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Uromodulin (Tamm-Horsfall urinary glycoprotein) (THP) [Cleaved into: Uromodulin, secreted form]

 UROM_HUMAN              Reviewed;         640 AA.
P07911; B3KP48; B3KRN9; E9PEA4; Q540J6; Q6ZS84; Q8IYG0;
01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
01-AUG-1988, sequence version 1.
20-JUN-2018, entry version 184.
RecName: Full=Uromodulin;
AltName: Full=Tamm-Horsfall urinary glycoprotein;
Short=THP;
Contains:
RecName: Full=Uromodulin, secreted form;
Flags: Precursor;
Name=UMOD;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND
TISSUE SPECIFICITY.
PubMed=3453112; DOI=10.1126/science.3453112;
Pennica D., Kohr W.J., Kuang W.-J., Glaister D., Aggarwal B.B.,
Chen E.Y., Goeddel D.V.;
"Identification of human uromodulin as the Tamm-Horsfall urinary
glycoprotein.";
Science 236:83-88(1987).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, AND
FUNCTION.
PubMed=3498215; DOI=10.1126/science.3498215;
Hession C., Decker J.M., Sherblom A.P., Kumar S., Yue C.C.,
Mattaliano R.J., Tizard R., Kawashima E., Schmeissner U., Heletky S.,
Chow E.P., Burne C.A., Shaw A., Muchmore A.V.;
"Uromodulin (Tamm-Horsfall glycoprotein): a renal ligand for
lymphokines.";
Science 237:1479-1484(1987).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS HNFJ1 TYR-148 AND ARG-217,
AND VARIANT MCKD2 CYS-103.
PubMed=12471200; DOI=10.1136/jmg.39.12.882;
Hart T.C., Gorry M.C., Hart P.S., Woodard A.S., Shihabi Z., Sandhu J.,
Shirts B., Xu L., Zhu H., Barmada M.M., Bleyer A.J.;
"Mutations of the UMOD gene are responsible for medullary cystic
kidney disease 2 and familial juvenile hyperuricaemic nephropathy.";
J. Med. Genet. 39:882-892(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 4 AND 5).
TISSUE=Kidney;
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).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15616553; DOI=10.1038/nature03187;
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X.,
Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A.,
Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.,
Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L.,
Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A.,
Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D.,
Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J.,
Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I.,
Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W.,
Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A.,
Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S.,
Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L.,
Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A.,
Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L.,
Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N.,
Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M.,
Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L.,
Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D.,
Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P.,
Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M.,
Rubin E.M., Pennacchio L.A.;
"The sequence and analysis of duplication-rich human chromosome 16.";
Nature 432:988-994(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Kidney;
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).
[7]
PROTEIN SEQUENCE OF 578-587, PROTEOLYTIC CLEAVAGE, IDENTIFICATION BY
MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=18375198; DOI=10.1016/j.bbrc.2008.03.099;
Santambrogio S., Cattaneo A., Bernascone I., Schwend T., Jovine L.,
Bachi A., Rampoldi L.;
"Urinary uromodulin carries an intact ZP domain generated by a
conserved C-terminal proteolytic cleavage.";
Biochem. Biophys. Res. Commun. 370:410-413(2008).
[8]
TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
PubMed=7028707;
Sikri K.L., Foster C.L., MacHugh N., Marshall R.D.;
"Localization of Tamm-Horsfall glycoprotein in the human kidney using
immuno-fluorescence and immuno-electron microscopical techniques.";
J. Anat. 132:597-605(1981).
[9]
GPI-ANCHOR, AND SUBCELLULAR LOCATION.
PubMed=2249987;
Rindler M.J., Naik S.S., Li N., Hoops T.C., Peraldi M.-N.;
"Uromodulin (Tamm-Horsfall glycoprotein/uromucoid) is a
phosphatidylinositol-linked membrane protein.";
J. Biol. Chem. 265:20784-20789(1990).
[10]
SUBCELLULAR LOCATION, SUBUNIT, MUTAGENESIS OF ASP-430; LEU-435;
VAL-458; 586-ARG--SER-589; 598-VAL--ASN-600; 602-GLY-PRO-603 AND
605-THR--LYS-607, REGION, AND GLYCOSYLATION.
PubMed=19005207; DOI=10.1091/mbc.E08-08-0876;
Schaeffer C., Santambrogio S., Perucca S., Casari G., Rampoldi L.;
"Analysis of uromodulin polymerization provides new insights into the
mechanisms regulating ZP domain-mediated protein assembly.";
Mol. Biol. Cell 20:589-599(2009).
[11]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=20798515; DOI=10.1159/000320554;
Schmid M., Prajczer S., Gruber L.N., Bertocchi C., Gandini R.,
Pfaller W., Jennings P., Joannidis M.;
"Uromodulin facilitates neutrophil migration across renal epithelial
monolayers.";
Cell. Physiol. Biochem. 26:311-318(2010).
[12]
SUBCELLULAR LOCATION.
PubMed=20172860; DOI=10.1093/hmg/ddq077;
Zaucke F., Boehnlein J.M., Steffens S., Polishchuk R.S., Rampoldi L.,
Fischer A., Pasch A., Boehm C.W., Baasner A., Attanasio M., Hoppe B.,
Hopfer H., Beck B.B., Sayer J.A., Hildebrandt F., Wolf M.T.;
"Uromodulin is expressed in renal primary cilia and UMOD mutations
result in decreased ciliary uromodulin expression.";
Hum. Mol. Genet. 19:1985-1997(2010).
[13]
GLYCOSYLATION AT ASN-232; ASN-322 AND ASN-396, STRUCTURE OF
CARBOHYDRATES, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=22171320; DOI=10.1074/mcp.M111.013649;
Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.;
"Human urinary glycoproteomics; attachment site specific analysis of
N-and O-linked glycosylations by CID and ECD.";
Mol. Cell. Proteomics 11:1-17(2012).
[14]
SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INVOLVEMENT IN HNFJ1.
