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Q9WV91 (FPRP_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 110. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Prostaglandin F2 receptor negative regulator
Alternative name(s):
Prostaglandin F2-alpha receptor regulatory protein
Prostaglandin F2-alpha receptor-associated protein
CD_antigen=CD315
Gene names
Name:Ptgfrn
Synonyms:Fprp
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length879 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Inhibits the binding of prostaglandin F2-alpha (PGF2-alpha) to its specific FP receptor, by decreasing the receptor number rather than the affinity constant. Functional coupling with the prostaglandin F2-alpha receptor seems to occur By similarity.

Subunit structure

Interacts with CD9 and CD81. Also seems to interact with CD63, CD82 and CD151 By similarity.

Subcellular location

Endoplasmic reticulum membrane; Single-pass type I membrane protein By similarity. Golgi apparatustrans-Golgi network membrane; Single-pass type I membrane protein By similarity.

Sequence similarities

Contains 6 Ig-like C2-type (immunoglobulin-like) domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Potential
Chain22 – 879858Prostaglandin F2 receptor negative regulator
PRO_0000014763

Regions

Topological domain22 – 832811Extracellular Potential
Transmembrane833 – 85321Helical; Potential
Topological domain854 – 87926Cytoplasmic Potential
Domain22 – 137116Ig-like C2-type 1
Domain149 – 263115Ig-like C2-type 2
Domain276 – 389114Ig-like C2-type 3
Domain406 – 536131Ig-like C2-type 4
Domain544 – 662119Ig-like C2-type 5
Domain688 – 813126Ig-like C2-type 6
Motif89 – 913Cell attachment site Potential
Motif424 – 4274Endoplasmic reticulum retention signal
Motif703 – 7053Cell attachment site Potential

Amino acid modifications

Modified residue2711Phosphothreonine By similarity
Glycosylation441N-linked (GlcNAc...) Potential
Glycosylation3001N-linked (GlcNAc...) Ref.5
Glycosylation3831N-linked (GlcNAc...) Potential
Glycosylation4131N-linked (GlcNAc...) Potential
Glycosylation5251N-linked (GlcNAc...) Potential
Glycosylation6001N-linked (GlcNAc...) Ref.4 Ref.5
Glycosylation6181N-linked (GlcNAc...) Ref.4 Ref.5
Glycosylation6911N-linked (GlcNAc...) Ref.5
Disulfide bond43 ↔ 119 By similarity
Disulfide bond169 ↔ 247 By similarity
Disulfide bond299 ↔ 373 By similarity
Disulfide bond429 ↔ 515 By similarity
Disulfide bond571 ↔ 655 By similarity
Disulfide bond711 ↔ 793 By similarity

Experimental info

Sequence conflict1281V → A in AAD38383. Ref.1
Sequence conflict1361V → M in AAD38383. Ref.1
Sequence conflict2671V → E in AAD38383. Ref.1
Sequence conflict5001F → L in AAD38383. Ref.1
Sequence conflict5211T → A in AAD38383. Ref.1
Sequence conflict6471V → D in AAD38383. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9WV91 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 0E7037B9625B56A3

FASTA87998,722
        10         20         30         40         50         60 
MGRPAPRPLL LALLSLAVCR GRVVRVPAGT LVRVVGTELV IPCNVSDYDG PSEQNFDWSF 

        70         80         90        100        110        120 
SSSGSSFVEL ASTWEVGFPA QLYRERLQRG DILLRRTAND AVELHIKNVQ PSDQGHYKCS 

       130        140        150        160        170        180 
TPSTDATVQG NYEDTVQVKV LADALVVGPS SRPPPGLSLR EGEPFELRCI ASTTSPLHTH 

       190        200        210        220        230        240 
LALRWELHRG PVHRSILALS HEGRFHPGPG YEQRYHSGDV RLDTVGSDAY RLSVARALSA 

       250        260        270        280        290        300 
DQGSYRCVVS EWITEQGSWQ EIQEKAVEVA TVVIQPTALQ LAVPRTVSVT EGKDLDLSCN 

       310        320        330        340        350        360 
ITTDRVDDVR PEVTWYFKKT PDTSLLASHM LARLDRDSLV HSSPHVALSH VDTRSYHLLV 

       370        380        390        400        410        420 
RDVSKENSGY YLCLVALWAP GHNRSWHKVA EAMSAPSGVS VTWLEPEYQV YLNASKVPGF 

