PTAFR_BOVIN
ID PTAFR_BOVIN Reviewed; 342 AA.
AC Q9TTY5; A7Z046;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 2.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Platelet-activating factor receptor;
DE Short=PAF-R;
DE Short=PAFr;
GN Name=PTAFR {ECO:0000250|UniProtKB:P25105}; Synonyms=PAFR;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1] {ECO:0000312|EMBL:AAF01439.2}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11916258; DOI=10.3109/10425170109024998;
RA Yang W., Diehl J.R., Roudebush W.E.;
RT "Comparison of the coding sequence of the platelet-activating factor
RT receptor gene in three species.";
RL DNA Seq. 12:239-251(2001).
RN [2] {ECO:0000312|EMBL:CAC43290.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA He B., Tiemann U., Kanitz W., Weikard R., Laurent P., Schwerin M.,
RA Schmidt P.;
RT "Molecular characterization of bovine platelet-actvating factor receptor
RT transcripts and their detection in different tissues of cattle.";
RL Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000312|EMBL:CAC43290.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000305}
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=11438398; DOI=10.1016/s0739-7240(01)00095-9;
RA Tiemann U., Viergutz T., Jonas L., Wollenhaupt K., Pohland R., Kanitz W.;
RT "Fluorometric detection of platelet activating factor receptor in cultured
RT oviductal epithelial and stromal cells and endometrial stromal cells from
RT bovine at different stages of the oestrous cycle and early pregnancy.";
RL Domest. Anim. Endocrinol. 20:149-164(2001).
RN [5] {ECO:0000305}
RP TISSUE SPECIFICITY.
RX PubMed=11403499; DOI=10.1016/s0090-6980(01)00130-7;
RA Tiemann U., Tomek W., Schneider F., Wollenhaupt K., Kanitz W., Becker F.,
RA Pohland R., Alm H.;
RT "Platelet-activating factor (PAF)-like activity, localization of PAF
RT receptor (PAF-R) and PAF-acetylhydrolase (PAF-AH) activity in bovine
RT endometrium at different stages of the estrous cycle and early pregnancy.";
RL Prostaglandins Other Lipid Mediat. 65:125-141(2001).
CC -!- FUNCTION: Receptor for platelet activating factor, a chemotactic
CC phospholipid mediator that possesses potent inflammatory, smooth-muscle
CC contractile and hypotensive activity. Seems to mediate its action via a
CC G protein that activates a phosphatidylinositol-calcium second
CC messenger system. May be involved in the morphological and physical
CC modifications of the oviduct and uterus during the estrus cycle and
CC early pregnancy (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with ARRB1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11438398};
CC Multi-pass membrane protein {ECO:0000269|PubMed:11438398}.
CC -!- TISSUE SPECIFICITY: Found in oviductal epithelial and stroma cells.
CC Levels in the oviduct are raised at days 2-4 of both pregnancy and of
CC the estrus cycle. In the endometrium, localization is predominantly to
CC the apical borders of glandular and luminal epithelial cells. Expressed
CC at lower levels in endometrial stromal cells. Levels in the endometrium
CC are increased at day 20 of pregnancy (at protein level).
CC {ECO:0000269|PubMed:11403499, ECO:0000269|PubMed:11438398}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AF187321; AAF01439.2; -; Genomic_DNA.
DR EMBL; AJ295321; CAC43290.1; -; Genomic_DNA.
DR EMBL; BC153244; AAI53245.1; -; mRNA.
DR RefSeq; NP_001035628.1; NM_001040538.1.
DR AlphaFoldDB; Q9TTY5; -.
DR SMR; Q9TTY5; -.
DR STRING; 9913.ENSBTAP00000038567; -.
DR PaxDb; Q9TTY5; -.
DR Ensembl; ENSBTAT00000038757; ENSBTAP00000038567; ENSBTAG00000027051.
DR GeneID; 518283; -.
DR KEGG; bta:518283; -.
DR CTD; 5724; -.
DR VEuPathDB; HostDB:ENSBTAG00000027051; -.
DR VGNC; VGNC:33488; PTAFR.
DR eggNOG; ENOG502QTQI; Eukaryota.
DR GeneTree; ENSGT01050000244845; -.
DR HOGENOM; CLU_009579_8_2_1; -.
DR InParanoid; Q9TTY5; -.
DR OMA; AIHVIIC; -.
DR OrthoDB; 800525at2759; -.
DR TreeFam; TF350009; -.
DR Reactome; R-BTA-373076; Class A/1 (Rhodopsin-like receptors).
DR Reactome; R-BTA-416476; G alpha (q) signalling events.
DR Reactome; R-BTA-6798695; Neutrophil degranulation.
DR Proteomes; UP000009136; Chromosome 2.
DR Bgee; ENSBTAG00000027051; Expressed in neutrophil and 98 other tissues.
DR GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0045028; F:G protein-coupled purinergic nucleotide receptor activity; IBA:GO_Central.
DR GO; GO:0001530; F:lipopolysaccharide binding; IEA:Ensembl.
DR GO; GO:0001875; F:lipopolysaccharide immune receptor activity; IEA:Ensembl.
DR GO; GO:0005543; F:phospholipid binding; IEA:Ensembl.
DR GO; GO:0004992; F:platelet activating factor receptor activity; IEA:Ensembl.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR GO; GO:0007565; P:female pregnancy; IEP:UniProtKB.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0006954; P:inflammatory response; IEA:Ensembl.
DR GO; GO:0032959; P:inositol trisphosphate biosynthetic process; IEA:Ensembl.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IEA:Ensembl.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR002282; PAF_rcpt.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR01153; PAFRECEPTOR.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Chemotaxis; Disulfide bond; G-protein coupled receptor;
KW Glycoprotein; Membrane; Pregnancy; Receptor; Reference proteome;
KW Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..342
FT /note="Platelet-activating factor receptor"
FT /id="PRO_0000070089"
FT TOPO_DOM 1..16
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 17..38
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 39..54
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 55..74
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 75..91
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 92..113
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 114..133
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 134..155
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 156..184
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 185..205
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 206..233
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 234..254
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 255..276
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 277..296
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 297..342
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 4
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 163
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 169
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 90..173
FT /evidence="ECO:0000250|UniProtKB:P25105,
FT ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 342 AA; 39691 MW; 7C4236205AE937C9 CRC64;
MEPNNSFRVD SEFRYTLFPI FYSIVFVLGV IANSYVLWVF ARLYPSKKFN EIKIFMVNLT
MADLLFLVTL PLWIVYYYNQ GDWILPKFLC NLAGCFFFIN TYCSVAFLAV ITYNRFQAVT
RPIKTAQATT RKRGILLSLI IWVSIVGAAS YFFVLDSTNR EPNKTGSANI TRCFEHYEKG
SIPVLTIHIF LVFSFFLVFL IILFCNLVII RTLLTQQVQI QRNAEVKRRA LWMVCTVLAV
FIICFVPHHL VQLPWTLAEL GFQDTDFHQA INDAHQVTLC LLSTNCVLDP IIYCFLTKKF
RKHLTEKLYS MRESRKCSRA TSETGTEVVM QLKDVPVKSL KY
