S38A2_BOVIN
ID S38A2_BOVIN Reviewed; 506 AA.
AC A2VE31; Q95M41;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Sodium-coupled neutral amino acid transporter 2;
DE AltName: Full=Amino acid transporter A2;
DE AltName: Full=Protein 40-9-1;
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;
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].
RC STRAIN=Hereford; TISSUE=Fetal skin;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 223-506.
RA Schmidt T.;
RL Thesis (2001), University of Goettingen, Germany.
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. May
CC function in the transport of amino acids at the blood-brain barrier and
CC in the supply of maternal nutrients to the fetus through the placenta
CC (By 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}. Note=Insulin promotes recruitment to the plasma
CC membrane from a pool localized in the trans-Golgi network or endosomes.
CC May localize to an endosomal compartment. Enriched in the
CC somatodendritic compartment of neurons, it is also detected at the
CC axonal shaft but excluded from the nerve terminal. {ECO:0000250}.
CC -!- PTM: Polyubiquitination by NEDD4L regulates the degradation and the
CC activity of SLC38A2. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the amino acid/polyamine transporter 2 family.
CC {ECO:0000305}.
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DR EMBL; BC133547; AAI33548.1; -; mRNA.
DR EMBL; AJ344100; CAC51429.1; -; mRNA.
DR RefSeq; NP_001075893.1; NM_001082424.1.
DR AlphaFoldDB; A2VE31; -.
DR SMR; A2VE31; -.
DR STRING; 9913.ENSBTAP00000014749; -.
DR PaxDb; A2VE31; -.
DR PRIDE; A2VE31; -.
DR Ensembl; ENSBTAT00000014749; ENSBTAP00000014749; ENSBTAG00000011105.
DR GeneID; 338044; -.
DR KEGG; bta:338044; -.
DR CTD; 54407; -.
DR VEuPathDB; HostDB:ENSBTAG00000011105; -.
DR VGNC; VGNC:34849; SLC38A2.
DR eggNOG; KOG1305; Eukaryota.
DR GeneTree; ENSGT00940000155486; -.
DR HOGENOM; CLU_009020_0_1_1; -.
DR InParanoid; A2VE31; -.
DR OMA; QFWITAF; -.
DR OrthoDB; 1109791at2759; -.
DR TreeFam; TF328787; -.
DR Reactome; R-BTA-210500; Glutamate Neurotransmitter Release Cycle.
DR Reactome; R-BTA-352230; Amino acid transport across the plasma membrane.
DR Proteomes; UP000009136; Chromosome 5.
DR Bgee; ENSBTAG00000011105; Expressed in spermatocyte and 106 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
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:0005295; F:neutral amino acid:sodium symporter activity; IEA:Ensembl.
DR GO; GO:0003333; P:amino acid transmembrane transport; IBA:GO_Central.
DR GO; GO:1903841; P:cellular response to arsenite(3-); IEA:Ensembl.
DR GO; GO:0006868; P:glutamine transport; IBA:GO_Central.
DR GO; GO:0033120; P:positive regulation of RNA splicing; IEA:Ensembl.
DR GO; GO:0080135; P:regulation of cellular response to stress; IEA:Ensembl.
DR InterPro; IPR013057; AA_transpt_TM.
DR Pfam; PF01490; Aa_trans; 1.
PE 2: Evidence at transcript level;
KW Amino-acid transport; Cell membrane; Disulfide bond; Glycoprotein;
KW Ion transport; Membrane; Phosphoprotein; Reference proteome; Sodium;
KW Sodium transport; Symport; Transmembrane; Transmembrane helix; Transport;
KW Ubl conjugation.
FT CHAIN 1..506
FT /note="Sodium-coupled neutral amino acid transporter 2"
FT /id="PRO_0000311368"
FT TOPO_DOM 1..76
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 77..97
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 98..102
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 103..123
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 124..158
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 159..179
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 180..188
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 189..209
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 210..217
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 218..238
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 239..292
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 293..313
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 314..329
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 330..350
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 351..371
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 372..392
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 393..413
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 414..434
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 435..436
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 437..457
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 458..474
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 475..495
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 496..506
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 1..96
FT /note="Regulates protein turnover upon amino acid
FT deprivation"
FT /evidence="ECO:0000250"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96QD8"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8CFE6"
FT MOD_RES 22
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96QD8"
FT MOD_RES 55
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96QD8"
FT CARBOHYD 258
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 274
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 245..281
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT CONFLICT 409
FT /note="S -> N (in Ref. 2; CAC51429)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 506 AA; 56214 MW; 952C9D7F55E1659F CRC64;
MKKAEMGRFN ISPDEDSSSY SSNSDFNYSY PTKQAALKSH YADVDPENQN FLLESNLGKK
KYETDFHPGT TSFGMSVFNL SNAIVGSGIL GLSYAMANTG IALFIILLTF VSIFSLYSVH
LLLKTANEGG SLLYEQLGHK AFGMVGKLTA SGSITMQNIG AMSSYLFIVK YELPLVIQAL
MNIEDTNGLW YLNGDYLVLL VSLVLILPLS LLRNLGYLGY TSGLSLLCMM FFLIVVIFKK
FQISCPAEIA FLVNETVNSS LTQPATFLPD MGFNRTESDS CQPRYFIFNS QTVYAVPILT
FSFVCHPAIL PIYEELKGRS RRRMMNVSKI SFFAMFLMYL LAALFGYLTF YGHVESELLH
TYSSVMETDI LLLIVRLAVL VAVTLTVPVV IFPIRSSITH LLCASKEFSW WRHSVITVSI
LVFTNLLVIF VPNIRDIFGF IGASAAAMLI FILPSAFYIK LVKKEPMKSV QKIGAMFFLL
SGIVVMTGSM ALIVLDWVHN APGGGH
