ID UPAR_HUMAN Reviewed; 335 AA. AC Q03405; A8K409; Q12876; Q15845; Q16887; Q6IB52; Q9BWT0; Q9NYC8; Q9UD69; AC Q9UEA6; Q9UM92; Q9UMV0; DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1994, sequence version 1. DT 27-MAR-2024, entry version 223. DE RecName: Full=Urokinase plasminogen activator surface receptor; DE Short=U-PAR; DE Short=uPAR; DE AltName: Full=Monocyte activation antigen Mo3; DE AltName: CD_antigen=CD87; DE Flags: Precursor; GN Name=PLAUR; Synonyms=MO3, UPAR; 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 [MRNA] (ISOFORM 1), AND PROTEIN SEQUENCE OF 23-33. RX PubMed=1689240; DOI=10.1002/j.1460-2075.1990.tb08132.x; RA Roldan A.L., Cubellis M.V., Masucci M.T., Behrendt N., Lund L.R., Danoe K., RA Appella E., Blasi F.; RT "Cloning and expression of the receptor for human urokinase plasminogen RT activator, a central molecule in cell surface, plasmin dependent RT proteolysis."; RL EMBO J. 9:467-474(1990). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=1316922; RA Min H.Y., Semnani R., Mizukami I.F., Watt K., Todd R.F. III, Liu D.Y.; RT "cDNA for Mo3, a monocyte activation antigen, encodes the human receptor RT for urokinase plasminogen activator."; RL J. Immunol. 148:3636-3642(1992). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3). RX PubMed=8131971; DOI=10.1042/bst021395s; RA Bayraktutan U., Jones P.; RT "A novel urokinase receptor on monocyte-like macrophage cell line."; RL Biochem. Soc. Trans. 21:395-395(1993). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RX PubMed=8392005; DOI=10.1016/0014-5793(93)81763-p; RA Pyke C., Eriksen J., Solberg H., Schnack Nielsen B., Kristensen P., RA Lund L.R., Danoe K.; RT "An alternatively spliced variant of mRNA for the human receptor for RT urokinase plasminogen activator."; RL FEBS Lett. 326:69-74(1993). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 3). RC TISSUE=Placenta; RX PubMed=8049431; RA Casey J.R., Petranka J.G., Kottra J., Fleenor D.E., Rosse W.F.; RT "The structure of the urokinase-type plasminogen activator receptor gene."; RL Blood 84:1151-1156(1994). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). 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 [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS GLY-55; ALA-86; GLN-105; RP ARG-220; LYS-281 AND PRO-317. RG SeattleSNPs variation discovery resource; RL Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15057824; DOI=10.1038/nature02399; RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A., RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., RA Rubin E.M., Lucas S.M.; RT "The DNA sequence and biology of human chromosome 19."; RL Nature 428:529-535(2004). RN [10] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [11] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Skin; 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 [12] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-322 (ISOFORM 1). RC TISSUE=Lung cancer; RX PubMed=11051819; RA Zhu F., Jia S., He F.; RT "cDNA cloning and sequencing of human urokinase receptor."; RL Sheng Wu Gong Cheng Xue Bao 16:461-463(2000). RN [13] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-301 (ISOFORM 1). RA Fu J., Bai X., Wang W., Xi X., Ruan C.; RT "Experimental study of anti-metastatic effect of soluble receptor for RT