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Protein

Uromodulin

Gene

Umod

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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. May serve as a receptor for binding and endocytosis of cytokines (IL-1, IL-2) and TNF. Facilitates neutrophil migration across renal epithelia.By similarity
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.2 Publications

GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

ReactomeiR-MMU-446203 Asparagine N-linked glycosylation

Names & Taxonomyi

Protein namesi
Recommended name:
Uromodulin
Alternative name(s):
Tamm-Horsfall urinary glycoprotein
Short name:
THP
Cleaved into the following chain:
Gene namesi
Name:Umod
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:102674 Umod

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Cell projection, Membrane, Secreted

Pathology & Biotechi

Disruption phenotypei

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 mutant mice, but not in wild-type mice.2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 24By similarityAdd BLAST24
ChainiPRO_000004167325 – 618UromodulinAdd BLAST594
ChainiPRO_000040791025 – 588Uromodulin, secreted formAdd BLAST564
PropeptideiPRO_0000041674619 – 642Removed in mature formSequence analysisAdd BLAST24

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi25N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi32 ↔ 41PROSITE-ProRule annotation
Disulfide bondi35 ↔ 50PROSITE-ProRule annotation
Glycosylationi38N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi52 ↔ 63PROSITE-ProRule annotation
Disulfide bondi69 ↔ 82PROSITE-ProRule annotation
Glycosylationi76N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi77 ↔ 91PROSITE-ProRule annotation
Glycosylationi79N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi93 ↔ 105PROSITE-ProRule annotation
Disulfide bondi111 ↔ 125PROSITE-ProRule annotation
Disulfide bondi119 ↔ 134PROSITE-ProRule annotation
Disulfide bondi136 ↔ 147PROSITE-ProRule annotation
Glycosylationi233N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi276N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi298 ↔ 307By similarity
Disulfide bondi301 ↔ 316By similarity
Disulfide bondi318 ↔ 348By similarity
Glycosylationi323N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi336 ↔ 426By similarity
Disulfide bondi367 ↔ 390By similarity
Glycosylationi397N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi448N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi507 ↔ 567PROSITE-ProRule annotation
Glycosylationi514N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi528 ↔ 583By similarity
Disulfide bondi572 ↔ 579By similarity
Lipidationi618GPI-anchor amidated alanineSequence analysis1

Post-translational modificationi

N-glycosylated.2 Publications
Proteolytically cleaved at a conserved C-terminal proteolytic cleavage site to generate the secreted form found in urine (PubMed:18375198). This cleavage is catalyzed by HPN (PubMed:26673890).2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei588 – 589Cleavage2 Publications2

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

Proteomic databases

MaxQBiQ91X17
PaxDbiQ91X17
PRIDEiQ91X17

PTM databases

iPTMnetiQ91X17
PhosphoSitePlusiQ91X17

Expressioni

Tissue specificityi

Detected in urine (secreted form). Detected in kidney thick ascending limb epithelial cells (at protein level).1 Publication

Gene expression databases

BgeeiENSMUSG00000030963 Expressed in 67 organ(s), highest expression level in adult mammalian kidney
CleanExiMM_UMOD
ExpressionAtlasiQ91X17 baseline and differential
GenevisibleiQ91X17 MM

Interactioni

Subunit structurei

Uromodulin, secreted form: homodimer that then polymerizes into long filaments.1 Publication

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000033263

Structurei

3D structure databases

ProteinModelPortaliQ91X17
SMRiQ91X17
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini28 – 64EGF-like 1PROSITE-ProRule annotationAdd BLAST37
Domaini65 – 106EGF-like 2; calcium-bindingPROSITE-ProRule annotationAdd BLAST42
Domaini107 – 148EGF-like 3; calcium-bindingPROSITE-ProRule annotationAdd BLAST42
Domaini335 – 590ZPPROSITE-ProRule annotationAdd BLAST256

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni431 – 454Important for secretion and polymerization into filamentsBy similarityAdd BLAST24
Regioni587 – 590Essential for cleavage by HPNBy similarity4
Regioni599 – 608Regulates polymerization into filamentsBy similarity10

Domaini

The ZP domain mediates polymerization, leading to the formation of long filaments.2 Publications

Keywords - Domaini

EGF-like domain, Repeat, Signal

Phylogenomic databases

eggNOGiENOG410IVSV Eukaryota
ENOG410YDU6 LUCA
GeneTreeiENSGT00530000063244
HOGENOMiHOG000293303
HOVERGENiHBG004349
InParanoidiQ91X17
KOiK18274
OMAiGPCGTVM
OrthoDBiEOG091G06RJ
PhylomeDBiQ91X17
TreeFamiTF330284

Family and domain databases

InterProiView protein in InterPro
IPR001881 EGF-like_Ca-bd_dom
IPR013032 EGF-like_CS
IPR000742 EGF-like_dom
IPR000152 EGF-type_Asp/Asn_hydroxyl_site
IPR018097 EGF_Ca-bd_CS
IPR024731 EGF_dom
IPR009030 Growth_fac_rcpt_cys_sf
IPR001507 ZP_dom
IPR017977 ZP_dom_CS
PfamiView protein in Pfam
PF12947 EGF_3, 1 hit
PF07645 EGF_CA, 1 hit
PF00100 Zona_pellucida, 1 hit
PRINTSiPR00023 ZPELLUCIDA
SMARTiView protein in SMART
SM00181 EGF, 3 hits
SM00179 EGF_CA, 2 hits
SM00241 ZP, 1 hit
SUPFAMiSSF57184 SSF57184, 1 hit
PROSITEiView protein in PROSITE
PS00010 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

Sequence (1+)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 3 potential isoforms that are computationally mapped.Show allAlign All

Q91X17-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGIPLTWMLL VMMVTSWFTL AEASNSTEAR RCSECHNNAT CTVDGVVTTC
60 70 80 90 100
SCQTGFTGDG LVCEDMDECA TPWTHNCSNS SCVNTPGSFK CSCQDGFRLT
110 120 130 140 150
PELSCTDVDE CSEQGLSNCH ALATCVNTEG DYLCVCPEGF TGDGWYCECS
160 170 180 190 200
PGSCEPGLDC LPQGPDGKLV CQDPCNTYET LTEYWRSTEY GVGYSCDAGL
210 220 230 240 250
HGWYRFTGQG GVRMAETCVP VLRCNTAAPM WLNGSHPSSS EGIVSRTACA
260 270 280 290 300
HWSDQCCRWS TEIQVKACPG GFYIYNLTAP PECNLAYCTD PSSVEGTCEE
310 320 330 340 350
CRVDEDCISD NGRWRCQCKQ DSNITDVSQL EYRLECGAND IKMSLRKCQL
360 370 380 390 400
QSLGFMNVFM YLNDRQCSGF SESDERDWMS IVTPARNGPC GTVLRRNETH
410 420 430 440 450
ATYSNTLYLA NAIIIRDIII RMNFECSYPL DMKVSLKTSL QPMVSALNIS
460 470 480 490 500
LGGTGKFTVR MALFQSPTYT QPHQGPSVML STEAFLYVGT MLDGGDLSRF
510 520 530 540 550
VLLMTNCYAT PSSNSTDPVK YFIIQDSCPR TEDTTIQVTE NGESSQARFS
560 570 580 590 600
VQMFRFAGNY DLVYLHCEVY LCDSTSEQCK PTCSGTRFRS GNFIDQTRVL
610 620 630 640
NLGPITRQGV QASVSKAASS NLRLLSIWLL LFPSATLIFM VQ
Length:642
Mass (Da):70,845
Last modified:December 1, 2001 - v1
Checksum:i31B1461B4DCAE927
GO

Computationally mapped potential isoform sequencesi

There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A140LI10A0A140LI10_MOUSE
Uromodulin
Umod
187Annotation score:
A0A140LJ95A0A140LJ95_MOUSE
Uromodulin
Umod
87Annotation score:
A0A140LJ15A0A140LJ15_MOUSE
Uromodulin
Umod
77Annotation score:

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti22E → G in AAA73896 (PubMed:7873609).Curated1
Sequence conflicti102 – 104ELS → GLG in AAA73896 (PubMed:7873609).Curated3
Sequence conflicti138E → K in AAA73896 (PubMed:7873609).Curated1
Sequence conflicti152G → S in AAA73896 (PubMed:7873609).Curated1
Sequence conflicti200L → Q in AAA73896 (PubMed:7873609).Curated1
Sequence conflicti223R → A in AAA73896 (PubMed:7873609).Curated1
Sequence conflicti255Q → H in AAA73896 (PubMed:7873609).Curated1
Sequence conflicti279A → E in AAA73896 (PubMed:7873609).Curated1
Sequence conflicti340D → G in BAE38225 (PubMed:16141072).Curated1
Sequence conflicti473H → Y in AAA73896 (PubMed:7873609).Curated1
Sequence conflicti590S → C in AAA73896 (PubMed:7873609).Curated1
Sequence conflicti606T → TRQ in AAA73896 (PubMed:7873609).Curated1
Sequence conflicti616 – 617Missing in AAA73896 (PubMed:7873609).Curated2
Sequence conflicti633P → L in AAA73896 (PubMed:7873609).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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
CCDSiCCDS21780.1
PIRiS52111
RefSeqiNP_001265534.1, NM_001278605.1
NP_033496.1, NM_009470.5
UniGeneiMm.10826

Genome annotation databases

EnsembliENSMUST00000033263; ENSMUSP00000033263; ENSMUSG00000030963
ENSMUST00000209095; ENSMUSP00000146652; ENSMUSG00000030963
GeneIDi22242
KEGGimmu:22242
UCSCiuc009jlb.2 mouse

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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
CCDSiCCDS21780.1
PIRiS52111
RefSeqiNP_001265534.1, NM_001278605.1
NP_033496.1, NM_009470.5
UniGeneiMm.10826

3D structure databases

ProteinModelPortaliQ91X17
SMRiQ91X17
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000033263

PTM databases

iPTMnetiQ91X17
PhosphoSitePlusiQ91X17

Proteomic databases

MaxQBiQ91X17
PaxDbiQ91X17
PRIDEiQ91X17

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000033263; ENSMUSP00000033263; ENSMUSG00000030963
ENSMUST00000209095; ENSMUSP00000146652; ENSMUSG00000030963
GeneIDi22242
KEGGimmu:22242
UCSCiuc009jlb.2 mouse

Organism-specific databases

CTDi7369
MGIiMGI:102674 Umod

Phylogenomic databases

eggNOGiENOG410IVSV Eukaryota
ENOG410YDU6 LUCA
GeneTreeiENSGT00530000063244
HOGENOMiHOG000293303
HOVERGENiHBG004349
InParanoidiQ91X17
KOiK18274
OMAiGPCGTVM
OrthoDBiEOG091G06RJ
PhylomeDBiQ91X17
TreeFamiTF330284

Enzyme and pathway databases

ReactomeiR-MMU-446203 Asparagine N-linked glycosylation

Miscellaneous databases

ChiTaRSiUmod mouse
PROiPR:Q91X17
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000030963 Expressed in 67 organ(s), highest expression level in adult mammalian kidney
CleanExiMM_UMOD
ExpressionAtlasiQ91X17 baseline and differential
GenevisibleiQ91X17 MM

Family and domain databases

InterProiView protein in InterPro
IPR001881 EGF-like_Ca-bd_dom
IPR013032 EGF-like_CS
IPR000742 EGF-like_dom
IPR000152 EGF-type_Asp/Asn_hydroxyl_site
IPR018097 EGF_Ca-bd_CS
IPR024731 EGF_dom
IPR009030 Growth_fac_rcpt_cys_sf
IPR001507 ZP_dom
IPR017977 ZP_dom_CS
PfamiView protein in Pfam
PF12947 EGF_3, 1 hit
PF07645 EGF_CA, 1 hit
PF00100 Zona_pellucida, 1 hit
PRINTSiPR00023 ZPELLUCIDA
SMARTiView protein in SMART
SM00181 EGF, 3 hits
SM00179 EGF_CA, 2 hits
SM00241 ZP, 1 hit
SUPFAMiSSF57184 SSF57184, 1 hit
PROSITEiView protein in PROSITE
PS00010 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
ProtoNetiSearch...

Entry informationi

Entry nameiUROM_MOUSE
AccessioniPrimary (citable) accession number: Q91X17
Secondary accession number(s): Q3TN64, Q3TP60, Q62285
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: December 1, 2001
Last modified: September 12, 2018
This is version 141 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
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Main funding by: National Institutes of Health

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