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Q91X17 (UROM_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 110. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length642 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 By similarity. Ref.5 Ref.6

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.5 Ref.6

Subcellular location

Apical cell membrane; Lipid-anchorGPI-anchor By similarity. Basolateral cell membrane; Lipid-anchorGPI-anchor By similarity. Cell projectioncilium membrane By similarity. Note: Only a small fraction is sorts to the basolateral pole of tubular epithelial cells compared to apical localization By similarity.

Uromodulin, secreted form: Secreted By similarity.

Domain

The ZP domain is involved in the polymerization of the protein to promote the formation of complex gel-like structure. Ref.4

Post-translational modification

N-glycosylated. Ref.4

Disruption phenotype

Mice suffer significantly more frequently from urinary tract infections. They shown also spontaneous formation of calcium crystals in adult kidneys, and excessive intake of calcium and oxalate dramatically increases both the frequency and the severity of renal calcium crystal formation in deficient-mice but not in wild-type mice. Ref.5 Ref.6

Sequence similarities

Contains 3 EGF-like domains.

Contains 1 ZP domain.

Ontologies

Keywords
   Cellular componentCell membrane
Cell projection
Membrane
Secreted
   DomainEGF-like domain
Repeat
Signal
   PTMDisulfide bond
Glycoprotein
GPI-anchor
Lipoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processchemical homeostasis

Inferred from mutant phenotype PubMed 17264314. Source: MGI

excretion

Inferred from mutant phenotype PubMed 17264314. Source: MGI

metanephric ascending thin limb development

Inferred from expression pattern PubMed 18618131. Source: UniProtKB

metanephric distal convoluted tubule development

Inferred from expression pattern PubMed 18618131. Source: UniProtKB

metanephric thick ascending limb development

Inferred from expression pattern PubMed 18618131. Source: UniProtKB

regulation of ion homeostasis

Inferred from mutant phenotype Ref.6. Source: UniProtKB

response to organic substance

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentGolgi apparatus

Inferred from electronic annotation. Source: Ensembl

anchored component of membrane

Inferred from sequence or structural similarity. Source: UniProtKB

apical plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

basolateral plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

ciliary membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoplasmic vesicle

Inferred from electronic annotation. Source: Ensembl

extracellular space

Inferred from electronic annotation. Source: Ensembl

membrane raft

Inferred from electronic annotation. Source: Ensembl

primary cilium

Inferred from sequence or structural similarity. Source: UniProtKB

spindle pole

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functioncalcium ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Chain24 – 618595Uromodulin
PRO_0000041673
Chain25 – 588564Uromodulin, secreted form By similarity
PRO_0000407910
Propeptide619 – 64224Removed in mature form Potential
PRO_0000041674

Regions

Domain28 – 6437EGF-like 1
Domain65 – 10642EGF-like 2; calcium-binding Potential
Domain107 – 14842EGF-like 3; calcium-binding Potential
Domain335 – 590256ZP

Sites

Site588 – 5892Cleavage

Amino acid modifications

Lipidation6181GPI-anchor amidated alanine Potential
Glycosylation251N-linked (GlcNAc...) Potential
Glycosylation381N-linked (GlcNAc...) Potential
Glycosylation761N-linked (GlcNAc...) Potential
Glycosylation791N-linked (GlcNAc...) Potential
Glycosylation2331N-linked (GlcNAc...) Potential
Glycosylation2761N-linked (GlcNAc...) Potential
Glycosylation3231N-linked (GlcNAc...) Potential
Glycosylation3971N-linked (GlcNAc...) Potential
Glycosylation4481N-linked (GlcNAc...) Potential
Glycosylation5141N-linked (GlcNAc...) Potential
Disulfide bond32 ↔ 41 By similarity
Disulfide bond35 ↔ 50 By similarity
Disulfide bond52 ↔ 63 By similarity
Disulfide bond69 ↔ 82 By similarity
Disulfide bond77 ↔ 91 By similarity
Disulfide bond93 ↔ 105 By similarity
Disulfide bond111 ↔ 125 By similarity
Disulfide bond119 ↔ 134 By similarity
Disulfide bond136 ↔ 147 By similarity
Disulfide bond507 ↔ 567 By similarity

Experimental info

Sequence conflict221E → G in AAA73896. Ref.1
Sequence conflict102 – 1043ELS → GLG in AAA73896. Ref.1
Sequence conflict1381E → K in AAA73896. Ref.1
Sequence conflict1521G → S in AAA73896. Ref.1
Sequence conflict2001L → Q in AAA73896. Ref.1
Sequence conflict2231R → A in AAA73896. Ref.1
Sequence conflict2551Q → H in AAA73896. Ref.1
Sequence conflict2791A → E in AAA73896. Ref.1
Sequence conflict3401D → G in BAE38225. Ref.2
Sequence conflict4731H → Y in AAA73896. Ref.1
Sequence conflict5901S → C in AAA73896. Ref.1
Sequence conflict6061T → TRQ in AAA73896. Ref.1
Sequence conflict616 – 6172Missing in AAA73896. Ref.1
Sequence conflict6331P → L in AAA73896. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q91X17 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 31B1461B4DCAE927

FASTA64270,845
        10         20         30         40         50         60 
MGIPLTWMLL VMMVTSWFTL AEASNSTEAR RCSECHNNAT CTVDGVVTTC SCQTGFTGDG 

        70         80         90        100        110        120 
LVCEDMDECA TPWTHNCSNS SCVNTPGSFK CSCQDGFRLT PELSCTDVDE CSEQGLSNCH 

