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Prostaglandin F2 receptor negative regulator (CD9 partner 1) (CD9P-1) (Glu-Trp-Ile EWI motif-containing protein F) (EWI-F) (Prostaglandin F2-alpha receptor regulatory protein) (Prostaglandin F2-alpha receptor-associated protein) (CD antigen CD315)

 FPRP_HUMAN              Reviewed;         879 AA.
Q9P2B2; Q5VVU9; Q8N2K6;
01-FEB-2003, integrated into UniProtKB/Swiss-Prot.
01-FEB-2003, sequence version 2.
22-NOV-2017, entry version 147.
RecName: Full=Prostaglandin F2 receptor negative regulator;
AltName: Full=CD9 partner 1;
Short=CD9P-1;
AltName: Full=Glu-Trp-Ile EWI motif-containing protein F;
Short=EWI-F;
AltName: Full=Prostaglandin F2-alpha receptor regulatory protein;
AltName: Full=Prostaglandin F2-alpha receptor-associated protein;
AltName: CD_antigen=CD315;
Flags: Precursor;
Name=PTGFRN; Synonyms=CD9P1, EWIF, FPRP, KIAA1436;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=10718198; DOI=10.1093/dnares/7.1.65;
Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
"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.";
DNA Res. 7:65-73(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT THR-277.
TISSUE=Embryo;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
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.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
PARTIAL PROTEIN SEQUENCE, AND INTERACTION WITH CD9; CD63; CD81; CD82
AND CD151.
PubMed=11278880; DOI=10.1074/jbc.M011297200;
Charrin S., Le Naour F., Oualid M., Billard M., Faure G., Hanash S.M.,
Boucheix C., Rubinstein E.;
"The major CD9 and CD81 molecular partner. Identification and
characterization of the complexes.";
J. Biol. Chem. 276:14329-14337(2001).
[6]
GLYCOSYLATION AT ASN-44; ASN-286; ASN-300; ASN-383; ASN-413; ASN-525;
ASN-600; ASN-618 AND ASN-691.
PubMed=17960739; DOI=10.1002/pmic.200700355;
Andre M., Morelle W., Planchon S., Milhiet P.E., Rubinstein E.,
Mollicone R., Chamot-Rooke J., Le Naour F.;
"Glycosylation status of the membrane protein CD9P-1.";
Proteomics 7:3880-3895(2007).
[7]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-286 AND ASN-300.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
-!- 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). {ECO:0000250}.
-!- SUBUNIT: Interacts with CD9 and CD81. Also seems to interact with
CD63, CD82 and CD151. {ECO:0000269|PubMed:11278880}.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Golgi apparatus, trans-Golgi network membrane {ECO:0000250};
Single-pass type I membrane protein {ECO:0000250}.
-!- SEQUENCE CAUTION:
Sequence=BAA92674.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=BAC11104.1; Type=Erroneous termination; Positions=864; Note=Translated as Gln.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AB037857; BAA92674.1; ALT_INIT; mRNA.
EMBL; AK074637; BAC11104.1; ALT_SEQ; mRNA.
EMBL; AL445231; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL157904; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC152454; AAI52455.1; -; mRNA.
CCDS; CCDS890.1; -.
RefSeq; NP_065173.2; NM_020440.3.
UniGene; Hs.418093; -.
ProteinModelPortal; Q9P2B2; -.
BioGrid; 111710; 21.
IntAct; Q9P2B2; 1.
STRING; 9606.ENSP00000376899; -.
iPTMnet; Q9P2B2; -.
PhosphoSitePlus; Q9P2B2; -.
SwissPalm; Q9P2B2; -.
BioMuta; PTGFRN; -.
DMDM; 28201801; -.
EPD; Q9P2B2; -.
MaxQB; Q9P2B2; -.
PaxDb; Q9P2B2; -.
PeptideAtlas; Q9P2B2; -.
PRIDE; Q9P2B2; -.
DNASU; 5738; -.
Ensembl; ENST00000393203; ENSP00000376899; ENSG00000134247.
GeneID; 5738; -.
KEGG; hsa:5738; -.
UCSC; uc001egv.2; human.
CTD; 5738; -.
DisGeNET; 5738; -.
EuPathDB; HostDB:ENSG00000134247.9; -.
GeneCards; PTGFRN; -.
HGNC; HGNC:9601; PTGFRN.
HPA; HPA017074; -.
MIM; 601204; gene.
neXtProt; NX_Q9P2B2; -.
OpenTargets; ENSG00000134247; -.
PharmGKB; PA33950; -.
eggNOG; ENOG410IHZG; Eukaryota.
eggNOG; ENOG4111FCJ; LUCA.
GeneTree; ENSGT00390000010278; -.
HOGENOM; HOG000112641; -.
HOVERGEN; HBG031554; -.
InParanoid; Q9P2B2; -.
KO; K06729; -.
OMA; QTSGPIF; -.
OrthoDB; EOG091G01C5; -.
PhylomeDB; Q9P2B2; -.
TreeFam; TF332702; -.
ChiTaRS; PTGFRN; human.
GeneWiki; PTGFRN; -.
GenomeRNAi; 5738; -.
PRO; PR:Q9P2B2; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000134247; -.
