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S38A9_CAEEL
ID   S38A9_CAEEL             Reviewed;         615 AA.
AC   Q19425;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   06-JUN-2002, sequence version 2.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=Sodium-coupled neutral amino acid transporter 9 homolog;
GN   ORFNames=F13H10.3;
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   IDENTIFICATION.
RX   PubMed=25567906; DOI=10.1126/science.1257132;
RA   Wang S., Tsun Z.Y., Wolfson R.L., Shen K., Wyant G.A., Plovanich M.E.,
RA   Yuan E.D., Jones T.D., Chantranupong L., Comb W., Wang T., Bar-Peled L.,
RA   Zoncu R., Straub C., Kim C., Park J., Sabatini B.L., Sabatini D.M.;
RT   "Metabolism. Lysosomal amino acid transporter SLC38A9 signals arginine
RT   sufficiency to mTORC1.";
RL   Science 347:188-194(2015).
CC   -!- FUNCTION: Lysosomal amino acid transporter involved in the activation
CC       of mTORC1 in response to amino acid levels. Probably acts as an amino
CC       acid sensor of the Rag GTPases and Ragulator complexes, 2 complexes
CC       involved in amino acid sensing and activation of mTORC1, a signaling
CC       complex promoting cell growth in response to growth factors, energy
CC       levels, and amino acids. {ECO:0000250|UniProtKB:Q8NBW4}.
CC   -!- ACTIVITY REGULATION: Amino acid transport is sodium-dependent (By
CC       similarity). Transport of leucine, tyrosine and phenylalanine is
CC       increased by arginine binding (By similarity).
CC       {ECO:0000250|UniProtKB:Q08BA4, ECO:0000250|UniProtKB:Q8NBW4}.
CC   -!- SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250|UniProtKB:Q8NBW4};
CC       Multi-pass membrane protein {ECO:0000255}. Late endosome membrane
CC       {ECO:0000250|UniProtKB:Q8NBW4}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the amino acid/polyamine transporter 2 family.
CC       SLC38A9 subfamily. {ECO:0000305}.
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DR   EMBL; Z68748; CAA92953.2; -; Genomic_DNA.
DR   PIR; T20863; T20863.
DR   RefSeq; NP_741486.1; NM_171417.5.
DR   AlphaFoldDB; Q19425; -.
DR   SMR; Q19425; -.
DR   STRING; 6239.F13H10.3b; -.
DR   PaxDb; Q19425; -.
DR   EnsemblMetazoa; F13H10.3a.1; F13H10.3a.1; WBGene00008774.
DR   GeneID; 177997; -.
DR   KEGG; cel:CELE_F13H10.3; -.
DR   UCSC; F13H10.3a; c. elegans.
DR   CTD; 177997; -.
DR   WormBase; F13H10.3a; CE27959; WBGene00008774; -.
DR   eggNOG; KOG1305; Eukaryota.
DR   InParanoid; Q19425; -.
DR   Reactome; R-CEL-1632852; Macroautophagy.
DR   Reactome; R-CEL-165159; MTOR signalling.
DR   Reactome; R-CEL-166208; mTORC1-mediated signalling.
DR   Reactome; R-CEL-380972; Energy dependent regulation of mTOR by LKB1-AMPK.
DR   Reactome; R-CEL-5628897; TP53 Regulates Metabolic Genes.
DR   Reactome; R-CEL-8943724; Regulation of PTEN gene transcription.
DR   Reactome; R-CEL-9639288; Amino acids regulate mTORC1.
DR   PRO; PR:Q19425; -.
DR   Proteomes; UP000001940; Chromosome IV.
DR   Bgee; WBGene00008774; Expressed in germ line (C elegans) and 4 other tissues.
DR   ExpressionAtlas; Q19425; baseline and differential.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015179; F:L-amino acid transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003333; P:amino acid transmembrane transport; IBA:GO_Central.