PubMed=22776760; DOI=10.1159/000339752;
Wei X., Xu R., Yang Z., Li Z., Liao Y., Johnson R.J., Yu X., Chen W.;
"Novel uromodulin mutation in familial juvenile hyperuricemic
nephropathy.";
Am. J. Nephrol. 36:114-120(2012).
[15]
SUBUNIT, ELECTRON MICROSCOPY, SUBCELLULAR LOCATION, GLYCOSYLATION,
MUTAGENESIS OF 586-ARG--SER-589, PROTEOLYTIC CLEAVAGE BY HPN, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=26673890; DOI=10.7554/eLife.08887;
Brunati M., Perucca S., Han L., Cattaneo A., Consolato F., Andolfo A.,
Schaeffer C., Olinger E., Peng J., Santambrogio S., Perrier R., Li S.,
Bokhove M., Bachi A., Hummler E., Devuyst O., Wu Q., Jovine L.,
Rampoldi L.;
"The serine protease hepsin mediates urinary secretion and
polymerisation of Zona Pellucida domain protein uromodulin.";
Elife 4:0-0(2015).
[16]
X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 295-610, ELECTRON MICROSCOPY,
SUBUNIT, SUBCELLULAR LOCATION, DISULFIDE BOND, DOMAIN, GLYCOSYLATION
AT ASN-396, MUTAGENESIS OF LEU-333; ILE-421 AND 586-ARG--SER-589, AND
REGION.
PubMed=26811476; DOI=10.1073/pnas.1519803113;
Bokhove M., Nishimura K., Brunati M., Han L., de Sanctis D.,
Rampoldi L., Jovine L.;
"A structured interdomain linker directs self-polymerization of human
uromodulin.";
Proc. Natl. Acad. Sci. U.S.A. 113:1552-1557(2016).
[17]
VARIANT HNFJ1 TYR-223.
PubMed=12900848; DOI=10.1016/S0272-6386(03)00670-X;
Bleyer A.J., Trachtman H., Sandhu J., Gorry M.C., Hart T.C.;
"Renal manifestations of a mutation in the uromodulin (Tamm Horsfall
protein) gene.";
Am. J. Kidney Dis. 42:E20-E26(2003).
[18]
INVOLVEMENT IN MCKD2, VARIANTS HNFJ1 TRP-148; SER-150 AND TYR-317,
VARIANT GCKDHI ARG-315, CHARACTERIZATION OF VARIANTS HNFJ1 TRP-148;
SER-150 AND TYR-317, AND CHARACTERIZATION OF VARIANT GCKDHI ARG-315.
PubMed=14570709; DOI=10.1093/hmg/ddg353;
Rampoldi L., Caridi G., Santon D., Boaretto F., Bernascone I.,
Lamorte G., Tardanico R., Dagnino M., Colussi G., Scolari F.,
Ghiggeri G.M., Amoroso A., Casari G.;
"Allelism of MCKD, FJHN and GCKD caused by impairment of uromodulin
export dynamics.";
Hum. Mol. Genet. 12:3369-3384(2003).
[19]
INVOLVEMENT IN HNFJ1, AND VARIANTS HNFJ1 ALA-59; ARG-112; ARG-126;
TYR-170; SER-185; GLY-204; GLY-217; PRO-222; MET-225 AND ARG-282.
PubMed=14569098; DOI=10.1097/01.ASN.0000092147.83480.B5;
Dahan K., Devuyst O., Smaers M., Vertommen D., Loute G., Poux J.M.,
Viron B., Jacquot C., Gagnadoux M.F., Chauveau D., Buchler M.,
Cochat P., Cosyns J.P., Mougenot B., Rider M.H., Antignac C.,
Verellen-Dumoulin C., Pirson Y.;
"A cluster of mutations in the UMOD gene causes familial juvenile
hyperuricemic nephropathy with abnormal expression of uromodulin.";
J. Am. Soc. Nephrol. 14:2883-2893(2003).
[20]
VARIANTS HNFJ1 TYR-77; ARG-126; SER-128; TYR-255 AND GLY-300.
PubMed=12629136; DOI=10.1210/jc.2002-021973;
Turner J.J.O., Stacey J.M., Harding B., Kotanko P., Lhotta K.,
Puig J.G., Roberts I., Torres R.J., Thakker R.V.;
"UROMODULIN mutations cause familial juvenile hyperuricemic
nephropathy.";
J. Clin. Endocrinol. Metab. 88:1398-1401(2003).
[21]
VARIANTS MCKD2 93-VAL--GLY-97 DELINS ALA-ALA-SER-CYS; LYS-225 AND
TRP-248.
PubMed=14531790; DOI=10.1046/j.1523-1755.2003.00269.x;
Wolf M.T.F., Mucha B.E., Attanasio M., Zalewski I., Karle S.M.,
Neumann H.P.H., Rahman N., Bader B., Baldamus C.A., Otto E.,
Witzgall R., Fuchshuber A., Hildebrandt F.;
"Mutations of the Uromodulin gene in MCKD type 2 patients cluster in
exon 4, which encodes three EGF-like domains.";
Kidney Int. 64:1580-1587(2003).
[22]
INVOLVEMENT IN HNFJ1, AND VARIANTS HNFJ1 TRP-52; SER-135; PHE-195;
SER-202 AND LEU-236.
PubMed=15086896; DOI=10.1111/j.1523-1755.2004.00559.x;
Kudo E., Kamatani N., Tezuka O., Taniguchi A., Yamanaka H., Yabe S.,
Osabe D., Shinohara S., Nomura K., Segawa M., Miyamoto T.,
Moritani M., Kunika K., Itakura M.;
"Familial juvenile hyperuricemic nephropathy: detection of mutations
in the uromodulin gene in five Japanese families.";
Kidney Int. 65:1589-1597(2004).
[23]
VARIANT HNFJ1 GLY-347, AND CHARACTERIZATION OF VARIANT HNFJ1 GLY-347.