CleanEx; HS_PTGFRN; -.
Genevisible; Q9P2B2; HS.
GO; GO:0009986; C:cell surface; IDA:UniProtKB.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
GO; GO:0034389; P:lipid particle organization; IEA:Ensembl.
Gene3D; 2.60.40.10; -; 6.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR003599; Ig_sub.
InterPro; IPR013106; Ig_V-set.
Pfam; PF07686; V-set; 2.
SMART; SM00409; IG; 6.
SMART; SM00406; IGv; 3.
SUPFAM; SSF48726; SSF48726; 4.
PROSITE; PS50835; IG_LIKE; 5.
1: Evidence at protein level;
Complete proteome; Direct protein sequencing; Disulfide bond;
Endoplasmic reticulum; Glycoprotein; Golgi apparatus;
Immunoglobulin domain; Membrane; Phosphoprotein; Polymorphism;
Reference proteome; Repeat; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 25 {ECO:0000255}.
CHAIN 26 879 Prostaglandin F2 receptor negative
regulator.
/FTId=PRO_0000014762.
TOPO_DOM 26 832 Extracellular. {ECO:0000255}.
TRANSMEM 833 853 Helical. {ECO:0000255}.
TOPO_DOM 854 879 Cytoplasmic. {ECO:0000255}.
DOMAIN 26 129 Ig-like C2-type 1.
DOMAIN 149 268 Ig-like C2-type 2.
DOMAIN 276 394 Ig-like C2-type 3.
DOMAIN 406 536 Ig-like C2-type 4.
DOMAIN 544 662 Ig-like C2-type 5.
DOMAIN 688 813 Ig-like C2-type 6.
MOTIF 424 427 Endoplasmic reticulum retention signal.
MOTIF 703 705 Cell attachment site. {ECO:0000255}.
MOD_RES 271 271 Phosphothreonine.
{ECO:0000250|UniProtKB:Q62786}.
CARBOHYD 44 44 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:17960739}.
CARBOHYD 286 286 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:17960739,
ECO:0000269|PubMed:19159218}.
CARBOHYD 300 300 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:17960739,
ECO:0000269|PubMed:19159218}.
CARBOHYD 383 383 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:17960739}.
CARBOHYD 413 413 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:17960739}.
CARBOHYD 525 525 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:17960739}.
CARBOHYD 600 600 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:17960739}.
CARBOHYD 618 618 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:17960739}.
CARBOHYD 691 691 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:17960739}.
DISULFID 43 119 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 169 247 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 299 373 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 429 515 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 571 655 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 711 793 {ECO:0000255|PROSITE-ProRule:PRU00114}.
VARIANT 277 277 S -> T (in dbSNP:rs4546904).
{ECO:0000269|PubMed:14702039}.
/FTId=VAR_059388.
VARIANT 837 837 V -> I (in dbSNP:rs10801922).
/FTId=VAR_024496.
CONFLICT 109 109 V -> A (in Ref. 2; BAC11104).
{ECO:0000305}.
SEQUENCE 879 AA; 98556 MW; 9712C398A74DF570 CRC64;
MGRLASRPLL LALLSLALCR GRVVRVPTAT LVRVVGTELV IPCNVSDYDG PSEQNFDWSF
SSLGSSFVEL ASTWEVGFPA QLYQERLQRG EILLRRTAND AVELHIKNVQ PSDQGHYKCS
TPSTDATVQG NYEDTVQVKV LADSLHVGPS ARPPPSLSLR EGEPFELRCT AASASPLHTH
LALLWEVHRG PARRSVLALT HEGRFHPGLG YEQRYHSGDV RLDTVGSDAY RLSVSRALSA
DQGSYRCIVS EWIAEQGNWQ EIQEKAVEVA TVVIQPSVLR AAVPKNVSVA EGKELDLTCN
ITTDRADDVR PEVTWSFSRM PDSTLPGSRV LARLDRDSLV HSSPHVALSH VDARSYHLLV
RDVSKENSGY YYCHVSLWAP GHNRSWHKVA EAVSSPAGVG VTWLEPDYQV YLNASKVPGF
ADDPTELACR VVDTKSGEAN VRFTVSWYYR MNRRSDNVVT SELLAVMDGD WTLKYGERSK
QRAQDGDFIF SKEHTDTFNF RIQRTTEEDR GNYYCVVSAW TKQRNNSWVK SKDVFSKPVN
IFWALEDSVL VVKARQPKPF FAAGNTFEMT CKVSSKNIKS PRYSVLIMAE KPVGDLSSPN
ETKYIISLDQ DSVVKLENWT DASRVDGVVL EKVQEDEFRY RMYQTQVSDA GLYRCMVTAW
SPVRGSLWRE AATSLSNPIE IDFQTSGPIF NASVHSDTPS VIRGDLIKLF CIITVEGAAL
DPDDMAFDVS WFAVHSFGLD KAPVLLSSLD RKGIVTTSRR DWKSDLSLER VSVLEFLLQV
HGSEDQDFGN YYCSVTPWVK SPTGSWQKEA EIHSKPVFIT VKMDVLNAFK YPLLIGVGLS
TVIGLLSCLI GYCSSHWCCK KEVQETRRER RRLMSMEMD


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