DR   InterPro; IPR013057; AA_transpt_TM.
DR   Pfam; PF01490; Aa_trans; 2.
PE   3: Inferred from homology;
KW   Amino-acid transport; Disulfide bond; Endosome; Glycoprotein; Lysosome;
KW   Membrane; Metal-binding; Reference proteome; Sodium; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..615
FT                   /note="Sodium-coupled neutral amino acid transporter 9
FT                   homolog"
FT                   /id="PRO_0000093832"
FT   TOPO_DOM        1..165
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        166..186
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000250|UniProtKB:Q08BA4"
FT   TOPO_DOM        187..192
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        193..213
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000250|UniProtKB:Q08BA4"
FT   TOPO_DOM        214..246
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        247..273
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000250|UniProtKB:Q08BA4"
FT   TOPO_DOM        274..341
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        342..358
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000250|UniProtKB:Q08BA4"
FT   TOPO_DOM        359..367
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        368..392
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000250|UniProtKB:Q08BA4"
FT   TOPO_DOM        393..413
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        414..434
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000250|UniProtKB:Q08BA4"
FT   TOPO_DOM        435..451
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        452..472
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000250|UniProtKB:Q08BA4"
FT   TOPO_DOM        473..491
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        492..512
FT                   /note="Helical; Name=8"
FT                   /evidence="ECO:0000250|UniProtKB:Q08BA4"
FT   TOPO_DOM        513..533
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        534..554
FT                   /note="Helical; Name=9"
FT                   /evidence="ECO:0000250|UniProtKB:Q08BA4"
FT   TOPO_DOM        555..561
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        562..582
FT                   /note="Helical; Name=10"
FT                   /evidence="ECO:0000250|UniProtKB:Q08BA4"
FT   TOPO_DOM        583..594
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        595..615
FT                   /note="Helical; Name=11"
FT                   /evidence="ECO:0000250|UniProtKB:Q08BA4"
FT   REGION          41..65
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          175..180
FT                   /note="Important for arginine binding and amino acid
FT                   transport"
FT                   /evidence="ECO:0000250|UniProtKB:Q08BA4"
FT   CARBOHYD        286
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        295
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        304..478
FT                   /evidence="ECO:0000250|UniProtKB:Q08BA4"
SQ   SEQUENCE   615 AA;  68693 MW;  5092F2A8F4A3A420 CRC64;
     MPPFFAEFTE SVFRHFRRNE PDEENSAICS EKMSSYGAIG VDDNDTDPLL DDEPPRRLPP
     AGGVPIGRRR AISASQIGSI PSQSAATRQP YLFTGGLGLR DESLLSLHSE DDLHREHNNA
     LRYRLYNRLD PGGEHLTMPD HVLPPNLFSI LPFEELKDVS GKQGSIVTIF SIWNTMMGTS
     LLAMPWALQQ AGLVLGIIIM LSMAAICFYT AYIVIESPKR LQDLSVDPLL AEFSDVCKSL
     FGRIGEYCAV VFSVCVLIGG VIVYWVLMSN FLYYTGAVVY ESMQPNSTTI PVMENKTFTC
     DVYCPEQTSQ WTIPQWEKQL YDAVSEMEGG ETGDDSWSFD KFWTLRGTVP IYLAFALFPL
     MNFKSPTFFT KFNVLGTISV MYLLMFVFSK LLECGVNMDF SNPKSIHYVQ LANMHFPALS
     GTLTLSYFIH NAVLTILRNQ KHPENNARDL SIGYCLVAFC YVFIGFTFFA AFPVQRSCIS
     DNFLNNFGAG DVLSSTARLF LLFQMITVLP LLMFLVRSQL FYAIFGQTWP GAIRVIILNV
     LLIAVAVGFA TFYPNVGSIL RYVGSISGLV YVFALPAMVY IKQSEAAGTL TPMKKYAHYG
     IIVIGVANLI AQFVI
 
 
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