PubMed=15575003; DOI=10.1093/ndt/gfh524;
Tinschert S., Ruf N., Bernascone I., Sacherer K., Lamorte G.,
Neumayer H.H., Nurnberg P., Luft F.C., Rampoldi L.;
"Functional consequences of a novel uromodulin mutation in a family
with familial juvenile hyperuricaemic nephropathy.";
Nephrol. Dial. Transplant. 19:3150-3154(2004).
[24]
VARIANT HNFJ1 PRO-316.
PubMed=15983957; DOI=10.1053/j.ajkd.2005.04.003;
Lens X.M., Banet J.F., Outeda P., Barrio-Lucia V.;
"A novel pattern of mutation in uromodulin disorders: autosomal
dominant medullary cystic kidney disease type 2, familial juvenile
hyperuricemic nephropathy, and autosomal dominant glomerulocystic
kidney disease.";
Am. J. Kidney Dis. 46:52-57(2005).
[25]
VARIANT HNFJ1 ARG-236, CHARACTERIZATION OF VARIANTS HNFJ1 ALA-59;
SER-128; TRP-148; SER-150; GLY-204; ARG-217 AND ARG-236,
CHARACTERIZATION OF VARIANT MCKD2 LYS-225, AND CHARACTERIZATION OF
VARIANT GCKDHI ARG-315.
PubMed=17010121; DOI=10.1111/j.1600-0854.2006.00481.x;
Bernascone I., Vavassori S., Di Pentima A., Santambrogio S.,
Lamorte G., Amoroso A., Scolari F., Ghiggeri G.M., Casari G.,
Polishchuk R., Rampoldi L.;
"Defective intracellular trafficking of uromodulin mutant isoforms.";
Traffic 7:1567-1579(2006).
[26]
VARIANT HNFJ1 GLU-461.
PubMed=21060763; DOI=10.3346/jkms.2010.25.11.1680;
Lee D.H., Kim J.K., Oh S.E., Noh J.W., Lee Y.K.;
"A case of familial juvenile hyperuricemic nephropathy with novel
uromodulin gene mutation, a novel heterozygous missense mutation in
Korea.";
J. Korean Med. Sci. 25:1680-1682(2010).
[27]
VARIANT HNFJ1 ARG-230.
PubMed=23197950; DOI=10.1159/000337343;
Nakayama M., Mori Y., Ota N., Ishida M., Shiotsu Y., Matsuoka E.,
Kado H., Ishida R., Nakata M., Kitani T., Tamagaki K., Sekita C.,
Taniguchi A.;
"A Japanese family suffering from familial juvenile hyperuricemic
nephropathy due to a rare mutation of the uromodulin gene.";
Case Rep. Nephrol. Urol. 2:15-19(2012).
[28]
VARIANTS HNFJ1 GLU-109; GLN-236 AND TRP-248, CHARACTERIZATION OF
VARIANTS HNFJ1 GLU-109; GLN-236 AND TRP-248, SUBCELLULAR LOCATION, AND
TISSUE SPECIFICITY.
PubMed=23988501; DOI=10.1016/j.gene.2013.08.041;
Liu M., Chen Y., Liang Y., Liu Y., Wang S., Hou P., Zhang H., Zhao M.;
"Novel UMOD mutations in familial juvenile hyperuricemic nephropathy
lead to abnormal uromodulin intracellular trafficking.";
Gene 531:363-369(2013).
[29]
VARIANT ARG-155, CHARACTERIZATION OF VARIANT MCKD2 93-VAL--GLY-97
DELINS ALA-ALA-SER-CYS, CHARACTERIZATION OF VARIANTS HNFJ1 SER-150,
AND CHARACTERIZATION OF VARIANT ARG-155.
PubMed=25436415; DOI=10.1016/j.febslet.2014.11.029;
Stewart A.P., Sandford R.N., Karet Frankl F.E., Edwardson J.M.;
"Pathogenic uromodulin mutations result in premature intracellular
polymerization.";
FEBS Lett. 589:89-93(2015).
[30]
VARIANT MCKD2 GLY-120, AND CHARACTERIZATION OF VARIANT MCKD2 GLY-120.
PubMed=27729211; DOI=10.1016/j.clinbiochem.2016.10.003;
Satanovskij R., Bader A., Block M., Herbst V., Schlumberger W.,
Haack T., Nockher W.A., Heemann U., Renders L., Schmaderer C.,
Angermann S., Wen M., Meitinger T., Scherberich J., Steubl D.;
"A new missense mutation in UMOD gene leads to severely reduced serum
uromodulin concentrations - A tool for the diagnosis of uromodulin-
associated kidney disease.";
Clin. Biochem. 50:155-158(2017).
-!- FUNCTION: Uromodulin: Functions in biogenesis and organization of
the apical membrane of epithelial cells of the thick ascending
limb of Henle's loop (TALH), where it promotes formation of
complex filamentous gel-like structure that may play a role in the
water barrier permeability (Probable). May serve as a receptor for
binding and endocytosis of cytokines (IL-1, IL-2) and TNF
(PubMed:3498215). Facilitates neutrophil migration across renal
epithelia (PubMed:20798515). {ECO:0000269|PubMed:20798515,
ECO:0000269|PubMed:3498215, ECO:0000305}.
-!- FUNCTION: Uromodulin, secreted form: In the urine, may contribute
to colloid osmotic pressure, retards passage of positively charged
electrolytes, prevents urinary tract infection and inhibits
formation of liquid containing supersaturated salts and subsequent
formation of salt crystals. {ECO:0000250|UniProtKB:Q91X17,
ECO:0000305}.
-!- SUBUNIT: Uromodulin, secreted form: homodimer that then
polymerizes into long filaments. {ECO:0000269|PubMed:19005207,
ECO:0000269|PubMed:26673890, ECO:0000269|PubMed:26811476}.
