SATT_BOVIN
ID SATT_BOVIN Reviewed; 530 AA.
AC A2VDL4;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Neutral amino acid transporter A;
DE AltName: Full=Solute carrier family 1 member 4;
GN Name=SLC1A4; Synonyms=SATT;
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=Brain cortex;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Sodium-dependent neutral amino-acid transporter that mediates
CC transport of alanine, serine, cysteine, proline, hydroxyproline and
CC threonine. {ECO:0000250|UniProtKB:P43007}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-threonine(in) + Na(+)(in) = L-threonine(out) + Na(+)(out);
CC Xref=Rhea:RHEA:69999, ChEBI:CHEBI:29101, ChEBI:CHEBI:57926;
CC Evidence={ECO:0000250|UniProtKB:P43007};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-serine(in) + Na(+)(in) = L-serine(out) + Na(+)(out);
CC Xref=Rhea:RHEA:29575, ChEBI:CHEBI:29101, ChEBI:CHEBI:33384;
CC Evidence={ECO:0000250|UniProtKB:P43007};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-cysteine(in) + Na(+)(in) = L-cysteine(out) + Na(+)(out);
CC Xref=Rhea:RHEA:68232, ChEBI:CHEBI:29101, ChEBI:CHEBI:35235;
CC Evidence={ECO:0000250|UniProtKB:P43007};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-alanine(in) + Na(+)(in) = L-alanine(out) + Na(+)(out);
CC Xref=Rhea:RHEA:29283, ChEBI:CHEBI:29101, ChEBI:CHEBI:57972;
CC Evidence={ECO:0000250|UniProtKB:P43007};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-proline(in) + Na(+)(in) = L-proline(out) + Na(+)(out);
CC Xref=Rhea:RHEA:28967, ChEBI:CHEBI:29101, ChEBI:CHEBI:60039;
CC Evidence={ECO:0000250|UniProtKB:P43007};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-hydroxy-L-proline(in) + Na(+)(in) = 4-hydroxy-L-proline(out)
CC + Na(+)(out); Xref=Rhea:RHEA:70023, ChEBI:CHEBI:29101,
CC ChEBI:CHEBI:58419; Evidence={ECO:0000250|UniProtKB:P43007};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P43007}; Multi-
CC pass membrane protein {ECO:0000255}. Melanosome
CC {ECO:0000250|UniProtKB:P43007}. Note=Identified by mass spectrometry in
CC melanosome fractions from stage I to stage IV.
CC {ECO:0000250|UniProtKB:P43007}.
CC -!- SIMILARITY: Belongs to the dicarboxylate/amino acid:cation symporter
CC (DAACS) (TC 2.A.23) family. SLC1A4 subfamily. {ECO:0000305}.
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DR EMBL; BC133295; AAI33296.1; -; mRNA.
DR RefSeq; NP_001075046.1; NM_001081577.1.
DR AlphaFoldDB; A2VDL4; -.
DR SMR; A2VDL4; -.
DR STRING; 9913.ENSBTAP00000010206; -.
DR PaxDb; A2VDL4; -.
DR PeptideAtlas; A2VDL4; -.
DR PRIDE; A2VDL4; -.
DR Ensembl; ENSBTAT00000010206; ENSBTAP00000010206; ENSBTAG00000007763.
DR GeneID; 326577; -.
DR KEGG; bta:326577; -.
DR CTD; 6509; -.
DR VEuPathDB; HostDB:ENSBTAG00000007763; -.
DR VGNC; VGNC:34714; SLC1A4.
DR eggNOG; KOG3787; Eukaryota.
DR GeneTree; ENSGT00940000157081; -.
DR HOGENOM; CLU_019375_3_2_1; -.
DR InParanoid; A2VDL4; -.
DR OMA; ICSFVVP; -.
DR OrthoDB; 1184392at2759; -.
DR TreeFam; TF315206; -.
DR Proteomes; UP000009136; Chromosome 11.
