PARL_PONAB
ID PARL_PONAB Reviewed; 379 AA.
AC Q5R5H4;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Presenilins-associated rhomboid-like protein, mitochondrial;
DE EC=3.4.21.105 {ECO:0000250|UniProtKB:Q9H300};
DE AltName: Full=Mitochondrial intramembrane-cleaving protease PARL;
DE Contains:
DE RecName: Full=P-beta;
DE Short=Pbeta;
DE Flags: Precursor;
GN Name=PARL; Synonyms=PSARL;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Required for the control of apoptosis during postnatal
CC growth. Essential for proteolytic processing of an antiapoptotic form
CC of OPA1 which prevents the release of mitochondrial cytochrome c in
CC response to intrinsic apoptotic signals (By similarity). Required for
CC the maturation of PINK1 into its 52kDa mature form after its cleavage
CC by mitochondrial-processing peptidase (MPP). Promotes changes in
CC mitochondria morphology regulated by phosphorylation of P-beta domain
CC (By similarity). {ECO:0000250|UniProtKB:Q5XJY4,
CC ECO:0000250|UniProtKB:Q9H300}.
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 Evidence={ECO:0000250|UniProtKB:Q9H300};
CC -!- SUBUNIT: Interacts with PSEN1 and PSEN2. Binds OPA1 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:Q9H300}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q9H300}.
CC -!- SUBCELLULAR LOCATION: [P-beta]: Nucleus {ECO:0000250|UniProtKB:Q9H300}.
CC Note=Translocated into the nucleus by an unknown mechanism.
CC {ECO:0000250|UniProtKB:Q9H300}.
CC -!- PTM: P-beta is proteolytically processed (beta-cleavage) in a PARL-
CC dependent manner. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase S54 family. {ECO:0000305}.
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DR EMBL; CR860885; CAH92992.1; -; mRNA.
DR RefSeq; NP_001126768.1; NM_001133296.1.
DR AlphaFoldDB; Q5R5H4; -.
DR STRING; 9601.ENSPPYP00000024436; -.
DR MEROPS; S54.009; -.
DR Ensembl; ENSPPYT00000016678; ENSPPYP00000016034; ENSPPYG00000014338.
DR GeneID; 100173771; -.
DR KEGG; pon:100173771; -.
DR CTD; 55486; -.
DR eggNOG; KOG2980; Eukaryota.
DR GeneTree; ENSGT00390000013063; -.
DR HOGENOM; CLU_034022_0_1_1; -.
DR InParanoid; Q5R5H4; -.
DR OrthoDB; 1554324at2759; -.
DR Proteomes; UP000001595; Chromosome 3.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
KW Hydrolase; Membrane; Mitochondrion; Mitochondrion inner membrane; Nucleus;
KW Phosphoprotein; Protease; Reference proteome; Serine protease;
KW Transit peptide; Transmembrane; Transmembrane helix.
FT TRANSIT 1..52
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 53..379
FT /note="Presenilins-associated rhomboid-like protein,
FT mitochondrial"
FT /id="PRO_0000027390"
FT PEPTIDE 53..77
FT /note="P-beta"
FT /evidence="ECO:0000250"
FT /id="PRO_0000027391"
FT TOPO_DOM 53..101
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 102..121
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 122..167
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 168..187
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 188..207
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 208..230
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 231..244
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 245..262
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 263..273
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 274..292
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 293..295
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 296..318
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 319..332
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 333..354
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 355..379
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT ACT_SITE 277
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 335
FT /evidence="ECO:0000250"
FT MOD_RES 65
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H300"
FT MOD_RES 69
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9H300"
FT MOD_RES 70
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H300"
SQ SEQUENCE 379 AA; 42208 MW; C8B9EB0C9CFD247F CRC64;
MAWRGWAQRG WGCGQAWAAS VGGRSCEELT AALTPPRLLG RRFNFFIQQK CGFRKAPRKV
EPRRSDTGTS GEAYKRSALI PPVEETVFYP SPYPIRSLIK PLFFTVGFTG CAFGSAAIWQ
YESLKSRVQS YFDGIKADWL DSIRPQKEGD FRKEINKWWN NLSDGQRTVT GIIAANVLVF
CLWRVPSLQR TMIRYFTSNP ASKVLCSPML LSTFSHFSLF HMAANMYVLW SFSSSIVNIL
GQEQFMAVYL SAGVISNFVS YVGKVATGRY GPSLGASGAI MTVLAAVCTK IPEGRLAIIF
LPMFTFTAGN ALKAIIAMDT AGMILGWKFF DHAAHLGGAL FGIWYVTYGH ELIWKNREPL
VKIWHEIRTN GPKKGGGSK
