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Protein

Prostaglandin F2 receptor negative regulator

Gene

PTGFRN

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

GO - Biological processi

  1. lipid particle organization Source: Ensembl
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Prostaglandin F2 receptor negative regulator
Alternative name(s):
CD9 partner 1
Short name:
CD9P-1
Glu-Trp-Ile EWI motif-containing protein F
Short name:
EWI-F
Prostaglandin F2-alpha receptor regulatory protein
Prostaglandin F2-alpha receptor-associated protein
CD_antigen: CD315
Gene namesi
Name:PTGFRN
Synonyms:CD9P1, EWIF, FPRP, KIAA1436
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:9601. PTGFRN.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini26 – 832807ExtracellularSequence AnalysisAdd
BLAST
Transmembranei833 – 85321HelicalSequence AnalysisAdd
BLAST
Topological domaini854 – 87926CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. cell surface Source: UniProtKB
  2. endoplasmic reticulum membrane Source: UniProtKB-SubCell
  3. Golgi apparatus Source: UniProtKB-SubCell
  4. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Golgi apparatus, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33950.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2525Sequence AnalysisAdd
BLAST
Chaini26 – 879854Prostaglandin F2 receptor negative regulatorPRO_0000014762Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi43 ↔ 119PROSITE-ProRule annotation
Glycosylationi44 – 441N-linked (GlcNAc...)1 Publication
Disulfide bondi169 ↔ 247PROSITE-ProRule annotation
Modified residuei271 – 2711PhosphothreonineBy similarity
Glycosylationi286 – 2861N-linked (GlcNAc...)2 Publications
Disulfide bondi299 ↔ 373PROSITE-ProRule annotation
Glycosylationi300 – 3001N-linked (GlcNAc...)2 Publications
Glycosylationi383 – 3831N-linked (GlcNAc...)1 Publication
Glycosylationi413 – 4131N-linked (GlcNAc...)1 Publication
Disulfide bondi429 ↔ 515PROSITE-ProRule annotation
Glycosylationi525 – 5251N-linked (GlcNAc...)1 Publication
Disulfide bondi571 ↔ 655PROSITE-ProRule annotation
Glycosylationi600 – 6001N-linked (GlcNAc...)1 Publication
Glycosylationi618 – 6181N-linked (GlcNAc...)1 Publication
Glycosylationi691 – 6911N-linked (GlcNAc...)1 Publication
Disulfide bondi711 ↔ 793PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ9P2B2.
PaxDbiQ9P2B2.
PeptideAtlasiQ9P2B2.
PRIDEiQ9P2B2.

PTM databases

PhosphoSiteiQ9P2B2.

Expressioni

Gene expression databases

BgeeiQ9P2B2.
CleanExiHS_PTGFRN.
ExpressionAtlasiQ9P2B2. baseline and differential.
GenevestigatoriQ9P2B2.

Organism-specific databases

HPAiHPA017074.

Interactioni

Subunit structurei

Interacts with CD9 and CD81. Also seems to interact with CD63, CD82 and CD151.1 Publication

Protein-protein interaction databases

BioGridi111710. 14 interactions.
IntActiQ9P2B2. 1 interaction.
STRINGi9606.ENSP00000376899.

Structurei

3D structure databases

ProteinModelPortaliQ9P2B2.
SMRiQ9P2B2. Positions 98-124, 153-251.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini26 – 129104Ig-like C2-type 1Add
BLAST
Domaini149 – 268120Ig-like C2-type 2Add
BLAST
Domaini276 – 394119Ig-like C2-type 3Add
BLAST
Domaini406 – 536131Ig-like C2-type 4Add
BLAST
Domaini544 – 662119Ig-like C2-type 5Add
BLAST
Domaini688 – 813126Ig-like C2-type 6Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi424 – 4274Endoplasmic reticulum retention signal
Motifi703 – 7053Cell attachment siteSequence Analysis

Sequence similaritiesi

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG39204.
GeneTreeiENSGT00390000010278.
HOGENOMiHOG000112641.
HOVERGENiHBG031554.
InParanoidiQ9P2B2.
KOiK06729.
OMAiQTSGPIF.
OrthoDBiEOG7RNJZG.
PhylomeDBiQ9P2B2.
TreeFamiTF332702.