-!- SUBCELLULAR LOCATION: Apical cell membrane
{ECO:0000269|PubMed:22776760, ECO:0000269|PubMed:23988501,
ECO:0000269|PubMed:26673890, ECO:0000269|PubMed:7028707}; Lipid-
anchor, GPI-anchor {ECO:0000269|PubMed:2249987}. Basolateral cell
membrane {ECO:0000269|PubMed:7028707}; Lipid-anchor, GPI-anchor
{ECO:0000269|PubMed:2249987}. Cell projection, cilium membrane
{ECO:0000269|PubMed:20172860}. Note=Only a small fraction sorts to
the basolateral pole of tubular epithelial cells compared to
apical localization (PubMed:22776760). Secreted into urine after
cleavage (PubMed:18375198, PubMed:26811476). Colocalizes with
NPHP1 and KIF3A (PubMed:20172860). {ECO:0000269|PubMed:18375198,
ECO:0000269|PubMed:20172860, ECO:0000269|PubMed:26811476,
ECO:0000269|PubMed:3453112, ECO:0000269|PubMed:7028707}.
-!- SUBCELLULAR LOCATION: Uromodulin, secreted form: Secreted
{ECO:0000269|PubMed:18375198, ECO:0000269|PubMed:19005207,
ECO:0000269|PubMed:26673890, ECO:0000269|PubMed:26811476,
ECO:0000269|PubMed:3453112, ECO:0000269|PubMed:7028707}.
Note=Detected in urine. {ECO:0000269|PubMed:18375198,
ECO:0000269|PubMed:26811476, ECO:0000269|PubMed:3453112,
ECO:0000269|PubMed:7028707}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=1;
IsoId=P07911-1; Sequence=Displayed;
Name=2;
IsoId=P07911-2; Sequence=VSP_017565;
Note=No experimental confirmation available.;
Name=3;
IsoId=P07911-3; Sequence=VSP_017566;
Note=No experimental confirmation available.;
Name=4;
IsoId=P07911-4; Sequence=VSP_040973;
Name=5;
IsoId=P07911-5; Sequence=VSP_054828;
-!- TISSUE SPECIFICITY: Expressed in the tubular cells of the kidney.
Most abundant protein in normal urine (at protein level).
Synthesized exclusively in the kidney. Expressed exclusively by
epithelial cells of the thick ascending limb of Henle's loop
(TALH) and of distal convoluted tubule lumen.
{ECO:0000269|PubMed:18375198, ECO:0000269|PubMed:22776760,
ECO:0000269|PubMed:23988501, ECO:0000269|PubMed:3453112,
ECO:0000269|PubMed:7028707}.
-!- DOMAIN: The ZP domain mediates polymerization, leading to the
formation of long filaments. {ECO:0000269|PubMed:26811476}.
-!- PTM: N-glycosylated (PubMed:19005207, PubMed:26673890,
PubMed:26811476). N-glycan heterogeneity at Asn-232: Hex7HexNAc6
(major) and dHex1Hex7HexNAc6 (minor); at Asn-322: dHex1Hex6HexNAc5
(minor), dHex1Hex7HexNAc6 (major) and dHex1Hex8HexNAc7 (minor); at
Asn-396: Hex6HexNAc5 (major), dHex1Hex6HexNAc5 (minor) and
Hex7HexNAc6 (minor) (PubMed:22171320).
{ECO:0000269|PubMed:19005207, ECO:0000269|PubMed:22171320,
ECO:0000269|PubMed:26673890, ECO:0000269|PubMed:26811476}.
-!- PTM: Proteolytically cleaved at a conserved C-terminal proteolytic
cleavage site to generate the secreted form found in urine
(PubMed:18375198, PubMed:19005207). This cleavage is catalyzed by
HPN (PubMed:26673890). {ECO:0000269|PubMed:18375198,
ECO:0000269|PubMed:19005207, ECO:0000269|PubMed:26673890}.
-!- DISEASE: Familial juvenile hyperuricemic nephropathy 1 (HNFJ1)
[MIM:162000]: A renal disease characterized by juvenile onset of
hyperuricemia, polyuria, progressive renal failure, and gout. The
disease is associated with interstitial pathological changes
resulting in fibrosis. {ECO:0000269|PubMed:12471200,
ECO:0000269|PubMed:12629136, ECO:0000269|PubMed:12900848,
ECO:0000269|PubMed:14569098, ECO:0000269|PubMed:14570709,
ECO:0000269|PubMed:15086896, ECO:0000269|PubMed:15575003,
ECO:0000269|PubMed:15983957, ECO:0000269|PubMed:17010121,
ECO:0000269|PubMed:21060763, ECO:0000269|PubMed:22776760,
ECO:0000269|PubMed:23197950, ECO:0000269|PubMed:23988501,
ECO:0000269|PubMed:25436415}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Medullary cystic kidney disease 2 (MCKD2) [MIM:603860]: A
form of tubulointerstitial nephropathy characterized by formation
of renal cysts at the corticomedullary junction. It is
characterized by adult onset of impaired renal function and salt
wasting resulting in end-stage renal failure by the sixth decade.
{ECO:0000269|PubMed:12471200, ECO:0000269|PubMed:14531790,
ECO:0000269|PubMed:14570709, ECO:0000269|PubMed:17010121,
ECO:0000269|PubMed:25436415, ECO:0000269|PubMed:27729211}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Glomerulocystic kidney disease with hyperuricemia and
isosthenuria (GCKDHI) [MIM:609886]: A renal disorder characterized
by a cystic dilation of Bowman space, a collapse of glomerular
tuft, and hyperuricemia due to low fractional excretion of uric
acid and severe impairment of urine concentrating ability.
{ECO:0000269|PubMed:14570709, ECO:0000269|PubMed:17010121}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-----------------------------------------------------------------------
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EMBL; M15881; AAA36798.1; -; mRNA.
EMBL; M17778; AAA36799.1; -; mRNA.
EMBL; AY162970; AAO64446.1; -; Genomic_DNA.
EMBL; AY162963; AAO64446.1; JOINED; Genomic_DNA.
