GTR9_PONAB
ID GTR9_PONAB Reviewed; 566 AA.
AC Q5RB09;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Solute carrier family 2, facilitated glucose transporter member 9 {ECO:0000305};
DE AltName: Full=Glucose transporter type 9 {ECO:0000250|UniProtKB:Q9NRM0};
DE Short=GLUT-9 {ECO:0000250|UniProtKB:Q9NRM0};
DE AltName: Full=Urate transporter {ECO:0000305};
GN Name=SLC2A9 {ECO:0000250|UniProtKB:Q9NRM0};
GN Synonyms=GLUT9 {ECO:0000250|UniProtKB:Q9NRM0};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: High-capacity urate transporter, which may play a role in the
CC urate reabsorption by proximal tubules. May have a residual high-
CC affinity, low-capacity glucose and fructose transporter activity.
CC Transports urate at rates 45- to 60-fold faster than glucose. Does not
CC transport galactose. May mediate small uptake of adenine but not of
CC other nucleobases. {ECO:0000250|UniProtKB:Q9NRM0}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=urate(out) = urate(in); Xref=Rhea:RHEA:60368,
CC ChEBI:CHEBI:17775; Evidence={ECO:0000250|UniProtKB:Q9NRM0};
CC -!- SUBCELLULAR LOCATION: Basolateral cell membrane
CC {ECO:0000250|UniProtKB:Q3T9X0}; Multi-pass membrane protein
CC {ECO:0000255}. Apical cell membrane {ECO:0000250|UniProtKB:Q3T9X0};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Sugar
CC transporter (TC 2.A.1.1) family. {ECO:0000305}.
CC -!- CAUTION: High-capacity urate transporter that was first described as a
CC fructose and glucose transporter. Also described in the literature as
CC high-affinity and low-capacity glucose and fructose transporter (By
CC similarity). However, another group could not confirm transporter
CC activity for glucose or fructose (By similarity).
CC {ECO:0000250|UniProtKB:Q9NRM0}.
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DR EMBL; CR858850; CAH91051.1; -; mRNA.
DR AlphaFoldDB; Q5RB09; -.
DR SMR; Q5RB09; -.
DR STRING; 9601.ENSPPYP00000016315; -.
DR eggNOG; KOG0569; Eukaryota.
DR InParanoid; Q5RB09; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR GO; GO:0016323; C:basolateral plasma membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0015143; F:urate transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0015747; P:urate transport; ISS:UniProtKB.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR045263; GLUT.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR005828; MFS_sugar_transport-like.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR003663; Sugar/inositol_transpt.
DR InterPro; IPR005829; Sugar_transporter_CS.
DR PANTHER; PTHR23503; PTHR23503; 1.
DR Pfam; PF00083; Sugar_tr; 1.
DR PRINTS; PR00171; SUGRTRNSPORT.
DR SUPFAM; SSF103473; SSF103473; 1.
DR TIGRFAMs; TIGR00879; SP; 1.
DR PROSITE; PS50850; MFS; 1.
DR PROSITE; PS00216; SUGAR_TRANSPORT_1; 1.
DR PROSITE; PS00217; SUGAR_TRANSPORT_2; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Glycoprotein; Membrane; Phosphoprotein; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..566
FT /note="Solute carrier family 2, facilitated glucose
FT transporter member 9"
FT /id="PRO_0000292552"
FT TOPO_DOM 1..51
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 52..72
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 73..107
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 108..128
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 129..140
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 141..161
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 162..171
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 172..192
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 193..200
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 201..221
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 222..231
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 232..252
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 253..316
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 317..337
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 338..354
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 355..375
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 376..381
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 382..402
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 403..415
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 416..436
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 437..451
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 452..472
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 473..478
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 479..499
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 500..566
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 524..543
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NRM0"
FT MOD_RES 514
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NRM0"
FT CARBOHYD 74
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 90
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 566 AA; 61913 MW; 92F7300BA995789E CRC64;
MARKQNRNSK ELGLAPLADD TSHAGPPGPG RALLECDHLR SGLPDGRRRK DWSCSLLVAS
LAGAFGSSFL YGYNLSVVNA PTPYIKAFYN ESWERRHGRP IDPDTLTLLW SVTVSIFAIG
GLVGTLMVKM IGKVLGRKHT LLANNGFAIS AALLMACSLQ AGAFEMLIVG RFIMGIDGGI
ALSVLPMYLS EISPKEIRGS LGQVTAIFIC IGVFTGQLLG LPELLGKEST WPYLFGVIVV
PAVVQLLSLP FLPDSPRYLL LEKRNEARAV KAFQTFLGKA DVSREVEEVA ESRVQRSIRL
VSVLELLRAP YVRWQVVTVI VTMACYQLCG LNAIWFYTNS IFGKAGIPPA KIPYVTLSTG
GIETLAAIFS GLVIEHLGRR PLLIGGFGLM ALFFGTLTVT LTLQDRAPWV PYLSIVGILA
IIASFCSGPG GIPFILTGEF FQQSQRPAAF IIAGTVNWLS NFAVGLLFPF IQKSLDTYCF
LVFATICMTG AIYLYFVLPE TKNRTYAEIS QAFSKRNKAY PPEEKIDSAV TDGKTKGRPE
QVSSSTLDNY VKNRIVYMDD LTFQET
