UT1_RAT
ID UT1_RAT Reviewed; 384 AA.
AC P97689; E9PSP0; P70633;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 2.
DT 03-AUG-2022, entry version 102.
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; Synonyms=UT11, UT3;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=Sprague-Dawley;
RA Tsukaguchi H., Shayakul C., Berger U.V., Tokui T., Brown D., Hediger M.A.;
RL Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-382, FUNCTION, TRANSPORTER ACTIVITY, AND
RP TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Kidney;
RX PubMed=8982255; DOI=10.1016/s0167-4781(96)00172-8;
RA Couriaud C., Ripoche P., Rousselet G.;
RT "Cloning and functional characterization of a rat urea transporter:
RT expression in the brain.";
RL Biochim. Biophys. Acta 1309:197-199(1996).
CC -!- FUNCTION: Mediates the transport of urea driven by a concentration
CC gradient across the cell membrane (PubMed:8982255). Mediates the
CC transport of urea across the cell membranes of erythrocytes and the
CC renal inner medullary collecting duct which is critical to the urinary
CC concentrating mechanism (By similarity). Facilitates water transport in
CC erythrocytes (By similarity). {ECO:0000250|UniProtKB:Q8VHL0,
CC ECO:0000269|PubMed:8982255}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=urea(in) = urea(out); Xref=Rhea:RHEA:32799, ChEBI:CHEBI:16199;
CC Evidence={ECO:0000269|PubMed:8982255};
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:0000250|UniProtKB:Q8VHL0};
CC Multi-pass membrane protein {ECO:0000255}. Basolateral cell membrane
CC {ECO:0000250|UniProtKB:Q8VHL0}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Restricted to the basolateral membrane in various
CC portions of the urothelium. {ECO:0000250|UniProtKB:Q8VHL0}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P97689-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P97689-2; Sequence=VSP_041576;
CC -!- TISSUE SPECIFICITY: Expressed in brain, spleen, kidney, testis and
CC lung, with highest levels in brain. {ECO:0000269|PubMed:8982255}.
CC -!- SIMILARITY: Belongs to the urea transporter family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA67049.1; Type=Miscellaneous discrepancy; Evidence={ECO:0000305};
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DR EMBL; U81518; AAB39937.1; -; mRNA.
DR EMBL; X98399; CAA67049.1; ALT_SEQ; mRNA.
DR RefSeq; NP_062219.2; NM_019346.2.
DR AlphaFoldDB; P97689; -.
DR SMR; P97689; -.
DR BioGRID; 248521; 1.
DR STRING; 10116.ENSRNOP00000022598; -.
DR BindingDB; P97689; -.
DR ChEMBL; CHEMBL3739247; -.
DR GuidetoPHARMACOLOGY; 982; -.
DR TCDB; 1.A.28.1.3; the urea transporter (ut) family.
DR GlyGen; P97689; 1 site.
DR PaxDb; P97689; -.
DR PRIDE; P97689; -.
DR GeneID; 54301; -.
DR KEGG; rno:54301; -.
DR CTD; 6563; -.
DR RGD; 3688; Slc14a1.
DR eggNOG; ENOG502S2GD; Eukaryota.
DR InParanoid; P97689; -.
DR OrthoDB; 1478665at2759; -.
DR Reactome; R-RNO-425366; Transport of bile salts and organic acids, metal ions and amine compounds.
DR PRO; PR:P97689; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0016323; C:basolateral plasma membrane; ISS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0015265; F:urea channel activity; ISS:UniProtKB.
DR GO; GO:0015204; F:urea transmembrane transporter activity; IDA:RGD.
DR GO; GO:0005372; F:water transmembrane transporter activity; ISO:RGD.
DR GO; GO:0071918; P:urea transmembrane transport; ISS:UniProtKB.
DR GO; GO:0015840; P:urea transport; IDA:RGD.
DR GO; GO:0006833; P:water transport; ISO:RGD.
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 2: Evidence at transcript level;
KW Alternative splicing; Cell membrane; Glycoprotein; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..384
FT /note="Urea transporter 1"
FT /id="PRO_0000410964"
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 279..299
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 -> MNGQSLSGGTDDSHHDPLWIDPFGNRAGKAAPGGFRRLNLFLAQRWQ
FT EQEPEEEMA (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_041576"
FT CONFLICT 25
FT /note="C -> W (in Ref. 1; AAB39937)"
FT /evidence="ECO:0000305"
FT CONFLICT 47
FT /note="K -> E (in Ref. 1; AAB39937)"
FT /evidence="ECO:0000305"
FT CONFLICT 50
FT /note="V -> G (in Ref. 1; AAB39937)"
FT /evidence="ECO:0000305"
FT CONFLICT 180
FT /note="S -> A (in Ref. 1; AAB39937)"
FT /evidence="ECO:0000305"
FT CONFLICT 266
FT /note="G -> R (in Ref. 1; AAB39937)"
FT /evidence="ECO:0000305"
FT CONFLICT 325
FT /note="M -> I (in Ref. 1; AAB39937)"
FT /evidence="ECO:0000305"
FT CONFLICT 339
FT /note="L -> F (in Ref. 1; AAB39937)"
FT /evidence="ECO:0000305"
FT CONFLICT 378..379
FT /note="RV -> SA (in Ref. 1; AAB39937)"
FT /evidence="ECO:0000305"
FT CONFLICT 382
FT /note="S -> R (in Ref. 1; AAB39937)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 384 AA; 42034 MW; 1BBD9E8D60CFD6CA CRC64;
MEDIPTMVKV DRGESQILSC RGRRCGLKVL GYVTGDMKEF ANWLKDKPVV LQFMDWILRG
ISQVVFVSNP ISGILILAGL LVQNPWWALC GCVGTVVSTL TALLLSQDRS AIAAGLQGYN
ATLVGILMAV FSDKGDYFWW LIFPVSAMSM TCPVFSSALS SLFSKWDLPV FTLPFNMALS
LYLSATGHYN TFFPSKLFMP VSSVPNITWS ELSALELLKS LPVGVGQIYG CDNPWTGAIF
LCAILLSSPL MCLHAAIGSL LGVIAGLSLA APFKDIYSGL WGFNSSLACI AIGGMFMALT
WQTHLLALAC ALFTAYFGAC MTHLMAAVHL PACTWSFCLA TLLFLLLTTE NPNIYRMPLS
KVTYSEENRI FYLQNKKRVV DSPL
