ID   UT1_CAPHI               Reviewed;         384 AA.
AC   D3INW7;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   23-MAR-2010, sequence version 1.
DT   27-MAR-2024, entry version 48.
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   Capra hircus (Goat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Capra.
OX   NCBI_TaxID=9925;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Zeng J.Y., Zhong R.Z., Tan C.Y., Tang S.X., Han X.F., Xu Q., Yan Q.X.,
RA   Wang M., Zhou C.S., Yuan Z.Q., Tan Z.L.;
RT   "Effect of tea polyphenols on nitrogen metabolism of growing goats.";
RL   Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). Facilitates water transport in
CC       erythrocytes (By similarity). {ECO:0000250|UniProtKB:Q8VHL0}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=urea(in) = urea(out); Xref=Rhea:RHEA:32799, ChEBI:CHEBI:16199;
CC         Evidence={ECO:0000250|UniProtKB:Q13336};
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   -!- SIMILARITY: Belongs to the urea transporter family. {ECO:0000305}.
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DR   EMBL; GQ148778; ADB79799.1; -; mRNA.
DR   RefSeq; XP_005697222.1; XM_005697165.3.
DR   AlphaFoldDB; D3INW7; -.
DR   SMR; D3INW7; -.
DR   STRING; 9925.ENSCHIP00000002595; -.
DR   GlyCosmos; D3INW7; 1 site, No reported glycans.
DR   Ensembl; ENSCHIT00000008263.1; ENSCHIP00000002601.1; ENSCHIG00000006085.1.
DR   Ensembl; ENSCHIT00000008300.1; ENSCHIP00000002608.1; ENSCHIG00000006085.1.
DR   GeneID; 100860878; -.
DR   KEGG; chx:100860878; -.
DR   CTD; 6563; -.
DR   GeneTree; ENSGT00390000018729; -.
DR   OMA; YFPEVKI; -.
DR   OrthoDB; 3682310at2759; -.
DR   Proteomes; UP000291000; Chromosome 24.
DR   Proteomes; UP000694566; Unplaced.
DR   Proteomes; UP000694900; Genome assembly.
DR   Bgee; ENSCHIG00000006085; Expressed in testis and 12 other cell types or tissues.
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; ISS:UniProtKB.
DR   GO; GO:0071918; P:urea transmembrane transport; ISS:UniProtKB.
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   Cell membrane; Glycoprotein; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..384
FT                   /note="Urea transporter 1"
FT                   /id="PRO_0000410963"
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        237..257
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        279..299
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        327..347
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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"
SQ   SEQUENCE   384 AA;  41515 MW;  C695A2F1E98B1ACA CRC64;
     MDDNPTAVKL DQGGNQAPQG QGRRRLPKAL GYITGDMKEF ANWLKDKPQA LQFVDWVLRG
     ISQVVFVSNP ISGILILVGL LVQNPWCALN GCVGTVVSTL TALLLNQDRS AITAGLQGYN
     ATLVGILMAI YSDKGNYFWW LLFPVSAMSM TCPIFSSALN SVLSKWDLPV FTLPFNMALS
     MYLSATGHYN PFFPSTLVTP VTSVPNVTWP DLSALQLLKS LPVGVGQIYG CDNPWAGGIF
     LGAILLSSPL MCLHAAIGSL LGIIAGLSLS APFENIYAGL WGFNSSLACI AIGGMFMALT
     WQTHLLALAC ALFTAYLGAS MSHVMAVVGL PSCTWPFCLA TLLFLLLTTK NPNIYKMPIS
     KVTYPEENRI FYLQSTKRTV QGPL
//