FPRP_HUMAN
ID FPRP_HUMAN Reviewed; 879 AA.
AC Q9P2B2; Q5VVU9; Q8N2K6;
DT 01-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2003, sequence version 2.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Prostaglandin F2 receptor negative regulator;
DE AltName: Full=CD9 partner 1;
DE Short=CD9P-1;
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=CD9P1, EWIF, FPRP, KIAA1436;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=10718198; DOI=10.1093/dnares/7.1.65;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVI. The
RT complete sequences of 150 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:65-73(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT THR-277.
RC TISSUE=Embryo;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [5]
RP PARTIAL PROTEIN SEQUENCE, AND INTERACTION WITH CD9; CD63; CD81; CD82 AND
RP CD151.
RX PubMed=11278880; DOI=10.1074/jbc.m011297200;
RA Charrin S., Le Naour F., Oualid M., Billard M., Faure G., Hanash S.M.,
RA Boucheix C., Rubinstein E.;
RT "The major CD9 and CD81 molecular partner. Identification and
RT characterization of the complexes.";
RL J. Biol. Chem. 276:14329-14337(2001).
RN [6]
RP GLYCOSYLATION AT ASN-44; ASN-286; ASN-300; ASN-383; ASN-413; ASN-525;
RP ASN-600; ASN-618 AND ASN-691.
RX PubMed=17960739; DOI=10.1002/pmic.200700355;
RA Andre M., Morelle W., Planchon S., Milhiet P.E., Rubinstein E.,
RA Mollicone R., Chamot-Rooke J., Le Naour F.;
RT "Glycosylation status of the membrane protein CD9P-1.";
RL Proteomics 7:3880-3895(2007).
RN [7]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-286 AND ASN-300.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
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 (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:Q9WV91}.
CC -!- SUBUNIT: Interacts with CD9 and CD81 (PubMed:11278880). Part of a
CC complex composed of CD9, CD81 and IGSF8 (By similarity). Also seems to
CC interact with CD63, CD82 and CD151 (PubMed:11278880).
CC {ECO:0000250|UniProtKB:Q9WV91, ECO:0000269|PubMed:11278880}.
CC -!- INTERACTION:
CC Q9P2B2; P21926: CD9; NbExp=10; IntAct=EBI-4290465, EBI-4280101;
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 -!- SEQUENCE CAUTION:
CC Sequence=BAA92674.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC11104.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB037857; BAA92674.1; ALT_INIT; mRNA.
DR EMBL; AK074637; BAC11104.1; ALT_SEQ; mRNA.
DR EMBL; AL445231; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL157904; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC152454; AAI52455.1; -; mRNA.
DR CCDS; CCDS890.1; -.
DR RefSeq; NP_065173.2; NM_020440.3.
DR AlphaFoldDB; Q9P2B2; -.
DR BioGRID; 111710; 63.
DR IntAct; Q9P2B2; 14.
DR MINT; Q9P2B2; -.
DR STRING; 9606.ENSP00000376899; -.
DR GlyConnect; 1647; 35 N-Linked glycans (5 sites).
DR GlyGen; Q9P2B2; 10 sites, 35 N-linked glycans (5 sites), 1 O-linked glycan (1 site).
DR iPTMnet; Q9P2B2; -.
DR PhosphoSitePlus; Q9P2B2; -.
DR SwissPalm; Q9P2B2; -.
DR BioMuta; PTGFRN; -.
DR DMDM; 28201801; -.
DR EPD; Q9P2B2; -.
DR jPOST; Q9P2B2; -.
DR MassIVE; Q9P2B2; -.
DR MaxQB; Q9P2B2; -.
DR PaxDb; Q9P2B2; -.
DR PeptideAtlas; Q9P2B2; -.
DR PRIDE; Q9P2B2; -.
DR ProteomicsDB; 83765; -.
DR Antibodypedia; 2447; 148 antibodies from 27 providers.
DR DNASU; 5738; -.
DR Ensembl; ENST00000393203.3; ENSP00000376899.2; ENSG00000134247.10.
DR GeneID; 5738; -.
DR KEGG; hsa:5738; -.
DR MANE-Select; ENST00000393203.3; ENSP00000376899.2; NM_020440.4; NP_065173.2.
DR UCSC; uc001egv.2; human.
DR CTD; 5738; -.
DR DisGeNET; 5738; -.
DR GeneCards; PTGFRN; -.
DR HGNC; HGNC:9601; PTGFRN.
DR HPA; ENSG00000134247; Low tissue specificity.
DR MIM; 601204; gene.
DR neXtProt; NX_Q9P2B2; -.
DR OpenTargets; ENSG00000134247; -.
DR PharmGKB; PA33950; -.
DR VEuPathDB; HostDB:ENSG00000134247; -.
DR eggNOG; ENOG502QVD2; Eukaryota.
DR GeneTree; ENSGT00940000158367; -.
DR HOGENOM; CLU_005187_1_0_1; -.
DR InParanoid; Q9P2B2; -.
DR OMA; GGGRWHM; -.
DR OrthoDB; 151148at2759; -.
DR PhylomeDB; Q9P2B2; -.
DR TreeFam; TF332702; -.
DR PathwayCommons; Q9P2B2; -.
DR SignaLink; Q9P2B2; -.
DR BioGRID-ORCS; 5738; 10 hits in 1080 CRISPR screens.
DR ChiTaRS; PTGFRN; human.
DR GeneWiki; PTGFRN; -.
DR GenomeRNAi; 5738; -.
DR Pharos; Q9P2B2; Tbio.
DR PRO; PR:Q9P2B2; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9P2B2; protein.
DR Bgee; ENSG00000134247; Expressed in cardiac muscle of right atrium and 162 other tissues.
DR Genevisible; Q9P2B2; HS.
DR GO; GO:0009986; C:cell surface; HDA:UniProtKB.
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; IEA:Ensembl.
DR GO; GO:0014905; P:myoblast fusion involved in skeletal muscle regeneration; ISS:UniProtKB.
DR Gene3D; 2.60.40.10; -; 4.
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; 4.
DR PROSITE; PS50835; IG_LIKE; 5.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Endoplasmic reticulum;
KW Glycoprotein; Golgi apparatus; Immunoglobulin domain; Membrane;
KW Phosphoprotein; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..879
FT /note="Prostaglandin F2 receptor negative regulator"
FT /id="PRO_0000014762"
FT TOPO_DOM 26..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 26..129
FT /note="Ig-like C2-type 1"
FT DOMAIN 149..268
FT /note="Ig-like C2-type 2"
FT DOMAIN 276..394
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 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:0000269|PubMed:17960739"
FT CARBOHYD 286
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17960739,
FT ECO:0000269|PubMed:19159218"
FT CARBOHYD 300
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17960739,
FT ECO:0000269|PubMed:19159218"
FT CARBOHYD 383
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17960739"
FT CARBOHYD 413
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17960739"
FT CARBOHYD 525
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17960739"
FT CARBOHYD 600
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17960739"
FT CARBOHYD 618
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17960739"
FT CARBOHYD 691
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17960739"
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 VARIANT 277
FT /note="S -> T (in dbSNP:rs4546904)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_059388"
FT VARIANT 837
FT /note="V -> I (in dbSNP:rs10801922)"
FT /id="VAR_024496"
FT CONFLICT 109
FT /note="V -> A (in Ref. 2; BAC11104)"
FT /evidence="ECO:0000305"
SQ 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
