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UniProtKB - P55085 (PAR2_HUMAN)

Entry version 183 (16 Oct 2019)
Sequence version 1 (01 Oct 1996)
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Protein

Proteinase-activated receptor 2

Gene

F2RL1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Receptor for trypsin and trypsin-like enzymes coupled to G proteins (PubMed:28445455). Its function is mediated through the activation of several signaling pathways including phospholipase C (PLC), intracellular calcium, mitogen-activated protein kinase (MAPK), I-kappaB kinase/NF-kappaB and Rho (PubMed:28445455). Can also be transactivated by cleaved F2R/PAR1. Involved in modulation of inflammatory responses and regulation of innate and adaptive immunity, and acts as a sensor for proteolytic enzymes generated during infection. Generally is promoting inflammation. Can signal synergistically with TLR4 and probably TLR2 in inflammatory responses and modulates TLR3 signaling. Has a protective role in establishing the endothelial barrier; the activity involves coagulation factor X. Regulates endothelial cell barrier integrity during neutrophil extravasation, probably following proteolytic cleavage by PRTN3 (PubMed:23202369). Proposed to have a bronchoprotective role in airway epithelium, but also shown to compromise the airway epithelial barrier by interrupting E-cadherin adhesion (PubMed:10086357). Involved in the regulation of vascular tone; activation results in hypotension presumably mediated by vasodilation. Associates with a subset of G proteins alpha subunits such as GNAQ, GNA11, GNA14, GNA12 and GNA13, but probably not with G(o) alpha, G(i) subunit alpha-1 and G(i) subunit alpha-2. However, according to PubMed:21627585 can signal through G(i) subunit alpha. Believed to be a class B receptor which internalizes as a complex with arrestin and traffic with it to endosomal vesicles, presumably as desensitized receptor, for extended periods of time. Mediates inhibition of TNF-alpha stimulated JNK phosphorylation via coupling to GNAQ and GNA11; the function involves dissociation of RIPK1 and TRADD from TNFR1. Mediates phosphorylation of nuclear factor NF-kappa-B RELA subunit at 'Ser-536'; the function involves IKBKB and is predominantly independent of G proteins. Involved in cellular migration. Involved in cytoskeletal rearrangement and chemotaxis through beta-arrestin-promoted scaffolds; the function is independent of GNAQ and GNA11 and involves promotion of cofilin dephosphorylation and actin filament severing. Induces redistribution of COPS5 from the plasma membrane to the cytosol and activation of the JNK cascade is mediated by COPS5. Involved in the recruitment of leukocytes to the sites of inflammation and is the major PAR receptor capable of modulating eosinophil function such as proinflammatory cytokine secretion, superoxide production and degranulation. During inflammation promotes dendritic cell maturation, trafficking to the lymph nodes and subsequent T-cell activation. Involved in antimicrobial response of innate immune cells; activation enhances phagocytosis of Gram-positive and killing of Gram-negative bacteria. Acts synergistically with interferon-gamma in enhancing antiviral responses. Implicated in a number of acute and chronic inflammatory diseases such as of the joints, lungs, brain, gastrointestinal tract, periodontium, skin, and vascular systems, and in autoimmune disorders.26 Publications

Miscellaneous

Synthetic PAR agonist peptides (APs) that mimic the first six amino acids of the newly formed N-terminus activate the native, uncleaved receptor nonenzymatically by binding directly to the corresponding second extracellular loop to mediate signaling.

