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)

Q8VHL0

- UT1_MOUSE

UniProt

Q8VHL0 - UT1_MOUSE

Protein

Urea transporter 1

Gene

Slc14a1

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 93 (01 Oct 2014)
      Sequence version 2 (28 Jun 2011)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Urea channel that facilitates transmembrane urea transport down a concentration gradient. A constriction of the transmembrane channel functions as selectivity filter through which urea is expected to pass in dehydrated form. The rate of urea conduction is increased by hypotonic stress. Plays an important role in the kidney medulla collecting ducts, where it allows rapid equilibration between the lumen of the collecting ducts and the interstitium, and thereby prevents water loss driven by the high concentration of urea in the urine. Facilitates urea transport across erythrocyte membranes. May also play a role in transmembrane water transport, possibly by indirect means.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei334 – 3341Important for channel permeabilityBy similarity

    GO - Molecular functioni

    1. urea channel activity Source: UniProtKB
    2. urea transmembrane transporter activity Source: MGI
    3. water transmembrane transporter activity Source: MGI

    GO - Biological processi

    1. urea transmembrane transport Source: UniProtKB
    2. urea transport Source: MGI
    3. water transport Source: MGI

    Keywords - Biological processi

    Transport

    Enzyme and pathway databases

    ReactomeiREACT_217615. Transport of glucose and other sugars, bile salts and organic acids, metal ions and amine compounds.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Urea transporter 1
    Alternative name(s):
    Solute carrier family 14 member 1
    Urea transporter B
    Short name:
    UT-B
    Urea transporter, erythrocyte
    Gene namesi
    Name:Slc14a1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 18

    Organism-specific databases

    MGIiMGI:1351654. Slc14a1.

    Subcellular locationi

    Cell membrane; Multi-pass membrane protein. Basolateral cell membrane; Multi-pass membrane protein
    Note: Restricted to the basolateral membrane in various portions of the urothelium.

    GO - Cellular componenti

    1. basolateral plasma membrane Source: UniProtKB-SubCell
    2. integral component of membrane Source: MGI
    3. integral component of plasma membrane Source: UniProtKB
    4. plasma membrane Source: MGI

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Disruption phenotypei

    Mutant mice exhibit grossly normal appearance, activity and behavior. Plasma sodium, potassium, chloride, bicarbonate and creatinine concentrations, as well as hematocrit, are similar to wild type animals. Urea permeability in erythrocytes is 45-fold lower than that from wild-type mice. Daily urine output is 1.5-fold greater and urine osmolarity is lower than in wild-type mice. After 24 hours of water deprivation, plasma urea concentration is 30% higher and urine urea concentration 35% lower in mutant mice than in wild-type animals. Mice lacking both Aqp1 and Slc14a1 are born at the expected Mendelian ratio, but do not thrive; half of them die within ten days after birth and none are alive after two weeks. Urine osmolality is somewhat lower than that observed with mice lacking Aqp1. Besides, erythrocyte water permeability is significantly lower than in mice lacking only Aqp1.2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 384384Urea transporter 1PRO_0000065738Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi206 – 2061N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    N-glycosylated in red blood cells, as well as in most non-erythroid tissues, except in the gastrocnemius muscle and in the gastrointestinal tract, including liver, colon and stomach.1 Publication

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    MaxQBiQ8VHL0.
    PaxDbiQ8VHL0.
    PRIDEiQ8VHL0.

    Expressioni

    Tissue specificityi

    Expressed in brain, kidney, heart, liver, lung, skeletal muscle, spleen, testis, ureter and urinary bladder (at protein level). Along the gastrointestinal tract, detected in colon, jejunum and stomach (at protein level). In the kidney, expressed in some microvessels of the inner and outer medulla, but not all (at protein level). Not detected in the cortex (at protein level). Detected in the urothelium all along the urinary tract, including the papilla surface, the ureter, the bladder and the urethra (at protein level). In the brain, expressed at the border of the corpus callosum and striatum in astrocytic cellular processes surrounding blood microvessels (at protein level). Detected in erythrocytes (at protein level).3 Publications

    Inductioni

    Down-regulated by water deprivation in urinary bladder and ureter, but not in kidney medulla, colon, testis nor brain.1 Publication

    Gene expression databases

    BgeeiQ8VHL0.
    GenevestigatoriQ8VHL0.

    Interactioni

    Subunit structurei

    Homotrimer; each subunit contains a pore through which urea permeates. Identified in a complex with STOM By similarity.By similarity

    Protein-protein interaction databases

    STRINGi10090.ENSMUSP00000025433.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8VHL0.
    SMRiQ8VHL0. Positions 31-376.
    ModBaseiSearch...
    MobiDBiSearch...

    Intramembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Intramembranei47 – 6418HelicalBy similarityAdd
    BLAST
    Intramembranei68 – 8316HelicalBy similarityAdd
    BLAST
    Intramembranei215 – 22915HelicalBy similarityAdd
    BLAST
    Intramembranei234 – 24512HelicalBy similarityAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei86 – 10520HelicalBy similarityAdd
    BLAST
    Transmembranei110 – 13223HelicalBy similarityAdd
    BLAST
    Transmembranei139 – 16325HelicalBy similarityAdd
    BLAST
    Transmembranei168 – 18821HelicalBy similarityAdd
    BLAST
    Transmembranei250 – 26920HelicalBy similarityAdd
    BLAST
    Transmembranei279 – 29921HelicalBy similarityAdd
    BLAST
    Transmembranei304 – 32522HelicalBy similarityAdd
    BLAST
    Transmembranei328 – 34821HelicalBy similarityAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the urea transporter family.Curated

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG4413.
    GeneTreeiENSGT00390000018729.
    HOGENOMiHOG000065705.
    HOVERGENiHBG000540.
    InParanoidiQ3U542.
    KOiK08716.
    OMAiPNIYKMP.
    OrthoDBiEOG7GBFX8.
    TreeFamiTF332858.

    Family and domain databases

    Gene3Di1.10.3430.10. 1 hit.
    InterProiIPR029020. Ammonium/urea_transptr.
    IPR004937. Urea_transporter.
    [Graphical view]
    PANTHERiPTHR10464. PTHR10464. 1 hit.
    PfamiPF03253. UT. 1 hit.
    [Graphical view]
    PIRSFiPIRSF016502. Urea_transporter. 1 hit.

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q8VHL0-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MEDSPTMVKV DRGENQILSC RGRRCGFKVL GYVTGDMKEF ANWLKDKPVV    50
    LQFMDWILRG ISQVVFVSNP ISGILILVGL LVQNPWWALC GCVGTVVSTL 100
    TALLLSQDRS AIAAGLQGYN ATLVGILMAV FSNKGDYFWW LIFPVSAMSM 150
    TCPVFSSALS SVLSKWDLPV FTLPFNMALS MYLSATGHYN TFFPSKLFTP 200
    VSSVPNITWS ELSALELLKS LPVGVGQIYG CDNPWTGGIF LCAILLSSPL 250
    MCLHAAIGSL LGVIAGLSLA APFEDIYFGL WGFNSSLACI AIGGMFMALT 300
    WQTHLLALAC ALFTAYFGAC MAHLMAVVHL PACTWSFCLA TLLFLLLTTK 350
    NPNIYRMPLS KVTYSEENRI FYLQNKKRMV ESPL 384
    Length:384
    Mass (Da):42,126
    Last modified:June 28, 2011 - v2
    Checksum:iE66ED087341C07B7
    GO
    Isoform 2 (identifier: Q8VHL0-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MNGQSLTGGTDDAHHGPLWIDPFGNRGDKAAPEGFRRLSLALAQRWREQEPEEEIAM

    Show »
    Length:440
    Mass (Da):48,338
    Checksum:iBA248DED75D9772A
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti8 – 81V → A in AAL47138. (PubMed:11792714)Curated
    Sequence conflicti50 – 501V → A in AAI00571. (PubMed:15489334)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 11M → MNGQSLTGGTDDAHHGPLWI DPFGNRGDKAAPEGFRRLSL ALAQRWREQEPEEEIAM in isoform 2. 1 PublicationVSP_041574

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF448798 mRNA. Translation: AAL47138.1.
    AJ420967 mRNA. Translation: CAD12807.1.
    AK012066 mRNA. Translation: BAB28004.1.
    AK041979 mRNA. Translation: BAC31119.1.
    AK153891 mRNA. Translation: BAE32238.1.
    CH466528 Genomic DNA. Translation: EDL09437.1.
    CH466528 Genomic DNA. Translation: EDL09438.1.
    BC058594 mRNA. Translation: AAH58594.2.
    BC086673 mRNA. Translation: AAH86673.1.
    BC100570 mRNA. Translation: AAI00571.2.
    CCDSiCCDS29360.1. [Q8VHL0-1]
    CCDS50330.1. [Q8VHL0-2]
    RefSeqiNP_001164481.1. NM_001171010.1. [Q8VHL0-2]
    NP_001164482.1. NM_001171011.1. [Q8VHL0-1]
    NP_082398.1. NM_028122.4. [Q8VHL0-1]
    UniGeneiMm.33832.

