ID   S36A1_MOUSE             Reviewed;         475 AA.
AC   Q8K4D3; Q811N9;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   27-MAR-2024, entry version 145.
DE   RecName: Full=Proton-coupled amino acid transporter 1 {ECO:0000305|PubMed:11959859};
DE            Short=Proton/amino acid transporter 1 {ECO:0000305|PubMed:11959859};
DE   AltName: Full=Solute carrier family 36 member 1 {ECO:0000312|MGI:MGI:2445299};
GN   Name=Slc36a1 {ECO:0000312|MGI:MGI:2445299};
GN   Synonyms=Pat1 {ECO:0000303|PubMed:11959859};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TRANSPORTER ACTIVITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RC   STRAIN=C57BL/6J;
RX   PubMed=11959859; DOI=10.1074/jbc.m200374200;
RA   Boll M., Foltz M., Rubio-Aliaga I., Kottra G., Daniel H.;
RT   "Functional characterization of two novel mammalian electrogenic proton-
RT   dependent amino acid cotransporters.";
RL   J. Biol. Chem. 277:22966-22973(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=15058382; DOI=10.1007/s00335-003-2319-3;
RA   Bermingham J.R. Jr., Pennington J.;
RT   "Organization and expression of the SLC36 cluster of amino acid transporter
RT   genes.";
RL   Mamm. Genome 15:114-125(2004).
CC   -!- FUNCTION: Electrogenic proton/amino acid symporter with selectivity for
CC       small apolar L-amino acids, their D-enantiomers and selected amino acid
CC       derivatives such as 4-aminobutanoate/GABA (PubMed:11959859). May be
CC       involved in the efflux from the lysosomal compartment of neutral amino
CC       acids resulting from proteolysis (By similarity). May play a role in
CC       specifying sites for exocytosis in neurons (By similarity).
CC       {ECO:0000250|UniProtKB:Q924A5, ECO:0000269|PubMed:11959859}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glycine(in) + H(+)(in) = glycine(out) + H(+)(out);
CC         Xref=Rhea:RHEA:28899, ChEBI:CHEBI:15378, ChEBI:CHEBI:57305;
CC         Evidence={ECO:0000269|PubMed:11959859};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+)(in) + L-alanine(in) = H(+)(out) + L-alanine(out);
CC         Xref=Rhea:RHEA:29443, ChEBI:CHEBI:15378, ChEBI:CHEBI:57972;
CC         Evidence={ECO:0000269|PubMed:11959859};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-alanine(in) + H(+)(in) = D-alanine(out) + H(+)(out);
CC         Xref=Rhea:RHEA:28903, ChEBI:CHEBI:15378, ChEBI:CHEBI:57416;
CC         Evidence={ECO:0000269|PubMed:11959859};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+)(out) + L-proline(out) = H(+)(in) + L-proline(in);
CC         Xref=Rhea:RHEA:28963, ChEBI:CHEBI:15378, ChEBI:CHEBI:60039;
CC         Evidence={ECO:0000269|PubMed:11959859};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-proline(out) + H(+)(out) = D-proline(in) + H(+)(in);
CC         Xref=Rhea:RHEA:70643, ChEBI:CHEBI:15378, ChEBI:CHEBI:57726;
CC         Evidence={ECO:0000269|PubMed:11959859};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+)(in) + L-serine(in) = H(+)(out) + L-serine(out);
CC         Xref=Rhea:RHEA:28887, ChEBI:CHEBI:15378, ChEBI:CHEBI:33384;
CC         Evidence={ECO:0000269|PubMed:11959859};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-serine(out) + H(+)(out) = D-serine(in) + H(+)(in);
CC         Xref=Rhea:RHEA:70647, ChEBI:CHEBI:15378, ChEBI:CHEBI:35247;
CC         Evidence={ECO:0000269|PubMed:11959859};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-aminobutanoate(in) + H(+)(in) = 4-aminobutanoate(out) +
CC         H(+)(out); Xref=Rhea:RHEA:28915, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:59888; Evidence={ECO:0000269|PubMed:11959859};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=beta-alanine(in) + H(+)(in) = beta-alanine(out) + H(+)(out);
CC         Xref=Rhea:RHEA:29459, ChEBI:CHEBI:15378, ChEBI:CHEBI:57966;
CC         Evidence={ECO:0000269|PubMed:11959859};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=7 mM for glycine {ECO:0000269|PubMed:11959859};
CC         KM=7.5 mM for L-alanine {ECO:0000269|PubMed:11959859};
CC         KM=2.8 mM for L-proline {ECO:0000269|PubMed:11959859};
CC         KM=69 mM for L-serine {ECO:0000269|PubMed:11959859};
CC         KM=6.3 mM for D-alanine {ECO:0000269|PubMed:11959859};
CC         KM=3.1 mM for 4-aminobutanoate/GABA {ECO:0000269|PubMed:11959859};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11959859};
CC       Multi-pass membrane protein {ECO:0000255}. Apical cell membrane
CC       {ECO:0000250|UniProtKB:Q7Z2H8}; Multi-pass membrane protein
CC       {ECO:0000255}. Lysosome membrane {ECO:0000250|UniProtKB:Q924A5}; Multi-
CC       pass membrane protein {ECO:0000255}. Note=In neurons, colocalizes with
CC       the exocyst complex in the axonal processes.
