LAAT1_CAEEL
ID LAAT1_CAEEL Reviewed; 311 AA.
AC Q95XZ6;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 2.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Lysosomal amino acid transporter 1;
GN Name=laat-1 {ECO:0000312|WormBase:Y43H11AL.2a};
GN ORFNames=Y43H11AL.2 {ECO:0000312|WormBase:Y43H11AL.2a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
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]
RP FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP PRO-59 AND 303-LEU-LEU-304.
RX PubMed=22822152; DOI=10.1126/science.1220281;
RA Liu B., Du H., Rutkowski R., Gartner A., Wang X.;
RT "LAAT-1 is the lysosomal lysine/arginine transporter that maintains amino
RT acid homeostasis.";
RL Science 337:351-354(2012).
RN [3]
RP FUNCTION.
RX PubMed=25124690; DOI=10.15252/embr.201438618;
RA Wu Y., Cheng S., Zhao H., Zou W., Yoshina S., Mitani S., Zhang H., Wang X.;
RT "PI3P phosphatase activity is required for autophagosome maturation and
RT autolysosome formation.";
RL EMBO Rep. 15:973-981(2014).
CC -!- FUNCTION: Amino acid transporter that specifically mediates the pH-
CC dependent export of the cationic amino acids arginine, histidine and
CC lysine from lysosomes (PubMed:22822152). May play a role in the
CC degradation of autophagic substrates in autolysosomes by regulating
CC lysosome function (PubMed:25124690). {ECO:0000269|PubMed:22822152,
CC ECO:0000269|PubMed:25124690}.
CC -!- SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:22822152};
CC Multi-pass membrane protein {ECO:0000269|PubMed:22822152}.
CC -!- DOMAIN: The di-leucine motif mediates lysosomal localization.
CC {ECO:0000269|PubMed:22822152}.
CC -!- DISRUPTION PHENOTYPE: Mutants are viable but develop slowly. They
CC accumulate enlarged lysosomes and show an impaired lysosomal
CC degradation of phagocytic, endocytic, and autophagic cargos.
CC {ECO:0000269|PubMed:22822152}.
CC -!- SIMILARITY: Belongs to the laat-1 family. {ECO:0000305}.
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DR EMBL; BX284602; CCD71489.1; -; Genomic_DNA.
DR RefSeq; NP_493686.2; NM_061285.4.
DR AlphaFoldDB; Q95XZ6; -.
DR SMR; Q95XZ6; -.
DR STRING; 6239.Y43H11AL.2; -.
DR TCDB; 2.A.43.2.2; the lysosomal cystine transporter (lct) family.
DR EPD; Q95XZ6; -.
DR PaxDb; Q95XZ6; -.
DR PeptideAtlas; Q95XZ6; -.
DR EnsemblMetazoa; Y43H11AL.2a.1; Y43H11AL.2a.1; WBGene00021546.
DR GeneID; 3565323; -.
DR KEGG; cel:CELE_Y43H11AL.2; -.
DR UCSC; Y43H11AL.2; c. elegans.
DR CTD; 3565323; -.
DR WormBase; Y43H11AL.2a; CE32969; WBGene00021546; laat-1.
DR eggNOG; KOG2913; Eukaryota.
DR GeneTree; ENSGT00940000175512; -.
DR HOGENOM; CLU_019699_3_0_1; -.
DR InParanoid; Q95XZ6; -.
DR OMA; IYFYQHY; -.
DR OrthoDB; 977963at2759; -.
DR PhylomeDB; Q95XZ6; -.
DR Reactome; R-CEL-5223345; Miscellaneous transport and binding events.
DR PRO; PR:Q95XZ6; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00021546; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR ExpressionAtlas; Q95XZ6; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0031301; C:integral component of organelle membrane; IDA:UniProtKB.
DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
DR GO; GO:0015174; F:basic amino acid transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0061459; F:L-arginine transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0015189; F:L-lysine transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0080144; P:amino acid homeostasis; IDA:UniProtKB.
DR GO; GO:1903826; P:L-arginine transmembrane transport; IDA:UniProtKB.
DR GO; GO:0015819; P:lysine transport; IDA:UniProtKB.
DR GO; GO:0010508; P:positive regulation of autophagy; IMP:UniProtKB.
DR InterPro; IPR006603; PQ-loop_rpt.
DR Pfam; PF04193; PQ-loop; 2.
DR SMART; SM00679; CTNS; 2.
PE 1: Evidence at protein level;
KW Amino-acid transport; Glycoprotein; Lysosome; Membrane; Reference proteome;
KW Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..311
FT /note="Lysosomal amino acid transporter 1"
FT /id="PRO_0000419468"
FT TOPO_DOM 1..37
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 38..58
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 59..74
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 75..95
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 96..102
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 103..123
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 124..138
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 139..159
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 160..189
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 190..210
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 211..233
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 234..254
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 255..266
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 267..287
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 288..311
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 55..86
FT /note="PQ-loop 1"
FT DOMAIN 214..245
FT /note="PQ-loop 2"
FT MOTIF 303..304
FT /note="Di-leucine motif"
FT CARBOHYD 18
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 59
FT /note="P->L: Abolishes the uptake of arginine and lysine."
FT /evidence="ECO:0000269|PubMed:22822152"
FT MUTAGEN 303..304
FT /note="Missing: Abolishes lysosomal localization."
FT /evidence="ECO:0000269|PubMed:22822152"
SQ SEQUENCE 311 AA; 34960 MW; 6A144B5210237353 CRC64;
MKTGGLSDFA DFGEEDANCT QGIQWIKDVF TDCVDTDLKL LGFIIGLISL ALWLIPLFPQ
LWQNYKTKKC EGLSLAFLFF WLVGDTCNML GAILTNQQPI QKIIGVYYII QDLVLWTQYG
YYLKIYNRPT TSSARSNTIV VPVLALASVG SFFVFESALP PVGDHRVKRS FLESLNHQEG
LPLEGILKMW PIFTSYTDML GYIIGSMAAV CYFGGRIPQI IKNYRHSSCE GLSLTMFYII
VAANFTYGIS VLLATTSWLY LLRHLPWLAG SLGCCCFDAV IISQYYLYRP KTPLAEDTER
AGLLNSQDDS D
