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Database: UniProt
Entry: F1S2H4_PIG
LinkDB: F1S2H4_PIG
Original site: F1S2H4_PIG 
ID   F1S2H4_PIG              Unreviewed;       397 AA.
AC   F1S2H4;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 85.
DE   SubName: Full=F2R like trypsin receptor 1 {ECO:0000313|Ensembl:ENSSSCP00000014983.2};
DE   SubName: Full=Proteinase-activated receptor 2 {ECO:0000313|EMBL:HDA47695.1, ECO:0000313|EMBL:HDC33620.1};
GN   Name=F2RL1 {ECO:0000313|Ensembl:ENSSSCP00000014983.2,
GN   ECO:0000313|VGNC:VGNC:87861};
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000014983.2, ECO:0000313|Proteomes:UP000008227};
RN   [1] {ECO:0000313|Ensembl:ENSSSCP00000014983.2, ECO:0000313|Proteomes:UP000008227}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000014983.2,
RC   ECO:0000313|Proteomes:UP000008227};
RG   Porcine genome sequencing project;
RL   Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:HDA47695.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=30723633; DOI=.7717/peerj.6374;
RA   Gilbert D.G.;
RT   "Genes of the pig, Sus scrofa, reconstructed with EvidentialGene.";
RL   PeerJ 7:E6374-E6374(2019).
RN   [3] {ECO:0000313|Ensembl:ENSSSCP00000014983.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC       Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; DQIR01092219; HDA47695.1; -; Transcribed_RNA.
DR   EMBL; DQIR01278142; HDC33620.1; -; Transcribed_RNA.
DR   RefSeq; XP_003123761.1; XM_003123713.3.
DR   STRING; 9823.ENSSSCP00000014983; -.
DR   PaxDb; 9823-ENSSSCP00000014983; -.
DR   Ensembl; ENSSSCT00000015392.5; ENSSSCP00000014983.2; ENSSSCG00000014091.5.
DR   GeneID; 100519703; -.
DR   KEGG; ssc:100519703; -.
DR   CTD; 2150; -.
DR   VGNC; VGNC:87861; F2RL1.
DR   eggNOG; ENOG502QR8S; Eukaryota.
DR   GeneTree; ENSGT01050000244840; -.
DR   HOGENOM; CLU_009579_8_2_1; -.
DR   OMA; SQSHVYA; -.
DR   OrthoDB; 4075920at2759; -.
DR   TreeFam; TF330775; -.
DR   Reactome; R-SSC-375276; Peptide ligand-binding receptors.
DR   Reactome; R-SSC-416476; G alpha (q) signalling events.
DR   Proteomes; UP000008227; Chromosome 2.
DR   Bgee; ENSSSCG00000014091; Expressed in colon and 21 other cell types or tissues.
DR   Genevisible; F1S2H4; SS.
DR   GO; GO:0005769; C:early endosome; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0031143; C:pseudopodium; ISS:UniProtKB.
DR   GO; GO:0004930; F:G protein-coupled receptor activity; ISS:UniProtKB.
DR   GO; GO:0001965; F:G-protein alpha-subunit binding; ISS:UniProtKB.
DR   GO; GO:0031681; F:G-protein beta-subunit binding; ISS:UniProtKB.
DR   GO; GO:0002020; F:protease binding; IEA:Ensembl.
DR   GO; GO:0015057; F:thrombin-activated receptor activity; IEA:InterPro.
DR   GO; GO:0007596; P:blood coagulation; IEA:InterPro.
DR   GO; GO:0045217; P:cell-cell junction maintenance; IEA:Ensembl.
DR   GO; GO:0051607; P:defense response to virus; ISS:UniProtKB.
DR   GO; GO:0061028; P:establishment of endothelial barrier; IEA:Ensembl.
DR   GO; GO:0050900; P:leukocyte migration; IEA:Ensembl.
DR   GO; GO:0070661; P:leukocyte proliferation; ISS:UniProtKB.
DR   GO; GO:0097029; P:mature conventional dendritic cell differentiation; ISS:UniProtKB.
DR   GO; GO:0032682; P:negative regulation of chemokine production; IEA:Ensembl.
DR   GO; GO:0046676; P:negative regulation of insulin secretion; IEA:Ensembl.
DR   GO; GO:0046329; P:negative regulation of JNK cascade; IEA:Ensembl.
DR   GO; GO:0034140; P:negative regulation of toll-like receptor 3 signaling pathway; IEA:Ensembl.
DR   GO; GO:0010804; P:negative regulation of tumor necrosis factor-mediated signaling pathway; IEA:Ensembl.
DR   GO; GO:0042119; P:neutrophil activation; IEA:Ensembl.
DR   GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0030836; P:positive regulation of actin filament depolymerization; IEA:Ensembl.
DR   GO; GO:0043123; P:positive regulation of canonical NF-kappaB signal transduction; IEA:Ensembl.
DR   GO; GO:0030335; P:positive regulation of cell migration; ISS:UniProtKB.
DR   GO; GO:0032722; P:positive regulation of chemokine production; ISS:UniProtKB.