       130        140        150        160        170        180 
ALATCVNTEG DYLCVCPEGF TGDGWYCECS PGSCEPGLDC LPQGPDGKLV CQDPCNTYET 

       190        200        210        220        230        240 
LTEYWRSTEY GVGYSCDAGL HGWYRFTGQG GVRMAETCVP VLRCNTAAPM WLNGSHPSSS 

       250        260        270        280        290        300 
EGIVSRTACA HWSDQCCRWS TEIQVKACPG GFYIYNLTAP PECNLAYCTD PSSVEGTCEE 

       310        320        330        340        350        360 
CRVDEDCISD NGRWRCQCKQ DSNITDVSQL EYRLECGAND IKMSLRKCQL QSLGFMNVFM 

       370        380        390        400        410        420 
YLNDRQCSGF SESDERDWMS IVTPARNGPC GTVLRRNETH ATYSNTLYLA NAIIIRDIII 

       430        440        450        460        470        480 
RMNFECSYPL DMKVSLKTSL QPMVSALNIS LGGTGKFTVR MALFQSPTYT QPHQGPSVML 

       490        500        510        520        530        540 
STEAFLYVGT MLDGGDLSRF VLLMTNCYAT PSSNSTDPVK YFIIQDSCPR TEDTTIQVTE 

       550        560        570        580        590        600 
NGESSQARFS VQMFRFAGNY DLVYLHCEVY LCDSTSEQCK PTCSGTRFRS GNFIDQTRVL 

       610        620        630        640 
NLGPITRQGV QASVSKAASS NLRLLSIWLL LFPSATLIFM VQ 

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence and peptide motifs of mouse uromodulin (Tamm-Horsfall protein) -- the most abundant protein in mammalian urine."
Prasadan K., Bates J., Badgett A., Dell M., Sukhatme V., Yu H., Kumar S.
Biochim. Biophys. Acta 1260:328-332(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Kidney.
[3]"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].
Strain: FVB/N.
Tissue: Liver.
[4]"The ZP domain is a conserved module for polymerization of extracellular proteins."
Jovine L., Qi H., Williams Z., Litscher E., Wassarman P.M.
Nat. Cell Biol. 4:457-461(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION, DOMAIN ZP.
[5]"Tamm-Horsfall protein knockout mice are more prone to urinary tract infection: rapid communication."
Bates J.M., Raffi H.M., Prasadan K., Mascarenhas R., Laszik Z., Maeda N., Hultgren S.J., Kumar S.
Kidney Int. 65:791-797(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE, FUNCTION.
[6]"Tamm-Horsfall protein is a critical renal defense factor protecting against calcium oxalate crystal formation."
Mo L., Huang H.Y., Zhu X.H., Shapiro E., Hasty D.L., Wu X.R.
Kidney Int. 66:1159-1166(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE, FUNCTION.
[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 573-587, PROTEOLYTIC CLEAVAGE, IDENTIFICATION BY MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L33406 mRNA. Translation: AAA73896.1.
AK085460 mRNA. Translation: BAC39452.1.
AK144065 mRNA. Translation: BAE25681.1.
AK164688 mRNA. Translation: BAE37877.1.
AK165507 mRNA. Translation: BAE38225.1.
BC012973 mRNA. Translation: AAH12973.1.
CCDSCCDS21780.1.
PIRS52111.
RefSeqNP_001265534.1. NM_001278605.1.
NP_033496.1. NM_009470.5.
UniGeneMm.10826.

3D structure databases

ProteinModelPortalQ91X17.
SMRQ91X17. Positions 35-143.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000033263.

Proteomic databases

PaxDbQ91X17.
PRIDEQ91X17.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000033263; ENSMUSP00000033263; ENSMUSG00000030963.
GeneID22242.
KEGGmmu:22242.
UCSCuc009jlb.1. mouse.

Organism-specific databases

CTD7369.
MGIMGI:102674. Umod.

Phylogenomic databases

eggNOGNOG44010.
GeneTreeENSGT00530000063244.
HOGENOMHOG000293303.
HOVERGENHBG004349.
InParanoidQ91X17.
KOK18274.
OMADANASCE.
OrthoDBEOG7SFHWJ.
PhylomeDBQ91X17.
TreeFamTF330284.

Gene expression databases

BgeeQ91X17.
CleanExMM_UMOD.
GenevestigatorQ91X17.

Family and domain databases

Gene3D2.40.155.10. 1 hit.
InterProIPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
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_N_dom.
IPR001507. ZP_dom.
IPR017977. ZP_dom_CS.
[Graphical view]
PfamPF12947. EGF_3. 1 hit.
PF07645. EGF_CA. 1 hit.
PF00100. Zona_pellucida. 1 hit.
[Graphical view]
PRINTSPR00023. ZPELLUCIDA.
SMARTSM00181. EGF. 1 hit.
SM00179. EGF_CA. 2 hits.
SM00241. ZP. 1 hit.
[Graphical view]
SUPFAMSSF57184. SSF57184. 1 hit.
PROSITEPS00010. ASX_HYDROXYL. 2 hits.
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]
ProtoNetSearch...

Other

ChiTaRSUMOD. mouse.
NextBio302309.
PROQ91X17.
SOURCESearch...

Entry information

Entry nameUROM_MOUSE
AccessionPrimary (citable) accession number: Q91X17
Secondary accession number(s): Q3TN64, Q3TP60, Q62285
Entry history
Integrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: December 1, 2001
Last modified: July 9, 2014
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot