UT1_MOUSE
ID UT1_MOUSE Reviewed; 384 AA.
AC Q8VHL0; Q3U542; Q497G1; Q5RJG2; Q6PDP4; Q9CZX3;
DT 30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Urea transporter 1;
DE AltName: Full=Solute carrier family 14 member 1;
DE AltName: Full=Urea transporter B;
DE Short=UT-B;
DE AltName: Full=Urea transporter, erythrocyte;
GN Name=Slc14a1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TRANSPORTER ACTIVITY,
RP TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RC STRAIN=C57BL/6J; TISSUE=Kidney;
RX PubMed=11792714; DOI=10.1074/jbc.m200207200;
RA Yang B., Bankir L., Gillespie A., Epstein C.J., Verkman A.S.;
RT "Urea-selective concentrating defect in transgenic mice lacking urea
RT transporter UT-B.";
RL J. Biol. Chem. 277:10633-10637(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, GLYCOSYLATION, AND INDUCTION.
RC STRAIN=BALB/cJ; TISSUE=Kidney;
RX PubMed=15563580; DOI=10.1152/ajpregu.00286.2004;
RA Lucien N., Bruneval P., Lasbennes F., Belair M.F., Mandet C., Cartron J.P.,
RA Bailly P., Trinh-Trang-Tan M.M.;
RT "UT-B1 urea transporter is expressed along the urinary and gastrointestinal
RT tracts of the mouse.";
RL Am. J. Physiol. 288:R1046-R1056(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Embryo, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J, and C57BL/6NCr;
RC TISSUE=Eye, Head, and Hematopoietic stem cell;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=12133842; DOI=10.1074/jbc.m206948200;
RA Yang B., Verkman A.S.;
RT "Analysis of double knockout mice lacking aquaporin-1 and urea transporter
RT UT-B. Evidence for UT-B-facilitated water transport in erythrocytes.";
RL J. Biol. Chem. 277:36782-36786(2002).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39 (ISOFORM 2), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Mediates the transport of urea driven by a concentration
CC gradient across the cell membranes of erythrocytes and the renal inner
CC medullary collecting duct which is critical to the urinary
CC concentrating mechanism (PubMed:11792714). Facilitates water transport
CC in erythrocytes (PubMed:12133842). {ECO:0000269|PubMed:11792714,
CC ECO:0000269|PubMed:12133842}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=urea(in) = urea(out); Xref=Rhea:RHEA:32799, ChEBI:CHEBI:16199;
CC Evidence={ECO:0000269|PubMed:11792714};
CC -!- SUBUNIT: Homotrimer; each subunit contains a pore through which urea
CC permeates (By similarity). Identified in a complex with STOM (By
CC similarity). {ECO:0000250|UniProtKB:Q13336,
CC ECO:0000250|UniProtKB:Q5QF96}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12133842,
CC ECO:0000269|PubMed:15563580}; Multi-pass membrane protein
CC {ECO:0000255}. Basolateral cell membrane {ECO:0000269|PubMed:15563580};
CC Multi-pass membrane protein {ECO:0000255}. Note=Restricted to the
CC basolateral membrane in various portions of the urothelium.
CC {ECO:0000269|PubMed:15563580}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8VHL0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8VHL0-2; Sequence=VSP_041574;
CC -!- TISSUE SPECIFICITY: Expressed in brain, kidney, heart, liver, lung,
CC skeletal muscle, spleen, testis, ureter and urinary bladder (at protein
CC level). Along the gastrointestinal tract, detected in colon, jejunum
CC and stomach (at protein level). In the kidney, expressed in some
CC microvessels of the inner and outer medulla, but not all (at protein
CC level). Not detected in the cortex (at protein level). Detected in the
CC urothelium all along the urinary tract, including the papilla surface,
CC the ureter, the bladder and the urethra (at protein level). In the
CC brain, expressed at the border of the corpus callosum and striatum in
CC astrocytic cellular processes surrounding blood microvessels (at
CC protein level). Detected in erythrocytes (at protein level).
CC {ECO:0000269|PubMed:11792714, ECO:0000269|PubMed:12133842,
CC ECO:0000269|PubMed:15563580}.
