Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q91X17

- UROM_MOUSE

UniProt

Q91X17 - UROM_MOUSE

Protein

Uromodulin

Gene

Umod

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 111 (01 Oct 2014)
      Sequence version 1 (01 Dec 2001)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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.By similarity
    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

    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 By similarity; Lipid-anchorGPI-anchor By similarity. Basolateral cell membrane By similarity; 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. anchored component of membrane Source: UniProtKB
    2. apical plasma membrane Source: UniProtKB
    3. basolateral plasma membrane Source: UniProtKB
    4. ciliary membrane Source: UniProtKB-SubCell
    5. cytoplasmic vesicle Source: Ensembl
    6. extracellular space Source: Ensembl
    7. Golgi apparatus Source: Ensembl
    8. membrane raft Source: Ensembl
    9. primary cilium Source: UniProtKB
    10. spindle pole Source: UniProtKB

    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 – 2323Sequence AnalysisAdd
    BLAST
    Chaini24 – 618595UromodulinPRO_0000041673Add
    BLAST
    Chaini25 – 588564Uromodulin, secreted formBy similarityPRO_0000407910Add
    BLAST
    Propeptidei619 – 64224Removed in mature formSequence AnalysisPRO_0000041674Add
    BLAST

    Amino acid modifications

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

    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini28 – 6437EGF-like 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini65 – 10642EGF-like 2; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini107 – 14842EGF-like 3; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini335 – 590256ZPPROSITE-ProRule annotationAdd
    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.PROSITE-ProRule annotation
    Contains 1 ZP domain.PROSITE-ProRule annotation

    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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti22 – 221E → G in AAA73896. (PubMed:7873609)Curated
    Sequence conflicti102 – 1043ELS → GLG in AAA73896. (PubMed:7873609)Curated
    Sequence conflicti138 – 1381E → K in AAA73896. (PubMed:7873609)Curated
    Sequence conflicti152 – 1521G → S in AAA73896. (PubMed:7873609)Curated
    Sequence conflicti200 – 2001L → Q in AAA73896. (PubMed:7873609)Curated
    Sequence conflicti223 – 2231R → A in AAA73896. (PubMed:7873609)Curated
    Sequence conflicti255 – 2551Q → H in AAA73896. (PubMed:7873609)Curated
    Sequence conflicti279 – 2791A → E in AAA73896. (PubMed:7873609)Curated
    Sequence conflicti340 – 3401D → G in BAE38225. (PubMed:16141072)Curated
    Sequence conflicti473 – 4731H → Y in AAA73896. (PubMed:7873609)Curated
    Sequence conflicti590 – 5901S → C in AAA73896. (PubMed:7873609)Curated
    Sequence conflicti606 – 6061T → TRQ in AAA73896. (PubMed:7873609)Curated
    Sequence conflicti616 – 6172Missing in AAA73896. (PubMed:7873609)Curated
    Sequence conflicti633 – 6331P → L in AAA73896. (PubMed:7873609)Curated

    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

    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: October 1, 2014
    This is version 111 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