EMBL; AY162964; AAO64446.1; JOINED; Genomic_DNA.
EMBL; AY162965; AAO64446.1; JOINED; Genomic_DNA.
EMBL; AY162967; AAO64446.1; JOINED; Genomic_DNA.
EMBL; AY162968; AAO64446.1; JOINED; Genomic_DNA.
EMBL; AY162969; AAO64446.1; JOINED; Genomic_DNA.
EMBL; AK127643; BAC87070.1; -; mRNA.
EMBL; AK055722; BAG51560.1; -; mRNA.
EMBL; AK091961; BAG52451.1; -; mRNA.
EMBL; AC106796; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC035975; AAH35975.1; -; mRNA.
CCDS; CCDS10583.1; -. [P07911-1]
CCDS; CCDS61876.1; -. [P07911-5]
PIR; A30452; A30452.
RefSeq; NP_001008390.1; NM_001008389.2. [P07911-1]
RefSeq; NP_001265543.1; NM_001278614.1. [P07911-5]
RefSeq; NP_003352.2; NM_003361.3. [P07911-1]
UniGene; Hs.654425; -.
PDB; 4WRN; X-ray; 3.20 A; A/B=295-610.
PDBsum; 4WRN; -.
ProteinModelPortal; P07911; -.
SMR; P07911; -.
BioGrid; 113216; 2.
IntAct; P07911; 2.
STRING; 9606.ENSP00000306279; -.
GlyConnect; 613; -.
iPTMnet; P07911; -.
PhosphoSitePlus; P07911; -.
UniCarbKB; P07911; -.
BioMuta; UMOD; -.
DMDM; 137116; -.
PaxDb; P07911; -.
PeptideAtlas; P07911; -.
PRIDE; P07911; -.
ProteomicsDB; 52038; -.
ProteomicsDB; 52039; -. [P07911-2]
ProteomicsDB; 52040; -. [P07911-3]
ProteomicsDB; 52041; -. [P07911-4]
Ensembl; ENST00000302509; ENSP00000306279; ENSG00000169344. [P07911-1]
Ensembl; ENST00000396134; ENSP00000379438; ENSG00000169344. [P07911-5]
Ensembl; ENST00000570689; ENSP00000460548; ENSG00000169344. [P07911-1]
GeneID; 7369; -.
KEGG; hsa:7369; -.
UCSC; uc002dgz.5; human. [P07911-1]
CTD; 7369; -.
DisGeNET; 7369; -.
EuPathDB; HostDB:ENSG00000169344.15; -.
GeneCards; UMOD; -.
GeneReviews; UMOD; -.
H-InvDB; HIX0012858; -.
HGNC; HGNC:12559; UMOD.
HPA; CAB009446; -.
HPA; HPA043420; -.
HPA; HPA054721; -.
MalaCards; UMOD; -.
MIM; 162000; phenotype.
MIM; 191845; gene.
MIM; 603860; phenotype.
MIM; 609886; phenotype.
neXtProt; NX_P07911; -.
OpenTargets; ENSG00000169344; -.
Orphanet; 34149; Autosomal dominant medullary cystic kidney disease with or without hyperuricemia.
Orphanet; 209886; Familial juvenile hyperuricemic nephropathy type 1.
PharmGKB; PA37199; -.
eggNOG; ENOG410IVSV; Eukaryota.
eggNOG; ENOG410YDU6; LUCA.
GeneTree; ENSGT00530000063244; -.
HOGENOM; HOG000293303; -.
HOVERGEN; HBG004349; -.
InParanoid; P07911; -.
KO; K18274; -.
PhylomeDB; P07911; -.
TreeFam; TF330284; -.
Reactome; R-HSA-446203; Asparagine N-linked glycosylation.
SIGNOR; P07911; -.
GeneWiki; Tamm%E2%80%93Horsfall_protein; -.
GenomeRNAi; 7369; -.
PRO; PR:P07911; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000169344; -.
CleanEx; HS_UMOD; -.
ExpressionAtlas; P07911; baseline and differential.
Genevisible; P07911; HS.
GO; GO:0031225; C:anchored component of membrane; IDA:UniProtKB.
GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB.
GO; GO:0060170; C:ciliary membrane; IEA:UniProtKB-SubCell.
GO; GO:0005929; C:cilium; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0019898; C:extrinsic component of membrane; TAS:ProtInc.
GO; GO:0005796; C:Golgi lumen; TAS:Reactome.
GO; GO:0000922; C:spindle pole; IDA:UniProtKB.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0019864; F:IgG binding; IDA:BHF-UCL.
GO; GO:0006968; P:cellular defense response; TAS:ProtInc.
GO; GO:0007588; P:excretion; IEA:Ensembl.
GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; IDA:BHF-UCL.
GO; GO:0050801; P:ion homeostasis; IEA:Ensembl.
GO; GO:0007159; P:leukocyte cell-cell adhesion; IDA:BHF-UCL.
GO; GO:0072218; P:metanephric ascending thin limb development; IEA:Ensembl.
GO; GO:0072221; P:metanephric distal convoluted tubule development; IEA:Ensembl.
GO; GO:0072233; P:metanephric thick ascending limb development; IEA:Ensembl.
GO; GO:0008285; P:negative regulation of cell proliferation; TAS:ProtInc.
GO; GO:1990266; P:neutrophil migration; IDA:BHF-UCL.
InterPro; IPR001881; EGF-like_Ca-bd_dom.
InterPro; IPR013032; EGF-like_CS.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
InterPro; IPR018097; EGF_Ca-bd_CS.
InterPro; IPR024731; EGF_dom.
InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
InterPro; IPR001507; ZP_dom.
InterPro; IPR017977; ZP_dom_CS.
Pfam; PF12947; EGF_3; 1.
Pfam; PF07645; EGF_CA; 2.
Pfam; PF00100; Zona_pellucida; 1.
PRINTS; PR00023; ZPELLUCIDA.
SMART; SM00181; EGF; 3.
SMART; SM00179; EGF_CA; 2.
SMART; SM00241; ZP; 1.
SUPFAM; SSF57184; SSF57184; 1.
PROSITE; PS00010; ASX_HYDROXYL; 2.
PROSITE; PS01186; EGF_2; 3.
PROSITE; PS50026; EGF_3; 3.
PROSITE; PS01187; EGF_CA; 2.
PROSITE; PS00682; ZP_1; 1.
PROSITE; PS51034; ZP_2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell membrane; Cell projection;
Ciliopathy; Cilium; Complete proteome; Direct protein sequencing;
Disease mutation; Disulfide bond; EGF-like domain; Glycoprotein;
GPI-anchor; Lipoprotein; Membrane; Nephronophthisis; Polymorphism;
Reference proteome; Repeat; Secreted; Signal.
SIGNAL 1 24
CHAIN 25 614 Uromodulin.
/FTId=PRO_0000041671.
CHAIN 25 587 Uromodulin, secreted form.
/FTId=PRO_0000407909.
PROPEP 615 640 Removed in mature form. {ECO:0000255}.
/FTId=PRO_0000041672.
DOMAIN 28 64 EGF-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 65 107 EGF-like 2; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 108 149 EGF-like 3; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 334 589 ZP. {ECO:0000255|PROSITE-
ProRule:PRU00375}.
REGION 430 453 Important for secretion and
polymerization into filaments.
{ECO:0000269|PubMed:26811476}.
REGION 586 589 Essential for cleavage by HPN.
{ECO:0000269|PubMed:19005207,
ECO:0000269|PubMed:26673890,
ECO:0000269|PubMed:26811476}.
REGION 598 607 Regulates polymerization into filaments.
{ECO:0000269|PubMed:19005207}.
SITE 587 588 Cleavage. {ECO:0000269|PubMed:18375198}.
LIPID 614 614 GPI-anchor amidated serine.
{ECO:0000255}.
CARBOHYD 38 38 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 76 76 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 80 80 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 232 232 N-linked (GlcNAc...) (complex)
asparagine. {ECO:0000269|PubMed:22171320,
ECO:0000269|PubMed:26811476}.
CARBOHYD 275 275 N-linked (GlcNAc...) asparagine.
/FTId=CAR_000178.
CARBOHYD 322 322 N-linked (GlcNAc...) (complex)
asparagine.
{ECO:0000269|PubMed:22171320}.
CARBOHYD 396 396 N-linked (GlcNAc...) (complex)
asparagine.
{ECO:0000269|PubMed:22171320}.
DISULFID 32 41 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 35 50 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 52 63 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 69 83 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 77 92 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 94 106 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 112 126 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 120 135 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 137 148 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 297 306 {ECO:0000269|PubMed:26811476}.
DISULFID 300 315 {ECO:0000269|PubMed:26811476}.
DISULFID 317 347 {ECO:0000269|PubMed:26811476}.
DISULFID 335 425 {ECO:0000269|PubMed:26811476}.
DISULFID 366 389 {ECO:0000269|PubMed:26811476}.
DISULFID 506 566 {ECO:0000255|PROSITE-ProRule:PRU00076,
ECO:0000269|PubMed:26811476}.
DISULFID 527 582 {ECO:0000269|PubMed:26811476}.
DISULFID 571 578 {ECO:0000269|PubMed:26811476}.
VAR_SEQ 29 29 A -> ARTKYNCPARWSWRTPQRGGDTEQGPDEDFTSQG
(in isoform 5).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_054828.
VAR_SEQ 67 199 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_017565.
VAR_SEQ 133 154 Missing (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_040973.
VAR_SEQ 205 234 FVGQGGARMAETCVPVLRCNTAAPMWLNGT -> P (in
isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_017566.
VARIANT 52 52 C -> W (in HNFJ1).
{ECO:0000269|PubMed:15086896}.
/FTId=VAR_073052.
VARIANT 59 59 D -> A (in HNFJ1; results in defective
trafficking of mutant protein to the
plasma membrane; the mutant is retained
in the ER). {ECO:0000269|PubMed:14569098,
ECO:0000269|PubMed:17010121}.
/FTId=VAR_073053.
VARIANT 77 77 C -> Y (in HNFJ1; dbSNP:rs121917768).
{ECO:0000269|PubMed:12629136}.
/FTId=VAR_025950.
VARIANT 93 97 VCPEG -> AASC (in MCKD2; results in
mutant retention in the ER; results is
abnormal intracellular polymerization of
the mutant protein).
{ECO:0000269|PubMed:14531790,
ECO:0000269|PubMed:25436415}.
/FTId=VAR_025951.
VARIANT 103 103 G -> C (in MCKD2; dbSNP:rs28934584).
{ECO:0000269|PubMed:12471200}.
/FTId=VAR_017666.
VARIANT 109 109 V -> E (in HNFJ1; causes a delay in
protein export to the plasma membrane due
to a longer retention time in the ER;
dbSNP:rs780462125).
{ECO:0000269|PubMed:23988501}.
/FTId=VAR_071398.
VARIANT 112 112 C -> R (in HNFJ1).
{ECO:0000269|PubMed:14569098}.
/FTId=VAR_073054.
VARIANT 120 120 C -> G (in MCKD2; serum levels severely
reduced). {ECO:0000269|PubMed:27729211}.
/FTId=VAR_077514.
VARIANT 126 126 C -> R (in HNFJ1; dbSNP:rs121917769).
{ECO:0000269|PubMed:12629136,
ECO:0000269|PubMed:14569098}.
/FTId=VAR_025952.
VARIANT 128 128 N -> S (in HNFJ1; results in defective
trafficking of mutant protein to the
plasma membrane; the mutant is retained
in the ER; dbSNP:rs121917770).
{ECO:0000269|PubMed:12629136,
ECO:0000269|PubMed:17010121}.
/FTId=VAR_025953.
VARIANT 135 135 C -> S (in HNFJ1).
