P07911 (UROM_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Uromodulin

Alternative name(s):
Tamm-Horsfall urinary glycoprotein
Short name=THP

Cleaved into the following chain:

1. Uromodulin, secreted form

Gene names

Name:

UMOD

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	640 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

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 providing the water barrier permeability. May serve as a receptor for binding and endocytosis for cytokines (IL-1, IL-2) and TNF. Facilitates neutrophil migration across renal epithelial. Ref.10 Uromodulin, secreted form: Secreted into urine after proteolytically cleaveage. Into the urine, may contribute to colloid osmotic pressure, retards passage of positively charged electrolytes, prevents urinary tract infection and modulates formation of supersaturated salts and their crystals. Ref.10
Subcellular location	Apical cell membrane; Lipid-anchor › GPI-anchor. Basolateral cell membrane; Lipid-anchor › GPI-anchor. Cell projection › cilium membrane. Note: Only a small fraction is sort to the basolateral pole of tubular epithelial cells compared to apical localization. Secreted into urine after cleavage. Colocalized with NPHP1 and KIF3A. Ref.8 Ref.9 Ref.10 Ref.11 Uromodulin, secreted form: Secreted Ref.8 Ref.10 Ref.11.
Tissue specificity	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. Most abundant protein in normal urine. Ref.8
Domain	The ZP domain is involved in the polymerization of the protein to promote the formation of complex gel-like structure.
Post-translational modification	N-glycosylated. 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). Ref.12 Proteolytically cleaved at a conserved C-terminal proteolytic cleavage site to generate the secreted form found into urine. Ref.7
Involvement in 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. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.3 Ref.13 Ref.15 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. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.3 Ref.14 Ref.16 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. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.14
Miscellaneous	A specific, but as yet unidentified, protease(s) cleaves off and releases UMOD into urine.
Sequence similarities	Contains 3 EGF-like domains. Contains 1 ZP domain.

Ontologies

Keywords
Cellular component	Cell membrane Cell projection Cilium Membrane Secreted
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Ciliopathy Disease mutation Nephronophthisis
Domain	EGF-like domain Repeat Signal
PTM	Disulfide bond GPI-anchor Glycoprotein Lipoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cellular defense response Traceable author statement PubMed 2409603. Source: ProtInc chemical homeostasis Inferred from electronic annotation. Source: Compara excretion Inferred from electronic annotation. Source: Compara metanephric ascending thin limb development Inferred from electronic annotation. Source: Compara metanephric distal convoluted tubule development Inferred from electronic annotation. Source: Compara metanephric thick ascending limb development Inferred from electronic annotation. Source: Compara negative regulation of cell proliferation Traceable author statement PubMed 2409603. Source: ProtInc regulation of ion homeostasis Inferred from electronic annotation. Source: Compara response to organic substance Inferred from electronic annotation. Source: Compara
Cellular_component	Golgi apparatus Inferred from electronic annotation. Source: Compara anchored to membrane Inferred from direct assay PubMed 91065873. Source: UniProtKB apical plasma membrane Inferred from direct assay Ref.8. Source: UniProtKB basolateral plasma membrane Inferred from direct assay Ref.8. Source: UniProtKB cilium membrane Inferred from electronic annotation. Source: UniProtKB-SubCell cytoplasmic vesicle Inferred from electronic annotation. Source: Compara extracellular space Inferred from electronic annotation. Source: Compara extrinsic to membrane Traceable author statement PubMed 7873609. Source: ProtInc membrane raft Inferred from electronic annotation. Source: Compara primary cilium Inferred from direct assay Ref.11. Source: UniProtKB spindle pole Inferred from direct assay Ref.11. Source: UniProtKB
Molecular_function	calcium ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P07911-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P07911-2)

The sequence of this isoform differs from the canonical sequence as follows:
     67-199: Missing.

Note: No experimental confirmation available.

Isoform 3 (identifier: P07911-3)

The sequence of this isoform differs from the canonical sequence as follows:
     205-234: FVGQGGARMAETCVPVLRCNTAAPMWLNGT → P

Note: No experimental confirmation available.