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionG-protein coupled receptor, Receptor, Transducer
Biological processImmunity, Inflammatory response, Innate immunity

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-375276 Peptide ligand-binding receptors
R-HSA-416476 G alpha (q) signalling events

SIGNOR Signaling Network Open Resource

More...SIGNORi		P55085

Protein family/group databases

Transport Classification Database

More...TCDBi		9.A.14.13.12 the g-protein-coupled receptor (gpcr) family

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Proteinase-activated receptor 2
Short name:
PAR-2
Alternative name(s):
Coagulation factor II receptor-like 1
G-protein coupled receptor 11
Thrombin receptor-like 1
Cleaved into the following 2 chains:
Proteinase-activated receptor 2, alternate cleaved 1
Proteinase-activated receptor 2, alternate cleaved 2
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:F2RL1
Synonyms:GPR11, PAR2
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 5

Organism-specific databases

Human Gene Nomenclature Database

More...HGNCi		HGNC:3538 F2RL1

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		600933 gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_P55085

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini37 – 71Extracellular1 PublicationAdd BLAST35
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei72 – 101Helical; Name=11 PublicationAdd BLAST30
Topological domaini102 – 108Cytoplasmic1 Publication7
Transmembranei109 – 137Helical; Name=21 PublicationAdd BLAST29
Topological domaini138 – 149Extracellular1 PublicationAdd BLAST12
Transmembranei150 – 177Helical; Name=31 PublicationAdd BLAST28
Topological domaini178 – 183Cytoplasmic1 Publication6
Transmembranei184 – 211Helical; Name=41 PublicationAdd BLAST28
Topological domaini212 – 235Extracellular1 PublicationAdd BLAST24
Transmembranei236 – 269Helical; Name=51 PublicationAdd BLAST34
Topological domaini270 – 277Cytoplasmic1 Publication8
Transmembranei278 – 317Helical; Name=61 PublicationAdd BLAST40
Topological domaini318 – 323Extracellular1 Publication6
Transmembranei324 – 347Helical; Name=71 PublicationAdd BLAST24
Topological domaini348 – 397Cytoplasmic1 PublicationAdd BLAST50

Keywords - Cellular componenti

Cell membrane, Membrane

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi30N → A: Decreases cell surface expression; when associate with A-222. 1 Publication1
Mutagenesisi30N → A: Increase of sensitivity towards tryptase. 1 Publication1
Mutagenesisi135H → Y: Slight reduction in ligand-mediated receptor activation. 1 Publication1
Mutagenesisi154F → A: Severe reduction in ligand-mediated receptor activation. 1 Publication1
Mutagenesisi157G → C or M: Severe reduction in ligand-mediated receptor activation. 1 Publication1
Mutagenesisi210Y → L: No defect in ligand-mediated receptor activation. 1 Publication1
Mutagenesisi222N → A: Decreases cell surface expression; when associated with A-30. Loss of sensitivity towards all tested proteases. 1 Publication1
Mutagenesisi222N → Q: No defect in ligand-mediated receptor activation. 1 Publication1
Mutagenesisi227H → A: No defect in ligand-mediated receptor activation. 1 Publication1
Mutagenesisi227H → Q: Slight reduction in ligand-mediated receptor activation. 1 Publication1
Mutagenesisi228D → A or N: Severe reduction in ligand-mediated receptor activation. 1 Publication1
Mutagenesisi327I → L: Slight reduction in ligand-mediated receptor activation. 1 Publication1
Mutagenesisi355 – 363Missing : Abolishes signaling through accumulation of intracellular calcium and phosphoinositide; no effect in signaling through MAPK. 1 Publication9
Mutagenesisi361C → A: Loss of palmitoylation; increases surface expression and internalization following trypsin activation, decreases sensitivity and intracellular calcium signaling, increases ERK activation through G(i) subunit alpha. 1
Mutagenesisi363S → A: Reduces receptor desensitization and internalization, activates ERK1/2; when associated with A-366. 1 Publication1
Mutagenesisi366T → A: Reduces receptor desensitization and internalization, activates ERK1/2; when associated with A-363. 1 Publication1

Organism-specific databases

DisGeNET

More...DisGeNETi		2150

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA27947

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...Pharosi		P55085

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL5963

IUPHAR/BPS Guide to PHARMACOLOGY

More...GuidetoPHARMACOLOGYi		348

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		F2RL1

Domain mapping of disease mutations (DMDM)