       430        440        450        460        470        480 
SDDPTELQCR VIDTKRLEAG VRLTVSWYYR MTRRNDDVVA SELLAVMDGD WTLRYGERSK 

       490        500        510        520        530        540 
QRAQDGEFIF SKEHTDTFNF RIQRTTEEDR GNYYCVVSAW TRQRNNSWVK SKDVFSKPVN 

       550        560        570        580        590        600 
IFWASEDSVL VVKARQPKPF FAAGNTFEMT CKVSSKNIKS PRYSVLITAE KPVGDLSSPN 

       610        620        630        640        650        660 
ETKYIISLDQ DSVVKLENWT DASRVDGVVL EKVQEDEFRY RMYQTQVSDA GLYRCMVTAW 

       670        680        690        700        710        720 
SPIGGSLWRE AATSLSNPIE IDFQTSGPTF NASVHSDTPS VTRGDLIKLF CIVTVEGAVL 

       730        740        750        760        770        780 
DPDDMAFDVS WFAVHSFGLD KAPVLLSSLD RKGVVTTGQR DWKSTVSLER VSVLEFLLQV 

       790        800        810        820        830        840 
HGSEDQDFGN YYCSVTPWVR SPTGSWQREA EIHSRPIFIT VKMDVLNAFK YPLLIGVGLS 

       850        860        870 
TVIGLLSCLI GYCSSHWCCK KEVRETRRER RRLMSMEMD 

« Hide

References

« Hide 'large scale' references
[1]"The monoclonal antibodies 18d7/91f2 recognize a receptor regulatory protein on mouse bone marrow stromal cells."
Weng L., Falla N., Van den Heuvel R., Raymackers J., Karperien M., Van Bezooijen R., Van Vlasselaer P., Lowik C., Merregaert J.
J. Bone Miner. Res. 15:1286-1300(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[4]"The mouse C2C12 myoblast cell surface N-linked glycoproteome: identification, glycosite occupancy, and membrane orientation."
Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E., Wollscheid B.
Mol. Cell. Proteomics 8:2555-2569(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-600 AND ASN-618.
Tissue: Myoblast.
[5]"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-300; ASN-600; ASN-618 AND ASN-691.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF152344 mRNA. Translation: AAD38383.1.
AL672281, AL669937 Genomic DNA. Translation: CAI26220.1.
AL669937, AL672281 Genomic DNA. Translation: CAI26224.1.
AL669872, AL645930 Genomic DNA. Translation: CAM22064.1.
BC145713 mRNA. Translation: AAI45714.1.
BC145715 mRNA. Translation: AAI45716.1.
CCDSCCDS17680.1.
RefSeqNP_035327.2. NM_011197.3.
UniGeneMm.24807.

3D structure databases

ProteinModelPortalQ9WV91.
SMRQ9WV91. Positions 101-126.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ9WV91. 1 interaction.
MINTMINT-4095317.
STRING10090.ENSMUSP00000099755.

PTM databases

PhosphoSiteQ9WV91.

Proteomic databases

PaxDbQ9WV91.
PRIDEQ9WV91.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000102694; ENSMUSP00000099755; ENSMUSG00000027864.
GeneID19221.
KEGGmmu:19221.
UCSCuc008qre.1. mouse.

Organism-specific databases

CTD5738.
MGIMGI:1277114. Ptgfrn.

Phylogenomic databases

eggNOGNOG39204.
GeneTreeENSGT00390000010278.
HOGENOMHOG000112641.
HOVERGENHBG031554.
InParanoidQ5SRA8.
KOK06729.
OMAWKSDLSL.
OrthoDBEOG7RNJZG.
TreeFamTF332702.

Gene expression databases

ArrayExpressQ9WV91.
BgeeQ9WV91.
CleanExMM_PTGFRN.
GenevestigatorQ9WV91.

Family and domain databases

Gene3D2.60.40.10. 5 hits.
InterProIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR013106. Ig_V-set.
IPR003596. Ig_V-set_subgr.
[Graphical view]
PfamPF07686. V-set. 3 hits.
[Graphical view]
SMARTSM00409. IG. 5 hits.
SM00406. IGv. 1 hit.
[Graphical view]
PROSITEPS50835. IG_LIKE. 5 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio295996.
PROQ9WV91.
SOURCESearch...

Entry information

Entry nameFPRP_MOUSE
AccessionPrimary (citable) accession number: Q9WV91
Secondary accession number(s): Q5SRA8
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 2003
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 110 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot