PTAFR_PIG
ID PTAFR_PIG Reviewed; 342 AA.
AC Q9XSD4;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 2.
DT 25-MAY-2022, entry version 82.
DE RecName: Full=Platelet-activating factor receptor;
DE Short=PAF-R;
DE Short=PAFr;
GN Name=PTAFR {ECO:0000250|UniProtKB:P25105}; Synonyms=PAFR;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1] {ECO:0000312|EMBL:AAD28739.2}
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:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Heart {ECO:0000269|PubMed:14703076};
RX PubMed=14703076; DOI=10.1081/abio-120026487;
RA Yang W., Diehl J.R., Roudebush W.E.;
RT "Organization of porcine platelet-activating factor receptor gene.";
RL Anim. Biotechnol. 14:177-181(2003).
RN [3] {ECO:0000305}
RP TISSUE SPECIFICITY.
RX PubMed=11943497; DOI=10.1016/s0378-4320(02)00019-2;
RA Yang W., Diehl J.R., Grapes L., Rothschild M.F., Roudebush W.E.;
RT "The pig platelet-activating factor receptor gene is expressed at the mRNA
RT level in different tissues and is mapped to chromosome 6.";
RL Anim. Reprod. Sci. 70:277-282(2002).
RN [4] {ECO:0000305}
RP TISSUE SPECIFICITY.
RX PubMed=12420294; DOI=10.1002/mrd.10217;
RA Yang W., Diehl J.R., Yerle M., Ford J.J., Christenson R.K., Roudebush W.E.,
RA Plummer W.E.;
RT "Chromosomal location, structure, and temporal expression of the platelet-
RT activating factor receptor (PAFr) gene in porcine endometrium and embryos
RT relative to estrogen receptor alpha gene expression.";
RL Mol. Reprod. Dev. 64:4-12(2003).
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 have a role in peri-implantation development
CC during pregnancy (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with ARRB1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Differentially expressed in the lung, heart, liver,
CC skeletal muscle, kidney, spleen, small intestine, endometrium and white
CC blood cells. Expression levels are higher in the endometrium of
CC pregnant compared to non-pregnant individuals. Endometrial and
CC embryonic expression levels increase from day 10 to day 16 of
CC pregnancy. {ECO:0000269|PubMed:11943497, ECO:0000269|PubMed:12420294,
CC ECO:0000269|PubMed:14703076}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AF124054; AAD28739.2; -; Genomic_DNA.
DR AlphaFoldDB; Q9XSD4; -.
DR SMR; Q9XSD4; -.
DR PRIDE; Q9XSD4; -.
DR InParanoid; Q9XSD4; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045028; F:G protein-coupled purinergic nucleotide receptor activity; IBA:GO_Central.
DR GO; GO:0004992; F:platelet activating factor receptor activity; IEA:InterPro.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Cell membrane; Chemotaxis; Disulfide bond; G-protein coupled receptor;
KW Glycoprotein; Membrane; Receptor; Reference proteome; Transducer;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..342
FT /note="Platelet-activating factor receptor"
FT /id="PRO_0000070095"
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 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; 39436 MW; 830EA7542B528DAC CRC64;
MEPNDSWRVD SEFRYTLFPI FYSIIFVLGV IANSYVLWVF ARVYPSKKLN EIKIFMLNLT
MADLLFLVTL PLWIIYYYHE GNWILPKFLC NLAGCFFFIN TYCSVSFLAV ITYNRFQAVT
RPIKTAQATT RKRGISLSLI IWVAMVAAAS YFFVLDSTNI ELSKTGAGNL TRCFEHYEKG
SMPVLIIHIF LVFSFFLVFL VILFCNLVII RTLLTQSVQM QRNAEVKRRA LWMVCTVLAV
FIICFVPHHI VQLPWTLAEL GFQSGNFHQA INDAHQITLC LLSTNCVLDP IIYCFLTKKF
RKHLSEKFYS LRGSRKCSRV TTETGTEVVV PLSQVPVNSL KK