{ECO:0000269|PubMed:15086896}.
/FTId=VAR_073055.
VARIANT 148 148 C -> W (in HNFJ1; phenotype overlapping
with medullary cystic kidney disease;
causes a delay in protein export to the
plasma membrane due to a longer retention
time in the ER).
{ECO:0000269|PubMed:14570709,
ECO:0000269|PubMed:17010121}.
/FTId=VAR_025954.
VARIANT 148 148 C -> Y (in HNFJ1; dbSNP:rs28934582).
{ECO:0000269|PubMed:12471200}.
/FTId=VAR_017667.
VARIANT 150 150 C -> S (in HNFJ1; phenotype overlapping
with medullary cystic kidney disease;
causes a delay in protein export to the
plasma membrane due to a longer retention
time in the ER; results is abnormal
intracellular polymerization of the
mutant protein).
{ECO:0000269|PubMed:14570709,
ECO:0000269|PubMed:17010121,
ECO:0000269|PubMed:25436415}.
/FTId=VAR_025955.
VARIANT 155 155 C -> R (probable-disease association
mutation found in a patient with cystic
kidney disease; results in mutant
retention in the ER; results is abnormal
intracellular polymerization of the
mutant protein).
{ECO:0000269|PubMed:25436415}.
/FTId=VAR_073056.
VARIANT 170 170 C -> Y (in HNFJ1).
{ECO:0000269|PubMed:14569098}.
/FTId=VAR_073057.
VARIANT 185 185 R -> S (in HNFJ1).
{ECO:0000269|PubMed:14569098}.
/FTId=VAR_073058.
VARIANT 195 195 C -> F (in HNFJ1).
{ECO:0000269|PubMed:15086896}.
/FTId=VAR_073059.
VARIANT 202 202 W -> S (in HNFJ1).
{ECO:0000269|PubMed:15086896}.
/FTId=VAR_073060.
VARIANT 204 204 R -> G (in HNFJ1; results in defective
trafficking of mutant protein to the
plasma membrane; the mutant is retained
in the ER). {ECO:0000269|PubMed:14569098,
ECO:0000269|PubMed:17010121}.
/FTId=VAR_073061.
VARIANT 217 217 C -> G (in HNFJ1; dbSNP:rs28934583).
{ECO:0000269|PubMed:14569098}.
/FTId=VAR_073062.
VARIANT 217 217 C -> R (in HNFJ1; results in defective
trafficking of mutant protein to the
plasma membrane; the mutant is retained
in the ER; dbSNP:rs28934583).
{ECO:0000269|PubMed:12471200,
ECO:0000269|PubMed:17010121}.
/FTId=VAR_017668.
VARIANT 222 222 R -> P (in HNFJ1).
{ECO:0000269|PubMed:14569098}.
/FTId=VAR_073063.
VARIANT 223 223 C -> Y (in HNFJ1).
{ECO:0000269|PubMed:12900848}.
/FTId=VAR_025956.
VARIANT 225 225 T -> K (in MCKD2; results in defective
trafficking of mutant protein to the
plasma membrane; the mutant is retained
in the ER). {ECO:0000269|PubMed:14531790,
ECO:0000269|PubMed:17010121}.
/FTId=VAR_025957.
VARIANT 225 225 T -> M (in HNFJ1).
{ECO:0000269|PubMed:14569098}.
/FTId=VAR_073064.
VARIANT 230 230 W -> R (in HNFJ1).
{ECO:0000269|PubMed:23197950}.
/FTId=VAR_071399.
VARIANT 236 236 P -> L (in HNFJ1).
{ECO:0000269|PubMed:15086896}.
/FTId=VAR_073065.
VARIANT 236 236 P -> Q (in HNFJ1; causes a delay in
protein export to the plasma membrane due
to a longer retention time in the ER).
{ECO:0000269|PubMed:23988501}.
/FTId=VAR_071400.
VARIANT 236 236 P -> R (in HNFJ1; results in defective
trafficking of mutant protein to the
plasma membrane; the mutant is retained
in the ER).
{ECO:0000269|PubMed:17010121}.
/FTId=VAR_073066.
VARIANT 248 248 C -> W (in MCKD2 and HNFJ1; causes a
delay in protein export to the plasma
membrane due to a longer retention time
in the ER; dbSNP:rs886043751).
{ECO:0000269|PubMed:14531790,
ECO:0000269|PubMed:23988501}.
/FTId=VAR_025958.
VARIANT 255 255 C -> Y (in HNFJ1; dbSNP:rs121917771).
{ECO:0000269|PubMed:12629136}.
/FTId=VAR_025959.
VARIANT 282 282 C -> R (in HNFJ1).
{ECO:0000269|PubMed:14569098}.
/FTId=VAR_073067.
VARIANT 300 300 C -> G (in HNFJ1; dbSNP:rs121917772).
{ECO:0000269|PubMed:12629136}.
/FTId=VAR_025960.
VARIANT 315 315 C -> R (in GCKDHI; causes a delay in
protein export to the plasma membrane due
to a longer retention time in the ER;
dbSNP:rs121917773).
{ECO:0000269|PubMed:14570709,
ECO:0000269|PubMed:17010121}.
/FTId=VAR_025961.
VARIANT 316 316 Q -> P (in HNFJ1).
{ECO:0000269|PubMed:15983957}.
/FTId=VAR_073068.
VARIANT 317 317 C -> Y (in HNFJ1; phenotype overlapping
with medullary cystic kidney disease;
causes a delay in protein export to the
plasma membrane due to a longer retention
time in the ER).
{ECO:0000269|PubMed:14570709}.
/FTId=VAR_025962.
VARIANT 347 347 C -> G (in HNFJ1; causes a delay in
protein export to the plasma membrane due
to a longer retention time in the ER).
{ECO:0000269|PubMed:15575003}.
/FTId=VAR_073069.
VARIANT 458 458 V -> L (in dbSNP:rs55772253).
/FTId=VAR_061993.