urokinase plasminogen activator on human breast cancer cells."; RL Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases. RN [14] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-18. RX PubMed=7605992; RA Soravia E., Grebe A., De Luca P., Helin K., Suh T.T., Degen J.L., Blasi F.; RT "A conserved TATA-less proximal promoter drives basal transcription from RT the urokinase-type plasminogen activator receptor gene."; RL Blood 86:624-635(1995). RN [15] RP PARTIAL PROTEIN SEQUENCE. RX PubMed=2156852; DOI=10.1016/s0021-9258(19)39348-2; RA Behrendt N., Roenne E., Ploug M., Petri T., Loeber D., Nielsen L.S., RA Schleuning W.-D., Blasi F., Appella E., Danoe K.; RT "The human receptor for urokinase plasminogen activator. NH2-terminal amino RT acid sequence and glycosylation variants."; RL J. Biol. Chem. 265:6453-6460(1990). RN [16] RP PROTEIN SEQUENCE OF 106-116, AND CLEAVAGE BY U-PA. RX PubMed=9030717; DOI=10.1111/j.1432-1033.1997.0021a.x; RA Hoeyer-Hansen G., Ploug M., Behrendt N., Roenne E., Danoe K.; RT "Cell-surface acceleration of urokinase-catalyzed receptor cleavage."; RL Eur. J. Biochem. 243:21-26(1997). RN [17] RP PROTEIN SEQUENCE OF 210-230 (ISOFORMS 1/2/3). RC TISSUE=Serum; RX PubMed=7539799; DOI=10.1074/jbc.270.23.14107; RA Duke-Cohan J.S., Morimoto C., Rocker J.A., Schlossman S.F.; RT "A novel form of dipeptidylpeptidase IV found in human serum. Isolation, RT characterization, and comparison with T lymphocyte membrane RT dipeptidylpeptidase IV (CD26)."; RL J. Biol. Chem. 270:14107-14114(1995). RN [18] RP DISULFIDE BONDS, AND PARTIAL PROTEIN SEQUENCE. RX PubMed=8394346; DOI=10.1016/s0021-9258(19)85366-8; RA Ploug M., Kjalke M., Roenne E., Weidle U., Hoeyer-Hansen G., Danoe K.; RT "Localization of the disulfide bonds in the NH2-terminal domain of the RT cellular receptor for human urokinase-type plasminogen activator. A domain RT structure belonging to a novel superfamily of glycolipid-anchored membrane RT proteins."; RL J. Biol. Chem. 268:17539-17546(1993). RN [19] RP INTERACTION WITH MRC2. RX PubMed=10636902; DOI=10.1074/jbc.275.3.1993; RA Behrendt N., Jensen O.N., Engelholm L.H., Moertz E., Mann M., Danoe K.; RT "A urokinase receptor-associated protein with specific collagen binding RT properties."; RL J. Biol. Chem. 275:1993-2002(2000). RN [20] RP INTERACTION WITH FAP, AND SUBCELLULAR LOCATION. RX PubMed=12376466; DOI=10.1093/carcin/23.10.1593; RA Artym V.V., Kindzelskii A.L., Chen W.T., Petty H.R.; RT "Molecular proximity of seprase and the urokinase-type plasminogen RT activator receptor on malignant melanoma cell membranes: dependence on RT beta1 integrins and the cytoskeleton."; RL Carcinogenesis 23:1593-1601(2002). RN [21] RP INTERACTION WITH PLAU; SERPINE1 AND SORL1. RX PubMed=15053742; DOI=10.1042/bj20040149; RA Gliemann J., Hermey G., Nykjaer A., Petersen C.M., Jacobsen C., RA Andreasen P.A.; RT "The mosaic receptor sorLA/LR11 binds components of the plasminogen- RT activating system and platelet-derived growth factor-BB similarly to LRP1 RT (low-density lipoprotein receptor-related protein), but mediates slow RT internalization of bound ligand."; RL Biochem. J. 381:203-212(2004). RN [22] RP INTERACTION WITH LRP1 AND SORL1. RX PubMed=14764453; DOI=10.1161/01.res.0000120862.79154.0f; RA Zhu Y., Bujo H., Yamazaki H., Ohwaki