Isoform 4 (identifier: P07911-4)

The sequence of this isoform differs from the canonical sequence as follows:
     133-154: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 24	24
	Chain	25 – 614	590	Uromodulin		PRO_0000041671
	Chain	25 – 587	563	Uromodulin, secreted form		PRO_0000407909
	Propeptide	615 – 640	26	Removed in mature form Potential		PRO_0000041672
Regions
	Domain	28 – 64	37	EGF-like 1
	Domain	65 – 107	43	EGF-like 2; calcium-binding Potential
	Domain	108 – 149	42	EGF-like 3; calcium-binding Potential
	Domain	334 – 589	256	ZP
Sites
	Site	587 – 588	2	Cleavage
Amino acid modifications
	Lipidation	614	1	GPI-anchor amidated serine Potential
	Glycosylation	38	1	N-linked (GlcNAc...) Potential
	Glycosylation	76	1	N-linked (GlcNAc...) Potential
	Glycosylation	80	1	N-linked (GlcNAc...) Potential
	Glycosylation	232	1	N-linked (GlcNAc...) (complex) Ref.12
	Glycosylation	275	1	N-linked (GlcNAc...)		CAR_000178
	Glycosylation	322	1	N-linked (GlcNAc...) (complex) Ref.12
	Glycosylation	396	1	N-linked (GlcNAc...) (complex) Ref.12
	Disulfide bond	32 ↔ 41		By similarity
	Disulfide bond	35 ↔ 50		By similarity
	Disulfide bond	52 ↔ 63		By similarity
	Disulfide bond	69 ↔ 83		By similarity
	Disulfide bond	77 ↔ 92		By similarity
	Disulfide bond	94 ↔ 106		By similarity
	Disulfide bond	112 ↔ 126		By similarity
	Disulfide bond	120 ↔ 135		By similarity
	Disulfide bond	137 ↔ 148		By similarity
	Disulfide bond	506 ↔ 566		By similarity
Natural variations
	Alternative sequence	67 – 199	133	Missing in isoform 2.		VSP_017565
	Alternative sequence	133 – 154	22	Missing in isoform 4.		VSP_040973
	Alternative sequence	205 – 234	30	FVGQG…WLNGT → P in isoform 3.		VSP_017566
	Natural variant	77	1	C → Y in HNFJ1. Ref.15		VAR_025950
	Natural variant	93 – 97	5	VCPEG → AASC in MCKD2.		VAR_025951
	Natural variant	103	1	G → C in MCKD2. Ref.3 Corresponds to variant rs28934584 [ dbSNP | Ensembl ].		VAR_017666
	Natural variant	126	1	C → R in HNFJ1. Ref.15		VAR_025952
	Natural variant	128	1	N → S in HNFJ1. Ref.15		VAR_025953
	Natural variant	148	1	C → W in MCKD2/HNFJ1; causes a delay in protein export to the plasma membrane due to a longer retention time in the ER. Ref.14		VAR_025954
	Natural variant	148	1	C → Y in HNFJ1. Ref.3 Corresponds to variant rs28934582 [ dbSNP | Ensembl ].		VAR_017667
	Natural variant	150	1	C → S in MCKD2/HNFJ1; causes a delay in protein export to the plasma membrane due to a longer retention time in the ER. Ref.14		VAR_025955
	Natural variant	217	1	C → R in HNFJ1. Ref.3 Corresponds to variant rs28934583 [ dbSNP | Ensembl ].		VAR_017668
	Natural variant	223	1	C → Y in HNFJ1. Ref.13		VAR_025956
	Natural variant	225	1	T → K in MCKD2. Ref.16		VAR_025957
	Natural variant	248	1	C → W in MCKD2. Ref.16		VAR_025958
	Natural variant	255	1	C → Y in HNFJ1. Ref.15		VAR_025959
	Natural variant	300	1	C → G in HNFJ1. Ref.15		VAR_025960
