PARL_DANRE
ID PARL_DANRE Reviewed; 383 AA.
AC Q58EK4;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Presenilins-associated rhomboid-like protein, mitochondrial;
DE EC=3.4.21.105;
DE Flags: Precursor;
GN Name=parl {ECO:0000250|UniProtKB:Q9H300}; ORFNames=zgc:112986;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1] {ECO:0000312|EMBL:AAH91865.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo {ECO:0000312|EMBL:AAH91865.1};
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (MAR-2005) 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). {ECO:0000250}.
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 -!- 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 -!- SIMILARITY: Belongs to the peptidase S54 family. {ECO:0000255}.
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DR EMBL; BC091865; AAH91865.1; -; mRNA.
DR RefSeq; NP_001014320.1; NM_001014298.1.
DR AlphaFoldDB; Q58EK4; -.
DR STRING; 7955.ENSDARP00000057438; -.
DR PaxDb; Q58EK4; -.
DR PRIDE; Q58EK4; -.
DR GeneID; 541485; -.
DR KEGG; dre:541485; -.
DR CTD; 541485; -.
DR ZFIN; ZDB-GENE-050327-8; parla.
DR eggNOG; KOG2980; Eukaryota.
DR InParanoid; Q58EK4; -.
DR OrthoDB; 1554324at2759; -.
DR PhylomeDB; Q58EK4; -.
DR PRO; PR:Q58EK4; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; 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: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; Protease;
KW Reference proteome; Serine protease; Transit peptide; Transmembrane;
KW Transmembrane helix.
FT TRANSIT 1..37
FT /note="Mitochondrion"
FT /evidence="ECO:0000250|UniProtKB:Q9H300"
FT CHAIN 38..383
FT /note="Presenilins-associated rhomboid-like protein,
FT mitochondrial"
FT /id="PRO_0000259406"
FT TOPO_DOM 38..83
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 84..104
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 105..168
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 169..189
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 190..219
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 220..240
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 241..245
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 246..266
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 267..271
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 272..292
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 293..298
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 299..319
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 320..334
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 335..355
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 356..383
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT REGION 35..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..56
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 278
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 336
FT /evidence="ECO:0000250"
SQ SEQUENCE 383 AA; 42409 MW; 73F20BDEE19FC64C CRC64;
MAWRSCFMKW TQINSINASS LCPKSTRLNI HPQQRCGFRK TERPSESKKG VQETEAEAGG
HNRAVPPKPV PPLPPRRPHQ LFRPLVFTVG FTGCSFGAAA ILQYESVKSR VQLAIEEAKE
EKRDTLLEGH DTTYWHNWWN QLSNFQKQVI LLISAVDDFW SGLSEGQKTV TGIIALNTVV
LCCWRVPAMQ RFLVKYFTSN PASKTRCLPM VLSSFSHYSV IHMVVNMYVL WTFSSSIVSL
LGREQFLALY LSGGVISTFV SYVFKTATGR LGPSLGASGS IMTVLAAVCT KIPEAKLGIV
LLPVISFSAG NALKALVALD IAGLVLGWRF FDHAAHLGGA LFGVWYIGYG HELIWRKREP
LIKFWHELRN MSPGRPGPGG GGG