K., Jiang M., Hirayama S., Kanaki T., RA Shibasaki M., Takahashi K., Schneider W.J., Saito Y.; RT "LR11, an LDL receptor gene family member, is a novel regulator of smooth RT muscle cell migration."; RL Circ. Res. 94:752-758(2004). RN [23] RP INTERACTION WITH SRPX2. RX PubMed=18718938; DOI=10.1093/hmg/ddn256; RA Royer-Zemmour B., Ponsole-Lenfant M., Gara H., Roll P., Leveque C., RA Massacrier A., Ferracci G., Cillario J., Robaglia-Schlupp A., RA Vincentelli R., Cau P., Szepetowski P.; RT "Epileptic and developmental disorders of the speech cortex: RT ligand/receptor interaction of wild-type and mutant SRPX2 with the RT plasminogen activator receptor uPAR."; RL Hum. Mol. Genet. 17:3617-3630(2008). RN [24] RP INTERACTION WITH SORL1. RX PubMed=23486467; DOI=10.1074/jbc.m112.442491; RA Nishii K., Nakaseko C., Jiang M., Shimizu N., Takeuchi M., Schneider W.J., RA Bujo H.; RT "The soluble form of LR11 protein is a regulator of hypoxia-induced, RT urokinase-type plasminogen activator receptor (uPAR)-mediated adhesion of RT immature hematological cells."; RL J. Biol. Chem. 288:11877-11886(2013). RN [25] RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 23-335 OF MUTANT GLN-222 IN RP COMPLEX WITH PEPTIDE ANTAGONIST, GLYCOSYLATION AT ASN-74; ASN-184; ASN-194 RP AND ASN-255, AND DISULFIDE BONDS. RX PubMed=15861141; DOI=10.1038/sj.emboj.7600635; RA Llinas P., Le Du M.H., Gaardsvoll H., Danoe K., Ploug M., Gilquin B., RA Stura E.A., Menez A.; RT "Crystal structure of the human urokinase plasminogen activator receptor RT bound to an antagonist peptide."; RL EMBO J. 24:1655-1663(2005). RN [26] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 23-297 IN COMPLEX WITH PLAU, RP GLYCOSYLATION AT ASN-74 AND ASN-194, AND DISULFIDE BONDS. RX PubMed=16456079; DOI=10.1126/science.1121143; RA Huai Q., Mazar A.P., Kuo A., Parry G.C., Shaw D.E., Callahan J., Li Y., RA Yuan C., Bian C., Chen L., Furie B., Furie B.C., Cines D.B., Huang M.; RT "Structure of human urokinase plasminogen activator in complex with its RT receptor."; RL Science 311:656-659(2006). RN [27] RP X-RAY CRYSTALLOGRAPHY (2.39 ANGSTROMS) OF 23-305 OF MUTANT CYS-69 AND RP CYS-281 ALONE AND IN COMPLEX WITH PLAU, DISULFIDE BONDS, AND GLYCOSYLATION RP AT ASN-74 AND ASN-222. RX PubMed=22285761; DOI=10.1016/j.jmb.2011.12.058; RA Xu X., Gardsvoll H., Yuan C., Lin L., Ploug M., Huang M.; RT "Crystal structure of the urokinase receptor in a ligand-free form."; RL J. Mol. Biol. 416:629-641(2012). CC -!- FUNCTION: Acts as a receptor for urokinase plasminogen activator. Plays CC a role in localizing and promoting plasmin formation. Mediates the CC proteolysis-independent signal transduction activation effects of U-PA. CC It is subject to negative-feedback regulation by U-PA which cleaves it CC into an inactive form. CC -!- SUBUNIT: Monomer (Probable). Interacts with MRC2. Interacts (via the CC UPAR/Ly6 domains) with SRPX2. Interacts with FAP (seprase); the CC interaction occurs at the cell surface of invadopodia membrane. CC Interacts with SORL1 (via N-terminal ectodomain); this interaction CC decreases PLAUR internalization (PubMed:14764453, PubMed:23486467). The CC ternary complex composed of PLAUR-PLAU-SERPINE1 also interacts with CC SORL1 (PubMed:15053742). {ECO:0000269|PubMed:10636902, CC ECO:0000269|PubMed:12376466, ECO:0000269|PubMed:14764453, CC ECO:0000269|PubMed:15053742, ECO:0000269|PubMed:15861141, CC ECO:0000269|PubMed:16456079, ECO:0000269|PubMed:18718938, CC ECO:0000269|PubMed:22285761, ECO:0000269|PubMed:23486467, ECO:0000305}. CC -!