S28A3_EPTST
ID S28A3_EPTST Reviewed; 683 AA.
AC Q9UA35;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Solute carrier family 28 member 3;
DE AltName: Full=Concentrative Na(+)-nucleoside cotransporter 3;
DE AltName: Full=hfCNT;
GN Name=SLC28A3; Synonyms=CNT3;
OS Eptatretus stoutii (Pacific hagfish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Cyclostomata; Myxini;
OC Myxiniformes; Myxinidae; Eptatretinae; Eptatretus.
OX NCBI_TaxID=7765;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10455109; DOI=10.1074/jbc.274.35.24475;
RA Loewen S.K., Ng A.M.L., Yao S.Y.M., Cass C.E., Baldwin S.A., Young J.D.;
RT "Identification of amino acid residues responsible for the pyrimidine and
RT purine nucleoside specificities of human concentrative Na(+) nucleoside
RT cotransporters hCNT1 and hCNT2.";
RL J. Biol. Chem. 274:24475-24484(1999).
CC -!- FUNCTION: Sodium-dependent, pyrimidine- and purine-selective. Involved
CC in the homeostasis of endogenous nucleosides. Exhibits the transport
CC characteristics of the nucleoside transport system cib or N3 subtype
CC (N3/cib) (with marked transport of both thymidine and inosine). Employs
CC a 2:1 sodium/nucleoside ratio. Also able to transport gemcitabine, 3'-
CC azido-3'-deoxythymidine (AZT), ribavirin and 3-deazauridine.
CC {ECO:0000250|UniProtKB:Q9HAS3}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 Na(+)(out) + thymidine(out) = 2 Na(+)(in) + thymidine(in);
CC Xref=Rhea:RHEA:69899, ChEBI:CHEBI:17748, ChEBI:CHEBI:29101;
CC Evidence={ECO:0000250|UniProtKB:Q9HAS3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cytidine(out) + 2 Na(+)(out) = cytidine(in) + 2 Na(+)(in);
CC Xref=Rhea:RHEA:69903, ChEBI:CHEBI:17562, ChEBI:CHEBI:29101;
CC Evidence={ECO:0000250|UniProtKB:Q9HAS3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 Na(+)(out) + uridine(out) = 2 Na(+)(in) + uridine(in);
CC Xref=Rhea:RHEA:69907, ChEBI:CHEBI:16704, ChEBI:CHEBI:29101;
CC Evidence={ECO:0000250|UniProtKB:Q9HAS3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine(out) + 2 Na(+)(out) = adenosine(in) + 2 Na(+)(in);
CC Xref=Rhea:RHEA:69911, ChEBI:CHEBI:16335, ChEBI:CHEBI:29101;
CC Evidence={ECO:0000250|UniProtKB:Q9HAS3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=guanosine(out) + 2 Na(+)(out) = guanosine(in) + 2 Na(+)(in);
CC Xref=Rhea:RHEA:69915, ChEBI:CHEBI:16750, ChEBI:CHEBI:29101;
CC Evidence={ECO:0000250|UniProtKB:Q9HAS3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=inosine(out) + 2 Na(+)(out) = inosine(in) + 2 Na(+)(in);
CC Xref=Rhea:RHEA:69919, ChEBI:CHEBI:17596, ChEBI:CHEBI:29101;
CC Evidence={ECO:0000250|UniProtKB:Q9HAS3};
CC -!- SUBUNIT: Homotrimer. {ECO:0000250|UniProtKB:Q9HAS3}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9HAS3};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the concentrative nucleoside transporter (CNT)
CC (TC 2.A.41) family. {ECO:0000305}.
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DR EMBL; AF132298; AAD52151.1; -; mRNA.
DR AlphaFoldDB; Q9UA35; -.
DR SMR; Q9UA35; -.
DR TCDB; 2.A.41.2.5; the concentrative nucleoside transporter (cnt) family.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
DR GO; GO:0005337; F:nucleoside transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR InterPro; IPR008276; C_nuclsd_transpt.
DR InterPro; IPR018270; C_nuclsd_transpt_met_bac.
DR InterPro; IPR030211; CNT3.
DR InterPro; IPR011657; CNT_C_dom.
DR InterPro; IPR002668; CNT_N_dom.
DR InterPro; IPR011642; Gate_dom.
DR PANTHER; PTHR10590; PTHR10590; 1.
DR PANTHER; PTHR10590:SF18; PTHR10590:SF18; 1.