	Natural variant	315	1	C → R in GCKDHI; causes a delay in protein export to the plasma membrane due to a longer retention time in the ER. Ref.14		VAR_025961
	Natural variant	317	1	C → Y in MCKD2/HNFJ1; causes a delay in protein export to the plasma membrane due to a longer retention time in the ER. Ref.14		VAR_025962
	Natural variant	458	1	V → L. Corresponds to variant rs55772253 [ dbSNP | Ensembl ].		VAR_061993
Experimental info
	Sequence conflict	288	1	T → A in BAG51560. Ref.4
	Sequence conflict	503	1	M → I in BAG51560. Ref.4
	Sequence conflict	565	1	H → D in AAA36799. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified August 1, 1988. Version 1. Checksum: D26A07A76353AE48	FASTA	640	69,761
	10 20 30 40 50 60 MGQPSLTWML MVVVASWFIT TAATDTSEAR WCSECHSNAT CTEDEAVTTC TCQEGFTGDG 70 80 90 100 110 120 LTCVDLDECA IPGAHNCSAN SSCVNTPGSF SCVCPEGFRL SPGLGCTDVD ECAEPGLSHC 130 140 150 160 170 180 HALATCVNVV GSYLCVCPAG YRGDGWHCEC SPGSCGPGLD CVPEGDALVC ADPCQAHRTL 190 200 210 220 230 240 DEYWRSTEYG EGYACDTDLR GWYRFVGQGG ARMAETCVPV LRCNTAAPMW LNGTHPSSDE 250 260 270 280 290 300 GIVSRKACAH WSGHCCLWDA SVQVKACAGG YYVYNLTAPP ECHLAYCTDP SSVEGTCEEC 310 320 330 340 350 360 SIDEDCKSNN GRWHCQCKQD FNITDISLLE HRLECGANDM KVSLGKCQLK SLGFDKVFMY 370 380 390 400 410 420 LSDSRCSGFN DRDNRDWVSV VTPARDGPCG TVLTRNETHA TYSNTLYLAD EIIIRDLNIK 430 440 450 460 470 480 INFACSYPLD MKVSLKTALQ PMVSALNIRV GGTGMFTVRM ALFQTPSYTQ PYQGSSVTLS 490 500 510 520 530 540 TEAFLYVGTM LDGGDLSRFA LLMTNCYATP SSNATDPLKY FIIQDRCPHT RDSTIQVVEN 550 560 570 580 590 600 GESSQGRFSV QMFRFAGNYD LVYLHCEVYL CDTMNEKCKP TCSGTRFRSG SVIDQSRVLN 610 620 630 640 LGPITRKGVQ ATVSRAFSSL GLLKVWLPLL LSATLTLTFQ
	Isoform 2 [UniParc]. Checksum: FBFC739EA15E3D22	FASTA	507	55,960
	10 20 30 40 50 60 MGQPSLTWML MVVVASWFIT TAATDTSEAR WCSECHSNAT CTEDEAVTTC TCQEGFTGDG 70 80 90 100 110 120 LTCVDLRGWY RFVGQGGARM AETCVPVLRC NTAAPMWLNG THPSSDEGIV SRKACAHWSG 130 140 150 160 170 180 HCCLWDASVQ VKACAGGYYV YNLTAPPECH LAYCTDPSSV EGTCEECSID EDCKSNNGRW 190 200 210 220 230 240 HCQCKQDFNI TDISLLEHRL ECGANDMKVS LGKCQLKSLG FDKVFMYLSD SRCSGFNDRD 250 260 270 280 290 300 NRDWVSVVTP ARDGPCGTVL TRNETHATYS NTLYLADEII IRDLNIKINF ACSYPLDMKV 310 320 330 340 350 360 SLKTALQPMV SALNIRVGGT GMFTVRMALF QTPSYTQPYQ GSSVTLSTEA FLYVGTMLDG 370 380 390 400 410 420 GDLSRFALLM TNCYATPSSN ATDPLKYFII QDRCPHTRDS TIQVVENGES SQGRFSVQMF 430 440 450 460 470 480 RFAGNYDLVY LHCEVYLCDT MNEKCKPTCS GTRFRSGSVI DQSRVLNLGP ITRKGVQATV 490 500 SRAFSSLGLL KVWLPLLLSA TLTLTFQ
	Isoform 3 [UniParc]. Checksum: 459663CEADC74EA3	FASTA	611	66,724
	10 20 30 40 50 60 MGQPSLTWML MVVVASWFIT TAATDTSEAR WCSECHSNAT CTEDEAVTTC TCQEGFTGDG 70 80 90 100 110 120 LTCVDLDECA IPGAHNCSAN SSCVNTPGSF SCVCPEGFRL SPGLGCTDVD ECAEPGLSHC 130 140 150 160 170 180 HALATCVNVV GSYLCVCPAG YRGDGWHCEC SPGSCGPGLD CVPEGDALVC ADPCQAHRTL 190 200 210 220 230 240 DEYWRSTEYG EGYACDTDLR GWYRPHPSSD EGIVSRKACA HWSGHCCLWD ASVQVKACAG 250 260 270 280 290 300 GYYVYNLTAP PECHLAYCTD PSSVEGTCEE CSIDEDCKSN NGRWHCQCKQ DFNITDISLL 310 320 