CC -!- INDUCTION: Down-regulated by water deprivation in urinary bladder and
CC ureter, but not in kidney medulla, colon, testis nor brain.
CC {ECO:0000269|PubMed:15563580}.
CC -!- PTM: N-glycosylated in red blood cells, as well as in most non-
CC erythroid tissues, except in the gastrocnemius muscle and in the
CC gastrointestinal tract, including liver, colon and stomach.
CC {ECO:0000269|PubMed:15563580}.
CC -!- DISRUPTION PHENOTYPE: Mutant mice exhibit grossly normal appearance,
CC activity and behavior. Plasma sodium, potassium, chloride, bicarbonate
CC and creatinine concentrations, as well as hematocrit, are similar to
CC wild type animals. Urea permeability in erythrocytes is 45-fold lower
CC than that from wild-type mice. Daily urine output is 1.5-fold greater
CC and urine osmolarity is lower than in wild-type mice. After 24 hours of
CC water deprivation, plasma urea concentration is 30% higher and urine
CC urea concentration 35% lower in mutant mice than in wild-type animals.
CC Mice lacking both Aqp1 and Slc14a1 are born at the expected Mendelian
CC ratio, but do not thrive; half of them die within ten days after birth
CC and none are alive after two weeks. Urine osmolality is somewhat lower
CC than that observed with mice lacking Aqp1. Besides, erythrocyte water
CC permeability is significantly lower than in mice lacking only Aqp1.
CC {ECO:0000269|PubMed:11792714, ECO:0000269|PubMed:12133842}.
CC -!- SIMILARITY: Belongs to the urea transporter family. {ECO:0000305}.
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DR EMBL; AF448798; AAL47138.1; -; mRNA.
DR EMBL; AJ420967; CAD12807.1; -; mRNA.
DR EMBL; AK012066; BAB28004.1; -; mRNA.
DR EMBL; AK041979; BAC31119.1; -; mRNA.
DR EMBL; AK153891; BAE32238.1; -; mRNA.
DR EMBL; CH466528; EDL09437.1; -; Genomic_DNA.
DR EMBL; CH466528; EDL09438.1; -; Genomic_DNA.
DR EMBL; BC058594; AAH58594.2; -; mRNA.
DR EMBL; BC086673; AAH86673.1; -; mRNA.
DR EMBL; BC100570; AAI00571.2; -; mRNA.
DR CCDS; CCDS29360.1; -. [Q8VHL0-1]
DR CCDS; CCDS50330.1; -. [Q8VHL0-2]
DR RefSeq; NP_001164481.1; NM_001171010.1. [Q8VHL0-2]
DR RefSeq; NP_001164482.1; NM_001171011.1. [Q8VHL0-1]
DR RefSeq; NP_082398.1; NM_028122.4. [Q8VHL0-1]
DR AlphaFoldDB; Q8VHL0; -.
DR SMR; Q8VHL0; -.
DR STRING; 10090.ENSMUSP00000125114; -.
DR BindingDB; Q8VHL0; -.
DR ChEMBL; CHEMBL2163171; -.
DR GuidetoPHARMACOLOGY; 982; -.
DR GlyGen; Q8VHL0; 1 site.
DR iPTMnet; Q8VHL0; -.
DR PhosphoSitePlus; Q8VHL0; -.
DR SwissPalm; Q8VHL0; -.
DR EPD; Q8VHL0; -.
DR MaxQB; Q8VHL0; -.
DR PaxDb; Q8VHL0; -.
DR PeptideAtlas; Q8VHL0; -.
DR PRIDE; Q8VHL0; -.
DR ProteomicsDB; 299662; -. [Q8VHL0-1]
DR ProteomicsDB; 299663; -. [Q8VHL0-2]
DR Antibodypedia; 22414; 167 antibodies from 25 providers.
DR DNASU; 108052; -.
DR Ensembl; ENSMUST00000091813; ENSMUSP00000089421; ENSMUSG00000059336. [Q8VHL0-1]
DR Ensembl; ENSMUST00000160292; ENSMUSP00000125114; ENSMUSG00000059336. [Q8VHL0-2]
DR Ensembl; ENSMUST00000160639; ENSMUSP00000125367; ENSMUSG00000059336. [Q8VHL0-1]
DR GeneID; 108052; -.
