UT1_BOVIN
ID UT1_BOVIN Reviewed; 384 AA.
AC Q5QF96; Q2KJI0; Q2TM53;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 99.
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=UT-B;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), FUNCTION,
RP TRANSPORTER ACTIVITY, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=15845882; DOI=10.1152/ajpregu.00127.2005;
RA Stewart G.S., Graham C., Cattell S., Smith T.P., Simmons N.L., Smith C.P.;
RT "UT-B is expressed in bovine rumen: potential role in ruminal urea
RT transport.";
RL Am. J. Physiol. 289:R605-R612(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.36 ANGSTROMS), FUNCTION, TRANSPORTER ACTIVITY,
RP SUBUNIT, ACTIVITY REGULATION, SUBCELLULAR LOCATION, MUTAGENESIS OF THR-172
RP AND THR-334, AND SITE.
RX PubMed=22733730; DOI=10.1073/pnas.1207362109;
RA Levin E.J., Cao Y., Enkavi G., Quick M., Pan Y., Tajkhorshid E., Zhou M.;
RT "Structure and permeation mechanism of a mammalian urea transporter.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:11194-11199(2012).
CC -!- FUNCTION: Mediates the transport of urea driven by a concentration
CC gradient across the cell membrane (PubMed:15845882, PubMed:22733730).
CC Mediates the transport of urea across the cell membranes of
CC erythrocytes and the renal inner medullary collecting duct which is
CC critical to the urinary concentrating mechanism (By similarity).
CC Facilitates water transport in erythrocytes (By similarity).
CC {ECO:0000250|UniProtKB:Q8VHL0, ECO:0000269|PubMed:15845882,
CC ECO:0000269|PubMed:22733730}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=urea(in) = urea(out); Xref=Rhea:RHEA:32799, ChEBI:CHEBI:16199;
CC Evidence={ECO:0000269|PubMed:15845882, ECO:0000269|PubMed:22733730};
CC -!- ACTIVITY REGULATION: The rate of urea conduction is increased by
CC hypotonic stress. {ECO:0000269|PubMed:22733730}.
CC -!- SUBUNIT: Homotrimer; each subunit contains a pore through which urea
CC permeates (PubMed:22733730). Identified in a complex with STOM (By
CC similarity). {ECO:0000250|UniProtKB:Q13336,
CC ECO:0000269|PubMed:22733730}.
CC -!- INTERACTION:
CC Q5QF96-1; Q5QF96-1: SLC14A1; NbExp=2; IntAct=EBI-15992000, EBI-15992000;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15845882,
CC ECO:0000269|PubMed:22733730}; Multi-pass membrane protein
CC {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; Synonyms=UT-B1;
CC IsoId=Q5QF96-1; Sequence=Displayed;
CC Name=2; Synonyms=UT-B2;
CC IsoId=Q5QF96-2; Sequence=VSP_041575;
CC -!- TISSUE SPECIFICITY: [Isoform 1]: Expressed in both kidney and rumen (at
CC protein level). {ECO:0000269|PubMed:15845882}.
CC -!- TISSUE SPECIFICITY: [Isoform 2]: Expressed in both kidney and rumen and
CC is the predominant isoform in the rumen (at protein level).
CC {ECO:0000269|PubMed:15845882}.
CC -!- SIMILARITY: Belongs to the urea transporter family. {ECO:0000305}.
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DR EMBL; AY624602; AAU94647.1; -; mRNA.
DR EMBL; AY838799; AAW02793.1; -; Genomic_DNA.
DR EMBL; AY838799; AAW51203.1; -; Genomic_DNA.
DR EMBL; BC105333; AAI05334.1; -; mRNA.
DR RefSeq; NP_001008666.1; NM_001008666.1. [Q5QF96-1]
DR RefSeq; XP_005224169.1; XM_005224112.3. [Q5QF96-2]
DR RefSeq; XP_005224170.1; XM_005224113.3. [Q5QF96-2]
DR RefSeq; XP_005224171.1; XM_005224114.3. [Q5QF96-2]
DR RefSeq; XP_005224173.1; XM_005224116.3. [Q5QF96-1]
DR RefSeq; XP_010817116.1; XM_010818814.2. [Q5QF96-1]
DR PDB; 4EZC; X-ray; 2.36 A; A/B/C=1-384.
DR PDB; 4EZD; X-ray; 2.50 A; A/B/C=1-384.
DR PDBsum; 4EZC; -.
DR PDBsum; 4EZD; -.
DR AlphaFoldDB; Q5QF96; -.
DR SMR; Q5QF96; -.
DR DIP; DIP-60048N; -.
DR STRING; 9913.ENSBTAP00000044109; -.
DR PaxDb; Q5QF96; -.
DR PRIDE; Q5QF96; -.
DR Ensembl; ENSBTAT00000026475; ENSBTAP00000026475; ENSBTAG00000019870. [Q5QF96-1]
DR Ensembl; ENSBTAT00000046861; ENSBTAP00000044109; ENSBTAG00000019870. [Q5QF96-1]
DR Ensembl; ENSBTAT00000071419; ENSBTAP00000071511; ENSBTAG00000019870. [Q5QF96-1]
DR Ensembl; ENSBTAT00000077308; ENSBTAP00000068485; ENSBTAG00000019870. [Q5QF96-2]
DR Ensembl; ENSBTAT00000079410; ENSBTAP00000062552; ENSBTAG00000019870. [Q5QF96-1]
DR GeneID; 493988; -.
DR KEGG; bta:493988; -.
DR CTD; 6563; -.
