LOCUS       NP_062116                879 aa            linear   ROD 31-MAR-2024
DEFINITION  prostaglandin F2 receptor negative regulator precursor [Rattus
            norvegicus].
ACCESSION   NP_062116 XP_346637
VERSION     NP_062116.2
DBSOURCE    REFSEQ: accession NM_019243.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 879)
  AUTHORS   Charrin,S., Latil,M., Soave,S., Polesskaya,A., Chretien,F.,
            Boucheix,C. and Rubinstein,E.
  TITLE     Normal muscle regeneration requires tight control of muscle cell
            fusion by tetraspanins CD9 and CD81
  JOURNAL   Nat Commun 4, 1674 (2013)
   PUBMED   23575678
REFERENCE   2  (residues 1 to 879)
  AUTHORS   Teckchandani,A., Toida,N., Goodchild,J., Henderson,C., Watts,J.,
            Wollscheid,B. and Cooper,J.A.
  TITLE     Quantitative proteomics identifies a Dab2/integrin module
            regulating cell migration
  JOURNAL   J Cell Biol 186 (1), 99-111 (2009)
   PUBMED   19581412
REFERENCE   3  (residues 1 to 879)
  AUTHORS   Charrin,S., Le Naour,F., Oualid,M., Billard,M., Faure,G.,
            Hanash,S.M., Boucheix,C. and Rubinstein,E.
  TITLE     The major CD9 and CD81 molecular partner. Identification and
            characterization of the complexes
  JOURNAL   J Biol Chem 276 (17), 14329-14337 (2001)
   PUBMED   11278880
REFERENCE   4  (residues 1 to 879)
  AUTHORS   Orlicky,D.J., Lieber,J.G., Morin,C.L. and Evans,R.M.
  TITLE     Synthesis and accumulation of a receptor regulatory protein
            associated with lipid droplet accumulation in 3T3-L1 cells
  JOURNAL   J Lipid Res 39 (6), 1152-1161 (1998)
   PUBMED   9643346
REFERENCE   5  (residues 1 to 879)
  AUTHORS   Orlicky,D.J. and Nordeen,S.K.
  TITLE     Cloning, sequencing and proposed structure for a prostaglandin F2
            alpha receptor regulatory protein
  JOURNAL   Prostaglandins Leukot Essent Fatty Acids 55 (4), 261-268 (1996)
   PUBMED   8951995
REFERENCE   6  (residues 1 to 879)
  AUTHORS   Orlicky,D.J., Berry,R. and Sikela,J.M.
  TITLE     Human chromosome 1 localization of the gene for a prostaglandin
            F2alpha receptor negative regulatory protein
  JOURNAL   Hum Genet 97 (5), 655-658 (1996)
   PUBMED   8655148
REFERENCE   7  (residues 1 to 879)
  AUTHORS   Fekkes,D., Bode,W.T., Zijlstra,F.J. and Pepplinkhuizen,L.
  TITLE     Eicosanoid and amino acid metabolism in transient acute psychoses
            with psychedelic symptoms
  JOURNAL   Prostaglandins Leukot Essent Fatty Acids 54 (4), 261-264 (1996)
   PUBMED   8804122
REFERENCE   8  (residues 1 to 879)
  AUTHORS   Orlicky,D.J.
  TITLE     Negative regulatory activity of a prostaglandin F2 alpha receptor
            associated protein (FPRP)
  JOURNAL   Prostaglandins Leukot Essent Fatty Acids 54 (4), 247-259 (1996)
   PUBMED   8804121
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000002.1.
