FPRP_RAT
ID FPRP_RAT Reviewed; 879 AA.
AC Q62786;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Prostaglandin F2 receptor negative regulator;
DE AltName: Full=CD9 partner 1;
DE Short=CD9P-1;
DE AltName: Full=Glu-Trp-Ile EWI motif-containing protein F;
DE Short=EWI-F;
DE AltName: Full=Prostaglandin F2-alpha receptor regulatory protein;
DE AltName: Full=Prostaglandin F2-alpha receptor-associated protein;
DE AltName: CD_antigen=CD315;
DE Flags: Precursor;
GN Name=Ptgfrn; Synonyms=Fprp;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Ovary;
RX PubMed=8951995; DOI=10.1016/s0952-3278(96)90007-1;
RA Orlicky D.J., Nordeen S.K.;
RT "Cloning, sequencing and proposed structure for a prostaglandin F2 alpha
RT receptor regulatory protein.";
RL Prostaglandins Leukot. Essent. Fatty Acids 55:261-268(1996).
RN [2]
RP CHARACTERIZATION.
RC STRAIN=Sprague-Dawley; TISSUE=Ovary;
RX PubMed=8804121; DOI=10.1016/s0952-3278(96)90055-1;
RA Orlicky D.J.;
RT "Negative regulatory activity of a prostaglandin F2 alpha receptor
RT associated protein (FPRP).";
RL Prostaglandins Leukot. Essent. Fatty Acids 54:247-259(1996).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-271, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT regulation of aquaporin-2 phosphorylation at two sites.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
CC -!- FUNCTION: Inhibits the binding of prostaglandin F2-alpha (PGF2-alpha)
CC to its specific FP receptor, by decreasing the receptor number rather
CC than the affinity constant. Functional coupling with the prostaglandin
CC F2-alpha receptor seems to occur (By similarity). In myoblasts,
CC associates with tetraspanins CD9 and CD81 to prevent myotube fusion
CC during muscle regeneration (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:Q9WV91}.
CC -!- SUBUNIT: Interacts with CD9 and CD81 (By similarity). Part of a complex
CC composed of CD9, CD81 and IGSF8 (By similarity). Also seems to interact
CC with CD63, CD82 and CD151 (By similarity).
CC {ECO:0000250|UniProtKB:Q9P2B2, ECO:0000250|UniProtKB:Q9WV91}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type
CC I membrane protein. Golgi apparatus, trans-Golgi network membrane;
CC Single-pass type I membrane protein.
CC -!- TISSUE SPECIFICITY: Reproductive tissues, lung and heart.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U26595; AAC18426.1; -; mRNA.
DR RefSeq; NP_062116.1; NM_019243.1.
DR AlphaFoldDB; Q62786; -.
DR IntAct; Q62786; 1.
DR STRING; 10116.ENSRNOP00000021162; -.
DR GlyGen; Q62786; 8 sites.
DR iPTMnet; Q62786; -.
DR PhosphoSitePlus; Q62786; -.
DR SwissPalm; Q62786; -.
DR jPOST; Q62786; -.
DR PaxDb; Q62786; -.
DR PRIDE; Q62786; -.
DR GeneID; 29602; -.
DR KEGG; rno:29602; -.
DR UCSC; RGD:3437; rat.
DR CTD; 5738; -.
DR RGD; 3437; Ptgfrn.
DR eggNOG; ENOG502QVD2; Eukaryota.
DR InParanoid; Q62786; -.
DR OrthoDB; 151148at2759; -.
DR PhylomeDB; Q62786; -.
DR PRO; PR:Q62786; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0034389; P:lipid droplet organization; ISO:RGD.
DR GO; GO:0014905; P:myoblast fusion involved in skeletal muscle regeneration; ISS:UniProtKB.
DR GO; GO:0017148; P:negative regulation of translation; NAS:UniProtKB.
DR Gene3D; 2.60.40.10; -; 5.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR013106; Ig_V-set.
