S43A3_BOVIN
ID S43A3_BOVIN Reviewed; 489 AA.
AC Q1JPD8; Q2T9X4;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 1.
DT 25-MAY-2022, entry version 70.
DE RecName: Full=Equilibrative nucleobase transporter 1 {ECO:0000250|UniProtKB:Q8NBI5};
DE AltName: Full=Solute carrier family 43 member 3;
GN Name=SLC43A3; Synonyms=ENBT1 {ECO:0000250|UniProtKB:Q8NBI5};
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 [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Sodium-independent purine-selective nucleobase transporter
CC which mediates the equilibrative transport of extracellular purine
CC nucleobases such as adenine, guanine and hypoxanthine (By similarity).
CC May regulate fatty acid (FA) transport in adipocytes, acting as a
CC positive regulator of FA efflux and as a negative regulator of FA
CC uptake (By similarity). {ECO:0000250|UniProtKB:A2AVZ9,
CC ECO:0000250|UniProtKB:Q8NBI5}.
CC -!- SUBCELLULAR LOCATION: Basolateral cell membrane
CC {ECO:0000250|UniProtKB:Q8NBI5}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the SLC43A transporter (TC 2.A.1.44) family.
CC {ECO:0000305}.
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DR EMBL; BT025415; ABF57371.1; -; mRNA.
DR EMBL; BC111223; AAI11224.1; -; mRNA.
DR RefSeq; NP_001033215.1; NM_001038126.1.
DR AlphaFoldDB; Q1JPD8; -.
DR STRING; 9913.ENSBTAP00000013267; -.
DR PaxDb; Q1JPD8; -.
DR GeneID; 516840; -.
DR KEGG; bta:516840; -.
DR CTD; 29015; -.
DR eggNOG; ENOG502QRYG; Eukaryota.
DR HOGENOM; CLU_035676_1_1_1; -.
DR InParanoid; Q1JPD8; -.
DR OrthoDB; 639867at2759; -.
DR TreeFam; TF328358; -.
DR Proteomes; UP000009136; Unplaced.
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:0015207; F:adenine transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0015245; F:fatty acid transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0015208; F:guanine transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0042910; F:xenobiotic transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0035344; P:hypoxanthine transport; ISS:UniProtKB.
DR Gene3D; 1.20.1250.20; -; 2.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR027197; SLC43A3.
DR PANTHER; PTHR20765; PTHR20765; 1.
DR Pfam; PF07690; MFS_1; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Glycoprotein; Lipid transport; Membrane; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..489
FT /note="Equilibrative nucleobase transporter 1"
FT /id="PRO_0000305035"
FT TRANSMEM 17..37
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 72..92
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 102..122
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 123..143
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 158..180
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 277..297
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 318..338
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 358..380
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 402..422
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 426..446
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 455..475
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOD_RES 253
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NBI5"
FT MOD_RES 258
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8NBI5"
FT CARBOHYD 56
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 222
FT /note="H -> R (in Ref. 2; AAI11224)"
FT /evidence="ECO:0000305"
FT CONFLICT 240
FT /note="E -> G (in Ref. 2; AAI11224)"
FT /evidence="ECO:0000305"
FT CONFLICT 252
FT /note="L -> P (in Ref. 2; AAI11224)"
FT /evidence="ECO:0000305"
FT CONFLICT 308
FT /note="R -> S (in Ref. 2; AAI11224)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 489 AA; 54424 MW; FD239F1435B3EC9C CRC64;
MQGRSLPFRV ATLVTGLLEC LGFAGVLFGW TSLVFVFKKQ HYFEELCELD AGSLGNATGL
DECRARDERF SLIFTLASFT INFMTFPTGY IFDRFKTTVA RLIAIFLYTS ATLTIAFTSA
DSAVLLFLAM PMLAVGGILF LITNLQIGNL FGKHRSTIIT MYNGAFDSSS AVFLIIKLLY
EQGVTIKASF LFISVCSAWH VGRTLLLMPR GHIPYPLPAN YHYGLCSRDS PPEEDKKEAE
SEKLELQSKE FLSPKKETPG QQQAPGSFWS HTFSPRFAWH VVWLSVIQLW HYLFIGTLNS
LLNNLASRDS AIVSTYTNAF AVTQFFGVLC APWNGLLMDR LKHKYQEEAK RTGAVAKAAA
LRSVVPSLTL TSLLSLGFAV CASIPVLPLQ YATFILQVVS RSFLYGCNAA FLTLAFPSEH
FGKLFGLVMA LSAVVSLLQF PLFTLIKGPL QNDPLYVNLM LVLLTLLTFI HPFLVNRECQ
RKESPREVA