More...DMDMi		1709580

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 25Sequence analysisAdd BLAST25
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_000001275026 – 36Removed for receptor activationAdd BLAST11
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000041295437 – 397Proteinase-activated receptor 2Add BLAST361
ChainiPRO_000041295638 – 397Proteinase-activated receptor 2, alternate cleaved 1Add BLAST360
ChainiPRO_000001275139 – 397Proteinase-activated receptor 2, alternate cleaved 2Add BLAST359

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi30N-linked (GlcNAc...) asparagine1 Publication1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi148 ↔ 226PROSITE-ProRule annotationCombined sources1 Publication
Glycosylationi222N-linked (GlcNAc...) asparagine1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi361S-palmitoyl cysteine1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

A proteolytic cleavage generates a new N-terminus that functions as a tethered ligand (PubMed:10831593, PubMed:19864598, PubMed:9020112, PubMed:10805786, PubMed:16478888). Activating serine proteases include trypsin, mast cell tryptase, coagulation factors VII and Xa, myeloblastin/PRTN3 and membrane-type serine protease 1/ST14 (PubMed:10831593, PubMed:19864598, PubMed:9020112, PubMed:10805786, PubMed:16478888, PubMed:23202369). Subsequent cleavage by serine proteases, including neutrophil elastase and cathepsin G, leads to receptor deactivation (PubMed:12594060). At least in part, implicated proteases are also shown to activate the receptor; the glycosylation status of the receptor is thought to contribute to the difference (PubMed:12171601). In addition to conventional trypsin-like proteases activated by other proteases and glycosidases derived from bacteria, fungi and insects (PubMed:11447194, PubMed:11441110, PubMed:17404307, PubMed:18474671, PubMed:19864598). Activated by serine protease allergens such as dust mite Der p3 and Der p9 and mold Pen c13 (PubMed:11441110, PubMed:17404307). Activated by P.gingivalis arginine-specific (trypsin-like) cysteine proteinases called gingipains (PubMed:11447194). Activated by S.griseus exogenous chitinase (PubMed:18474671). Activated by A.alternata aspartate protease; the cleavage generates non-conventional processed forms (PubMed:19864598).12 Publications
N-glycosylated and sialylated.1 Publication
Multiple phosphorylated on serine and threonine residues in the cytoplasmic region upon receptor activation; required for receptor desensitization and recruitment of beta-arrestin.1 Publication
Monoubiquitinated by CBL at the plasma membrane and in early endosomes; not required for receptor endocytosis but for translocation to late endosomes or lysosomes. Deubiquitination involves STAMBP and USP8; required for lysosomal trafficking and receptor degradation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei36 – 37Cleavage; by trypsin2

Keywords - PTMi

Disulfide bond, Glycoprotein, Lipoprotein, Palmitate, Phosphoprotein, Ubl conjugation

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P55085

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...MassIVEi		P55085

MaxQB - The MaxQuant DataBase

More...MaxQBi		P55085

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		P55085

PeptideAtlas

More...PeptideAtlasi		P55085

PRoteomics IDEntifications database

More...PRIDEi		P55085

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		56787

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P55085

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...PhosphoSitePlusi		P55085

SwissPalm database of S-palmitoylation events

More...SwissPalmi		P55085

Miscellaneous databases

CutDB - Proteolytic event database

More...PMAP-CutDBi		P55085

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Widely expressed in tissues with especially high levels in pancreas, liver, kidney, small intestine, and colon (PubMed:7556175, PubMed:8615752). Moderate expression is detected in many organs, but none in brain or skeletal muscle (PubMed:7556175, PubMed:8615752). Expressed in endothelial cells (PubMed:23202369).3 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000164251 Expressed in 173 organ(s), highest expression level in colonic mucosa

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P55085 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P55085 HS

Organism-specific databases

Human Protein Atlas

More...HPAi		CAB012989
HPA014091

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Interacts with TLR4, COPS5 and TMED2.

Interacts with GNAQ, GNA11, GNA12, GNA13 and GNA14 (By similarity).

