PARL_BOVIN
ID PARL_BOVIN Reviewed; 377 AA.
AC Q2KHV4; A1L5A2; Q0V8C8; Q5EA93;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 106.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JAN-2006) 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; BT020676; AAX08693.1; -; mRNA.
DR EMBL; BT026291; ABG81447.1; -; mRNA.
DR EMBL; BT029889; ABM06139.1; -; mRNA.
DR EMBL; BC112869; AAI12870.1; -; mRNA.
DR RefSeq; NP_001015596.1; NM_001015596.1.
DR AlphaFoldDB; Q2KHV4; -.
DR STRING; 9913.ENSBTAP00000019227; -.
DR PaxDb; Q2KHV4; -.
DR PRIDE; Q2KHV4; -.
DR GeneID; 514191; -.
DR KEGG; bta:514191; -.
DR CTD; 55486; -.
DR eggNOG; KOG2980; Eukaryota.
DR HOGENOM; CLU_034022_0_1_1; -.
DR InParanoid; Q2KHV4; -.
DR OrthoDB; 1554324at2759; -.
DR TreeFam; TF313603; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0006465; P:signal peptide processing; IBA:GO_Central.
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:0000250"
FT CHAIN 53..377
FT /note="Presenilins-associated rhomboid-like protein,
FT mitochondrial"
FT /id="PRO_0000245093"
FT PEPTIDE 53..75
FT /note="P-beta"
FT /evidence="ECO:0000250"
FT /id="PRO_0000245094"
FT TOPO_DOM 53..99
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 100..119
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 120..165
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 166..185
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 186..205
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 206..228
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 229..242
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 243..260
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 261..270
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 271..287
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 288..293
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 294..316
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 317..330
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 331..352
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 353..377
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT ACT_SITE 275
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 333
FT /evidence="ECO:0000250"
FT MOD_RES 65
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H300"
FT MOD_RES 68
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H300"
FT CONFLICT 4
FT /note="R -> G (in Ref. 1; AAX08693)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 377 AA; 42301 MW; 657E9D56D803203D CRC64;
MAWRGWAQRG WGCGQAWTLP VCGGSYEELT AALAPSRLLR RRFNFFIQQK CGFRKAPRKV
EPRRSDTSSE AYKRSALIPP VEETAFYPSP YPIRTLVKPL FFTVGFTGCA FGSAAIWQYE
SLKSKVQSYF DGIKADWLDS IRPQKEGDFR KEINKWWNNL SDGQRTVTGI IAANVFVFCL
WRVPSLQRTM IRYFTSNPAS KVLCSPMLLS TFSHFSLFHM AANMYVLWSF SSSIVNILGQ
EQFMAVYLSA GVISTFVSYV CKVATGRYGP SLGASGAIMT VLAAVCTKIP EGRLAIIFLP
MFTFTAGNAL KAIIAMDTAG MILGWKFFDH AAHLGGALFG IWYITYGHEL IWKNREPLVK
IWHEMRTNSP KKGGGSK
