S38A2_CHICK
ID S38A2_CHICK Reviewed; 501 AA.
AC Q5F468;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 2.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Sodium-coupled neutral amino acid transporter 2;
DE AltName: Full=Amino acid transporter A2;
DE AltName: Full=Solute carrier family 38 member 2;
DE AltName: Full=System A amino acid transporter 2;
DE AltName: Full=System A transporter 1;
DE AltName: Full=System N amino acid transporter 2;
GN Name=SLC38A2; Synonyms=SNAT2; ORFNames=RCJMB04_2k20;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 327-477 (ISOFORM 1).
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
CC -!- FUNCTION: Functions as a sodium-dependent amino acid transporter.
CC Mediates the saturable, pH-sensitive and electrogenic cotransport of
CC neutral amino acids and sodium ions with a stoichiometry of 1:1 (By
CC similarity). {ECO:0000250}.
CC -!- ACTIVITY REGULATION: Inhibited by N-methyl-D-glucamine and choline.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5F468-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5F468-2; Sequence=VSP_029555;
CC -!- SIMILARITY: Belongs to the amino acid/polyamine transporter 2 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAH65066.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AJ397292; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AJ851432; CAH65066.1; ALT_FRAME; mRNA.
DR AlphaFoldDB; Q5F468; -.
DR SMR; Q5F468; -.
DR STRING; 9031.ENSGALP00000015772; -.
DR PaxDb; Q5F468; -.
DR VEuPathDB; HostDB:geneid_417807; -.
DR eggNOG; KOG1305; Eukaryota.
DR InParanoid; Q5F468; -.
DR OrthoDB; 1109791at2759; -.
DR PhylomeDB; Q5F468; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0015179; F:L-amino acid transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015186; F:L-glutamine transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR GO; GO:0003333; P:amino acid transmembrane transport; IBA:GO_Central.
DR GO; GO:0006868; P:glutamine transport; IBA:GO_Central.
DR GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-KW.
DR InterPro; IPR013057; AA_transpt_TM.
DR Pfam; PF01490; Aa_trans; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Amino-acid transport; Cell membrane; Disulfide bond;
KW Glycoprotein; Ion transport; Membrane; Reference proteome; Sodium;
KW Sodium transport; Symport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..501
FT /note="Sodium-coupled neutral amino acid transporter 2"
FT /id="PRO_0000311373"
FT TOPO_DOM 1..77
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 78..98
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 99..103
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 104..124
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 125..149
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 150..170
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 171..192
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 193..213
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 214..218
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 219..239
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 240..287
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 288..308
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 309..324
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 325..345
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 346..366
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 367..387
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 388..408
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 409..429
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 430..431
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 432..452
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 453..469
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 470..490
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 491..501
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 1..97
FT /note="Regulates protein turnover upon amino acid
FT deprivation"
FT /evidence="ECO:0000250"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 254
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 259
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 246..276
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 437
FT /note="G -> GKHLHITSGSPLKLEKCSYGLIELYLPVHNFFFCALLTG (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:15642098"
FT /id="VSP_029555"
SQ SEQUENCE 501 AA; 55531 MW; 5E6F35D1C25B7B1F CRC64;
MSSAEMGKFD ISPDEDSSSY SSNSNDFSYP YPTKPAAMKS HYADMDPENQ NFLLDSNVGK
KKYETQYHPG TTSFGMSVFN LSNAIVGSGI LGLSYAMANT GIALFVILLL VVSILSLYSV
HLLLKTANEG GSLLYEQLGM KAFGMPGKLA ASGSITMQNI GAMSSYLFIV KYELPLVIKT
FMNIEENAGH WYLNGDYLVL LVSVILILPL SLLKNLGYLG YTSGFSLLCM VFFLIVVIWK
MFQIPCPMES DIINATLINA TLAPFADENI TISDACKPEY FIFNSQTVYA VPILTFSFVC
HPAILPIYEE LKSRSRKRMM NVSYVSFFAM FLMYLLAALF GYLTFYGRVE SELLHTYSAF
LGADILLLIV RLAVLMAVTL TVPVVIFPIR SSVTQLLWAG KEFSWWRHCS ITVVLLAFTN
VLVIFVPTIR DIFGFIGASA AAMLIFILPS AFYIKLVKKE PMKSVQKIGA ALFFLSGILV
MTGCMTLIIL DWIHTDASDG H