By similarity

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		108449, 14 interactors

Database of interacting proteins

More...DIPi		DIP-42044N

Protein interaction database and analysis system

More...IntActi		P55085, 76 interactors

Molecular INTeraction database

More...MINTi		P55085

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000296677

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P55085

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1397
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		P55085

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi383 – 390Poly-Ser8

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the G-protein coupled receptor 1 family.PROSITE-ProRule annotation

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		ENOG410IGEM Eukaryota
ENOG4111CWR LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000116291

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P55085

KEGG Orthology (KO)

More...KOi		K04234

Database of Orthologous Groups

More...OrthoDBi		892946at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P55085

TreeFam database of animal gene trees

More...TreeFami		TF330775

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR000276 GPCR_Rhodpsn
IPR017452 GPCR_Rhodpsn_7TM
IPR002281 Pro_rcpt_2
IPR003912 Protea_act_rcpt

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00001 7tm_1, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00237 GPCRRHODOPSN
PR01428 PROTEASEAR
PR01152 PROTEASEAR2

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS50262 G_PROTEIN_RECEP_F1_2, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

P55085-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MRSPSAAWLL GAAILLAASL SCSGTIQGTN RSSKGRSLIG KVDGTSHVTG 
        60         70         80         90        100
KGVTVETVFS VDEFSASVLT GKLTTVFLPI VYTIVFVVGL PSNGMALWVF 
       110        120        130        140        150
LFRTKKKHPA VIYMANLALA DLLSVIWFPL KIAYHIHGNN WIYGEALCNV 
       160        170        180        190        200
LIGFFYGNMY CSILFMTCLS VQRYWVIVNP MGHSRKKANI AIGISLAIWL 
       210        220        230        240        250
LILLVTIPLY VVKQTIFIPA LNITTCHDVL PEQLLVGDMF NYFLSLAIGV 
       260        270        280        290        300
FLFPAFLTAS AYVLMIRMLR SSAMDENSEK KRKRAIKLIV TVLAMYLICF 
       310        320        330        340        350
TPSNLLLVVH YFLIKSQGQS HVYALYIVAL CLSTLNSCID PFVYYFVSHD 
       360        370        380        390 
FRDHAKNALL CRSVRTVKQM QVSLTSKKHS RKSSSYSSSS TTVKTSY
Length:397
Mass (Da):44,126
Last modified:October 1, 1996 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iF1A4E1D5AB9B362B
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
D6RJH3D6RJH3_HUMAN
Proteinase-activated receptor 2
F2RL1
112Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti138G → A in AAB47871 (PubMed:8615752).Curated1
Sequence conflicti291T → S in AAH18130 (PubMed:15489334).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_01284621S → F1 PublicationCorresponds to variant dbSNP:rs2243072Ensembl.1
Natural variantiVAR_04943530N → S. Corresponds to variant dbSNP:rs616235Ensembl.1
Natural variantiVAR_012847270R → Q1 PublicationCorresponds to variant dbSNP:rs2243062Ensembl.1
Natural variantiVAR_012848291T → A1 PublicationCorresponds to variant dbSNP:rs2243083Ensembl.1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
Z49993, Z49994 Genomic DNA Translation: CAA90290.1
U34038 mRNA Translation: AAB47871.1
AY336105 mRNA Translation: AAP97012.1
AF400075 Genomic DNA Translation: AAK77914.1
BT009856 mRNA Translation: AAP88858.1
CH471084 Genomic DNA Translation: EAW95782.1
BC012453 mRNA Translation: AAH12453.1
BC018130 mRNA Translation: AAH18130.1
U36753 Genomic DNA Translation: AAA90957.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS4033.1

Protein sequence database of the Protein Information Resource

More...PIRi		S66518

NCBI Reference Sequences

More...RefSeqi		NP_005233.3, NM_005242.5

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000296677; ENSP00000296677; ENSG00000164251