330 340 350 360 EHRLECGAND MKVSLGKCQL KSLGFDKVFM YLSDSRCSGF NDRDNRDWVS VVTPARDGPC 370 380 390 400 410 420 GTVLTRNETH ATYSNTLYLA DEIIIRDLNI KINFACSYPL DMKVSLKTAL QPMVSALNIR 430 440 450 460 470 480 VGGTGMFTVR MALFQTPSYT QPYQGSSVTL STEAFLYVGT MLDGGDLSRF ALLMTNCYAT 490 500 510 520 530 540 PSSNATDPLK YFIIQDRCPH TRDSTIQVVE NGESSQGRFS VQMFRFAGNY DLVYLHCEVY 550 560 570 580 590 600 LCDTMNEKCK PTCSGTRFRS GSVIDQSRVL NLGPITRKGV QATVSRAFSS LGLLKVWLPL 610 LLSATLTLTF Q
	Isoform 4 [UniParc]. Checksum: AF3732AED73ADEF2	FASTA	618	67,418
	10 20 30 40 50 60 MGQPSLTWML MVVVASWFIT TAATDTSEAR WCSECHSNAT CTEDEAVTTC TCQEGFTGDG 70 80 90 100 110 120 LTCVDLDECA IPGAHNCSAN SSCVNTPGSF SCVCPEGFRL SPGLGCTDVD ECAEPGLSHC 130 140 150 160 170 180 HALATCVNVV GSCGPGLDCV PEGDALVCAD PCQAHRTLDE YWRSTEYGEG YACDTDLRGW 190 200 210 220 230 240 YRFVGQGGAR MAETCVPVLR CNTAAPMWLN GTHPSSDEGI VSRKACAHWS GHCCLWDASV 250 260 270 280 290 300 QVKACAGGYY VYNLTAPPEC HLAYCTDPSS VEGTCEECSI DEDCKSNNGR WHCQCKQDFN 310 320 330 340 350 360 ITDISLLEHR LECGANDMKV SLGKCQLKSL GFDKVFMYLS DSRCSGFNDR DNRDWVSVVT 370 380 390 400 410 420 PARDGPCGTV LTRNETHATY SNTLYLADEI IIRDLNIKIN FACSYPLDMK VSLKTALQPM 430 440 450 460 470 480 VSALNIRVGG TGMFTVRMAL FQTPSYTQPY QGSSVTLSTE AFLYVGTMLD GGDLSRFALL 490 500 510 520 530 540 MTNCYATPSS NATDPLKYFI IQDRCPHTRD STIQVVENGE SSQGRFSVQM FRFAGNYDLV 550 560 570 580 590 600 YLHCEVYLCD TMNEKCKPTC SGTRFRSGSV IDQSRVLNLG PITRKGVQAT VSRAFSSLGL 610 LKVWLPLLLS ATLTLTFQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of human uromodulin as the Tamm-Horsfall urinary glycoprotein." Pennica D., Kohr W.J., Kuang W.-J., Glaister D., Aggarwal B.B., Chen E.Y., Goeddel D.V. Science 236:83-88(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	"Uromodulin (Tamm-Horsfall glycoprotein): a renal ligand for lymphokines." 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. Science 237:1479-1484(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE.
[3]	"Mutations of the UMOD gene are responsible for medullary cystic kidney disease 2 and familial juvenile hyperuricaemic nephropathy." 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. J. Med. Genet. 39:882-892(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS HNFJ1 TYR-148 AND ARG-217, VARIANT MCKD2 CYS-103.
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." 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. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4). Tissue: Kidney.
[5]	"The sequence and analysis of duplication-rich human chromosome 16." 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. Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). Tissue: Kidney.
[7]	"Urinary uromodulin carries an intact ZP domain generated by a conserved C-terminal proteolytic cleavage." Santambrogio S., Cattaneo A., Bernascone I., Schwend T., Jovine L., Bachi A., Rampoldi L. Biochem. Biophys. Res. Commun. 370:410-413(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 578-587, PROTEOLYTIC CLEAVAGE, MASS SPECTROMETRY.