DR VEuPathDB; HostDB:ENSBTAG00000019870; -.
DR eggNOG; ENOG502S2GD; Eukaryota.
DR GeneTree; ENSGT00390000018729; -.
DR HOGENOM; CLU_047509_1_0_1; -.
DR InParanoid; Q5QF96; -.
DR OMA; CPDWATA; -.
DR OrthoDB; 1478665at2759; -.
DR TreeFam; TF332858; -.
DR Proteomes; UP000009136; Chromosome 24.
DR Bgee; ENSBTAG00000019870; Expressed in rumen papilla and 64 other tissues.
DR ExpressionAtlas; Q5QF96; baseline.
DR GO; GO:0016323; C:basolateral plasma membrane; ISS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IMP:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0015265; F:urea channel activity; IDA:UniProtKB.
DR GO; GO:0015204; F:urea transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0005372; F:water transmembrane transporter activity; IEA:Ensembl.
DR GO; GO:0051649; P:establishment of localization in cell; IEA:Ensembl.
DR GO; GO:0071918; P:urea transmembrane transport; 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 1: Evidence at protein level;
KW 3D-structure; 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_0000410962"
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 237..257
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 REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 334
FT /note="Important for channel permeability"
FT /evidence="ECO:0000269|PubMed:22733730"
FT CARBOHYD 206
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1
FT /note="M -> MSGRSLIGAAGDAYPGPLWRGPFGKKSGEAAHRVFPWINLAVVQGPE
FT EQEPEETSM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15845882"
FT /id="VSP_041575"
FT MUTAGEN 172
FT /note="T->S: No effect on urea channel activity."
FT /evidence="ECO:0000269|PubMed:22733730"
FT MUTAGEN 334
FT /note="T->S: No effect on urea channel activity."
FT /evidence="ECO:0000269|PubMed:22733730"
FT MUTAGEN 334
FT /note="T->V: Nearly abolishes urea channel activity."
FT /evidence="ECO:0000269|PubMed:22733730"
FT CONFLICT 54
FT /note="V -> I (in Ref. 2; AAI05334)"
FT /evidence="ECO:0000305"
FT HELIX 38..45
FT /evidence="ECO:0007829|PDB:4EZC"
FT HELIX 49..62
FT /evidence="ECO:0007829|PDB:4EZC"
FT HELIX 63..65
FT /evidence="ECO:0007829|PDB:4EZC"
FT HELIX 70..83
FT /evidence="ECO:0007829|PDB:4EZC"
FT HELIX 85..104
FT /evidence="ECO:0007829|PDB:4EZC"
FT HELIX 109..114
FT /evidence="ECO:0007829|PDB:4EZC"
FT TURN 115..118
FT /evidence="ECO:0007829|PDB:4EZC"
FT HELIX 119..130
FT /evidence="ECO:0007829|PDB:4EZC"
FT HELIX 139..141
FT /evidence="ECO:0007829|PDB:4EZC"
FT HELIX 142..163
FT /evidence="ECO:0007829|PDB:4EZC"
FT HELIX 164..166
FT /evidence="ECO:0007829|PDB:4EZC"
FT HELIX 173..186
FT /evidence="ECO:0007829|PDB:4EZC"
FT STRAND 191..193
FT /evidence="ECO:0007829|PDB:4EZC"
FT HELIX 209..211
FT /evidence="ECO:0007829|PDB:4EZC"
FT HELIX 214..226
FT /evidence="ECO:0007829|PDB:4EZC"
FT HELIX 227..229
FT /evidence="ECO:0007829|PDB:4EZC"
FT HELIX 234..247
FT /evidence="ECO:0007829|PDB:4EZC"
FT HELIX 249..268
FT /evidence="ECO:0007829|PDB:4EZC"
FT HELIX 273..277
FT /evidence="ECO:0007829|PDB:4EZC"
FT TURN 278..282
FT /evidence="ECO:0007829|PDB:4EZC"
FT HELIX 283..292
FT /evidence="ECO:0007829|PDB:4EZC"
FT TURN 293..295
FT /evidence="ECO:0007829|PDB:4EZC"
FT HELIX 301..326
FT /evidence="ECO:0007829|PDB:4EZC"
FT TURN 327..329
FT /evidence="ECO:0007829|PDB:4EZC"
FT HELIX 335..345
FT /evidence="ECO:0007829|PDB:4EZC"
FT HELIX 359..361
FT /evidence="ECO:0007829|PDB:4EZC"
FT HELIX 365..374
FT /evidence="ECO:0007829|PDB:4EZC"
SQ SEQUENCE 384 AA; 41473 MW; 7AC8203F8A4E88A1 CRC64;
MDDNPTAVKL DQGGNQAPQG RGRRCLPKAL GYITGDMKEF ANWLKDKPQA LQFVDWVLRG
ISQVVFVSNP ISGILILVGL LVQNPWCALN GCVGTVVSTL TALLLSQDRS AITAGLQGYN
ATLVGILMAI YSDKGNYFWW LLFPVSAMSM TCPVFSSALN SVLSKWDLPV FTLPFNMALS
MYLSATGHYN PFFPSTLITP VTSVPNVTWP DLSALQLLKS LPVGVGQIYG CDNPWTGGIF
LGAILLSSPL MCLHAAIGSL LGIIAGLSLS APFEDIYAGL WGFNSSLACI AIGGTFMALT
WQTHLLALAC ALFTAYLGAS MSHVMAVVGL PSGTWPFCLA TLLFLLLTTK NPNIYKMPIS
KVTYPEENRI FYLQSRKRTV QGPL