DR Pfam; PF07686; V-set; 2.
DR SMART; SM00409; IG; 6.
DR SMART; SM00406; IGv; 3.
DR SUPFAM; SSF48726; SSF48726; 5.
DR PROSITE; PS50835; IG_LIKE; 5.
PE 1: Evidence at protein level;
KW Disulfide bond; Endoplasmic reticulum; Glycoprotein; Golgi apparatus;
KW Immunoglobulin domain; Membrane; Phosphoprotein; Reference proteome;
KW Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..879
FT /note="Prostaglandin F2 receptor negative regulator"
FT /id="PRO_0000014764"
FT TOPO_DOM 22..832
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 833..853
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 854..879
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 22..129
FT /note="Ig-like C2-type 1"
FT DOMAIN 149..268
FT /note="Ig-like C2-type 2"
FT DOMAIN 276..389
FT /note="Ig-like C2-type 3"
FT DOMAIN 406..527
FT /note="Ig-like C2-type 4"
FT DOMAIN 544..662
FT /note="Ig-like C2-type 5"
FT DOMAIN 688..813
FT /note="Ig-like C2-type 6"
FT MOTIF 89..91
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT MOTIF 424..427
FT /note="Endoplasmic reticulum retention signal"
FT MOTIF 703..705
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT MOD_RES 271
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16641100"
FT CARBOHYD 44
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 300
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 383
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 413
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 525
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 600
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 618
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 691
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 43..119
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 169..247
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 299..373
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 429..515
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 571..655
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 711..793
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VARIANT 47
FT /note="D -> G"
FT VARIANT 136
FT /note="M -> V"
FT VARIANT 782
FT /note="S -> G"
FT VARIANT 844
FT /note="G -> R"
SQ SEQUENCE 879 AA; 98731 MW; DE7012D3B346C0F7 CRC64;
MGRPAPRPLL LALLSLAVCR GRVVRVPAGT LVRVVGTELV IPCNVSDYDG PSEQNFDWSF
SSSGSSFVEL ASTWEVGFPA QQYRERLQRG DILLRRTAND AVELHIKNVQ PSDQGHYKCS
TPSTDATVQG NYEDTMQVKV LADALVVGPS SRPPPGLSLR EGEPFELRCI ASTTSPLHTH
LALRWELHRG PVHRSILALS HEGRFHPGPG YEQRYHSGDV RLDTVGSDAY RLSVARALSA
DQGSYRCVVS EWITEQGSWQ EIQEKAVEVA TVVIQPTALQ LAVPRTVSVT EGKDLDLSCN
ITTDRVDDVR PEVTWYFKKT PDTSLLASHM LARLDRDSLV HSSPHVALSH VDTRSYHLLV
RDVSKENSGY YLCLVALWAP GHNRSWHKVA EAMSAPSGVS VTWLEPEYQV YLNASKVPGF
SDDPTELQCR VIDTKRVDAG VRLTVSWYYR MNRRNDDVVA SELLAVMDGD WTLRYGERSK
QRAQDGEFIF SKEHTDTFSF RIQRTTEEDR GSYYCVVSAW TRQRNSSWVK SKDVFSKPVN
IFWASEDSVL VVKARQPKPF FAAGNTFEMT CKVSSKNIKS PRYSVLITAE KPVGDLSSPN
ETKYIISLDQ DSVVKLENWT DASRVDGVVL EKVQEDEFRY RMYQTQVSDA GLYRCMVTAW
SPIGGSLWRE AATSLSNPIE IDFQTSGPIF NASVHSDTLS VTRGDLIKLF CIVTVDGAVL
DPDDMAFDVS WFAVHSFGLD KAPILLSSLD RKGVVTTGQR DWKSTVSLER VSVLEFLLQV
HSSEDQDFGN YYCSVTPWVR SPTGSWQREA EIHSRPIFIT VKMDVLNAFK YPLLIGVGLS
TVIGLLSCLI GYCSSHWCCK KEVRETRRER RRLMSMEMD
