
FT TRANSIT 1..73
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 74..346
FT /note="Rhomboid protein 1, mitochondrial"
FT /id="PRO_0000027392"
FT TRANSMEM 109..129
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 145..165
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 203..223
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 246..266
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 275..295
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 308..328
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 256
FT /note="Nucleophile"
FT ACT_SITE 313
FT MUTAGEN 202
FT /note="N->A: Abolishes protease activity."
FT /evidence="ECO:0000269|PubMed:12901865"
FT MUTAGEN 252
FT /note="S->A,I: Does not abolish protease activity."
FT /evidence="ECO:0000269|PubMed:12417197,
FT ECO:0000269|PubMed:12901865"
FT MUTAGEN 254..256
FT /note="GAS->AAI: Abolishes protease activity."
FT /evidence="ECO:0000269|PubMed:12417197"
FT MUTAGEN 256
FT /note="S->A,I,G: Abolishes protease activity."
FT /evidence="ECO:0000269|PubMed:12417197,
FT ECO:0000269|PubMed:12774122, ECO:0000269|PubMed:12901865"
FT MUTAGEN 313
FT /note="H->A: Abolishes protease activity."
FT /evidence="ECO:0000269|PubMed:12901865"
SQ SEQUENCE 346 AA; 38815 MW; 692AC44C043C9A28 CRC64;
MSGVSSVMLG LRPATRIFFR SNISVSPSRT FVSYIGRSQS TSILKNAPNL EDNVTNLQKI
IPKRFFSQTS ILKSRWKPIF NEETTNRYVR LNRFQQYQQQ RSGGNPLGSM TILGLSLMAG
IYFGSPYLFE HVPPFTYFKT HPKNLVYALL GINVAVFGLW QLPKCWRFLQ KYMLLQKDYV
TSKISIIGSA FSHQEFWHLG MNMLALWSFG TSLATMLGAS NFFSLYMNSA IAGSLFSLWY
PKLARLAIVG PSLGASGALF GVLGCFSYLF PHAKILLFVF PVPGGAWVAF LASVAWNAAG
CALRWGSFDY AAHLGGSMMG VLYGWYISKA VEKQRQRRLQ AAGRWF
