AAA1_HUMAN
ID AAA1_HUMAN Reviewed; 523 AA.
AC Q9NS82; B2RE84;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Asc-type amino acid transporter 1;
DE Short=Asc-1;
DE AltName: Full=Solute carrier family 7 member 10;
GN Name=SLC7A10; Synonyms=ASC1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606 {ECO:0000312|EMBL:BAB03213.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=10863037; DOI=10.1016/s0304-3940(00)01169-1;
RA Nakauchi J., Matsuo H., Kim D.K., Goto A., Chairoungdua A., Cha S.H.,
RA Inatomi J., Shiokawa Y., Yamaguchi K., Saito I., Endou H., Kanai Y.;
RT "Cloning and characterization of a human brain Na+-independent transporter
RT for small neutral amino acids that transports D-serine with high
RT affinity.";
RL Neurosci. Lett. 287:231-235(2000).
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ASP-112.
RX PubMed=11509015; DOI=10.1006/mgme.2001.3209;
RA Leclerc D., Wu Q., Ellis J.R., Goodyer P., Rozen R.;
RT "Is the SLC7A10 gene on chromosome 19 a candidate locus for cystinuria?";
RL Mol. Genet. Metab. 73:333-339(2001).
RN [3] {ECO:0000312|EMBL:CAC81900.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Kidney;
RA Bassi M.T., Borsani G., Nunes V., Palacin M.;
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Amygdala;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Sodium-independent, high affinity transport of small neutral
CC D- and L-amino acids. May play a role in the modulation of
CC glutamatergic transmission through mobilization of D-serine at the
CC glutamatergic synapse. {ECO:0000269|PubMed:10863037}.
CC -!- SUBUNIT: Disulfide-linked heterodimer with the amino acid transport
CC protein SLC3A2/4F2hc. {ECO:0000250|UniProtKB:Q9JMH8}.
CC -!- INTERACTION:
CC Q9NS82; Q92624: APPBP2; NbExp=3; IntAct=EBI-12068238, EBI-743771;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in brain, heart, kidney, liver, lung,
CC pancreas, placenta, and skeletal muscle. {ECO:0000269|PubMed:10863037}.
CC -!- SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC)
CC superfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB037670; BAB03213.1; -; mRNA.
DR EMBL; AF340165; AAK93960.1; -; Genomic_DNA.
DR EMBL; AF340155; AAK93960.1; JOINED; Genomic_DNA.
DR EMBL; AF340156; AAK93960.1; JOINED; Genomic_DNA.
DR EMBL; AF340157; AAK93960.1; JOINED; Genomic_DNA.
DR EMBL; AF340158; AAK93960.1; JOINED; Genomic_DNA.
DR EMBL; AF340159; AAK93960.1; JOINED; Genomic_DNA.
DR EMBL; AF340160; AAK93960.1; JOINED; Genomic_DNA.
DR EMBL; AF340161; AAK93960.1; JOINED; Genomic_DNA.
DR EMBL; AF340162; AAK93960.1; JOINED; Genomic_DNA.
DR EMBL; AF340163; AAK93960.1; JOINED; Genomic_DNA.
DR EMBL; AF340164; AAK93960.1; JOINED; Genomic_DNA.
DR EMBL; AJ277731; CAC81900.1; -; mRNA.
DR EMBL; AK316594; BAG38181.1; -; mRNA.
DR EMBL; BC035627; AAH35627.1; -; mRNA.
DR CCDS; CCDS12431.1; -.
DR RefSeq; NP_062823.1; NM_019849.2.
DR AlphaFoldDB; Q9NS82; -.
DR SMR; Q9NS82; -.
DR BioGRID; 121136; 1.
DR IntAct; Q9NS82; 2.
DR STRING; 9606.ENSP00000253188; -.
DR TCDB; 2.A.3.8.21; the amino acid-polyamine-organocation (apc) family.
DR iPTMnet; Q9NS82; -.
DR PhosphoSitePlus; Q9NS82; -.
DR BioMuta; SLC7A10; -.
DR DMDM; 25089504; -.
DR jPOST; Q9NS82; -.
DR MassIVE; Q9NS82; -.
DR PaxDb; Q9NS82; -.
DR PeptideAtlas; Q9NS82; -.
DR PRIDE; Q9NS82; -.
DR ProteomicsDB; 82507; -.
DR Antibodypedia; 47948; 96 antibodies from 19 providers.
DR DNASU; 56301; -.
DR Ensembl; ENST00000253188.8; ENSP00000253188.2; ENSG00000130876.11.
DR GeneID; 56301; -.
