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Q8VHL0 (UT1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Urea transporter 1
Alternative name(s):
Solute carrier family 14 member 1
Urea transporter B
Short name=UT-B
Urea transporter, erythrocyte
Gene names
Name:Slc14a1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length384 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Low-affinity facilitative urea transporter that allow rapid equilibration between the urinary space and the hyperosmotic interstitium. the rate of urea conduction is increased by hypoosmotic stress By similarity. Mediates urea transport in erythrocytes. Ref.1

Subunit structure

Homotrimer By similarity.

Subcellular location

Cell membrane; Multi-pass membrane protein. Basolateral cell membrane. Note: Restricted to the basolateral membrane in various portions of the urothelium. Ref.2

Tissue specificity

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). Ref.1 Ref.2

Induction

Down-regulated by water deprivation in urinary bladder and ureter, but not in kidney medulla, colon, testis nor brain. Ref.2

Post-translational modification

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. Ref.2

Disruption phenotype

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 was 1.5-fold greater and urine osmolarity was 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. Ref.1

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8VHL0-1)

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.
Isoform 2 (identifier: Q8VHL0-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 384384Urea transporter 1
PRO_0000065738

Regions

Transmembrane61 – 8121Helical; Potential
Transmembrane85 – 10521Helical; Potential
Transmembrane111 – 13121Helical; Potential
Transmembrane138 – 15821Helical; Potential
Transmembrane168 – 18821Helical; Potential
Transmembrane250 – 27021Helical; Potential
Transmembrane276 – 29621Helical; Potential
Transmembrane305 – 32521Helical; Potential
Transmembrane327 – 34721Helical; Potential

Amino acid modifications

Glycosylation2061N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence11M → MNGQSLTGGTDDAHHGPLWI DPFGNRGDKAAPEGFRRLSL ALAQRWREQEPEEEIAM in isoform 2.
VSP_041574

Experimental info

Sequence conflict81V → A in AAL47138. Ref.1
Sequence conflict501V → A in AAI00571. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 28, 2011. Version 2.
Checksum: E66ED087341C07B7

FASTA38442,126
        10         20         30         40         50         60 
MEDSPTMVKV DRGENQILSC RGRRCGFKVL GYVTGDMKEF ANWLKDKPVV LQFMDWILRG 

        70         80         90        100        110        120 
ISQVVFVSNP ISGILILVGL LVQNPWWALC GCVGTVVSTL TALLLSQDRS AIAAGLQGYN 

       130        140        150        160        170        180 
ATLVGILMAV FSNKGDYFWW LIFPVSAMSM TCPVFSSALS SVLSKWDLPV FTLPFNMALS 

       190        200        210        220        230        240 
MYLSATGHYN TFFPSKLFTP VSSVPNITWS ELSALELLKS LPVGVGQIYG CDNPWTGGIF 

       250        260        270        280        290        300 
LCAILLSSPL MCLHAAIGSL LGVIAGLSLA APFEDIYFGL WGFNSSLACI AIGGMFMALT 

       310        320        330        340        350        360 
WQTHLLALAC ALFTAYFGAC MAHLMAVVHL PACTWSFCLA TLLFLLLTTK NPNIYRMPLS 

       370        380 
KVTYSEENRI FYLQNKKRMV ESPL 

« Hide

Isoform 2 [UniParc].

Checksum: BA248DED75D9772A
Show »

FASTA44048,338

References

« Hide 'large scale' references
[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. 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] (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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_001164481.1. NM_001171010.1.
NP_001164482.1. NM_001171011.1.
NP_082398.1. NM_028122.4.
UniGeneMm.33832.

3D structure databases

ProteinModelPortalQ8VHL0.
SMRQ8VHL0. Positions 31-376.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000025433.

Chemistry

ChEMBLCHEMBL2163171.

Proteomic databases

PaxDbQ8VHL0.
PRIDEQ8VHL0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000091813; ENSMUSP00000089421; ENSMUSG00000059336. [Q8VHL0-1]
ENSMUST00000160292; ENSMUSP00000125114; ENSMUSG00000059336. [Q8VHL0-2]
ENSMUST00000160639; ENSMUSP00000125367; ENSMUSG00000059336. [Q8VHL0-1]
GeneID108052.
KEGGmmu:108052.
UCSCuc008fsc.2. mouse. [Q8VHL0-1]
uc008fsd.2. mouse. [Q8VHL0-2]

Organism-specific databases

CTD6563.
MGIMGI:1351654. Slc14a1.

Phylogenomic databases

eggNOGCOG4413.
GeneTreeENSGT00390000018729.
HOGENOMHOG000065705.
HOVERGENHBG000540.
InParanoidQ3U542.
KOK08716.
OMAVGVGQIY.
OrthoDBEOG7GBFX8.
TreeFamTF332858.

Gene expression databases

BgeeQ8VHL0.
GenevestigatorQ8VHL0.

Family and domain databases

InterProIPR004937. Urea_transporter.
[Graphical view]
PANTHERPTHR10464. PTHR10464. 1 hit.
PfamPF03253. UT. 1 hit.
[Graphical view]
PIRSFPIRSF016502. Urea_transporter. 1 hit.
ProtoNetSearch...

Other

NextBio359947.
PROQ8VHL0.
SOURCESearch...

Entry information

Entry nameUT1_MOUSE
AccessionPrimary (citable) accession number: Q8VHL0
Secondary accession number(s): Q3U542 expand/collapse secondary AC list , Q497G1, Q5RJG2, Q6PDP4, Q9CZX3
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2002
Last sequence update: June 28, 2011
Last modified: April 16, 2014
This is version 88 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

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