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Protein

Presenilins-associated rhomboid-like protein, mitochondrial

Gene

PARL

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

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).By similarity

Catalytic activityi

Cleaves type-1 transmembrane domains using a catalytic dyad composed of serine and histidine that are contributed by different transmembrane domains.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei275NucleophileBy similarity1
Active sitei333By similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Names & Taxonomyi

Protein namesi
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:
P-beta
Short name:
Pbeta
Gene namesi
Name:PARL
Synonyms:PSARL
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 1

Subcellular locationi

  • Mitochondrion inner membrane By similarity; Multi-pass membrane protein By similarity
P-beta :
  • Nucleus By similarity

  • Note: Translocated into the nucleus by an unknown mechanism.By similarity

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini53 – 99Mitochondrial matrixSequence analysisAdd BLAST47
Transmembranei100 – 119HelicalSequence analysisAdd BLAST20
Topological domaini120 – 165Mitochondrial intermembraneSequence analysisAdd BLAST46
Transmembranei166 – 185HelicalSequence analysisAdd BLAST20
Topological domaini186 – 205Mitochondrial matrixSequence analysisAdd BLAST20
Transmembranei206 – 228HelicalSequence analysisAdd BLAST23
Topological domaini229 – 242Mitochondrial intermembraneSequence analysisAdd BLAST14
Transmembranei243 – 260HelicalSequence analysisAdd BLAST18
Topological domaini261 – 270Mitochondrial matrixSequence analysis10
Transmembranei271 – 287HelicalSequence analysisAdd BLAST17
Topological domaini288 – 293Mitochondrial intermembraneSequence analysis6
Transmembranei294 – 316HelicalSequence analysisAdd BLAST23
Topological domaini317 – 330Mitochondrial matrixSequence analysisAdd BLAST14
Transmembranei331 – 352HelicalSequence analysisAdd BLAST22
Topological domaini353 – 377Mitochondrial intermembraneSequence analysisAdd BLAST25

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 52MitochondrionBy similarityAdd BLAST52
ChainiPRO_000024509353 – 377Presenilins-associated rhomboid-like protein, mitochondrialAdd BLAST325
PeptideiPRO_000024509453 – 75P-betaBy similarityAdd BLAST23

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei65PhosphoserineBy similarity1
Modified residuei68PhosphoserineBy similarity1

Post-translational modificationi

P-beta is proteolytically processed (beta-cleavage) in a PARL-dependent manner.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ2KHV4.
PRIDEiQ2KHV4.

Expressioni

Gene expression databases

BgeeiENSBTAG00000014460.

Interactioni

Subunit structurei

Interacts with PSEN1 and PSEN2. Binds OPA1 (By similarity).By similarity

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000019227.

Structurei

3D structure databases

ProteinModelPortaliQ2KHV4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase S54 family.Curated

Keywords - Domaini

Transit peptide, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG2980. Eukaryota.
COG0705. LUCA.
GeneTreeiENSGT00390000013063.
HOGENOMiHOG000230670.
HOVERGENiHBG082107.
InParanoidiQ2KHV4.
KOiK09650.
OMAiHEMRTNS.
OrthoDBiEOG091G0B3Z.
TreeFamiTF313603.

Family and domain databases

Gene3Di1.20.1540.10. 1 hit.
InterProiIPR002610. Peptidase_S54_rhomboid.
IPR022764. Peptidase_S54_rhomboid_dom.
[Graphical view]
PANTHERiPTHR22936. PTHR22936. 1 hit.
PfamiPF01694. Rhomboid. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q2KHV4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAWRGWAQRG WGCGQAWTLP VCGGSYEELT AALAPSRLLR RRFNFFIQQK
60 70 80 90 100
CGFRKAPRKV EPRRSDTSSE AYKRSALIPP VEETAFYPSP YPIRTLVKPL
110 120 130 140 150
FFTVGFTGCA FGSAAIWQYE SLKSKVQSYF DGIKADWLDS IRPQKEGDFR
160 170 180 190 200
KEINKWWNNL SDGQRTVTGI IAANVFVFCL WRVPSLQRTM IRYFTSNPAS
210 220 230 240 250
KVLCSPMLLS TFSHFSLFHM AANMYVLWSF SSSIVNILGQ EQFMAVYLSA
260 270 280 290 300
GVISTFVSYV CKVATGRYGP SLGASGAIMT VLAAVCTKIP EGRLAIIFLP
310 320 330 340 350
MFTFTAGNAL KAIIAMDTAG MILGWKFFDH AAHLGGALFG IWYITYGHEL
360 370
IWKNREPLVK IWHEMRTNSP KKGGGSK
Length:377
Mass (Da):42,301
Last modified:March 7, 2006 - v1
Checksum:i657E9D56D803203D
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti4R → G in AAX08693 (PubMed:16305752).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BT020676 mRNA. Translation: AAX08693.1.
BT026291 mRNA. Translation: ABG81447.1.
BT029889 mRNA. Translation: ABM06139.1.
BC112869 mRNA. Translation: AAI12870.1.
RefSeqiNP_001015596.1. NM_001015596.1.
UniGeneiBt.4331.

Genome annotation databases

EnsembliENSBTAT00000019227; ENSBTAP00000019227; ENSBTAG00000014460.
GeneIDi514191.
KEGGibta:514191.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BT020676 mRNA. Translation: AAX08693.1.
BT026291 mRNA. Translation: ABG81447.1.
BT029889 mRNA. Translation: ABM06139.1.
BC112869 mRNA. Translation: AAI12870.1.
RefSeqiNP_001015596.1. NM_001015596.1.
UniGeneiBt.4331.

3D structure databases

ProteinModelPortaliQ2KHV4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000019227.

Proteomic databases

PaxDbiQ2KHV4.
PRIDEiQ2KHV4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000019227; ENSBTAP00000019227; ENSBTAG00000014460.
GeneIDi514191.
KEGGibta:514191.

Organism-specific databases

CTDi55486.

Phylogenomic databases

eggNOGiKOG2980. Eukaryota.
COG0705. LUCA.
GeneTreeiENSGT00390000013063.
HOGENOMiHOG000230670.
HOVERGENiHBG082107.
InParanoidiQ2KHV4.
KOiK09650.
OMAiHEMRTNS.
OrthoDBiEOG091G0B3Z.
TreeFamiTF313603.

Gene expression databases

BgeeiENSBTAG00000014460.

Family and domain databases

Gene3Di1.20.1540.10. 1 hit.
InterProiIPR002610. Peptidase_S54_rhomboid.
IPR022764. Peptidase_S54_rhomboid_dom.
[Graphical view]
PANTHERiPTHR22936. PTHR22936. 1 hit.
PfamiPF01694. Rhomboid. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPARL_BOVIN
AccessioniPrimary (citable) accession number: Q2KHV4
Secondary accession number(s): A1L5A2, Q0V8C8, Q5EA93
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2006
Last sequence update: March 7, 2006
Last modified: September 7, 2016
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.