Family and domain databases

Gene3Di2.60.40.10. 5 hits.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR013106. Ig_V-set.
[Graphical view]
PfamiPF07686. V-set. 2 hits.
[Graphical view]
SMARTiSM00409. IG. 6 hits.
[Graphical view]
PROSITEiPS50835. IG_LIKE. 5 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9P2B2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGRLASRPLL LALLSLALCR GRVVRVPTAT LVRVVGTELV IPCNVSDYDG
60 70 80 90 100
PSEQNFDWSF SSLGSSFVEL ASTWEVGFPA QLYQERLQRG EILLRRTAND
110 120 130 140 150
AVELHIKNVQ PSDQGHYKCS TPSTDATVQG NYEDTVQVKV LADSLHVGPS
160 170 180 190 200
ARPPPSLSLR EGEPFELRCT AASASPLHTH LALLWEVHRG PARRSVLALT
210 220 230 240 250
HEGRFHPGLG YEQRYHSGDV RLDTVGSDAY RLSVSRALSA DQGSYRCIVS
260 270 280 290 300
EWIAEQGNWQ EIQEKAVEVA TVVIQPSVLR AAVPKNVSVA EGKELDLTCN
310 320 330 340 350
ITTDRADDVR PEVTWSFSRM PDSTLPGSRV LARLDRDSLV HSSPHVALSH
360 370 380 390 400
VDARSYHLLV RDVSKENSGY YYCHVSLWAP GHNRSWHKVA EAVSSPAGVG
410 420 430 440 450
VTWLEPDYQV YLNASKVPGF ADDPTELACR VVDTKSGEAN VRFTVSWYYR
460 470 480 490 500
MNRRSDNVVT SELLAVMDGD WTLKYGERSK QRAQDGDFIF SKEHTDTFNF
510 520 530 540 550
RIQRTTEEDR GNYYCVVSAW TKQRNNSWVK SKDVFSKPVN IFWALEDSVL
560 570 580 590 600
VVKARQPKPF FAAGNTFEMT CKVSSKNIKS PRYSVLIMAE KPVGDLSSPN
610 620 630 640 650
ETKYIISLDQ DSVVKLENWT DASRVDGVVL EKVQEDEFRY RMYQTQVSDA
660 670 680 690 700
GLYRCMVTAW SPVRGSLWRE AATSLSNPIE IDFQTSGPIF NASVHSDTPS
710 720 730 740 750
VIRGDLIKLF CIITVEGAAL DPDDMAFDVS WFAVHSFGLD KAPVLLSSLD
760 770 780 790 800
RKGIVTTSRR DWKSDLSLER VSVLEFLLQV HGSEDQDFGN YYCSVTPWVK
810 820 830 840 850
SPTGSWQKEA EIHSKPVFIT VKMDVLNAFK YPLLIGVGLS TVIGLLSCLI
860 870
GYCSSHWCCK KEVQETRRER RRLMSMEMD
Length:879
Mass (Da):98,556
Last modified:February 1, 2003 - v2
Checksum:i9712C398A74DF570
GO

Sequence cautioni

The sequence BAA92674.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAC11104.1 differs from that shown. Reason: Erroneous termination at position 864. Translated as Gln.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti109 – 1091V → A in BAC11104 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti277 – 2771S → T.1 Publication
Corresponds to variant rs4546904 [ dbSNP | Ensembl ].
VAR_059388
Natural varianti837 – 8371V → I.
Corresponds to variant rs10801922 [ dbSNP | Ensembl ].
VAR_024496

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB037857 mRNA. Translation: BAA92674.1. Different initiation.
AK074637 mRNA. Translation: BAC11104.1. Sequence problems.
AL445231, AL157904 Genomic DNA. Translation: CAH71960.1.
AL157904, AL445231 Genomic DNA. Translation: CAI22650.1.
BC152454 mRNA. Translation: AAI52455.1.
CCDSiCCDS890.1.
RefSeqiNP_065173.2. NM_020440.3.
UniGeneiHs.418093.