    Genome annotation databases

    EnsembliENSMUST00000091813; ENSMUSP00000089421; ENSMUSG00000059336. [Q8VHL0-1]
    ENSMUST00000160292; ENSMUSP00000125114; ENSMUSG00000059336. [Q8VHL0-2]
    ENSMUST00000160639; ENSMUSP00000125367; ENSMUSG00000059336. [Q8VHL0-1]
    GeneIDi108052.
    KEGGimmu:108052.
    UCSCiuc008fsc.2. mouse. [Q8VHL0-1]
    uc008fsd.2. mouse. [Q8VHL0-2]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF448798 mRNA. Translation: AAL47138.1 .
    AJ420967 mRNA. Translation: CAD12807.1 .
    AK012066 mRNA. Translation: BAB28004.1 .
    AK041979 mRNA. Translation: BAC31119.1 .
    AK153891 mRNA. Translation: BAE32238.1 .
    CH466528 Genomic DNA. Translation: EDL09437.1 .
    CH466528 Genomic DNA. Translation: EDL09438.1 .
    BC058594 mRNA. Translation: AAH58594.2 .
    BC086673 mRNA. Translation: AAH86673.1 .
    BC100570 mRNA. Translation: AAI00571.2 .
    CCDSi CCDS29360.1. [Q8VHL0-1 ]
    CCDS50330.1. [Q8VHL0-2 ]
    RefSeqi NP_001164481.1. NM_001171010.1. [Q8VHL0-2 ]
    NP_001164482.1. NM_001171011.1. [Q8VHL0-1 ]
    NP_082398.1. NM_028122.4. [Q8VHL0-1 ]
    UniGenei Mm.33832.

    3D structure databases

    ProteinModelPortali Q8VHL0.
    SMRi Q8VHL0. Positions 31-376.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10090.ENSMUSP00000025433.

    Chemistry

    ChEMBLi CHEMBL2163171.

    Proteomic databases

    MaxQBi Q8VHL0.
    PaxDbi Q8VHL0.
    PRIDEi Q8VHL0.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000091813 ; ENSMUSP00000089421 ; ENSMUSG00000059336 . [Q8VHL0-1 ]
    ENSMUST00000160292 ; ENSMUSP00000125114 ; ENSMUSG00000059336 . [Q8VHL0-2 ]
    ENSMUST00000160639 ; ENSMUSP00000125367 ; ENSMUSG00000059336 . [Q8VHL0-1 ]
    GeneIDi 108052.
    KEGGi mmu:108052.
    UCSCi uc008fsc.2. mouse. [Q8VHL0-1 ]
    uc008fsd.2. mouse. [Q8VHL0-2 ]

    Organism-specific databases

    CTDi 6563.
    MGIi MGI:1351654. Slc14a1.

    Phylogenomic databases

    eggNOGi COG4413.
    GeneTreei ENSGT00390000018729.
    HOGENOMi HOG000065705.
    HOVERGENi HBG000540.
    InParanoidi Q3U542.
    KOi K08716.
    OMAi PNIYKMP.
    OrthoDBi EOG7GBFX8.
    TreeFami TF332858.

    Enzyme and pathway databases

    Reactomei REACT_217615. Transport of glucose and other sugars, bile salts and organic acids, metal ions and amine compounds.

    Miscellaneous databases

    NextBioi 359947.
    PROi Q8VHL0.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q8VHL0.
    Genevestigatori Q8VHL0.

    Family and domain databases

    Gene3Di 1.10.3430.10. 1 hit.
    InterProi IPR029020. Ammonium/urea_transptr.
    IPR004937. Urea_transporter.
    [Graphical view ]
    PANTHERi PTHR10464. PTHR10464. 1 hit.
    Pfami PF03253. UT. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF016502. Urea_transporter. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Urea-selective concentrating defect in transgenic mice lacking urea transporter UT-B."
      Yang B., Bankir L., Gillespie A., Epstein C.J., Verkman A.S.
      J. Biol. Chem. 277:10633-10637(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
      Strain: C57BL/6.
      Tissue: Kidney.
    2. "UT-B1 urea transporter is expressed along the urinary and gastrointestinal tracts of the mouse."
      Lucien N., Bruneval P., Lasbennes F., Belair M.F., Mandet C., Cartron J.P., Bailly P., Trinh-Trang-Tan M.M.
      Am. J. Physiol. 288:R1046-R1056(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE SPECIFICITY, GLYCOSYLATION, INDUCTION.
      Strain: BALB/c.
      Tissue: Kidney.
    3. "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] (ISOFORMS 1 AND 2).
      Strain: C57BL/6J and NOD.
      Tissue: Embryo and Thymus.
    4. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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 1).
      Strain: C57BL/6 and C57BL/6NCr.
      Tissue: Eye, Head and Hematopoietic stem cell.
    6. "Analysis of double knockout mice lacking aquaporin-1 and urea transporter UT-B. Evidence for UT-B-facilitated water transport in erythrocytes."
      Yang B., Verkman A.S.
      J. Biol. Chem. 277:36782-36786(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.

    Entry informationi

    Entry nameiUT1_MOUSE
    AccessioniPrimary (citable) accession number: Q8VHL0
    Secondary accession number(s): Q3U542
    , Q497G1, Q5RJG2, Q6PDP4, Q9CZX3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 30, 2002
    Last sequence update: June 28, 2011
    Last modified: October 1, 2014
    This is version 93 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, 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