Q3B8P0 (PARL_RAT) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 62.
History...
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Presenilins-associated rhomboid-like protein, mitochondrial EC=3.4.21.105 Alternative name(s): Mitochondrial intramembrane-cleaving protease PARL Cleaved into the following chain:
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| Gene names |
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| Organism | Rattus norvegicus (Rat) [Reference proteome] | ||||
| Taxonomic identifier | 10116 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus![]() |
Protein attributes
| Sequence length | 377 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at transcript level |
General annotation (Comments)
| Function | Required for the control of apoptosis during postnatal growth. Essential for proteolytic processing of an antiapoptotic form of OPA1 which prevents the release of mitochondrial cytochrome c in response to intrinsic apoptoptic signals By similarity. UniProtKB Q5XJY4 |
| Catalytic activity | Cleaves type-1 transmembrane domains using a catalytic dyad composed of serine and histidine that are contributed by different transmembrane domains. UniProtKB Q9H300 |
| Subunit structure | Interacts with PSEN1 and PSEN2. Binds OPA1 By similarity. UniProtKB Q9H300 UniProtKB Q5XJY4 |
| Subcellular location | Mitochondrion inner membrane; Multi-pass membrane protein By similarity. P-beta: Nucleus By similarity. Note: Translocated into the nucleus by an unknown mechanism By similarity. |
| Post-translational modification | P-beta is proteolytically processed (beta-cleavage) in a PARL-dependent manner By similarity. UniProtKB Q9H300 |
| Sequence similarities | Belongs to the peptidase S54 family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Membrane Mitochondrion Mitochondrion inner membrane Nucleus |
| Coding sequence diversity | Alternative splicing |
| Domain | Transit peptide Transmembrane Transmembrane helix |
| Molecular function | Hydrolase Protease Serine protease |
| PTM | Phosphoprotein |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | proteolysis Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular_component | integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW mitochondrial inner membraneInferred from electronic annotation. Source: UniProtKB-SubCell nucleusInferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | serine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Alternative products
| This entry describes 2 isoforms produced by alternative splicing. [Align] [Select] | ||||||
| Isoform 1 Ref.1 (identifier: Q3B8P0-1) This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. | ||||||
| Isoform 2 Ref.1 (identifier: Q3B8P0-2) The sequence of this isoform differs from the canonical sequence as follows: 93-105: Missing. | ||||||
| Note: No experimental confirmation available. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Transit peptide | 1 – 50 | 50 | Mitochondrion By similarity UniProtKB Q9H300 | ||||||
| Chain | 51 – 377 | 327 | Presenilins-associated rhomboid-like protein, mitochondrial UniProtKB Q9H300 | PRO_0000257987 | |||||
| Peptide | 51 – 75 | 25 | P-beta By similarity UniProtKB Q9H300 | PRO_0000257988 | |||||
Regions | |||||||||
| Topological domain | 51 – 95 | 45 | Mitochondrial matrix Potential | ||||||
| Transmembrane | 96 – 116 | 21 | Helical; Potential | ||||||
| Topological domain | 117 – 165 | 49 | Mitochondrial intermembrane Potential | ||||||
| Transmembrane | 166 – 186 | 21 | Helical; Potential | ||||||
| Topological domain | 187 – 214 | 28 | Mitochondrial matrix Potential | ||||||
| Transmembrane | 215 – 235 | 21 | Helical; Potential | ||||||
| Topological domain | 236 – 242 | 7 | Mitochondrial intermembrane Potential | ||||||
| Transmembrane | 243 – 263 | 21 | Helical; Potential | ||||||
| Topological domain | 264 – 268 | 5 | Mitochondrial matrix Potential | ||||||
| Transmembrane | 269 – 289 | 21 | Helical; Potential | ||||||
| Topological domain | 290 – 293 | 4 | Mitochondrial intermembrane Potential | ||||||
| Transmembrane | 294 – 314 | 21 | Helical; Potential | ||||||
| Topological domain | 315 – 331 | 17 | Mitochondrial matrix Potential | ||||||
| Transmembrane | 332 – 352 | 21 | Helical; Potential | ||||||
| Topological domain | 353 – 377 | 25 | Mitochondrial intermembrane Potential | ||||||
Sites | |||||||||
| Active site | 275 | 1 | Nucleophile By similarity UniProtKB P53259 | ||||||
| Active site | 333 | 1 | By similarity UniProtKB P53259 | ||||||
Amino acid modifications | |||||||||
| Modified residue | 63 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 68 | 1 | Phosphoserine By similarity | ||||||
Natural variations | |||||||||
| Alternative sequence | 93 – 105 | 13 | Missing in isoform 2. Ref.1 | VSP_052185 | |||||
Sequences
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References
| [1] | "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). Tissue: Liver and Thymus. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | BC088226 mRNA. Translation: AAH88226.1. BC105907 mRNA. Translation: AAI05908.1. |
| IPI | IPI00361872. IPI00781173. |
| RefSeq | NP_001030326.1. NM_001035249.1. |
| UniGene | Rn.7053. |
3D structure databases | |
| ProteinModelPortal | Q3B8P0. |
| ModBase | Search... |
PTM databases | |
| PhosphoSite | Q3B8P0. |
Proteomic databases | |
| PaxDb | Q3B8P0. |
| PRIDE | Q3B8P0. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 287979. |
| KEGG | rno:287979. |
Organism-specific databases | |
| CTD | 55486. |
| RGD | 1306191. Parl. |
Phylogenomic databases | |
| eggNOG | COG0705. |
| HOGENOM | HOG000230670. |
| HOVERGEN | HBG082107. |
| InParanoid | Q3B8P0. |
| KO | K09650. |
| OrthoDB | EOG4ZGPCC. |
Gene expression databases | |
| ArrayExpress | Q3B8P0. |
| Genevestigator | Q3B8P0. |
| GermOnline | ENSRNOG00000023271. Rattus norvegicus. |
Family and domain databases | |
| InterPro | IPR002610. Peptidase_S54_rhomboid. IPR022764. Peptidase_S54_rhomboid_dom. [Graphical view] |
| PANTHER | PTHR22936. PTHR22936. 1 hit. |
| Pfam | PF01694. Rhomboid. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other | |
| NextBio | 627335. |
Entry information
| Entry name | PARL_RAT | ||||||||
| Accession | Primary (citable) accession number: Q3B8P0 Secondary accession number(s): Q5I0L2 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| Peptidase families Classification of peptidase families and list of entries |
| SIMILARITY comments Index of protein domains and families |

Clusters with
