UPAR_HUMAN
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 03-AUG-2022, entry version 214.
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="http://atlasgeneticsoncology.org/Genes/PLAURID41741ch19q13.html";
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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; 123.
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; 73.
DR STRING; 9606.ENSP00000339328; -.
DR BindingDB; Q03405; -.
DR ChEMBL; CHEMBL4883; -.
DR DrugBank; DB00009; Alteplase.
DR DrugBank; DB06245; Lanoteplase.
DR DrugBank; DB00031; Tenecteplase.
DR DrugBank; DB00013; Urokinase.
DR DrugBank; DB05476; WX-UK1.
DR GlyGen; Q03405; 5 sites.
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; Q03405; -.
DR PeptideAtlas; Q03405; -.
DR PRIDE; Q03405; -.
DR ProteomicsDB; 58208; -. [Q03405-1]
DR ProteomicsDB; 58209; -. [Q03405-2]
DR ProteomicsDB; 58210; -. [Q03405-3]
DR ABCD; Q03405; 18 sequenced antibodies.
DR Antibodypedia; 31096; 620 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 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; ECASCAS; -.
DR OrthoDB; 1102918at2759; -.
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; 8 hits in 1083 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 190 other tissues.
DR ExpressionAtlas; Q03405; baseline and differential.
DR Genevisible; Q03405; HS.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
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: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:0016021; C:integral component of membrane; NAS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:Ensembl.
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; IC:ComplexPortal.
DR GO; GO:0010755; P:regulation of plasminogen activation; IC: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; IC:ComplexPortal.
DR CDD; cd00117; LU; 3.
DR Gene3D; 2.10.60.10; -; 3.
DR InterPro; IPR018363; CD59_antigen_CS.
DR InterPro; IPR016054; LY6_UPA_recep-like.
DR InterPro; IPR045860; Snake_toxin-like_sf.
DR InterPro; IPR033084; U-PAR.
DR PANTHER; PTHR10624:SF6; PTHR10624:SF6; 1.
DR Pfam; PF00021; UPAR_LY6; 2.
DR SMART; SM00134; LU; 3.
DR SUPFAM; SSF57302; SSF57302; 3.
DR PROSITE; PS00983; LY6_UPAR; 3.
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