- INTERACTION: CC Q03405; P03950: ANG; NbExp=5; IntAct=EBI-716505, EBI-525291; CC Q03405-1; P00749: PLAU; NbExp=2; IntAct=EBI-15695188, EBI-3905042; CC Q03405-2; P54252: ATXN3; NbExp=3; IntAct=EBI-11028203, EBI-946046; CC Q03405-2; P06396: GSN; NbExp=3; IntAct=EBI-11028203, EBI-351506; CC Q03405-2; D3DTS7: PMP22; NbExp=3; IntAct=EBI-11028203, EBI-25882629; CC Q03405-2; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-11028203, EBI-5235340; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12376466}. Cell CC projection, invadopodium membrane {ECO:0000269|PubMed:12376466}. CC Note=Colocalized with FAP (seprase) preferentially at the cell surface CC of invadopodia membrane in a cytoskeleton-, integrin- and vitronectin- CC dependent manner. {ECO:0000269|PubMed:12376466}. CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane CC {ECO:0000250|UniProtKB:P49616}; Lipid-anchor, GPI-anchor CC {ECO:0000250|UniProtKB:P49616}. CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Secreted CC {ECO:0000250|UniProtKB:P49616}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; Synonyms=uPAR1, GPI-anchored; CC IsoId=Q03405-1; Sequence=Displayed; CC Name=2; Synonyms=uPAR2, Secreted; CC IsoId=Q03405-2; Sequence=VSP_006715; CC Name=3; CC IsoId=Q03405-3; Sequence=VSP_046345, VSP_046346; CC -!- TISSUE SPECIFICITY: Expressed in neurons of the rolandic area of the CC brain (at protein level). Expressed in the brain. CC -!- WEB RESOURCE: Name=SeattleSNPs; CC URL="http://pga.gs.washington.edu/data/plaur/"; CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/41741/PLAUR"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X51675; CAA35981.1; -; mRNA. DR EMBL; M83246; AAA59862.1; -; mRNA. DR EMBL; X74039; CAA52191.1; -; mRNA. DR EMBL; U09346; AAA17979.1; -; Genomic_DNA. DR EMBL; U09347; AAA17978.1; -; mRNA. DR EMBL; U08839; AAB60333.1; -; mRNA. DR EMBL; U09937; AAB60690.1; -; Genomic_DNA. DR EMBL; U09931; AAB60690.1; JOINED; Genomic_DNA. DR EMBL; U09932; AAB60690.1; JOINED; Genomic_DNA. DR EMBL; U09933; AAB60690.1; JOINED; Genomic_DNA. DR EMBL; U09935; AAB60690.1; JOINED; Genomic_DNA. DR EMBL; U09936; AAB60690.1; JOINED; Genomic_DNA. DR EMBL; AY194849; AAN86351.1; -; Genomic_DNA. DR EMBL; AK290774; BAF83463.1; -; mRNA. DR EMBL; CR456952; CAG33233.1; -; mRNA. DR EMBL; AC005525; AAC32739.1; -; Genomic_DNA. DR EMBL; AC006953; AAD17387.1; -; Genomic_DNA. DR EMBL; AC006953; AAD17388.1; -; Genomic_DNA. DR EMBL; CH471126; EAW57220.1; -; Genomic_DNA. DR EMBL; BC002788; AAH02788.1; -; mRNA. DR EMBL; AF257789; AAF71751.1; -; mRNA. DR EMBL; AY029180; AAK31795.1; -; mRNA. DR EMBL; S78532; AAD14289.1; -; Genomic_DNA. DR CCDS; CCDS12628.1; -. [Q03405-1] DR CCDS; CCDS33041.1; -. [Q03405-2] DR CCDS; CCDS33042.1; -. [Q03405-3] DR PIR; I52614; I52614. DR PIR; S12376; A39743. DR PIR; S39495; S39495. DR RefSeq; NP_001005376.1; NM_001005376.2. [Q03405-2] DR RefSeq; NP_001005377.1; NM_001005377.2. [Q03405-3] DR RefSeq; NP_001287966.1; NM_001301037.1. DR RefSeq; NP_002650.1; NM_002659.3. [Q03405-1] DR PDB; 1YWH; X-ray; 2.70 A; A/C/E/G/I/K/M/O=23-335. DR