FPRP_MOUSE
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 03-AUG-2022, entry version 158.
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}.
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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; 1.
DR STRING; 10090.ENSMUSP00000099755; -.
DR GlyConnect; 2616; 1 N-Linked glycan (2 sites).
DR GlyGen; Q9WV91; 8 sites, 1 N-linked glycan (2 sites).
DR iPTMnet; Q9WV91; -.
DR PhosphoSitePlus; Q9WV91; -.
DR SwissPalm; Q9WV91; -.
DR MaxQB; Q9WV91; -.
DR PaxDb; Q9WV91; -.
DR PRIDE; Q9WV91; -.
DR ProteomicsDB; 271798; -.
DR Antibodypedia; 2447; 148 antibodies from 27 providers.
DR DNASU; 19221; -.
DR Ensembl; ENSMUST00000102694; ENSMUSP00000099755; ENSMUSG00000027864.
DR GeneID; 19221; -.
DR KEGG; mmu:19221; -.
DR UCSC; uc008qre.1; mouse.
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; GGGRWHM; -.
DR OrthoDB; 151148at2759; -.
DR PhylomeDB; Q9WV91; -.
DR TreeFam; TF332702; -.
DR BioGRID-ORCS; 19221; 3 hits in 74 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 222 other tissues.
DR Genevisible; Q9WV91; MM.
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; IMP:MGI.
DR GO; GO:0014905; P:myoblast fusion involved in skeletal muscle regeneration; IMP: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_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