DR Pfam; PF07670; Gate; 1.
DR Pfam; PF07662; Nucleos_tra2_C; 1.
DR Pfam; PF01773; Nucleos_tra2_N; 1.
DR TIGRFAMs; TIGR00804; nupC; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Membrane; Symport; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..683
FT /note="Solute carrier family 28 member 3"
FT /id="PRO_0000324149"
FT TOPO_DOM 1..97
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 98..118
FT /note="Helical; Name=TM1"
FT /evidence="ECO:0000250|UniProtKB:Q9HAS3"
FT TOPO_DOM 119..123
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 124..144
FT /note="Helical; Name=TM2"
FT /evidence="ECO:0000250|UniProtKB:Q9HAS3"
FT TOPO_DOM 145..168
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 169..189
FT /note="Helical; Name=TM3"
FT /evidence="ECO:0000250|UniProtKB:Q9HAS3"
FT TOPO_DOM 190..192
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 193..214
FT /note="Helical; Name=TM4"
FT /evidence="ECO:0000250|UniProtKB:Q9HAS3"
FT TOPO_DOM 215..222
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 223..242
FT /note="Helical; Name=TM5"
FT /evidence="ECO:0000250|UniProtKB:Q9HAS3"
FT TOPO_DOM 243..279
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 280..300
FT /note="Helical; Name=TM6"
FT /evidence="ECO:0000250|UniProtKB:Q9HAS3"
FT TOPO_DOM 301..324
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT INTRAMEM 325..343
FT /note="Helical; Name=HP1"
FT /evidence="ECO:0000250|UniProtKB:Q9HAS3"
FT TOPO_DOM 344..356
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 357..379
FT /note="Helical; Name=TM7"
FT /evidence="ECO:0000250|UniProtKB:Q9HAS3"
FT TOPO_DOM 380..381
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 382..403
FT /note="Helical; Name=TM8"
FT /evidence="ECO:0000250|UniProtKB:Q9HAS3"
FT TOPO_DOM 404..438
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 439..464
FT /note="Helical; Name=TM9"
FT /evidence="ECO:0000250|UniProtKB:Q9HAS3"
FT TOPO_DOM 465..502
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 503..522
FT /note="Helical; Name=HP2"
FT /evidence="ECO:0000250|UniProtKB:Q9HAS3"
FT TOPO_DOM 523..561
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 562..572
FT /note="Helical; Name=TM10"
FT /evidence="ECO:0000250|UniProtKB:Q9HAS3"
FT TOPO_DOM 573..585
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 586..608
FT /note="Helical; Name=TM11"
FT /evidence="ECO:0000250|UniProtKB:Q9HAS3"
FT TOPO_DOM 609..683
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT REGION 1..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..26
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..71
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 683 AA; 75917 MW; 605AB111B5D23508 CRC64;
MSAFKARGVE NPSYEDPDEK QKPDLEMSKT NGIGVDNPSY YKNPEKYLGN ENEEGKSNND
NEEEEEGEED QGAVERCVNK FYGGIHNFYK RNKKIIHYTF LGLLLVGYFA LVIAACIVNF
KQSLALLVLT LIAIFFFFWD LFIAKYGDKI AEALKPCQKF LDNHWSIIRW FVYGALLLAV
ILWLTLDTAK RGANQVIPFF GLILYILLVF IFSKHPTKVR WRIVIWGLLL QFIFGLIILR
TKPGLDAFNW LGIQVQTFLK YTDAGSRFLF GDDFQDHFFA FAVLPIVIFF STVMSMMYYL
GLMQWLILKV GWLMQITMGT SPMESMVSAG NIFVGQTESP LLIRPYLADL TISEMHSVMS
SGFATIAGSV LGAYISLGIP AAHLLTASVM SAPAALAISK TFWPETKKSK NSTQTSIKLE
KGQENNLVEA ASQGASAAVP LVANIAANLI AFLAVLAFIN ATLSWLGSMF NYPQFSFEII
CSYVLMPFAF MMGVNYDDSF LVAELLGMKT FFNEFVAYQR LSEYIHNRES GGPLFVDGVR
QYMSVRSEAI ATYALCGFAN FGSLGIMIGG LSSLAPHRKS DIASCGIRAL IAGTIACFST
ACIAGVLYIP ELYCPNLLMS TLFENGTTVN TTNLMSCCTD LFKSTTMLTP KNITFTEGFN
TTMLNGCCTF FPSGFNCSEV RPE