[8]	"Localization of Tamm-Horsfall glycoprotein in the human kidney using immuno-fluorescence and immuno-electron microscopical techniques." Sikri K.L., Foster C.L., MacHugh N., Marshall R.D. J. Anat. 132:597-605(1981) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
[9]	"Uromodulin (Tamm-Horsfall glycoprotein/uromucoid) is a phosphatidylinositol-linked membrane protein." Rindler M.J., Naik S.S., Li N., Hoops T.C., Peraldi M.-N. J. Biol. Chem. 265:20784-20789(1990) [PubMed] [Europe PMC] [Abstract] Cited for: GPI-ANCHOR.
[10]	"Uromodulin facilitates neutrophil migration across renal epithelial monolayers." Schmid M., Prajczer S., Gruber L.N., Bertocchi C., Gandini R., Pfaller W., Jennings P., Joannidis M. Cell. Physiol. Biochem. 26:311-318(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[11]	"Uromodulin is expressed in renal primary cilia and UMOD mutations result in decreased ciliary uromodulin expression." 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. Hum. Mol. Genet. 19:1985-1997(2010) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[12]	"Human urinary glycoproteomics; attachment site specific analysis of N-and O-linked glycosylations by CID and ECD." Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G. Mol. Cell. Proteomics 0:0-0(2011) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION AT ASN-232; ASN-322 AND ASN-396, STRUCTURE OF CARBOHYDRATES, MASS SPECTROMETRY.
[13]	"Renal manifestations of a mutation in the uromodulin (Tamm Horsfall protein) gene." Bleyer A.J., Trachtman H., Sandhu J., Gorry M.C., Hart T.C. Am. J. Kidney Dis. 42:E20-E26(2003) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT HNFJ1 TYR-223.
[14]	"Allelism of MCKD, FJHN and GCKD caused by impairment of uromodulin export dynamics." 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. Hum. Mol. Genet. 12:3369-3384(2003) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS MCKD2/HNFJ1 TRP-148; SER-150 AND TYR-317, VARIANT GCKDHI ARG-315, CHARACTERIZATION OF VARIANTS MCKD2/HNFJ1 TRP-148; SER-150 AND TYR-317, CHARACTERIZATION OF VARIANT GCKDHI ARG-315.
[15]	"UROMODULIN mutations cause familial juvenile hyperuricemic nephropathy." Turner J.J.O., Stacey J.M., Harding B., Kotanko P., Lhotta K., Puig J.G., Roberts I., Torres R.J., Thakker R.V. J. Clin. Endocrinol. Metab. 88:1398-1401(2003) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS HNFJ1 TYR-77; ARG-126; SER-128; TYR-255 AND GLY-300.
[16]	"Mutations of the Uromodulin gene in MCKD type 2 patients cluster in exon 4, which encodes three EGF-like domains." 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. Kidney Int. 64:1580-1587(2003) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS MCKD2 93-VAL--GLY-97 DELINS ALA-ALA-SER-CYS; LYS-225 AND TRP-248.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases
EMBL GenBank DDBJ	M15881 mRNA. Translation: AAA36798.1. M17778 mRNA. Translation: AAA36799.1. AY162970 , AY162963, AY162964, AY162965, AY162967, AY162968, AY162969 Genomic DNA. Translation: AAO64446.1. AK127643 mRNA. Translation: BAC87070.1. AK055722 mRNA. Translation: BAG51560.1. AK091961 mRNA. Translation: BAG52451.1. AC106796 Genomic DNA. No translation available. BC035975 mRNA. Translation: AAH35975.1.
IPI	IPI00013945. IPI00744076. IPI00902653. IPI01013836.
PIR	A30452.
RefSeq	NP_001008390.1. NM_001008389.1. NP_003352.2. NM_003361.2.
UniGene	Hs.654425.
3D structure databases
ProteinModelPortal	P07911.
ModBase	Search...
Protein-protein interaction databases
IntAct	P07911. 2 interactions.
STRING	9606.ENSP00000306279.
PTM databases
GlycoSuiteDB	P07911.
Polymorphism databases
DMDM	137116.
Proteomic databases
PaxDb	P07911.
PRIDE	P07911.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000302509; ENSP00000306279; ENSG00000169344. ENST00000396142; ENSP00000379446; ENSG00000169344. ENST00000570689; ENSP00000460548; ENSG00000169344.
GeneID	7369.
KEGG	hsa:7369.
UCSC	uc002dgz.3. human.
Organism-specific databases
CTD	7369.
GeneCards	GC16M020344.
H-InvDB	HIX0012858.
HGNC	HGNC:12559. UMOD.
HPA	CAB009446.
MIM	162000. phenotype. 191845. gene. 603860. phenotype. 609886. phenotype.
neXtProt	NX_P07911.
Orphanet	34149. Autosomal dominant medullary cystic kidney disease with or without hyperuricemia. 209886. Familial juvenile hyperuricemic nephropathy type 1.
PharmGKB	PA37199.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG44010.
HOGENOM	HOG000293303.
HOVERGEN	HBG004349.
OrthoDB	EOG498V0G.
PhylomeDB	P07911.
Gene expression databases
ArrayExpress	P07911.
Bgee	P07911.
CleanEx	HS_UMOD.
Genevestigator	P07911.
GermOnline	ENSG00000169344. Homo sapiens.
Family and domain databases
Gene3D	2.40.155.10. 1 hit.
InterPro	IPR000742. EG-like_dom. IPR001881. EGF-like_Ca-bd. IPR013032. EGF-like_CS. IPR000152. EGF-type_Asp/Asn_hydroxyl_site. IPR018097. EGF_Ca-bd_CS. IPR024731. EGF_dom_MSP1-like. IPR023413. GFP_like. IPR009030. Growth_fac_rcpt. IPR001507. ZP_dom. IPR017977. ZP_dom_CS. [Graphical view]
Pfam	PF12947. EGF_3. 1 hit. PF07645. EGF_CA. 2 hits. PF00100. Zona_pellucida. 1 hit. [Graphical view]
PRINTS	PR00023. ZPELLUCIDA.
SMART	SM00181. EGF. 1 hit. SM00179. EGF_CA. 2 hits. SM00241. ZP. 1 hit. [Graphical view]
SUPFAM	SSF57184. Grow_fac_recept. 1 hit.
PROSITE	PS00010. ASX_HYDROXYL. 2 hits. PS00022. EGF_1. False negative. PS01186. EGF_2. 3 hits. PS50026. EGF_3. 3 hits. PS01187. EGF_CA. 2 hits. PS00682. ZP_1. 1 hit. PS51034. ZP_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	7369.
NextBio	28856.
SOURCE	Search...

Entry information

Entry name

UROM_HUMAN

Accession

Primary (citable) accession number: P07911
Secondary accession number(s): B3KP48 , B3KRN9, Q540J6, Q6ZS84, Q8IYG0

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	August 1, 1988
Last modified:	May 1, 2013
This is version 136 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.