Genome annotation databases

EnsembliENST00000393203; ENSP00000376899; ENSG00000134247.
GeneIDi5738.
KEGGihsa:5738.
UCSCiuc001egv.1. human.

Polymorphism databases

DMDMi28201801.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB037857 mRNA. Translation: BAA92674.1. Different initiation.
AK074637 mRNA. Translation: BAC11104.1. Sequence problems.
AL445231, AL157904 Genomic DNA. Translation: CAH71960.1.
AL157904, AL445231 Genomic DNA. Translation: CAI22650.1.
BC152454 mRNA. Translation: AAI52455.1.
CCDSiCCDS890.1.
RefSeqiNP_065173.2. NM_020440.3.
UniGeneiHs.418093.

3D structure databases

ProteinModelPortaliQ9P2B2.
SMRiQ9P2B2. Positions 98-124, 153-251.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111710. 14 interactions.
IntActiQ9P2B2. 1 interaction.
STRINGi9606.ENSP00000376899.

PTM databases

PhosphoSiteiQ9P2B2.

Polymorphism databases

DMDMi28201801.

Proteomic databases

MaxQBiQ9P2B2.
PaxDbiQ9P2B2.
PeptideAtlasiQ9P2B2.
PRIDEiQ9P2B2.

Protocols and materials databases

DNASUi5738.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000393203; ENSP00000376899; ENSG00000134247.
GeneIDi5738.
KEGGihsa:5738.
UCSCiuc001egv.1. human.

Organism-specific databases

CTDi5738.
GeneCardsiGC01P117452.
HGNCiHGNC:9601. PTGFRN.
HPAiHPA017074.
MIMi601204. gene.
neXtProtiNX_Q9P2B2.
PharmGKBiPA33950.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG39204.
GeneTreeiENSGT00390000010278.
HOGENOMiHOG000112641.
HOVERGENiHBG031554.
InParanoidiQ9P2B2.
KOiK06729.
OMAiQTSGPIF.
OrthoDBiEOG7RNJZG.
PhylomeDBiQ9P2B2.
TreeFamiTF332702.

Miscellaneous databases

ChiTaRSiPTGFRN. human.
GeneWikiiPTGFRN.
GenomeRNAii5738.
NextBioi22336.
PROiQ9P2B2.
SOURCEiSearch...

Gene expression databases

BgeeiQ9P2B2.
CleanExiHS_PTGFRN.
ExpressionAtlasiQ9P2B2. baseline and differential.
GenevestigatoriQ9P2B2.

Family and domain databases

Gene3Di2.60.40.10. 5 hits.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR013106. Ig_V-set.
[Graphical view]
PfamiPF07686. V-set. 2 hits.
[Graphical view]
SMARTiSM00409. IG. 6 hits.
[Graphical view]
PROSITEiPS50835. IG_LIKE. 5 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.
    DNA Res. 7:65-73(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT THR-277.
    Tissue: Embryo.
  3. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  5. "The major CD9 and CD81 molecular partner. Identification and characterization of the complexes."
    Charrin S., Le Naour F., Oualid M., Billard M., Faure G., Hanash S.M., Boucheix C., Rubinstein E.
    J. Biol. Chem. 276:14329-14337(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE, INTERACTION WITH CD9; CD63; CD81; CD82 AND CD151.
  6. Cited for: GLYCOSYLATION AT ASN-44; ASN-286; ASN-300; ASN-383; ASN-413; ASN-525; ASN-600; ASN-618 AND ASN-691.
  7. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
    Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
    J. Proteome Res. 8:651-661(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-286 AND ASN-300.
    Tissue: Liver.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiFPRP_HUMAN
AccessioniPrimary (citable) accession number: Q9P2B2
Secondary accession number(s): Q5VVU9, Q8N2K6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 2003
Last sequence update: February 1, 2003
Last modified: March 4, 2015
This is version 126 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human cell differentiation molecules
    CD nomenclature of surface proteins of human leucocytes and list of entries
  2. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.