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Rhomboid protein 1, mitochondrial (EC 3.4.21.105) (Mitochondrial distribution and morphology protein 37) (Processing of cytochrome c peroxidase protein 1)

 PCP1_YEAST              Reviewed;         346 AA.
P53259; D6VUN3;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
25-OCT-2017, entry version 128.
RecName: Full=Rhomboid protein 1, mitochondrial;
EC=3.4.21.105;
AltName: Full=Mitochondrial distribution and morphology protein 37;
AltName: Full=Processing of cytochrome c peroxidase protein 1;
Flags: Precursor;
Name=PCP1; Synonyms=MDM37, RBD1, UGO2; OrderedLocusNames=YGR101W;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169869;
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.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
Nature 387:81-84(1997).
[2]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[3]
FUNCTION, AND MUTAGENESIS OF SER-252; 254-GLY--SER-256 AND SER-256.
PubMed=12417197; DOI=10.1016/S0022-2836(02)01000-8;
Esser K., Tursun B., Ingenhoven M., Michaelis G., Pratje E.;
"A novel two-step mechanism for removal of a mitochondrial signal
sequence involves the mAAA complex and the putative rhomboid protease
Pcp1.";
J. Mol. Biol. 323:835-843(2002).
[4]
FUNCTION.
PubMed=11907266; DOI=10.1091/mbc.01-12-0588;
Dimmer K.S., Fritz S., Fuchs F., Messerschmitt M., Weinbach N.,
Neupert W., Westermann B.;
"Genetic basis of mitochondrial function and morphology in
Saccharomyces cerevisiae.";
Mol. Biol. Cell 13:847-853(2002).
[5]
FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ASN-202; SER-252;
SER-256 AND HIS-313.
PubMed=12901865; DOI=10.1016/S0006-291X(03)01348-2;
Sesaki H., Southard S.M., Hobbs A.E.A., Jensen R.E.;
"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.";
Biochem. Biophys. Res. Commun. 308:276-283(2003).
[6]
FUNCTION.
PubMed=12707284; DOI=10.1074/jbc.M211311200;
Herlan M., Vogel F., Bornhoevd C., Neupert W., Reichert A.S.;
"Processing of Mgm1 by the rhomboid-type protease Pcp1 is required for
maintenance of mitochondrial morphology and of mitochondrial DNA.";
J. Biol. Chem. 278:27781-27788(2003).
[7]
FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF SER-256.
PubMed=12774122; DOI=10.1038/nature01633;
McQuibban G.A., Saurya S., Freeman M.;
"Mitochondrial membrane remodelling regulated by a conserved rhomboid
protease.";
Nature 423:537-541(2003).
[8]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=14562095; DOI=10.1038/nature02026;
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[9]
FUNCTION.
PubMed=15125685; DOI=10.1042/BJ20040566;
Amutha B., Gordon D.M., Gu Y., Pain D.;
"A novel role of Mgm1p, a dynamin-related GTPase, in ATP synthase
assembly and cristae formation/maintenance.";
Biochem. J. 381:19-23(2004).
-!- 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.
{ECO:0000269|PubMed:11907266, ECO:0000269|PubMed:12417197,
ECO:0000269|PubMed:12707284, ECO:0000269|PubMed:12774122,
ECO:0000269|PubMed:12901865, ECO:0000269|PubMed:15125685}.
-!- 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
{ECO:0000269|PubMed:12774122, ECO:0000269|PubMed:12901865,
ECO:0000269|PubMed:14562095}; Multi-pass membrane protein
{ECO:0000269|PubMed:12774122, ECO:0000269|PubMed:12901865,
ECO:0000269|PubMed:14562095}.
-!- SIMILARITY: Belongs to the peptidase S54 family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; Z72886; CAA97104.1; -; Genomic_DNA.
EMBL; BK006941; DAA08194.1; -; Genomic_DNA.
PIR; S64406; S64406.
RefSeq; NP_011615.1; NM_001181230.1.
ProteinModelPortal; P53259; -.
BioGrid; 33344; 138.
DIP; DIP-5524N; -.
MINT; MINT-518042; -.
STRING; 4932.YGR101W; -.
MEROPS; S54.007; -.
PRIDE; P53259; -.
EnsemblFungi; YGR101W; YGR101W; YGR101W.
GeneID; 852993; -.
KEGG; sce:YGR101W; -.
EuPathDB; FungiDB:YGR101W; -.
SGD; S000003333; PCP1.
GeneTree; ENSGT00390000013063; -.
HOGENOM; HOG000000958; -.
InParanoid; P53259; -.
KO; K09650; -.
OMA; AFSHQEF; -.
OrthoDB; EOG092C4ZDG; -.
BioCyc; YEAST:G3O-30811-MONOMER; -.
BRENDA; 3.4.21.105; 984.
PRO; PR:P53259; -.
Proteomes; UP000002311; Chromosome VII.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005743; C:mitochondrial inner membrane; IDA:SGD.
GO; GO:0004252; F:serine-type endopeptidase activity; IMP:SGD.
GO; GO:0010821; P:regulation of mitochondrion organization; IMP:SGD.
GO; GO:0006465; P:signal peptide processing; IMP:SGD.
Gene3D; 1.20.1540.10; -; 1.
InterPro; IPR022764; Peptidase_S54_rhomboid_dom.
InterPro; IPR035952; Rhomboid-like_sf.
Pfam; PF01694; Rhomboid; 1.
SUPFAM; SSF144091; SSF144091; 1.
1: Evidence at protein level;
Complete proteome; Hydrolase; Membrane; Mitochondrion;
Mitochondrion inner membrane; Protease; Reference proteome;
Serine protease; Transit peptide; Transmembrane; Transmembrane helix.
TRANSIT 1 73 Mitochondrion. {ECO:0000255}.
CHAIN 74 346 Rhomboid protein 1, mitochondrial.
/FTId=PRO_0000027392.
TRANSMEM 109 129 Helical. {ECO:0000255}.
TRANSMEM 145 165 Helical. {ECO:0000255}.
TRANSMEM 203 223 Helical. {ECO:0000255}.
TRANSMEM 246 266 Helical. {ECO:0000255}.
TRANSMEM 275 295 Helical. {ECO:0000255}.
TRANSMEM 308 328 Helical. {ECO:0000255}.
ACT_SITE 256 256 Nucleophile.
ACT_SITE 313 313
MUTAGEN 202 202 N->A: Abolishes protease activity.
{ECO:0000269|PubMed:12901865}.
MUTAGEN 252 252 S->A,I: Does not abolish protease
activity. {ECO:0000269|PubMed:12417197,
ECO:0000269|PubMed:12901865}.
MUTAGEN 254 256 GAS->AAI: Abolishes protease activity.
{ECO:0000269|PubMed:12417197}.
MUTAGEN 256 256 S->A,I,G: Abolishes protease activity.
{ECO:0000269|PubMed:12417197,
ECO:0000269|PubMed:12774122,
ECO:0000269|PubMed:12901865}.
MUTAGEN 313 313 H->A: Abolishes protease activity.
{ECO:0000269|PubMed:12901865}.
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


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