Database of genes from NCBI RefSeq genomes

More...GeneIDi		2150

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:2150

UCSC genome browser

More...UCSCi		uc003keo.4 human

Keywords - Coding sequence diversityi

Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Wikipedia

Protease-activated receptor entry

SeattleSNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z49993, Z49994 Genomic DNA Translation: CAA90290.1
U34038 mRNA Translation: AAB47871.1
AY336105 mRNA Translation: AAP97012.1
AF400075 Genomic DNA Translation: AAK77914.1
BT009856 mRNA Translation: AAP88858.1
CH471084 Genomic DNA Translation: EAW95782.1
BC012453 mRNA Translation: AAH12453.1
BC018130 mRNA Translation: AAH18130.1
U36753 Genomic DNA Translation: AAA90957.1
CCDSiCCDS4033.1
PIRiS66518
RefSeqiNP_005233.3, NM_005242.5

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5NDDX-ray2.80A59-269[»]
A276-377[»]
5NDZX-ray3.60A59-269[»]
A276-377[»]
5NJ6X-ray4.00A55-269[»]
A276-377[»]
SMRiP55085
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi108449, 14 interactors
DIPiDIP-42044N
IntActiP55085, 76 interactors
MINTiP55085
STRINGi9606.ENSP00000296677

Chemistry databases

BindingDBiP55085
ChEMBLiCHEMBL5963
GuidetoPHARMACOLOGYi348

Protein family/group databases

TCDBi9.A.14.13.12 the g-protein-coupled receptor (gpcr) family

Information system for G protein-coupled receptors (GPCRs)

More...GPCRDBi		Search...

PTM databases

iPTMnetiP55085
PhosphoSitePlusiP55085
SwissPalmiP55085

Polymorphism and mutation databases

BioMutaiF2RL1
DMDMi1709580

Proteomic databases

jPOSTiP55085
MassIVEiP55085
MaxQBiP55085
PaxDbiP55085
PeptideAtlasiP55085
PRIDEiP55085
ProteomicsDBi56787

Protocols and materials databases

ABCD curated depository of sequenced antibodies

More...ABCDi		P55085

The DNASU plasmid repository

More...DNASUi		2150

Genome annotation databases

EnsembliENST00000296677; ENSP00000296677; ENSG00000164251
GeneIDi2150
KEGGihsa:2150
UCSCiuc003keo.4 human

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		2150
DisGeNETi2150

GeneCards: human genes, protein and diseases

More...GeneCardsi		F2RL1
HGNCiHGNC:3538 F2RL1
HPAiCAB012989
HPA014091
MIMi600933 gene
neXtProtiNX_P55085
PharmGKBiPA27947

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiENOG410IGEM Eukaryota
ENOG4111CWR LUCA
HOGENOMiHOG000116291
InParanoidiP55085
KOiK04234
OrthoDBi892946at2759
PhylomeDBiP55085
TreeFamiTF330775

Enzyme and pathway databases

ReactomeiR-HSA-375276 Peptide ligand-binding receptors
R-HSA-416476 G alpha (q) signalling events
SIGNORiP55085

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...ChiTaRSi		F2RL1 human

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		Protease_activated_receptor_2

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...GenomeRNAii		2150
PharosiP55085
PMAP-CutDBiP55085

Protein Ontology

More...PROi		PR:P55085

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000164251 Expressed in 173 organ(s), highest expression level in colonic mucosa
ExpressionAtlasiP55085 baseline and differential
GenevisibleiP55085 HS

Family and domain databases

InterProiView protein in InterPro
IPR000276 GPCR_Rhodpsn
IPR017452 GPCR_Rhodpsn_7TM
IPR002281 Pro_rcpt_2
IPR003912 Protea_act_rcpt
PfamiView protein in Pfam
PF00001 7tm_1, 1 hit
PRINTSiPR00237 GPCRRHODOPSN
PR01428 PROTEASEAR
PR01152 PROTEASEAR2
PROSITEiView protein in PROSITE
PS50262 G_PROTEIN_RECEP_F1_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiPAR2_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P55085
Secondary accession number(s): Q13317, Q13346, Q53XJ8
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: October 16, 2019
This is version 183 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. 7-transmembrane G-linked receptors
    List of 7-transmembrane G-linked receptor entries
  5. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  6. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  7. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
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