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Q91X17

- UROM_MOUSE

UniProt

Q91X17 - UROM_MOUSE

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Protein
Uromodulin
Gene
Umod
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - 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 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.2 Publications
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.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei588 – 5892Cleavage

GO - Molecular functioni

  1. calcium ion binding Source: InterPro

GO - Biological processi

  1. chemical homeostasis Source: MGI
  2. excretion Source: MGI
  3. metanephric ascending thin limb development Source: UniProtKB
  4. metanephric distal convoluted tubule development Source: UniProtKB
  5. metanephric thick ascending limb development Source: UniProtKB
  6. regulation of ion homeostasis Source: UniProtKB
  7. response to organic substance Source: Ensembl
Complete GO annotation...

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 7

Organism-specific databases

MGIiMGI:102674. Umod.

Subcellular locationi

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.

GO - Cellular componenti

  1. Golgi apparatus Source: Ensembl
  2. anchored component of membrane Source: UniProtKB
  3. apical plasma membrane Source: UniProtKB
  4. basolateral plasma membrane Source: UniProtKB
  5. ciliary membrane Source: UniProtKB-SubCell
  6. cytoplasmic vesicle Source: Ensembl
  7. extracellular space Source: Ensembl
  8. membrane raft Source: Ensembl
  9. primary cilium Source: UniProtKB
  10. spindle pole Source: UniProtKB
Complete GO annotation...

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 deficient-mice but not in wild-type mice.2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323 Reviewed prediction
Add
BLAST
Chaini24 – 618595Uromodulin
PRO_0000041673Add
BLAST
Chaini25 – 588564Uromodulin, secreted form By similarity
PRO_0000407910Add
BLAST
Propeptidei619 – 64224Removed in mature form Reviewed prediction
PRO_0000041674Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi25 – 251N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi32 ↔ 41 By similarity
Disulfide bondi35 ↔ 50 By similarity
Glycosylationi38 – 381N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi52 ↔ 63 By similarity
Disulfide bondi69 ↔ 82 By similarity
Glycosylationi76 – 761N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi77 ↔ 91 By similarity
Glycosylationi79 – 791N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi93 ↔ 105 By similarity
Disulfide bondi111 ↔ 125 By similarity
Disulfide bondi119 ↔ 134 By similarity
Disulfide bondi136 ↔ 147 By similarity
Glycosylationi233 – 2331N-linked (GlcNAc...) Reviewed prediction
Glycosylationi276 – 2761N-linked (GlcNAc...) Reviewed prediction
Glycosylationi323 – 3231N-linked (GlcNAc...) Reviewed prediction
Glycosylationi397 – 3971N-linked (GlcNAc...) Reviewed prediction
Glycosylationi448 – 4481N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi507 ↔ 567 By similarity
Glycosylationi514 – 5141N-linked (GlcNAc...) Reviewed prediction
Lipidationi618 – 6181GPI-anchor amidated alanine Reviewed prediction

Post-translational modificationi

N-glycosylated.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

Proteomic databases

PaxDbiQ91X17.
PRIDEiQ91X17.

Expressioni

Gene expression databases

BgeeiQ91X17.
CleanExiMM_UMOD.
GenevestigatoriQ91X17.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000033263.

Structurei

3D structure databases

ProteinModelPortaliQ91X17.
SMRiQ91X17. Positions 35-143.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini28 – 6437EGF-like 1
Add
BLAST
Domaini65 – 10642EGF-like 2; calcium-binding Reviewed prediction
Add
BLAST
Domaini107 – 14842EGF-like 3; calcium-binding Reviewed prediction
Add
BLAST
Domaini335 – 590256ZP
Add
BLAST

Domaini

The ZP domain is involved in the polymerization of the protein to promote the formation of complex gel-like structure.1 Publication

Sequence similaritiesi

Contains 3 EGF-like domains.
Contains 1 ZP domain.

Keywords - Domaini

EGF-like domain, Repeat, Signal

Phylogenomic databases

eggNOGiNOG44010.
GeneTreeiENSGT00530000063244.
HOGENOMiHOG000293303.
HOVERGENiHBG004349.
InParanoidiQ91X17.
KOiK18274.
OMAiDANASCE.
OrthoDBiEOG7SFHWJ.
PhylomeDBiQ91X17.
TreeFamiTF330284.

Family and domain databases

Gene3Di2.40.155.10. 1 hit.
InterProiIPR000742. 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]
PfamiPF12947. EGF_3. 1 hit.
PF07645. EGF_CA. 1 hit.
PF00100. Zona_pellucida. 1 hit.
[Graphical view]
PRINTSiPR00023. ZPELLUCIDA.
SMARTiSM00181. EGF. 1 hit.
SM00179. EGF_CA. 2 hits.
SM00241. ZP. 1 hit.
[Graphical view]
SUPFAMiSSF57184. SSF57184. 1 hit.
PROSITEiPS00010. 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]

Sequencei

Sequence statusi: Complete.

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

Q91X17-1 [UniParc]FASTAAdd to Basket

« Hide

MGIPLTWMLL VMMVTSWFTL AEASNSTEAR RCSECHNNAT CTVDGVVTTC    50
SCQTGFTGDG LVCEDMDECA TPWTHNCSNS SCVNTPGSFK CSCQDGFRLT 100
PELSCTDVDE CSEQGLSNCH ALATCVNTEG DYLCVCPEGF TGDGWYCECS 150
PGSCEPGLDC LPQGPDGKLV CQDPCNTYET LTEYWRSTEY GVGYSCDAGL 200
HGWYRFTGQG GVRMAETCVP VLRCNTAAPM WLNGSHPSSS EGIVSRTACA 250
HWSDQCCRWS TEIQVKACPG GFYIYNLTAP PECNLAYCTD PSSVEGTCEE 300
CRVDEDCISD NGRWRCQCKQ DSNITDVSQL EYRLECGAND IKMSLRKCQL 350
QSLGFMNVFM YLNDRQCSGF SESDERDWMS IVTPARNGPC GTVLRRNETH 400
ATYSNTLYLA NAIIIRDIII RMNFECSYPL DMKVSLKTSL QPMVSALNIS 450
LGGTGKFTVR MALFQSPTYT QPHQGPSVML STEAFLYVGT MLDGGDLSRF 500
VLLMTNCYAT PSSNSTDPVK YFIIQDSCPR TEDTTIQVTE NGESSQARFS 550
VQMFRFAGNY DLVYLHCEVY LCDSTSEQCK PTCSGTRFRS GNFIDQTRVL 600
NLGPITRQGV QASVSKAASS NLRLLSIWLL LFPSATLIFM VQ 642
Length:642
Mass (Da):70,845
Last modified:December 1, 2001 - v1
Checksum:i31B1461B4DCAE927
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti22 – 221E → G in AAA73896. 1 Publication
Sequence conflicti102 – 1043ELS → GLG in AAA73896. 1 Publication
Sequence conflicti138 – 1381E → K in AAA73896. 1 Publication
Sequence conflicti152 – 1521G → S in AAA73896. 1 Publication
Sequence conflicti200 – 2001L → Q in AAA73896. 1 Publication
Sequence conflicti223 – 2231R → A in AAA73896. 1 Publication
Sequence conflicti255 – 2551Q → H in AAA73896. 1 Publication
Sequence conflicti279 – 2791A → E in AAA73896. 1 Publication
Sequence conflicti340 – 3401D → G in BAE38225. 1 Publication
Sequence conflicti473 – 4731H → Y in AAA73896. 1 Publication
Sequence conflicti590 – 5901S → C in AAA73896. 1 Publication
Sequence conflicti606 – 6061T → TRQ in AAA73896. 1 Publication
Sequence conflicti616 – 6172Missing in AAA73896. 1 Publication
Sequence conflicti633 – 6331P → L in AAA73896. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
GeneIDi22242.
KEGGimmu:22242.
UCSCiuc009jlb.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS21780.1.
PIRi S52111.
RefSeqi NP_001265534.1. NM_001278605.1.
NP_033496.1. NM_009470.5.
UniGenei Mm.10826.

3D structure databases

ProteinModelPortali Q91X17.
SMRi Q91X17. Positions 35-143.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10090.ENSMUSP00000033263.

Proteomic databases

PaxDbi Q91X17.
PRIDEi Q91X17.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000033263 ; ENSMUSP00000033263 ; ENSMUSG00000030963 .
GeneIDi 22242.
KEGGi mmu:22242.
UCSCi uc009jlb.1. mouse.

Organism-specific databases

CTDi 7369.
MGIi MGI:102674. Umod.

Phylogenomic databases

eggNOGi NOG44010.
GeneTreei ENSGT00530000063244.
HOGENOMi HOG000293303.
HOVERGENi HBG004349.
InParanoidi Q91X17.
KOi K18274.
OMAi DANASCE.
OrthoDBi EOG7SFHWJ.
PhylomeDBi Q91X17.
TreeFami TF330284.

Miscellaneous databases

ChiTaRSi UMOD. mouse.
NextBioi 302309.
PROi Q91X17.
SOURCEi Search...

Gene expression databases

Bgeei Q91X17.
CleanExi MM_UMOD.
Genevestigatori Q91X17.

Family and domain databases

Gene3Di 2.40.155.10. 1 hit.
InterProi IPR000742. 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 ]
Pfami PF12947. EGF_3. 1 hit.
PF07645. EGF_CA. 1 hit.
PF00100. Zona_pellucida. 1 hit.
[Graphical view ]
PRINTSi PR00023. ZPELLUCIDA.
SMARTi SM00181. EGF. 1 hit.
SM00179. EGF_CA. 2 hits.
SM00241. ZP. 1 hit.
[Graphical view ]
SUPFAMi SSF57184. SSF57184. 1 hit.
PROSITEi 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.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiUROM_MOUSE
AccessioniPrimary (citable) accession number: Q91X17
Secondary accession number(s): Q3TN64, Q3TP60, Q62285
Entry historyi
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 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
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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