PDB; 2FD6; X-ray; 1.90 A; U=23-297. DR PDB; 2I9B; X-ray; 2.80 A; E/F/G/H=23-299. DR PDB; 3BT1; X-ray; 2.80 A; U=23-303. DR PDB; 3BT2; X-ray; 2.50 A; U=23-303. DR PDB; 3U73; X-ray; 3.19 A; U=23-305. DR PDB; 3U74; X-ray; 2.39 A; U=23-305. DR PDB; 4K24; X-ray; 4.50 A; U=23-303. DR PDB; 4QTI; X-ray; 3.00 A; U=23-305. DR PDB; 7E17; X-ray; 2.96 A; A/B=23-299. DR PDB; 7V63; X-ray; 2.91 A; A/B=23-299. DR PDBsum; 1YWH; -. DR PDBsum; 2FD6; -. DR PDBsum; 2I9B; -. DR PDBsum; 3BT1; -. DR PDBsum; 3BT2; -. DR PDBsum; 3U73; -. DR PDBsum; 3U74; -. DR PDBsum; 4K24; -. DR PDBsum; 4QTI; -. DR PDBsum; 7E17; -. DR PDBsum; 7V63; -. DR AlphaFoldDB; Q03405; -. DR SASBDB; Q03405; -. DR SMR; Q03405; -. DR BioGRID; 111345; 130. DR ComplexPortal; CPX-487; uPA-uPAR complex. DR ComplexPortal; CPX-501; uPA-uPAR-vitronectin complex. DR CORUM; Q03405; -. DR DIP; DIP-137N; -. DR IntAct; Q03405; 74. DR STRING; 9606.ENSP00000339328; -. DR BindingDB; Q03405; -. DR ChEMBL; CHEMBL4883; -. DR DrugBank; DB06245; Lanoteplase. DR DrugBank; DB00031; Tenecteplase. DR DrugBank; DB00013; Urokinase. DR DrugBank; DB05476; WX-UK1. DR GlyCosmos; Q03405; 5 sites, No reported glycans. DR GlyGen; Q03405; 6 sites, 1 O-linked glycan (1 site). DR iPTMnet; Q03405; -. DR PhosphoSitePlus; Q03405; -. DR SwissPalm; Q03405; -. DR BioMuta; PLAUR; -. DR DMDM; 465003; -. DR EPD; Q03405; -. DR jPOST; Q03405; -. DR MassIVE; Q03405; -. DR MaxQB; Q03405; -. DR PaxDb; 9606-ENSP00000339328; -. DR PeptideAtlas; Q03405; -. DR ProteomicsDB; 58208; -. [Q03405-1] DR ProteomicsDB; 58209; -. [Q03405-2] DR ProteomicsDB; 58210; -. [Q03405-3] DR Pumba; Q03405; -. DR ABCD; Q03405; 18 sequenced antibodies. DR Antibodypedia; 31096; 733 antibodies from 42 providers. DR DNASU; 5329; -. DR Ensembl; ENST00000221264.8; ENSP00000221264.3; ENSG00000011422.12. [Q03405-3] DR Ensembl; ENST00000339082.7; ENSP00000342049.2; ENSG00000011422.12. [Q03405-2] DR Ensembl; ENST00000340093.8; ENSP00000339328.3; ENSG00000011422.12. [Q03405-1] DR GeneID; 5329; -. DR KEGG; hsa:5329; -. DR MANE-Select; ENST00000340093.8; ENSP00000339328.3; NM_002659.4; NP_002650.1. DR UCSC; uc002oxd.3; human. [Q03405-1] DR AGR; HGNC:9053; -. DR CTD; 5329; -. DR DisGeNET; 5329; -. DR GeneCards; PLAUR; -. DR HGNC; HGNC:9053; PLAUR. DR HPA; ENSG00000011422; Tissue enriched (bone). DR MIM; 173391; gene. DR neXtProt; NX_Q03405; -. DR OpenTargets; ENSG00000011422; -. DR PharmGKB; PA33383; -. DR VEuPathDB; HostDB:ENSG00000011422; -. DR eggNOG; ENOG502S36D; Eukaryota. DR GeneTree; ENSGT00940000153599; -. DR HOGENOM; CLU_072612_0_0_1; -. DR InParanoid; Q03405; -. DR OMA; TGNGCNH; -. DR OrthoDB; 4599852at2759; -. DR PhylomeDB; Q03405; -. DR TreeFam; TF338662; -. DR PathwayCommons; Q03405; -. DR Reactome; R-HSA-162791; Attachment of GPI anchor to uPAR. DR Reactome; R-HSA-6798695; Neutrophil degranulation. DR Reactome; R-HSA-75205; Dissolution of Fibrin Clot. DR SignaLink; Q03405; -. DR SIGNOR; Q03405; -. DR BioGRID-ORCS; 5329; 12 hits in 1170 CRISPR screens. DR ChiTaRS; PLAUR; human. DR EvolutionaryTrace; Q03405; -. DR GeneWiki; Urokinase_receptor; -. DR GenomeRNAi; 5329; -. DR Pharos; Q03405; Tchem. DR PRO; PR:Q03405; -. DR Proteomes; UP000005640; Chromosome 19. DR RNAct; Q03405; Protein. DR Bgee; ENSG00000011422; Expressed in periodontal ligament and 192 other cell types or tissues. DR ExpressionAtlas; Q03405; baseline and differential. DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-SubCell. DR GO; GO:0009986; C:cell surface; IDA:CAFA. DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome. DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome. DR GO; GO:0009897; C:external side of plasma membrane; NAS:ComplexPortal. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0019898; C:extrinsic component of membrane; TAS:ProtInc. DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB. DR GO; GO:0016020; C:membrane; NAS:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IDA:AgBase. DR GO; GO:0098637; C:protein complex involved in cell-matrix adhesion; IPI:ComplexPortal. DR GO; GO:1905370; C:serine-type endopeptidase complex; IPI:ComplexPortal. DR GO; GO:0035579; C:specific granule membrane; TAS:Reactome. DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB. DR GO; GO:0019904; F:protein domain specific binding; IPI:AgBase. DR GO; GO:0038023; F:signaling receptor activity; TAS:ProtInc. DR GO; GO:0005102; F:signaling receptor binding; IPI:AgBase. DR GO; GO:0030377; F:urokinase plasminogen activator receptor activity; NAS:UniProtKB. DR GO; GO:0007596; P:blood coagulation; TAS:ProtInc. DR GO; GO:0006935; P:chemotaxis; TAS:ProtInc. DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:CACAO. DR GO; GO:2001268; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway; IMP:CACAO. DR GO; GO:2001243; P:negative regulation of intrinsic apoptotic signaling pathway; IMP:CACAO. DR GO; GO:0043388; P:positive regulation of DNA binding; IDA:CACAO. DR GO; GO:0045742; P:positive regulation of epidermal growth factor receptor signaling pathway; IMP:CACAO. DR GO; GO:0034112; P:positive regulation of homotypic cell-cell adhesion; IMP:ARUK-UCL. DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IMP:CACAO. DR GO; GO:0090200; P:positive regulation of release of cytochrome c from mitochondria; IMP:CACAO. DR GO; GO:0030155; P:regulation of cell adhesion; IDA:ComplexPortal. DR GO; GO:0051917; P:regulation of fibrinolysis; NAS:ComplexPortal. DR GO; GO:0010755; P:regulation of plasminogen activation; NAS:ComplexPortal. DR GO; GO:0030162; P:regulation of proteolysis; NAS:UniProtKB. DR GO; GO:0007165; P:signal transduction; TAS:ProtInc. DR GO; GO:0038195; P:urokinase plasminogen activator signaling pathway; NAS:ComplexPortal. DR CDD; cd00117; LU; 3. DR Gene3D; 2.10.60.10; CD59; 3. DR InterPro; IPR018363; CD59_antigen_CS. DR InterPro; IPR016054; LY6_UPA_recep-like. DR InterPro; IPR045860; Snake_toxin-like_sf. DR PANTHER; PTHR10624:SF6; UROKINASE PLASMINOGEN ACTIVATOR SURFACE RECEPTOR; 1. DR PANTHER; PTHR10624; UROKINASE PLASMINOGEN ACTIVATOR SURFACE RECEPTOR-RELATED; 1. DR Pfam; PF00021; UPAR_LY6; 3. DR SMART; SM00134; LU; 3. DR SUPFAM; SSF57302; Snake toxin-like; 3. DR PROSITE; PS00983; LY6_UPAR; 3. DR Genevisible; Q03405; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell junction; Cell membrane; KW Cell projection; Direct protein sequencing; Disulfide bond; Glycoprotein; KW GPI-anchor; Lipoprotein; Membrane; Receptor; Reference proteome; Repeat; KW Secreted; Signal. FT SIGNAL 1..22 FT /evidence="ECO:0000269|PubMed:1689240" FT CHAIN 23..305 FT /note="Urokinase plasminogen activator surface receptor" FT /id="PRO_0000036090" FT PROPEP 306..335 FT /note="Removed in mature form" FT /evidence="ECO:0000255" FT /id="PRO_0000036091" FT DOMAIN 23..114 FT /note="UPAR/Ly6 1" FT DOMAIN 115..213 FT /note="UPAR/Ly6 2" FT DOMAIN 214..305 FT /note="UPAR/Ly6 3" FT SITE 105..106 FT /note="Cleavage; by U-PA" FT SITE 111..112 FT /note="Cleavage; by U-PA" FT LIPID 305 FT /note="GPI-anchor amidated glycine" FT /evidence="ECO:0000255" FT CARBOHYD 74 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:15861141, FT ECO:0000269|PubMed:16456079, ECO:0000269|PubMed:22285761" FT CARBOHYD 184 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:15861141" FT CARBOHYD 194 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:15861141, FT ECO:0000269|PubMed:16456079" FT CARBOHYD 222 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:22285761" FT CARBOHYD 255 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:15861141" FT DISULFID 25..46 FT /evidence="ECO:0000269|PubMed:15861141, FT ECO:0000269|PubMed:16456079, ECO:0000269|PubMed:22285761" FT DISULFID 28..34 FT /evidence="ECO:0000269|PubMed:15861141, FT ECO:0000269|PubMed:16456079, ECO:0000269|PubMed:22285761" FT DISULFID 39..67 FT /evidence="ECO:0000269|PubMed:15861141, FT ECO:0000269|PubMed:16456079, ECO:0000269|PubMed:22285761" FT DISULFID 93..98 FT /evidence="ECO:0000269|PubMed:15861141, FT ECO:0000269|PubMed:16456079, ECO:0000269|PubMed:22285761" FT DISULFID 117..144 FT /evidence="ECO:0000269|PubMed:15861141, FT ECO:0000269|PubMed:16456079, ECO:0000269|PubMed:22285761" FT DISULFID 120..127 FT /evidence="ECO:0000269|PubMed:15861141, FT ECO:0000269|PubMed:16456079, ECO:0000269|PubMed:22285761" FT DISULFID 137..169 FT /evidence="ECO:0000269|PubMed:15861141, FT ECO:0000269|PubMed:16456079, ECO:0000269|PubMed:22285761" FT DISULFID 175..192 FT /evidence="ECO:0000269|PubMed:15861141, FT ECO:0000269|PubMed:16456079, ECO:0000269|PubMed:22285761" FT DISULFID 193..198 FT /evidence="ECO:0000269|PubMed:15861141, FT ECO:0000269|PubMed:16456079, ECO:0000269|PubMed:22285761" FT DISULFID 216..244 FT /evidence="ECO:0000269|PubMed:15861141, FT ECO:0000269|PubMed:16456079, ECO:0000269|PubMed:22285761" FT DISULFID 219..227 FT /evidence="ECO:0000269|PubMed:15861141, FT ECO:0000269|PubMed:16456079, ECO:0000269|PubMed:22285761" FT DISULFID 237..263 FT /evidence="ECO:0000269|PubMed:15861141, FT ECO:0000269|PubMed:16456079, ECO:0000269|PubMed:22285761" FT DISULFID 269..287 FT /evidence="ECO:0000269|PubMed:15861141, FT ECO:0000269|PubMed:16456079, ECO:0000269|PubMed:22285761" FT DISULFID 288..293 FT /evidence="ECO:0000269|PubMed:15861141, FT ECO:0000269|PubMed:16456079, ECO:0000269|PubMed:22285761" FT VAR_SEQ 158..202 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:8049431, FT ECO:0000303|PubMed:8131971" FT /id="VSP_046345" FT VAR_SEQ 203 FT /note="I -> V (in isoform 3)" FT /evidence="ECO:0000303|PubMed:8049431, FT ECO:0000303|PubMed:8131971" FT /id="VSP_046346" FT VAR_SEQ 253..335 FT /note="PKNQSYMVRGCATASMCQHAHLGDAFSMNHIDVSCCTKSGCNHPDLDVQYRS FT GAAPQPGPAHLSLTITLLMTARLWGGTLLWT -> RSLWGSWLPCKSTTALRPPCCEEA FT QATHV (in isoform 2)" FT /evidence="ECO:0000303|PubMed:8392005, ECO:0000303|Ref.7" FT /id="VSP_006715" FT VARIANT 55 FT /note="E -> G (in dbSNP:rs4251813)" FT /evidence="ECO:0000269|Ref.8" FT /id="VAR_016322" FT VARIANT 86 FT /note="T -> A (in dbSNP:rs399145)" FT /evidence="ECO:0000269|Ref.8" FT /id="VAR_016323" FT VARIANT 105 FT /note="R -> Q (in dbSNP:rs4251878)" FT /evidence="ECO:0000269|Ref.8" FT /id="VAR_016324" FT VARIANT 220 FT /note="K -> R (in dbSNP:rs2302524)" FT /evidence="ECO:0000269|Ref.8" FT /id="VAR_016325" FT VARIANT 281 FT /note="N -> K (in dbSNP:rs4251921)" FT /evidence="ECO:0000269|Ref.8" FT /id="VAR_016326" FT VARIANT 297 FT /note="D -> A (in dbSNP:rs16976608)" FT /id="VAR_052698" FT VARIANT 317 FT /note="L -> P (in dbSNP:rs4760)" FT /evidence="ECO:0000269|Ref.8" FT /id="VAR_014922" FT CONFLICT 28 FT /note="C -> N (in Ref. 1; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 165 FT /note="H -> P (in Ref. 13; AAK31795)" FT /evidence="ECO:0000305" FT CONFLICT 213 FT /note="G -> E (in Ref. 17; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 249 FT /note="G -> D (in Ref. 12; AAF71751)" FT /evidence="ECO:0000305" FT CONFLICT 252 FT /note="E -> G (in Ref. 12; AAF71751)" FT /evidence="ECO:0000305" FT STRAND 24..28 FT /evidence="ECO:0007829|PDB:2FD6" FT STRAND 34..38 FT /evidence="ECO:0007829|PDB:2FD6" FT STRAND 45..54 FT /evidence="ECO:0007829|PDB:2FD6" FT STRAND 60..68 FT /evidence="ECO:0007829|PDB:2FD6" FT STRAND 75..81 FT /evidence="ECO:0007829|PDB:2FD6" FT STRAND 84..93 FT /evidence="ECO:0007829|PDB:2FD6" FT TURN 96..99 FT /evidence="ECO:0007829|PDB:2FD6" FT STRAND 110..114 FT /evidence="ECO:0007829|PDB:7E17" FT STRAND 116..121 FT /evidence="ECO:0007829|PDB:2FD6" FT TURN 122..130 FT /evidence="ECO:0007829|PDB:2FD6" FT STRAND 133..136 FT /evidence="ECO:0007829|PDB:2FD6" FT STRAND 138..141 FT /evidence="ECO:0007829|PDB:2I9B" FT STRAND 143..150 FT /evidence="ECO:0007829|PDB:2FD6" FT STRAND 155..158 FT /evidence="ECO:0007829|PDB:3BT1" FT STRAND 164..171 FT /evidence="ECO:0007829|PDB:2FD6" FT STRAND 176..183 FT /evidence="ECO:0007829|PDB:2FD6" FT STRAND 186..193 FT /evidence="ECO:0007829|PDB:2FD6" FT TURN 196..199 FT /evidence="ECO:0007829|PDB:2FD6" FT HELIX 206..208 FT /evidence="ECO:0007829|PDB:2FD6" FT STRAND 211..222 FT /evidence="ECO:0007829|PDB:2FD6" FT TURN 223..225 FT /evidence="ECO:0007829|PDB:2FD6" FT STRAND 226..228 FT /evidence="ECO:0007829|PDB:2FD6" FT TURN 229..231 FT /evidence="ECO:0007829|PDB:2FD6" FT STRAND 233..238 FT /evidence="ECO:0007829|PDB:2FD6" FT STRAND 243..251 FT /evidence="ECO:0007829|PDB:2FD6" FT TURN 252..255 FT /evidence="ECO:0007829|PDB:2FD6" FT STRAND 256..264 FT /evidence="ECO:0007829|PDB:2FD6" FT HELIX 266..268 FT /evidence="ECO:0007829|PDB:2FD6" FT STRAND 270..273 FT /evidence="ECO:0007829|PDB:3BT1" FT HELIX 275..278 FT /evidence="ECO:0007829|PDB:2FD6" FT STRAND 284..288 FT /evidence="ECO:0007829|PDB:2FD6" FT TURN 291..294 FT /evidence="ECO:0007829|PDB:2FD6" FT HELIX 296..298 FT /evidence="ECO:0007829|PDB:3U74" FT CONFLICT Q03405-3:158 FT /note="V -> I (in Ref. 3; no nucleotide entry)" FT /evidence="ECO:0000305" SQ SEQUENCE 335 AA; 36978 MW; AB1963EA3DC77171 CRC64; MGHPPLLPLL LLLHTCVPAS WGLRCMQCKT NGDCRVEECA LGQDLCRTTI VRLWEEGEEL ELVEKSCTHS EKTNRTLSYR TGLKITSLTE VVCGLDLCNQ GNSGRAVTYS RSRYLECISC GSSDMSCERG RHQSLQCRSP EEQCLDVVTH WIQEGEEGRP KDDRHLRGCG YLPGCPGSNG FHNNDTFHFL KCCNTTKCNE GPILELENLP QNGRQCYSCK GNSTHGCSSE ETFLIDCRGP MNQCLVATGT HEPKNQSYMV RGCATASMCQ HAHLGDAFSM NHIDVSCCTK SGCNHPDLDV QYRSGAAPQP GPAHLSLTIT LLMTARLWGG TLLWT //