AAT6_CAEEL
ID AAT6_CAEEL Reviewed; 523 AA.
AC Q22397; B2D6M4;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 2.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Amino acid transporter protein 6 {ECO:0000312|WormBase:T11F9.4a};
GN Name=aat-6 {ECO:0000312|WormBase:T11F9.4a};
GN ORFNames=T11F9.4 {ECO:0000312|WormBase:T11F9.4a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP INTERACTION WITH NRFL-1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP MUTAGENESIS OF 521-THR--MET-523.
RX PubMed=22916205; DOI=10.1371/journal.pone.0043050;
RA Hagiwara K., Nagamori S., Umemura Y.M., Ohgaki R., Tanaka H., Murata D.,
RA Nakagomi S., Nomura K.H., Kage-Nakadai E., Mitani S., Nomura K., Kanai Y.;
RT "NRFL-1, the C. elegans NHERF orthologue, interacts with amino acid
RT transporter 6 (AAT-6) for age-dependent maintenance of AAT-6 on the
RT membrane.";
RL PLoS ONE 7:E43050-E43050(2012).
RN [3] {ECO:0000305}
RP FUNCTION.
RX PubMed=30560135; DOI=10.3389/fmolb.2018.00109;
RA Spanier B., Wallwitz J., Zapoglou D., Idrissou B.M.G., Fischer C.,
RA Troll M., Petzold K., Daniel H.;
RT "The Reproduction Rate of Peptide Transporter PEPT-1 Deficient C. elegans
RT Is Dependent on Dietary Glutamate Supply.";
RL Front. Mol. Biosci. 5:109-109(2018).
CC -!- FUNCTION: Amino acid transporter that mediates the uptake of the L-
CC enantiomers of various amino acids, including L-glutamate (Probable).
CC May play a role in promoting fertility (PubMed:30560135).
CC {ECO:0000269|PubMed:30560135, ECO:0000305|PubMed:30560135}.
CC -!- SUBUNIT: Interacts (via PDZ-binding motif) with nfrl-1 (via PDZ 2
CC domain); the interaction with nrfl-1 is required to sequester aat-6 to
CC the apical cell membrane of intestinal cells.
CC {ECO:0000269|PubMed:22916205}.
CC -!- INTERACTION:
CC Q22397; G5EDM4-1: nrfl-1; NbExp=2; IntAct=EBI-21449230, EBI-25423624;
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000269|PubMed:22916205}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Co-localizes with nrfl-1 at the apical cell
CC membrane of intestinal cells. {ECO:0000269|PubMed:22916205}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a {ECO:0000312|WormBase:T11F9.4a};
CC IsoId=Q22397-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:T11F9.4b};
CC IsoId=Q22397-2; Sequence=VSP_060386;
CC -!- TISSUE SPECIFICITY: Expressed at the apical cell membrane of intestinal
CC cells. {ECO:0000269|PubMed:22916205}.
CC -!- SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC)
CC superfamily. {ECO:0000305}.
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DR EMBL; BX284605; CAA98529.2; -; Genomic_DNA.
DR EMBL; BX284605; CAQ35057.1; -; Genomic_DNA.
DR PIR; T24837; T24837.
DR RefSeq; NP_001123014.1; NM_001129542.2. [Q22397-2]
DR RefSeq; NP_505905.2; NM_073504.4. [Q22397-1]
DR AlphaFoldDB; Q22397; -.
DR SMR; Q22397; -.
DR ComplexPortal; CPX-4311; nrfl-1-aat-6 complex.
DR IntAct; Q22397; 1.
DR STRING; 6239.T11F9.4a; -.
DR TCDB; 2.A.3.8.27; the amino acid-polyamine-organocation (apc) family.
DR EPD; Q22397; -.
DR PaxDb; Q22397; -.
DR EnsemblMetazoa; T11F9.4a.1; T11F9.4a.1; WBGene00000007. [Q22397-1]
DR EnsemblMetazoa; T11F9.4b.1; T11F9.4b.1; WBGene00000007. [Q22397-2]
DR GeneID; 188421; -.
DR KEGG; cel:CELE_T11F9.4; -.
DR UCSC; T11F9.4a; c. elegans.
DR CTD; 188421; -.
DR WormBase; T11F9.4a; CE31995; WBGene00000007; aat-6. [Q22397-1]
DR WormBase; T11F9.4b; CE42501; WBGene00000007; aat-6. [Q22397-2]
DR eggNOG; KOG1287; Eukaryota.
DR HOGENOM; CLU_007946_3_3_1; -.
DR InParanoid; Q22397; -.
DR OMA; FRNATHV; -.
DR OrthoDB; 621852at2759; -.
DR PhylomeDB; Q22397; -.
DR PRO; PR:Q22397; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00000007; Expressed in larva and 3 other tissues.
DR GO; GO:1990184; C:amino acid transport complex; IC:ComplexPortal.
DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0015179; F:L-amino acid transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0030165; F:PDZ domain binding; IPI:UniProtKB.
DR GO; GO:0080144; P:amino acid homeostasis; IC:ComplexPortal.
DR GO; GO:0015807; P:L-amino acid transport; IC:ComplexPortal.
DR InterPro; IPR002293; AA/rel_permease1.
DR Pfam; PF13520; AA_permease_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Amino-acid transport; Cell membrane; Glycoprotein;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..523
FT /note="Amino acid transporter protein 6"
FT /id="PRO_0000448296"
FT TOPO_DOM 1..19
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 20..40
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 41..51
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 52..72
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 73..86
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 87..107
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 108..145
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 146..166
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 167..173
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 174..194
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 195..214
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 215..235
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 236..249
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 250..270
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 271..290
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 291..311
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 312..348
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 349..369
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 370..404
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 405..425
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 426..429
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 430..450
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 451..523
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT MOTIF 521..523
FT /note="PDZ-binding motif"
FT /evidence="ECO:0000269|PubMed:22916205"
FT CARBOHYD 289
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 462
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT VAR_SEQ 1..10
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_060386"
FT MUTAGEN 521..523
FT /note="Missing: Abolishes the interaction with nrfl-1."
FT /evidence="ECO:0000269|PubMed:22916205"
SQ SEQUENCE 523 AA; 57369 MW; 7F68479A2F496060 CRC64;
MLNVFGVSAS MPDDSRSQKM GLLGAISYIV GNIVGSGIFI TPTSIIENVN SVGLSLAIWI
LAAFISMLGS FCYVELGTSI RLSGGDFAYL CFMKWYPVAF AFMCIGCTIN YPATLAVQAQ
TFAEYVFRGA GVELDETSEF WAKKLLGFSL IILLMFMNFF SLKTFVQRFS ILASLAKIAA
TLLIIITGFY YLIFKHWKQN LEEPFKGSNW NPGPFVNALF AGLFSYDGWD ILNFGAEEIE
NPKRTMPLSI IIGMTCIGVI YVAVNVAYSI VLSPTEMIAS NAVAIDFANK TLGAAAFVVP
VMVAILLIGS LNSTMFSASR YLQAVSRQGH IPSAISGIAP NCDSPRVALL VHILIAIAVS
FLGDPDKLIN YVAFAQWSQR AFTMSALLYL RIRGRPRHPD RIQLPIIMPI LFFLVCTSMV
VISIIDDFKS SAVGLGILLG GLIIFIIFVW DRALPSSHTF RNATHVINEE STKFMQIIFN
VVPERVGDEE MKNAIGGAES ESEKVPAYKI SPTGNGQFKC TRM
