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Protein

Proteinase-activated receptor 1

Gene

F2R

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

High affinity receptor for activated thrombin coupled to G proteins that stimulate phosphoinositide hydrolysis. May play a role in platelets activation and in vascular development.1 Publication

GO - Molecular functioni

  • G-protein alpha-subunit binding Source: UniProtKB
  • G-protein beta-subunit binding Source: UniProtKB
  • G-protein coupled receptor activity Source: UniProtKB
  • receptor binding Source: BHF-UCL
  • thrombin-activated receptor activity Source: BHF-UCL

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

G-protein coupled receptor, Receptor, Transducer

Keywords - Biological processi

Blood coagulation, Hemostasis

Enzyme and pathway databases

BioCyciZFISH:ENSG00000181104-MONOMER.
ReactomeiR-HSA-140875. Common Pathway of Fibrin Clot Formation.
R-HSA-375276. Peptide ligand-binding receptors.
R-HSA-416476. G alpha (q) signalling events.
R-HSA-456926. Thrombin signalling through proteinase activated receptors (PARs).
SIGNORiP25116.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteinase-activated receptor 1
Short name:
PAR-1
Alternative name(s):
Coagulation factor II receptor
Thrombin receptor
Gene namesi
Name:F2R
Synonyms:CF2R, PAR1, TR
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:3537. F2R.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini42 – 102ExtracellularSequence analysisAdd BLAST61
Transmembranei103 – 128Helical; Name=1Sequence analysisAdd BLAST26
Topological domaini129 – 137CytoplasmicSequence analysis9
Transmembranei138 – 157Helical; Name=2Sequence analysisAdd BLAST20
Topological domaini158 – 176ExtracellularSequence analysisAdd BLAST19
Transmembranei177 – 198Helical; Name=3Sequence analysisAdd BLAST22
Topological domaini199 – 218CytoplasmicSequence analysisAdd BLAST20
Transmembranei219 – 239Helical; Name=4Sequence analysisAdd BLAST21
Topological domaini240 – 268ExtracellularSequence analysisAdd BLAST29
Transmembranei269 – 288Helical; Name=5Sequence analysisAdd BLAST20
Topological domaini289 – 311CytoplasmicSequence analysisAdd BLAST23
Transmembranei312 – 334Helical; Name=6Sequence analysisAdd BLAST23
Topological domaini335 – 350ExtracellularSequence analysisAdd BLAST16
Transmembranei351 – 374Helical; Name=7Sequence analysisAdd BLAST24
Topological domaini375 – 425CytoplasmicSequence analysisAdd BLAST51

GO - Cellular componenti

  • caveola Source: BHF-UCL
  • cell surface Source: UniProtKB
  • early endosome Source: UniProtKB
  • extracellular region Source: Reactome
  • Golgi apparatus Source: ProtInc
  • integral component of plasma membrane Source: ProtInc
  • late endosome Source: UniProtKB
  • neuromuscular junction Source: UniProtKB
  • plasma membrane Source: UniProtKB
  • platelet dense tubular network Source: BHF-UCL
  • postsynaptic membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Organism-specific databases

DisGeNETi2149.
OpenTargetsiENSG00000181104.
PharmGKBiPA27946.

Chemistry databases

ChEMBLiCHEMBL3974.
DrugBankiDB00086. Streptokinase.
DB09030. Vorapaxar.
GuidetoPHARMACOLOGYi347.

Polymorphism and mutation databases

BioMutaiF2R.
DMDMi20178318.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 211 PublicationAdd BLAST21
PropeptideiPRO_000001274022 – 41Add BLAST20
ChainiPRO_000001274142 – 425Proteinase-activated receptor 1Add BLAST384

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi35N-linked (GlcNAc...)Sequence analysis1
Glycosylationi62N-linked (GlcNAc...)Sequence analysis1
Glycosylationi75N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi175 ↔ 254PROSITE-ProRule annotation
Glycosylationi250N-linked (GlcNAc...)Sequence analysis1
Glycosylationi259N-linked (GlcNAc...)Sequence analysis1
Modified residuei418PhosphoserineCombined sources1

Post-translational modificationi

A proteolytic cleavage generates a new N-terminus that functions as a tethered ligand.
Phosphorylated in the C-terminal tail; probably mediating desensitization prior to the uncoupling and internalization of the receptor.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei41 – 42Cleavage; by thrombin2

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiP25116.
PaxDbiP25116.
PeptideAtlasiP25116.
PRIDEiP25116.

PTM databases

iPTMnetiP25116.
PhosphoSitePlusiP25116.
SwissPalmiP25116.

Miscellaneous databases

PMAP-CutDBP25116.

Expressioni

Tissue specificityi

Platelets and vascular endothelial cells.

Gene expression databases

BgeeiENSG00000181104.
CleanExiHS_F2R.
ExpressionAtlasiP25116. baseline and differential.
GenevisibleiP25116. HS.