DR Bgee; ENSBTAG00000007763; Expressed in oviduct epithelium and 106 other tissues.
DR ExpressionAtlas; A2VDL4; baseline and differential.
DR GO; GO:0005813; C:centrosome; IEA:Ensembl.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005882; C:intermediate filament; IEA:Ensembl.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005254; F:chloride channel activity; IEA:Ensembl.
DR GO; GO:0015180; F:L-alanine transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015183; F:L-aspartate transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015184; F:L-cystine transmembrane transporter activity; IEA:Ensembl.
DR GO; GO:0034590; F:L-hydroxyproline transmembrane transporter activity; IEA:Ensembl.
DR GO; GO:0015193; F:L-proline transmembrane transporter activity; IEA:Ensembl.
DR GO; GO:0015194; F:L-serine transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015195; F:L-threonine transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015175; F:neutral amino acid transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR GO; GO:0050890; P:cognition; IEA:Ensembl.
DR GO; GO:1904273; P:L-alanine import across plasma membrane; IEA:Ensembl.
DR GO; GO:0140009; P:L-aspartate import across plasma membrane; IEA:Ensembl.
DR GO; GO:0015813; P:L-glutamate transmembrane transport; IBA:GO_Central.
DR GO; GO:1903812; P:L-serine import across plasma membrane; IEA:Ensembl.
DR GO; GO:0015825; P:L-serine transport; IBA:GO_Central.
DR GO; GO:0015824; P:proline transport; IEA:Ensembl.
DR Gene3D; 1.10.3860.10; -; 1.
DR InterPro; IPR001991; Na-dicarboxylate_symporter.
DR InterPro; IPR018107; Na-dicarboxylate_symporter_CS.
DR InterPro; IPR036458; Na:dicarbo_symporter_sf.
DR Pfam; PF00375; SDF; 1.
DR SUPFAM; SSF118215; SSF118215; 1.
DR PROSITE; PS00713; NA_DICARBOXYL_SYMP_1; 1.
DR PROSITE; PS00714; NA_DICARBOXYL_SYMP_2; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Glycoprotein; Membrane; Phosphoprotein; Reference proteome;
KW Symport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..530
FT /note="Neutral amino acid transporter A"
FT /id="PRO_0000284452"
FT TOPO_DOM 1..41
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 42..62
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 88..108
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 119..139
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 140..216
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 217..237
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 257..277
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 298..318
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 328..348
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 373..393
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 418..438
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 488..530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 501..530
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P43007"
FT MOD_RES 507
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P43007"
FT MOD_RES 525
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O35874"
FT MOD_RES 528
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O35874"
FT CARBOHYD 201
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 530 AA; 56007 MW; 49D94C07C2D602F3 CRC64;
MEKSSETNGY LDSAQEGPAA GPGEPGTTAR RAGRCAGFLR RHGLVLLTVS GVVAGAGLGA
ALRGLQLNRT QVTYLAFPGE MLLRMLRMII LPLVVCSLVS GAASLDASSL GRLGGIAIAY
FGLTTLGASA LAVALAFIIK PGSGSQTLQS SDLGLEDSGP PPVPKETVDS FLDLTRNLFP
SNLVVAAFRT YATDYREVTY NTSAGKVTIE KIPIGTEIEG MNILGLVLFA LVLGVALKKL
GSEGEELIRF FNAFNEATMV LVSWIMWYVP VGIMFLVGSK IVEMKDIIML VTSLGKYIFT
SILGHFIHGG IVLPLIYFVF TRKNPFRFLL GLLTPFATAF ATCSSSATLP SMMKCIEENN
GVDKRISRFI LPIGATVNMD GAAIFQCVAA VFIAQLNNVE LRAGQIFTIL VTATASSVGA
AGVPAGGVLT IAIILEAIGL PTHDLSLILA VDWIVDRTTT VVNVEGDALG AGILHHLNQK
AMKRGEQELS EVKVEAIPNS KSEEETSPLV THPNPTGPAA STPESKESVL
