AAAT_MACFA
ID AAAT_MACFA Reviewed; 542 AA.
AC Q4R8W8;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Neutral amino acid transporter B(0);
DE Short=ATB(0);
DE AltName: Full=Solute carrier family 1 member 5;
GN Name=SLC1A5; ORFNames=QtsA-11272;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Sodium-dependent amino acids transporter that has a broad
CC substrate specificity, with a preference for zwitterionic amino acids.
CC It accepts as substrates all neutral amino acids, including glutamine,
CC asparagine, and branched-chain and aromatic amino acids, and excludes
CC methylated, anionic, and cationic amino acids.
CC {ECO:0000250|UniProtKB:P51912}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000250|UniProtKB:Q15758}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P51912};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:Q15758}. Melanosome
CC {ECO:0000250|UniProtKB:Q15758}.
CC -!- SIMILARITY: Belongs to the dicarboxylate/amino acid:cation symporter
CC (DAACS) (TC 2.A.23) family. SLC1A5 subfamily. {ECO:0000305}.
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DR EMBL; AB168329; BAE00453.1; -; mRNA.
DR RefSeq; NP_001270983.1; NM_001284054.1.
DR AlphaFoldDB; Q4R8W8; -.
DR SMR; Q4R8W8; -.
DR STRING; 9541.XP_005595923.1; -.
DR PRIDE; Q4R8W8; -.
DR ABCD; Q4R8W8; 4 sequenced antibodies.
DR GeneID; 101867392; -.
DR CTD; 6510; -.
DR eggNOG; KOG3787; Eukaryota.
DR OrthoDB; 1184392at2759; -.
DR Proteomes; UP000233100; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015186; F:L-glutamine transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR GO; GO:0006868; P:glutamine transport; ISS:UniProtKB.
DR GO; GO:0070207; P:protein homotrimerization; ISS:UniProtKB.
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; Amino-acid transport; Cell membrane; Glycoprotein; Membrane;
KW Metal-binding; Phosphoprotein; Reference proteome; Sodium; Symport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..542
FT /note="Neutral amino acid transporter B(0)"
FT /id="PRO_0000284453"
FT TOPO_DOM 1..52
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 53..82
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT TOPO_DOM 83..95
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 96..117
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT TOPO_DOM 118..131
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 132..154
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT TOPO_DOM 155..225
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 226..249
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT TOPO_DOM 250..258
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 259..286
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT TOPO_DOM 287..307
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 308..329
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT TOPO_DOM 330..334
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT INTRAMEM 335..365
FT /note="Discontinuously helical"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT TOPO_DOM 366..374
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 375..401
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT TOPO_DOM 402..414
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 415..448
FT /note="Discontinuously helical"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT TOPO_DOM 449..461
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 462..483
FT /note="Helical; Name=8"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT TOPO_DOM 484..542
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 509..542
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 383
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O59010"
FT BINDING 385
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT BINDING 387
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O59010"
FT BINDING 472
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O59010"
FT BINDING 476
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O59010"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q15758"
FT MOD_RES 494
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15758"
FT MOD_RES 495
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q15758"
FT MOD_RES 504
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15758"
FT MOD_RES 536
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15758"
FT MOD_RES 540
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15758"
FT CARBOHYD 164
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 213
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 542 AA; 56764 MW; F7EC85041CD38132 CRC64;
MVADPPRGDS KGLAAAEPTA NGGLALASIE DQGEAAGGCC GSRDRVRRCL RANLLVLLTV
VAVVVGVALG LGVSGAGGAL ALGPERLSAF VFPGELLLRL LRMIILPLVV CSLIGGAASL
DPGALGRLGA WALLFFLVTT LLASALGVAL ALALQPGAAS AAINASVGAA GSAENAPKKE
VLDSFLDLAR NIFPSNLVSA AFRSYSTSYE ERNITGTRVK VPVGQEVEGM NILGLVVFAI
VFGVALRKLG PEGELLIRFF NSFNEATMVL VSWIMWYAPV GIMFLVAGKI VEMEDVGLLF
ARLGKYILCC LLGHAIHGLL VLPLIYFLFT RKNPYRFLWG IVTPLATAFG TSSSSATLPL
MMKCVEENNG VAKHISRFIL PIGATVNMDG AALFQCVAAV FIAQLSEQSL DFVKIITILV
TATASSVGAA GIPAGGVLTL AIILEAVNLP VDHISLILAV DWLVDRSCTV LNVEGDALGA
GLLQNYVDRT EVRSTEPELI QVKSELPLDP LPAPTEEGNP LLRHYRGPAG DATVASEKES
VM