VARIANT 461 461 A -> E (in HNFJ1).
{ECO:0000269|PubMed:21060763}.
/FTId=VAR_071401.
MUTAGEN 333 333 L->K: Abolishes polymerization and
filament formation of the secreted form.
{ECO:0000269|PubMed:26811476}.
MUTAGEN 421 421 I->K: Abolishes polymerization and
filament formation of the secreted form.
{ECO:0000269|PubMed:26811476}.
MUTAGEN 430 430 D->L: Impairs polymerization and filament
formation of the secreted form.
{ECO:0000269|PubMed:19005207}.
MUTAGEN 435 435 L->S: Impairs polymerization and filament
formation of the secreted form.
{ECO:0000269|PubMed:19005207}.
MUTAGEN 458 458 V->R: Leads to retention in the
endoplasmic reticulum, probably due to
misfolding.
{ECO:0000269|PubMed:19005207}.
MUTAGEN 586 589 RFRS->AAAA: Abolishes cleavage by HPN.
{ECO:0000269|PubMed:19005207,
ECO:0000269|PubMed:26673890,
ECO:0000269|PubMed:26811476}.
MUTAGEN 598 600 VLN->AAA: Decreased export from the
endoplasmic reticulum, leading to
decreased secretion. Impairs
polymerization.
{ECO:0000269|PubMed:19005207}.
MUTAGEN 602 603 GP->AA: Decreased export from the
endoplasmic reticulum, leading to
decreased secretion. Impairs
polymerization.
{ECO:0000269|PubMed:19005207}.
MUTAGEN 605 607 TRK->AAA: No effect on secretion. Does
not impair polymerization.
{ECO:0000269|PubMed:19005207}.
CONFLICT 288 288 T -> A (in Ref. 4; BAG51560).
{ECO:0000305}.
CONFLICT 503 503 M -> I (in Ref. 4; BAG51560).
{ECO:0000305}.
CONFLICT 565 565 H -> D (in Ref. 2; AAA36799).
{ECO:0000305}.
HELIX 296 299 {ECO:0000244|PDB:4WRN}.
STRAND 304 308 {ECO:0000244|PDB:4WRN}.
STRAND 313 317 {ECO:0000244|PDB:4WRN}.
HELIX 327 329 {ECO:0000244|PDB:4WRN}.
STRAND 332 335 {ECO:0000244|PDB:4WRN}.
STRAND 337 345 {ECO:0000244|PDB:4WRN}.
HELIX 346 350 {ECO:0000244|PDB:4WRN}.
TURN 351 353 {ECO:0000244|PDB:4WRN}.
STRAND 377 387 {ECO:0000244|PDB:4WRN}.
HELIX 388 390 {ECO:0000244|PDB:4WRN}.
STRAND 392 395 {ECO:0000244|PDB:4WRN}.
STRAND 397 408 {ECO:0000244|PDB:4WRN}.
TURN 411 414 {ECO:0000244|PDB:4WRN}.
STRAND 419 428 {ECO:0000244|PDB:4WRN}.
HELIX 431 437 {ECO:0000244|PDB:4WRN}.
STRAND 438 441 {ECO:0000244|PDB:4WRN}.
STRAND 443 450 {ECO:0000244|PDB:4WRN}.
TURN 451 453 {ECO:0000244|PDB:4WRN}.
STRAND 454 465 {ECO:0000244|PDB:4WRN}.
STRAND 473 475 {ECO:0000244|PDB:4WRN}.
STRAND 477 479 {ECO:0000244|PDB:4WRN}.
STRAND 485 494 {ECO:0000244|PDB:4WRN}.
TURN 496 498 {ECO:0000244|PDB:4WRN}.
STRAND 499 512 {ECO:0000244|PDB:4WRN}.
STRAND 520 524 {ECO:0000244|PDB:4WRN}.
STRAND 527 529 {ECO:0000244|PDB:4WRN}.
STRAND 535 550 {ECO:0000244|PDB:4WRN}.
HELIX 552 555 {ECO:0000244|PDB:4WRN}.
STRAND 560 572 {ECO:0000244|PDB:4WRN}.
TURN 573 575 {ECO:0000244|PDB:4WRN}.
HELIX 595 597 {ECO:0000244|PDB:4WRN}.
STRAND 598 606 {ECO:0000244|PDB:4WRN}.
SEQUENCE 640 AA; 69761 MW; D26A07A76353AE48 CRC64;
MGQPSLTWML MVVVASWFIT TAATDTSEAR WCSECHSNAT CTEDEAVTTC TCQEGFTGDG
LTCVDLDECA IPGAHNCSAN SSCVNTPGSF SCVCPEGFRL SPGLGCTDVD ECAEPGLSHC
HALATCVNVV GSYLCVCPAG YRGDGWHCEC SPGSCGPGLD CVPEGDALVC ADPCQAHRTL
DEYWRSTEYG EGYACDTDLR GWYRFVGQGG ARMAETCVPV LRCNTAAPMW LNGTHPSSDE
GIVSRKACAH WSGHCCLWDA SVQVKACAGG YYVYNLTAPP ECHLAYCTDP SSVEGTCEEC
SIDEDCKSNN GRWHCQCKQD FNITDISLLE HRLECGANDM KVSLGKCQLK SLGFDKVFMY
LSDSRCSGFN DRDNRDWVSV VTPARDGPCG TVLTRNETHA TYSNTLYLAD EIIIRDLNIK
INFACSYPLD MKVSLKTALQ PMVSALNIRV GGTGMFTVRM ALFQTPSYTQ PYQGSSVTLS
TEAFLYVGTM LDGGDLSRFA LLMTNCYATP SSNATDPLKY FIIQDRCPHT RDSTIQVVEN
GESSQGRFSV QMFRFAGNYD LVYLHCEVYL CDTMNEKCKP TCSGTRFRSG SVIDQSRVLN
LGPITRKGVQ ATVSRAFSSL GLLKVWLPLL LSATLTLTFQ


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