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   27-MAR-2024, entry version 168.
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP   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]
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]
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: Associates with SLC3A2/4F2hc to form a functional
CC       heterodimeric complex that translocates small neutral L- and D-amino
CC       acids across the plasma membrane. Preferentially mediates exchange
CC       transport, but can also operate via facilitated diffusion (By
CC       similarity) (PubMed:10863037). Acts as a major transporter for glycine,
CC       L- and D-serine in the central nervous system. At the spinal cord and
CC       brainstem regulates glycine metabolism and glycinergic inhibitory
CC       neurotransmission by providing for glycine de novo synthesis from L-
CC       serine and glycine recycling from astrocytes to glycinergic motor
CC       neurons (By similarity). At Schaffer collateral-CA1 synapses mediates
CC       D-serine and glycine release that modulates post-synaptic activation of
CC       NMDA receptors and excitatory glutamatergic transmission (By
CC       similarity). May regulate D-serine release from mesenchymal progenitors
CC       located in developing subcutaneous adipose tissue, favoring white
CC       adipocyte over thermogenic beige adipocyte lineage commitment (By
CC       similarity). {ECO:0000250|UniProtKB:P63115,
CC       ECO:0000250|UniProtKB:P63116, ECO:0000269|PubMed:10863037}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glycine(out) + L-alanine(in) = glycine(in) + L-alanine(out);
CC         Xref=Rhea:RHEA:74019, ChEBI:CHEBI:57305, ChEBI:CHEBI:57972;
CC         Evidence={ECO:0000250|UniProtKB:P63115};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-alanine(in) + L-serine(out) = L-alanine(out) + L-serine(in);
CC         Xref=Rhea:RHEA:74023, ChEBI:CHEBI:33384, ChEBI:CHEBI:57972;
CC         Evidence={ECO:0000250|UniProtKB:P63115};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-alanine(in) + L-threonine(out) = L-alanine(out) + L-
CC         threonine(in); Xref=Rhea:RHEA:74027, ChEBI:CHEBI:57926,
CC         ChEBI:CHEBI:57972; Evidence={ECO:0000250|UniProtKB:P63115};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-alanine(in) + L-cysteine(out) = L-alanine(out) + L-
CC         cysteine(in); Xref=Rhea:RHEA:74031, ChEBI:CHEBI:35235,
CC         ChEBI:CHEBI:57972; Evidence={ECO:0000250|UniProtKB:P63115};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-aminoisobutanoate(out) + L-alanine(in) = 2-
CC         aminoisobutanoate(in) + L-alanine(out); Xref=Rhea:RHEA:74063,
CC         ChEBI:CHEBI:57972, ChEBI:CHEBI:193090;
CC         Evidence={ECO:0000250|UniProtKB:P63115};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-serine(out) + L-alanine(in) = D-serine(in) + L-alanine(out);
CC         Xref=Rhea:RHEA:74035, ChEBI:CHEBI:35247, ChEBI:CHEBI:57972;
CC         Evidence={ECO:0000250|UniProtKB:P63115};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-alanine(out) + L-alanine(in) = D-alanine(in) + L-
CC         alanine(out); Xref=Rhea:RHEA:74039, ChEBI:CHEBI:57416,
CC         ChEBI:CHEBI:57972; Evidence={ECO:0000250|UniProtKB:P63115};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-alanine(in) + L-valine(out) = L-alanine(out) + L-valine(in);
CC         Xref=Rhea:RHEA:74047, ChEBI:CHEBI:57762, ChEBI:CHEBI:57972;
CC         Evidence={ECO:0000250|UniProtKB:P63115};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-alanine(in) + L-methionine(out) = L-alanine(out) + L-
CC         methionine(in); Xref=Rhea:RHEA:74043, ChEBI:CHEBI:57844,
CC         ChEBI:CHEBI:57972; Evidence={ECO:0000250|UniProtKB:P63115};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=beta-alanine(out) + L-alanine(in) = beta-alanine(in) + L-