Organism-specific databases

HPAiCAB008973.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
CAV1Q031353EBI-2803960,EBI-603614
PROCRQ9UNN83EBI-2803960,EBI-719705

GO - Molecular functioni

  • G-protein alpha-subunit binding Source: UniProtKB
  • G-protein beta-subunit binding Source: UniProtKB
  • receptor binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi108448. 21 interactors.
DIPiDIP-29703N.
IntActiP25116. 17 interactors.
STRINGi9606.ENSP00000321326.

Chemistry databases

BindingDBiP25116.

Structurei

Secondary structure

1425
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi39 – 41Combined sources3
Turni47 – 50Combined sources4
Helixi92 – 96Combined sources5
Helixi99 – 102Combined sources4
Helixi104 – 130Combined sources27
Helixi131 – 133Combined sources3
Helixi136 – 152Combined sources17
Helixi155 – 163Combined sources9
Helixi172 – 205Combined sources34
Helixi216 – 238Combined sources23
Beta strandi243 – 246Combined sources4
Turni247 – 250Combined sources4
Beta strandi251 – 257Combined sources7
Helixi265 – 296Combined sources32
Helixi305 – 324Combined sources20
Helixi327 – 338Combined sources12
Helixi347 – 360Combined sources14
Helixi363 – 373Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1NRNX-ray3.10R38-60[»]
1NROX-ray3.10R38-64[»]
1NRPX-ray3.00R38-60[»]
1NRQX-ray3.50R40-60[»]
1NRRX-ray2.40R43-60[»]
3BEFX-ray2.20C/F49-57[»]
3HKIX-ray2.20C/F42-62[»]
3HKJX-ray2.60C/F42-62[»]
3LU9X-ray1.80C/F33-57[»]
3VW7X-ray2.20A86-395[»]
ProteinModelPortaliP25116.
SMRiP25116.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP25116.

Family & Domainsi

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi57 – 60Asp/Glu-rich (acidic)4

Domaini

The cleaved signal peptide may not be degraded and may function as an intracellular angiogenesis inhibitor peptide known as parstatin.

Sequence similaritiesi

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

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IJCV. Eukaryota.
ENOG4110Q89. LUCA.
GeneTreeiENSGT00760000119001.
HOGENOMiHOG000232200.
HOVERGENiHBG108233.
InParanoidiP25116.
KOiK03914.
OMAiASKMDTC.
OrthoDBiEOG091G0I94.
PhylomeDBiP25116.
TreeFamiTF330775.

Family and domain databases

InterProiIPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
IPR003912. Protea_act_rcpt.
IPR000935. Thrmbn_rcpt.
[Graphical view]
PfamiPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSiPR00237. GPCRRHODOPSN.
PR01428. PROTEASEAR.
PR00908. THROMBINR.
PROSITEiPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P25116-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGPRRLLLVA ACFSLCGPLL SARTRARRPE SKATNATLDP RSFLLRNPND
60 70 80 90 100
KYEPFWEDEE KNESGLTEYR LVSINKSSPL QKQLPAFISE DASGYLTSSW
110 120 130 140 150
LTLFVPSVYT GVFVVSLPLN IMAIVVFILK MKVKKPAVVY MLHLATADVL
160 170 180 190 200
FVSVLPFKIS YYFSGSDWQF GSELCRFVTA AFYCNMYASI LLMTVISIDR
210 220 230 240 250
FLAVVYPMQS LSWRTLGRAS FTCLAIWALA IAGVVPLLLK EQTIQVPGLN
260 270 280 290 300
ITTCHDVLNE TLLEGYYAYY FSAFSAVFFF VPLIISTVCY VSIIRCLSSS
310 320 330 340 350
AVANRSKKSR ALFLSAAVFC IFIICFGPTN VLLIAHYSFL SHTSTTEAAY
360 370 380 390 400
FAYLLCVCVS SISCCIDPLI YYYASSECQR YVYSILCCKE SSDPSSYNSS
410 420
GQLMASKMDT CSSNLNNSIY KKLLT
Length:425
Mass (Da):47,441
Last modified:April 16, 2002 - v2
Checksum:i41B742A99EEC96AB
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti238L → V in AAA36743 (PubMed:1672265).Curated1
Sequence conflicti364C → S in AAA36743 (PubMed:1672265).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_014167166S → G.1 PublicationCorresponds to variant rs5893dbSNPEnsembl.1
Natural variantiVAR_049432187Y → N.Corresponds to variant rs2230849dbSNPEnsembl.1
Natural variantiVAR_049433257V → L.Corresponds to variant rs2227832dbSNPEnsembl.1
Natural variantiVAR_060680268A → P.Corresponds to variant rs1055103dbSNPEnsembl.1
Natural variantiVAR_060681335A → V.2 PublicationsCorresponds to variant rs17849599dbSNPEnsembl.1
Natural variantiVAR_049434412S → Y.Corresponds to variant rs2227799dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M62424 mRNA. Translation: AAA36743.1.
AF391809 Genomic DNA. Translation: AAK69768.1.
BT007279 mRNA. Translation: AAP35943.1.
BC002464 mRNA. Translation: AAH02464.1.
BC051909 mRNA. Translation: AAH51909.1.
CCDSiCCDS4032.1.
PIRiA37912.
RefSeqiNP_001298242.1. NM_001311313.1.
NP_001983.2. NM_001992.4.
UniGeneiHs.482562.

