ID   UT2_RABIT               Reviewed;         397 AA.
AC   Q28614;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Urea transporter 2;
DE   AltName: Full=Solute carrier family 14 member 2;
DE   AltName: Full=Urea transporter, kidney;
DE   AltName: Full=Vasopressin-regulated urea transporter;
GN   Name=SLC14A2; Synonyms=UT2;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TRANSPORTER ACTIVITY, ACTIVITY
RP   REGULATION, AND TISSUE SPECIFICITY.
RC   TISSUE=Kidney;
RX   PubMed=8413669; DOI=10.1038/365844a0;
RA   You G., Smith C.P., Kanai Y., Lee W.-S., Stelzner M., Hediger M.A.;
RT   "Cloning and characterization of the vasopressin-regulated urea
RT   transporter.";
RL   Nature 365:844-847(1993).
RN   [2]
RP   FUNCTION, TRANSPORTER ACTIVITY, AND ACTIVITY REGULATION.
RX   PubMed=8997401; DOI=10.1152/ajprenal.1996.271.6.f1264;
RA   Martial S., Olives B., Abrami L., Couriaud C., Bailly P., You G.,
RA   Hediger M.A., Cartron J.P., Ripoche P., Rousselet G.;
RT   "Functional differentiation of the human red blood cell and kidney urea
RT   transporters.";
RL   Am. J. Physiol. 271:F1264-F1268(1996).
CC   -!- FUNCTION: Mediates the transport of urea driven by a concentration
CC       gradient across the cell membrane of the renal inner medullary
CC       collecting duct which is critical to the urinary concentrating
CC       mechanism. {ECO:0000269|PubMed:8413669, ECO:0000269|PubMed:8997401}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=urea(in) = urea(out); Xref=Rhea:RHEA:32799, ChEBI:CHEBI:16199;
CC         Evidence={ECO:0000269|PubMed:8413669, ECO:0000269|PubMed:8997401};
CC   -!- ACTIVITY REGULATION: Inhibited by urea analogs and phloretin.
CC       {ECO:0000269|PubMed:8413669, ECO:0000269|PubMed:8997401}.
CC   -!- SUBCELLULAR LOCATION: Apical cell membrane
CC       {ECO:0000250|UniProtKB:Q8R4T9}; Multi-pass membrane protein
CC       {ECO:0000255}. Basolateral cell membrane
CC       {ECO:0000250|UniProtKB:Q8R4T9}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Kidney. {ECO:0000269|PubMed:8413669}.
CC   -!- SIMILARITY: Belongs to the urea transporter family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U10358; AAA19008.1; -; mRNA.
DR   PIR; S38283; S38283.
DR   RefSeq; NP_001075809.1; NM_001082340.1.
DR   AlphaFoldDB; Q28614; -.
DR   SMR; Q28614; -.
DR   STRING; 9986.ENSOCUP00000005837; -.
DR   GeneID; 100009190; -.
DR   KEGG; ocu:100009190; -.
DR   CTD; 8170; -.
DR   eggNOG; ENOG502QWSG; Eukaryota.
DR   InParanoid; Q28614; -.
DR   OrthoDB; 1478665at2759; -.
DR   Proteomes; UP000001811; Unplaced.
DR   GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0015204; F:urea transmembrane transporter activity; IDA:UniProtKB.
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   Cell membrane; Glycoprotein; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..397
FT                   /note="Urea transporter 2"
FT                   /id="PRO_0000065740"
FT   TRANSMEM        68..85
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        92..109
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        115..135
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        143..163
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        172..192
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        239..257
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        264..280
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        287..303
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        309..329
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        331..351
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        210
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   397 AA;  43136 MW;  D99B7968B078C44A CRC64;
     MEDSSEIKVE TASSRTSWIQ SSVAAGGKRI SRALGYITGE MKECAEGLKD KSPVFQFLDW
     VLRGTSQVMF VNNPLSGILI VIGLFVQNPW WAIAGCLGTV MSTLTALILS QDRSAIASGL
     HGYNGVLVGL LIAVFSDKGD YYWWLLLPVI VMSMSCPILS SALGTIFSKW DLPVFTLPFN
     IAVTLYLAAT GHYNLFFPTT LLQPVSSVPN ITWSEIQVPL LLRAIPVGIG QVYGCDNPWT
     GGIFLIALFI SSPLICLHAA IGSTMGMLAA LTIATPFDSI YFGLCGFNST LACIAVGGMF
     YVITWQTHLL AVACALFAAY VGAALTNVLS VFGLPTCTWP FCISALIFLL LTTNNPAIYK
     LPLSKVTYPE ANRTYYLTQE RNRRSSTITK YQAYDVS