DR KEGG; mmu:108052; -.
DR UCSC; uc008fsc.2; mouse. [Q8VHL0-1]
DR UCSC; uc008fsd.2; mouse. [Q8VHL0-2]
DR CTD; 6563; -.
DR MGI; MGI:1351654; Slc14a1.
DR VEuPathDB; HostDB:ENSMUSG00000059336; -.
DR eggNOG; ENOG502S2GD; Eukaryota.
DR GeneTree; ENSGT00390000018729; -.
DR HOGENOM; CLU_047509_1_0_1; -.
DR InParanoid; Q8VHL0; -.
DR OrthoDB; 1478665at2759; -.
DR TreeFam; TF332858; -.
DR Reactome; R-MMU-425366; Transport of bile salts and organic acids, metal ions and amine compounds.
DR BioGRID-ORCS; 108052; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Slc14a1; mouse.
DR PRO; PR:Q8VHL0; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q8VHL0; protein.
DR Bgee; ENSMUSG00000059336; Expressed in bone marrow and 89 other tissues.
DR Genevisible; Q8VHL0; MM.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; TAS:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0015265; F:urea channel activity; ISS:UniProtKB.
DR GO; GO:0015204; F:urea transmembrane transporter activity; IMP:MGI.
DR GO; GO:0005372; F:water transmembrane transporter activity; IDA:MGI.
DR GO; GO:0051649; P:establishment of localization in cell; IGI:MGI.
DR GO; GO:0071918; P:urea transmembrane transport; ISS:UniProtKB.
DR GO; GO:0015840; P:urea transport; IMP:MGI.
DR GO; GO:0006833; P:water transport; IDA:MGI.
DR Gene3D; 1.10.3430.10; -; 1.
DR InterPro; IPR029020; Ammonium/urea_transptr.
DR InterPro; IPR004937; Urea_transporter.
DR PANTHER; PTHR10464; PTHR10464; 1.
DR Pfam; PF03253; UT; 1.
DR PIRSF; PIRSF016502; Urea_transporter; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Glycoprotein; Membrane;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..384
FT /note="Urea transporter 1"
FT /id="PRO_0000065738"
FT TRANSMEM 61..81
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 85..105
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 111..131
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 138..158
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 168..188
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 250..270
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 276..296
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 305..325
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 327..347
FT /note="Helical"
FT /evidence="ECO:0000255"
FT SITE 334
FT /note="Important for channel permeability"
FT /evidence="ECO:0000250|UniProtKB:Q5QF96"
FT CARBOHYD 206
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1
FT /note="M -> MNGQSLTGGTDDAHHGPLWIDPFGNRGDKAAPEGFRRLSLALAQRWR
FT EQEPEEEIAM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_041574"
FT CONFLICT 8
FT /note="V -> A (in Ref. 1; AAL47138)"
FT /evidence="ECO:0000305"
FT CONFLICT 50
FT /note="V -> A (in Ref. 5; AAI00571)"
FT /evidence="ECO:0000305"
FT MOD_RES Q8VHL0-2:39
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 384 AA; 42126 MW; E66ED087341C07B7 CRC64;
MEDSPTMVKV DRGENQILSC RGRRCGFKVL GYVTGDMKEF ANWLKDKPVV LQFMDWILRG
ISQVVFVSNP ISGILILVGL LVQNPWWALC GCVGTVVSTL TALLLSQDRS AIAAGLQGYN
ATLVGILMAV FSNKGDYFWW LIFPVSAMSM TCPVFSSALS SVLSKWDLPV FTLPFNMALS
MYLSATGHYN TFFPSKLFTP VSSVPNITWS ELSALELLKS LPVGVGQIYG CDNPWTGGIF
LCAILLSSPL MCLHAAIGSL LGVIAGLSLA APFEDIYFGL WGFNSSLACI AIGGMFMALT
WQTHLLALAC ALFTAYFGAC MAHLMAVVHL PACTWSFCLA TLLFLLLTTK NPNIYRMPLS
KVTYSEENRI FYLQNKKRMV ESPL
