ID   FPRP_MOUSE              Reviewed;         879 AA.
AC   Q9WV91; Q5SRA8;
DT   01-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   27-MAR-2024, entry version 167.
DE   RecName: Full=Prostaglandin F2 receptor negative regulator;
DE   AltName: Full=CD9 partner 1;
DE            Short=CD9P-1 {ECO:0000303|PubMed:23575678};
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   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=10893677; DOI=10.1359/jbmr.2000.15.7.1286;
RA   Weng L., Falla N., Van den Heuvel R., Raymackers J., Karperien M.,
RA   Van Bezooijen R., Van Vlasselaer P., Lowik C., Merregaert J.;
RT   "The monoclonal antibodies 18d7/91f2 recognize a receptor regulatory
RT   protein on mouse bone marrow stromal cells.";
RL   J. Bone Miner. Res. 15:1286-1300(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-600 AND ASN-618.
RC   TISSUE=Myoblast;
RX   PubMed=19656770; DOI=10.1074/mcp.m900195-mcp200;
RA   Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D.,
RA   Elliott S.T., Boheler K.R., Van Eyk J.E., Wollscheid B.;
RT   "The mouse C2C12 myoblast cell surface N-linked glycoproteome:
RT   identification, glycosite occupancy, and membrane orientation.";
RL   Mol. Cell. Proteomics 8:2555-2569(2009).
RN   [5]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-300; ASN-600; ASN-618 AND
RP   ASN-691.
RX   PubMed=19349973; DOI=10.1038/nbt.1532;
RA   Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA   Schiess R., Aebersold R., Watts J.D.;
RT   "Mass-spectrometric identification and relative quantification of N-linked
RT   cell surface glycoproteins.";
RL   Nat. Biotechnol. 27:378-386(2009).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Heart, Kidney, Liver, Lung, and Pancreas;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [7]
RP   FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH CD81, INTERACTION WITH CD9,
RP   AND INTERACTION WITH IGSF8.
RX   PubMed=23575678; DOI=10.1038/ncomms2675;
RA   Charrin S., Latil M., Soave S., Polesskaya A., Chretien F., Boucheix C.,
RA   Rubinstein E.;
RT   "Normal muscle regeneration requires tight control of muscle cell fusion by
RT   tetraspanins CD9 and CD81.";
RL   Nat. Commun. 4:1674-1674(2013).
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. {ECO:0000250, ECO:0000269|PubMed:23575678}.
CC   -!- SUBUNIT: Interacts with CD9 and CD81 (By similarity). Part of a complex
CC       composed of CD9, CD81 and IGSF8 (PubMed:23575678). Also seems to
CC       interact with CD63, CD82 and CD151 (By similarity).
CC       {ECO:0000250|UniProtKB:Q9P2B2, ECO:0000269|PubMed:23575678}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC       Single-pass type I membrane protein {ECO:0000250}. Golgi apparatus,
CC       trans-Golgi network membrane {ECO:0000250}; Single-pass type I membrane
CC       protein {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed in myoblasts (at protein level).
CC       {ECO:0000269|PubMed:23575678}.
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; AF152344; AAD38383.1; -; mRNA.
DR   EMBL; AL645930; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL669872; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL669937; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL672281; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC145713; AAI45714.1; -; mRNA.
DR   EMBL; BC145715; AAI45716.1; -; mRNA.
DR   CCDS; CCDS17680.1; -.
DR   RefSeq; NP_035327.2; NM_011197.3.
DR   AlphaFoldDB; Q9WV91; -.
DR   BioGRID; 202459; 2.
DR   STRING; 10090.ENSMUSP00000099755; -.
DR   GlyConnect; 2616; 1 N-Linked glycan (2 sites).
DR   GlyCosmos; Q9WV91; 8 sites, 1 glycan.
DR   GlyGen; Q9WV91; 9 sites, 2 N-linked glycans (2 sites), 1 O-linked glycan (1 site).
DR   iPTMnet; Q9WV91; -.
DR   PhosphoSitePlus; Q9WV91; -.
DR   SwissPalm; Q9WV91; -.
DR   MaxQB; Q9WV91; -.
DR   PaxDb; 10090-ENSMUSP00000099755; -.
DR   ProteomicsDB; 271798; -.
DR   Pumba; Q9WV91; -.
DR   Antibodypedia; 2447; 158 antibodies from 27 providers.
DR   DNASU; 19221; -.
DR   Ensembl; ENSMUST00000102694.4; ENSMUSP00000099755.4; ENSMUSG00000027864.10.
DR   GeneID; 19221; -.