CC         alanine(out); Xref=Rhea:RHEA:74059, ChEBI:CHEBI:57966,
CC         ChEBI:CHEBI:57972; Evidence={ECO:0000250|UniProtKB:P63115};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-cysteine(out) + L-alanine(in) = D-cysteine(in) + L-
CC         alanine(out); Xref=Rhea:RHEA:74055, ChEBI:CHEBI:35236,
CC         ChEBI:CHEBI:57972; Evidence={ECO:0000250|UniProtKB:P63115};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-threonine(out) + L-alanine(in) = D-threonine(in) + L-
CC         alanine(out); Xref=Rhea:RHEA:74051, ChEBI:CHEBI:57757,
CC         ChEBI:CHEBI:57972; Evidence={ECO:0000250|UniProtKB:P63115};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-isoleucine(out) + D-serine(in) = D-isoleucine(in) + D-
CC         serine(out); Xref=Rhea:RHEA:74299, ChEBI:CHEBI:35247,
CC         ChEBI:CHEBI:193151; Evidence={ECO:0000250|UniProtKB:P63116};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:74300;
CC         Evidence={ECO:0000250|UniProtKB:P63116};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-serine(in) = D-serine(out); Xref=Rhea:RHEA:29455,
CC         ChEBI:CHEBI:35247; Evidence={ECO:0000250|UniProtKB:P63116};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=22.8 uM for D-serine {ECO:0000269|PubMed:10863037};
CC         KM=9.16 uM for L-alanine {ECO:0000269|PubMed:10863037};
CC   -!- SUBUNIT: Disulfide-linked heterodimer with the amino acid transport
CC       protein SLC3A2/4F2hc. {ECO:0000250|UniProtKB:P63115}.
CC   -!- INTERACTION:
CC       Q9NS82; Q92624: APPBP2; NbExp=3; IntAct=EBI-12068238, EBI-743771;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P63115};
CC       Multi-pass membrane protein {ECO:0000255}. Note=Colocalizes with OLIG2
CC       in astrocytic processes. Localizes to the plasma membrane in mature
CC       adipocytes and to intracellular structures in preadipocytes.
CC       {ECO:0000250|UniProtKB:P63115}.
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}.
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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; 2.
DR   ComplexPortal; CPX-8189; ASC1-4F2 heteromeric amino acid transporter complex.
DR   IntAct; Q9NS82; 3.
DR   MINT; Q9NS82; -.
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; 9606-ENSP00000253188; -.
DR   PeptideAtlas; Q9NS82; -.
DR   ProteomicsDB; 82507; -.
DR   Antibodypedia; 47948; 110 antibodies from 20 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   AGR; HGNC:11058; -.
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; PWRDVVP; -.
DR   OrthoDB; 1103451at2759; -.
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; 12 hits in 1147 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 93 other cell types or tissues.
DR   ExpressionAtlas; Q9NS82; baseline and differential.
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 L-amino acid transmembrane transporter activity; IDA:UniProtKB.
DR   GO; GO:0003333; P:amino acid transmembrane transport; IBA:GO_Central.
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:0015816; P:glycine transport; IEA:Ensembl.
DR   GO; GO:1903444; P:negative regulation of brown fat cell differentiation; IEA:Ensembl.
DR   GO; GO:0015804; P:neutral amino acid transport; IDA:UniProtKB.
DR   GO; GO:0060094; P:positive regulation of synaptic transmission, glycinergic; IEA:Ensembl.
DR   Gene3D; 1.20.1740.10; Amino acid/polyamine transporter I; 1.
DR   InterPro; IPR002293; AA/rel_permease1.
DR   PANTHER; PTHR11785; AMINO ACID TRANSPORTER; 1.
DR   PANTHER; PTHR11785:SF73; ASC-TYPE AMINO ACID TRANSPORTER 1; 1.
DR   Pfam; PF13520; AA_permease_2; 1.
DR   PIRSF; PIRSF006060; AA_transporter; 1.
DR   Genevisible; Q9NS82; HS.
PE   1: Evidence at protein level;
KW   Amino-acid transport; Cell membrane; Disulfide bond; Membrane;
KW   Reference proteome; 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
//