DR   GO; GO:0050921; P:positive regulation of chemotaxis; ISS:UniProtKB.
DR   GO; GO:0002720; P:positive regulation of cytokine production involved in immune response; IEA:Ensembl.
DR   GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISS:UniProtKB.
DR   GO; GO:0043311; P:positive regulation of eosinophil degranulation; IEA:Ensembl.
DR   GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
DR   GO; GO:0032731; P:positive regulation of interleukin-1 beta production; IEA:Ensembl.
DR   GO; GO:0032733; P:positive regulation of interleukin-10 production; IEA:Ensembl.
DR   GO; GO:0032755; P:positive regulation of interleukin-6 production; IEA:Ensembl.
DR   GO; GO:0032757; P:positive regulation of interleukin-8 production; IEA:Ensembl.
DR   GO; GO:0046330; P:positive regulation of JNK cascade; IEA:Ensembl.
DR   GO; GO:0002690; P:positive regulation of leukocyte chemotaxis; IEA:Ensembl.
DR   GO; GO:0070963; P:positive regulation of neutrophil mediated killing of gram-negative bacterium; IEA:Ensembl.
DR   GO; GO:0060100; P:positive regulation of phagocytosis, engulfment; IEA:Ensembl.
DR   GO; GO:0051897; P:positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; ISS:UniProtKB.
DR   GO; GO:0050927; P:positive regulation of positive chemotaxis; IEA:Ensembl.
DR   GO; GO:0031274; P:positive regulation of pseudopodium assembly; ISS:UniProtKB.
DR   GO; GO:1900135; P:positive regulation of renin secretion into blood stream; ISS:UniProtKB.
DR   GO; GO:0035025; P:positive regulation of Rho protein signal transduction; ISS:UniProtKB.
DR   GO; GO:0032930; P:positive regulation of superoxide anion generation; IEA:Ensembl.
DR   GO; GO:0034137; P:positive regulation of toll-like receptor 2 signaling pathway; IEA:Ensembl.
DR   GO; GO:0034141; P:positive regulation of toll-like receptor 3 signaling pathway; IEA:Ensembl.
DR   GO; GO:0034145; P:positive regulation of toll-like receptor 4 signaling pathway; IEA:Ensembl.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR   GO; GO:0032729; P:positive regulation of type II interferon production; ISS:UniProtKB.
DR   GO; GO:0045907; P:positive regulation of vasoconstriction; IMP:AgBase.
DR   GO; GO:0099109; P:potassium channel activating, G protein-coupled receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0030193; P:regulation of blood coagulation; IEA:Ensembl.
DR   GO; GO:2000341; P:regulation of chemokine (C-X-C motif) ligand 2 production; IEA:Ensembl.
DR   GO; GO:0002286; P:T cell activation involved in immune response; ISS:UniProtKB.
DR   GO; GO:0042311; P:vasodilation; ISS:UniProtKB.
DR   CDD; cd15370; 7tmA_PAR2; 1.
DR   Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   InterPro; IPR002281; Pro_rcpt_2.
DR   InterPro; IPR003912; Protea_act_rcpt.
DR   PANTHER; PTHR24232; G-PROTEIN COUPLED RECEPTOR; 1.
DR   PANTHER; PTHR24232:SF21; PROTEINASE-ACTIVATED RECEPTOR 2; 1.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR01428; PROTEASEAR.
DR   PRINTS; PR01152; PROTEASEAR2.
DR   SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW   ECO:0000256|PIRSR:PIRSR603912-52};
KW   G-protein coupled receptor {ECO:0000256|ARBA:ARBA00023040};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Receptor {ECO:0000313|EMBL:HDA47695.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008227};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transducer {ECO:0000256|ARBA:ARBA00023040};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..397
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5041197108"
FT   TRANSMEM        76..101
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        110..130
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        150..169
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        190..211
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        242..264
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        285..313
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        325..347
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          92..344
FT                   /note="G-protein coupled receptors family 1 profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50262"
FT   DISULFID        148..226
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603912-52"
SQ   SEQUENCE   397 AA;  44113 MW;  84E72D4322010AA8 CRC64;
     MRSLSAGWLL GGVILLAASV SCNRTVLGTS RPSKGRSLIG KADNTPPITG KGATVEPGFS
     VDEFSASVLT GKLTTVFLPV VYTIVFVVGL PSNGMALWVF LFRTKKKHPA VIYMANLALA
     DLLSVIWFPL KIAYHIHGNN WVYGESLCKV LIGFFYGNMY CSILFMTCLS VQRYWVIVNP
     MVHPRKKANV AIGVSLGIWL LILLVTIPLY VVKQTLYIPA LHITTCHDVL PEEVLVGDMF
     NYFLSLAIGV FLFPAFLTAA AYVLMIRTLR SSAMDENSGK KRQRAIKLII TVLAMYLICF
     TPSNLLLVVH YFLIKTWGQS HVYALYIVAL CLSTLNSCID PFVYYFISKD FRDHAKNALL
     CRSVRTVKQM QVSLSSTKFS RKSSSYSSSS TSVKTSY
//
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