            
            On Nov 26, 2020 this sequence version replaced NP_062116.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U26595.1, SRR26643298.12598.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760400,
                                           SAMN12840107 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..879
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q34"
     Protein         1..879
                     /product="prostaglandin F2 receptor negative regulator
                     precursor"
                     /note="prostaglandin F2-alpha receptor regulatory protein;
                     prostaglandin F2-alpha receptor-associated protein;
                     prostaglandin F2 receptor negative regulator; CD9 partner
                     1; glu-Trp-Ile EWI motif-containing protein F"
                     /calculated_mol_wt=96482
     sig_peptide     1..21
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2205
     mat_peptide     22..879
                     /product="Prostaglandin F2 receptor negative regulator.
                     /id=PRO_0000014764"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62786.1)"
                     /calculated_mol_wt=96482
     Region          39..121
                     /region_name="IGv"
                     /note="Immunoglobulin V-Type; smart00406"
                     /db_xref="CDD:214650"
     Site            44
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q62786.1)"
     Region          89..91
                     /region_name="Cell attachment site. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62786.1)"
     Region          102..106
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409378"
     Region          <104..140
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          116..121
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409512"
     Region          134..137
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409512"
     Region          153..254
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          165..169
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409355"
     Region          182..186
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409355"
     Region          230..234
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409355"
     Region          244..249
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409355"
     Site            271
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:16641100; propagated from
                     UniProtKB/Swiss-Prot (Q62786.1)"
     Region          283..373
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Site            300
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q62786.1)"
     Site            383
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q62786.1)"
     Site            413
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q62786.1)"
     Region          423..520
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          424..427
                     /region_name="Endoplasmic reticulum retention signal"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62786.1)"
     Region          425..429
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409355"
     Region          439..448
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409355"
     Region          498..502
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409355"
     Region          512..517
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409355"
     Site            525
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q62786.1)"
     Site            600
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q62786.1)"
     Site            618
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q62786.1)"
     Site            691
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q62786.1)"
     Region          703..705
                     /region_name="Cell attachment site. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62786.1)"
     Site            833..853
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62786.1)"
     CDS             1..879
                     /gene="Ptgfrn"
                     /gene_synonym="CD9P-1; EWI-F"
                     /coded_by="NM_019243.2:39..2678"
                     /db_xref="GeneID:29602"
                     /db_xref="RGD:3437"
ORIGIN      
        1 mgrpaprpll lallslavcr grvvrvpagt lvrvvgtelv ipcnvsdydg pseqnfdwsf
       61 sssgssfvel astwevgfpa qqyrerlqrg dillrrtand avelhiknvq psdqghykcs
      121 tpstdatvqg nyedtvqvkv ladalvvgps srpppglslr egepfelrci asttsplhth
      181 lalrwelhrg pvhrsilals hegrfhpgpg yeqryhsgdv rldtvgsday rlsvaralsa
      241 dqgsyrcvvs ewiteqgswq eiqekaveva tvviqptalq lavprtvsvt egkdldlscn
      301 ittdrvddvr pevtwyfkkt pdtsllashm larldrdslv hssphvalsh vdtrsyhllv
      361 rdvskensgy ylclvalwap ghnrswhkva eamsapsgvs vtwlepeyqv ylnaskvpgf
      421 sddptelqcr vidtkrvdag vrltvswyyr mnrrnddvva sellavmdgd wtlrygersk
      481 qraqdgefif skehtdtfsf riqrtteedr gsyycvvsaw trqrnsswvk skdvfskpvn
      541 ifwasedsvl vvkarqpkpf faagntfemt ckvsskniks prysvlitae kpvgdlsspn
      601 etkyiisldq dsvvklenwt dasrvdgvvl ekvqedefry rmyqtqvsda glyrcmvtaw
      661 spiggslwre aatslsnpie idfqtsgpif nasvhsdtls vtrgdliklf civtvdgavl
      721 dpddmafdvs wfavhsfgld kapillssld rkgvvttgqr dwkstvsler vsvlefllqv
      781 hgsedqdfgn yycsvtpwvr sptgswqrea eihsrpifit vkmdvlnafk yplligvgls
      841 tvigllscli gycsshwcck kevretrrer rrlmsmemd
//