DR   KEGG; mmu:19221; -.
DR   UCSC; uc008qre.1; mouse.
DR   AGR; MGI:1277114; -.
DR   CTD; 5738; -.
DR   MGI; MGI:1277114; Ptgfrn.
DR   VEuPathDB; HostDB:ENSMUSG00000027864; -.
DR   eggNOG; ENOG502QVD2; Eukaryota.
DR   GeneTree; ENSGT00940000158367; -.
DR   HOGENOM; CLU_005187_1_0_1; -.
DR   InParanoid; Q9WV91; -.
DR   OMA; KPVSIFW; -.
DR   OrthoDB; 4103343at2759; -.
DR   PhylomeDB; Q9WV91; -.
DR   TreeFam; TF332702; -.
DR   BioGRID-ORCS; 19221; 4 hits in 79 CRISPR screens.
DR   ChiTaRS; Ptgfrn; mouse.
DR   PRO; PR:Q9WV91; -.
DR   Proteomes; UP000000589; Chromosome 3.
DR   RNAct; Q9WV91; Protein.
DR   Bgee; ENSMUSG00000027864; Expressed in umbilical cord and 224 other cell types or tissues.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0034389; P:lipid droplet organization; IMP:MGI.
DR   GO; GO:0014905; P:myoblast fusion involved in skeletal muscle regeneration; IMP:UniProtKB.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 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   PANTHER; PTHR12207:SF3; PROSTAGLANDIN F2 RECEPTOR NEGATIVE REGULATOR; 1.
DR   PANTHER; PTHR12207; V-SET AND TRANSMEMBRANE DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF07686; V-set; 2.
DR   SMART; SM00409; IG; 6.
DR   SMART; SM00406; IGv; 3.
DR   SUPFAM; SSF48726; Immunoglobulin; 5.
DR   PROSITE; PS50835; IG_LIKE; 5.
DR   Genevisible; Q9WV91; MM.
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_0000014763"
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..137
FT                   /note="Ig-like C2-type 1"
FT   DOMAIN          149..263
FT                   /note="Ig-like C2-type 2"
FT   DOMAIN          276..389
FT                   /note="Ig-like C2-type 3"
FT   DOMAIN          406..536
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:0000250|UniProtKB:Q62786"
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:0000269|PubMed:19349973"
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:0000269|PubMed:19349973,
FT                   ECO:0000269|PubMed:19656770"
FT   CARBOHYD        618
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19349973,
FT                   ECO:0000269|PubMed:19656770"
FT   CARBOHYD        691
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19349973"
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   CONFLICT        128
FT                   /note="V -> A (in Ref. 1; AAD38383)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        136
FT                   /note="V -> M (in Ref. 1; AAD38383)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        267
FT                   /note="V -> E (in Ref. 1; AAD38383)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        500
FT                   /note="F -> L (in Ref. 1; AAD38383)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        521
FT                   /note="T -> A (in Ref. 1; AAD38383)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        647
FT                   /note="V -> D (in Ref. 1; AAD38383)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   879 AA;  98722 MW;  0E7037B9625B56A3 CRC64;
     MGRPAPRPLL LALLSLAVCR GRVVRVPAGT LVRVVGTELV IPCNVSDYDG PSEQNFDWSF
     SSSGSSFVEL ASTWEVGFPA QLYRERLQRG DILLRRTAND AVELHIKNVQ PSDQGHYKCS
     TPSTDATVQG NYEDTVQVKV 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 VIDTKRLEAG VRLTVSWYYR MTRRNDDVVA SELLAVMDGD WTLRYGERSK
     QRAQDGEFIF SKEHTDTFNF RIQRTTEEDR GNYYCVVSAW TRQRNNSWVK SKDVFSKPVN
     IFWASEDSVL VVKARQPKPF FAAGNTFEMT CKVSSKNIKS PRYSVLITAE KPVGDLSSPN
     ETKYIISLDQ DSVVKLENWT DASRVDGVVL EKVQEDEFRY RMYQTQVSDA GLYRCMVTAW
     SPIGGSLWRE AATSLSNPIE IDFQTSGPTF NASVHSDTPS VTRGDLIKLF CIVTVEGAVL
     DPDDMAFDVS WFAVHSFGLD KAPVLLSSLD RKGVVTTGQR DWKSTVSLER VSVLEFLLQV
     HGSEDQDFGN YYCSVTPWVR SPTGSWQREA EIHSRPIFIT VKMDVLNAFK YPLLIGVGLS
     TVIGLLSCLI GYCSSHWCCK KEVRETRRER RRLMSMEMD
//