Genome annotation databases

EnsembliENST00000319211; ENSP00000321326; ENSG00000181104.
GeneIDi2149.
KEGGihsa:2149.
UCSCiuc003ken.5. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

SeattleSNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M62424 mRNA. Translation: AAA36743.1.
AF391809 Genomic DNA. Translation: AAK69768.1.
BT007279 mRNA. Translation: AAP35943.1.
BC002464 mRNA. Translation: AAH02464.1.
BC051909 mRNA. Translation: AAH51909.1.
CCDSiCCDS4032.1.
PIRiA37912.
RefSeqiNP_001298242.1. NM_001311313.1.
NP_001983.2. NM_001992.4.
UniGeneiHs.482562.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1NRNX-ray3.10R38-60[»]
1NROX-ray3.10R38-64[»]
1NRPX-ray3.00R38-60[»]
1NRQX-ray3.50R40-60[»]
1NRRX-ray2.40R43-60[»]
3BEFX-ray2.20C/F49-57[»]
3HKIX-ray2.20C/F42-62[»]
3HKJX-ray2.60C/F42-62[»]
3LU9X-ray1.80C/F33-57[»]
3VW7X-ray2.20A86-395[»]
ProteinModelPortaliP25116.
SMRiP25116.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108448. 21 interactors.
DIPiDIP-29703N.
IntActiP25116. 17 interactors.
STRINGi9606.ENSP00000321326.

Chemistry databases

BindingDBiP25116.
ChEMBLiCHEMBL3974.
DrugBankiDB00086. Streptokinase.
DB09030. Vorapaxar.
GuidetoPHARMACOLOGYi347.

Protein family/group databases

GPCRDBiSearch...

PTM databases

iPTMnetiP25116.
PhosphoSitePlusiP25116.
SwissPalmiP25116.

Polymorphism and mutation databases

BioMutaiF2R.
DMDMi20178318.

Proteomic databases

MaxQBiP25116.
PaxDbiP25116.
PeptideAtlasiP25116.
PRIDEiP25116.

Protocols and materials databases

DNASUi2149.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000319211; ENSP00000321326; ENSG00000181104.
GeneIDi2149.
KEGGihsa:2149.
UCSCiuc003ken.5. human.

Organism-specific databases

CTDi2149.
DisGeNETi2149.
GeneCardsiF2R.
H-InvDBHIX0004960.
HGNCiHGNC:3537. F2R.
HPAiCAB008973.
MIMi187930. gene.
neXtProtiNX_P25116.
OpenTargetsiENSG00000181104.
PharmGKBiPA27946.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IJCV. Eukaryota.
ENOG4110Q89. LUCA.
GeneTreeiENSGT00760000119001.
HOGENOMiHOG000232200.
HOVERGENiHBG108233.
InParanoidiP25116.
KOiK03914.
OMAiASKMDTC.
OrthoDBiEOG091G0I94.
PhylomeDBiP25116.
TreeFamiTF330775.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000181104-MONOMER.
ReactomeiR-HSA-140875. Common Pathway of Fibrin Clot Formation.
R-HSA-375276. Peptide ligand-binding receptors.
R-HSA-416476. G alpha (q) signalling events.
R-HSA-456926. Thrombin signalling through proteinase activated receptors (PARs).
SIGNORiP25116.

Miscellaneous databases

ChiTaRSiF2R. human.
EvolutionaryTraceiP25116.
GeneWikiiCoagulation_factor_II_receptor.
GenomeRNAii2149.
PMAP-CutDBP25116.
PROiP25116.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000181104.
CleanExiHS_F2R.
ExpressionAtlasiP25116. baseline and differential.
GenevisibleiP25116. HS.

Family and domain databases

InterProiIPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
IPR003912. Protea_act_rcpt.
IPR000935. Thrmbn_rcpt.
[Graphical view]
PfamiPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSiPR00237. GPCRRHODOPSN.
PR01428. PROTEASEAR.
PR00908. THROMBINR.
PROSITEiPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPAR1_HUMAN
AccessioniPrimary (citable) accession number: P25116
Secondary accession number(s): Q53XV0, Q96RF7, Q9BUN4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: April 16, 2002
Last modified: November 30, 2016
This is version 187 of the entry and version 2 of the sequence. [Complete history]
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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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