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   27-MAR-2024, entry version 109.
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.ENSRNOP00000065722; -.
DR   BindingDB; P97689; -.
DR   ChEMBL; CHEMBL3739247; -.
DR   GuidetoPHARMACOLOGY; 982; -.
DR   TCDB; 1.A.28.1.3; the urea transporter (ut) family.
DR   GlyCosmos; P97689; 1 site, No reported glycans.
DR   GlyGen; P97689; 1 site.
DR   PhosphoSitePlus; P97689; -.
DR   PaxDb; 10116-ENSRNOP00000022598; -.
DR   GeneID; 54301; -.
DR   KEGG; rno:54301; -.
DR   AGR; RGD:3688; -.
DR   RGD; 3688; Slc14a1.
DR   eggNOG; ENOG502S2GD; Eukaryota.
DR   InParanoid; P97689; -.
DR   OrthoDB; 3682310at2759; -.
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: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:0051649; P:establishment of localization in cell; 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; Ammonium transporter AmtB like domains; 1.
DR   InterPro; IPR029020; Ammonium/urea_transptr.
DR   InterPro; IPR004937; Urea_transporter.
DR   PANTHER; PTHR10464; UREA TRANSPORTER; 1.
DR   PANTHER; PTHR10464:SF5; UREA TRANSPORTER 1; 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
//