DR KEGG; hsa:56301; -.
DR MANE-Select; ENST00000253188.8; ENSP00000253188.2; NM_019849.3; NP_062823.1.
DR UCSC; uc002num.2; human.
DR CTD; 56301; -.
DR DisGeNET; 56301; -.
DR GeneCards; SLC7A10; -.
DR HGNC; HGNC:11058; SLC7A10.
DR HPA; ENSG00000130876; Group enriched (adipose tissue, brain, breast).
DR MIM; 607959; gene.
DR neXtProt; NX_Q9NS82; -.
DR OpenTargets; ENSG00000130876; -.
DR PharmGKB; PA35918; -.
DR VEuPathDB; HostDB:ENSG00000130876; -.
DR eggNOG; KOG1287; Eukaryota.
DR GeneTree; ENSGT00940000156469; -.
DR HOGENOM; CLU_007946_3_0_1; -.
DR InParanoid; Q9NS82; -.
DR OMA; YDGWILI; -.
DR OrthoDB; 867824at2759; -.
DR PhylomeDB; Q9NS82; -.
DR TreeFam; TF313355; -.
DR PathwayCommons; Q9NS82; -.
DR Reactome; R-HSA-210991; Basigin interactions.
DR Reactome; R-HSA-352230; Amino acid transport across the plasma membrane.
DR SignaLink; Q9NS82; -.
DR BioGRID-ORCS; 56301; 11 hits in 1067 CRISPR screens.
DR GeneWiki; SLC7A10; -.
DR GenomeRNAi; 56301; -.
DR Pharos; Q9NS82; Tbio.
DR PRO; PR:Q9NS82; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q9NS82; protein.
DR Bgee; ENSG00000130876; Expressed in omental fat pad and 92 other tissues.
DR ExpressionAtlas; Q9NS82; baseline and differential.
DR Genevisible; Q9NS82; HS.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0016020; C:membrane; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0015179; F:L-amino acid transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015194; F:L-serine transmembrane transporter activity; TAS:ProtInc.
DR GO; GO:0015175; F:neutral amino acid transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0006865; P:amino acid transport; TAS:ProtInc.
DR GO; GO:0042941; P:D-alanine transport; IBA:GO_Central.
DR GO; GO:0042942; P:D-serine transport; IBA:GO_Central.
DR GO; GO:0015804; P:neutral amino acid transport; IDA:UniProtKB.
DR InterPro; IPR002293; AA/rel_permease1.
DR Pfam; PF13520; AA_permease_2; 1.
PE 1: Evidence at protein level;
KW Amino-acid transport; Disulfide bond; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..523
FT /note="Asc-type amino acid transporter 1"
FT /id="PRO_0000054276"
FT TRANSMEM 40..60
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 72..92
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 113..133
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 268..288
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 310..330
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 362..382
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 388..408
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 424..444
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 448..468
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 499..523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 112
FT /note="E -> D (in a family with cystinuria;
FT dbSNP:rs79717007)"
FT /evidence="ECO:0000269|PubMed:11509015"
FT /id="VAR_014282"
FT VARIANT 413
FT /note="R -> Q (in dbSNP:rs34663170)"
FT /id="VAR_048158"
SQ SEQUENCE 523 AA; 56798 MW; 24BA0B36521AC2D4 CRC64;
MAGHTQQPSG RGNPRPAPSP SPVPGTVPGA SERVALKKEI GLLSACTIII GNIIGSGIFI
SPKGVLEHSG SVGLALFVWV LGGGVTALGS LCYAELGVAI PKSGGDYAYV TEIFGGLAGF
LLLWSAVLIM YPTSLAVISM TFSNYVLQPV FPNCIPPTTA SRVLSMACLM LLTWVNSSSV
RWATRIQDMF TGGKLLALSL IIGVGLLQIF QGHFEELRPS NAFAFWMTPS VGHLALAFLQ
GSFAFSGWNF LNYVTEEMVD ARKNLPRAIF ISIPLVTFVY TFTNIAYFTA MSPQELLSSN
AVAVTFGEKL LGYFSWVMPV SVALSTFGGI NGYLFTYSRL CFSGAREGHL PSLLAMIHVR
HCTPIPALLV CCGATAVIML VGDTYTLINY VSFINYLCYG VTILGLLLLR WRRPALHRPI
KVNLLIPVAY LVFWAFLLVF SFISEPMVCG VGVIIILTGV PIFFLGVFWR SKPKCVHRLT
ESMTHWGQEL CFVVYPQDAP EEEENGPCPP SLLPATDKPS KPQ