CC       {ECO:0000250|UniProtKB:Q924A5}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in small intestine, colon, kidney
CC       and brain. {ECO:0000269|PubMed:11959859}.
CC   -!- SIMILARITY: Belongs to the amino acid/polyamine transporter 2 family.
CC       {ECO:0000305}.
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DR   EMBL; AF453743; AAM80480.1; -; mRNA.
DR   EMBL; AY211262; AAO37090.1; -; mRNA.
DR   CCDS; CCDS36156.1; -.
DR   RefSeq; NP_694779.3; NM_153139.4.
DR   AlphaFoldDB; Q8K4D3; -.
DR   SMR; Q8K4D3; -.
DR   IntAct; Q8K4D3; 1.
DR   MINT; Q8K4D3; -.
DR   STRING; 10090.ENSMUSP00000104500; -.
DR   TCDB; 2.A.18.8.1; the amino acid/auxin permease (aaap) family.
DR   GlyCosmos; Q8K4D3; 3 sites, No reported glycans.
DR   GlyGen; Q8K4D3; 3 sites.
DR   iPTMnet; Q8K4D3; -.
DR   PhosphoSitePlus; Q8K4D3; -.
DR   MaxQB; Q8K4D3; -.
DR   PaxDb; 10090-ENSMUSP00000104500; -.
DR   ProteomicsDB; 256889; -.
DR   Pumba; Q8K4D3; -.
DR   Antibodypedia; 49166; 103 antibodies from 18 providers.
DR   DNASU; 215335; -.
DR   Ensembl; ENSMUST00000020499.14; ENSMUSP00000020499.8; ENSMUSG00000020261.16.
DR   Ensembl; ENSMUST00000108867.2; ENSMUSP00000104495.2; ENSMUSG00000020261.16.
DR   Ensembl; ENSMUST00000108872.9; ENSMUSP00000104500.3; ENSMUSG00000020261.16.
DR   GeneID; 215335; -.
DR   KEGG; mmu:215335; -.
DR   UCSC; uc007izd.1; mouse.
DR   AGR; MGI:2445299; -.
DR   CTD; 206358; -.
DR   MGI; MGI:2445299; Slc36a1.
DR   VEuPathDB; HostDB:ENSMUSG00000020261; -.
DR   eggNOG; KOG1304; Eukaryota.
DR   GeneTree; ENSGT00940000156583; -.
DR   HOGENOM; CLU_009646_0_2_1; -.
DR   InParanoid; Q8K4D3; -.
DR   OMA; HWELVVD; -.
DR   OrthoDB; 3601817at2759; -.
DR   PhylomeDB; Q8K4D3; -.
DR   TreeFam; TF314873; -.
DR   Reactome; R-MMU-352230; Amino acid transport across the plasma membrane.
DR   Reactome; R-MMU-428559; Proton-coupled neutral amino acid transporters.
DR   SABIO-RK; Q8K4D3; -.
DR   BioGRID-ORCS; 215335; 2 hits in 80 CRISPR screens.
DR   ChiTaRS; Slc36a1; mouse.
DR   PRO; PR:Q8K4D3; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   RNAct; Q8K4D3; Protein.
DR   Bgee; ENSMUSG00000020261; Expressed in superior cervical ganglion and 207 other cell types or tissues.
DR   ExpressionAtlas; Q8K4D3; baseline and differential.
DR   GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR   GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005764; C:lysosome; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0005774; C:vacuolar membrane; IBA:GO_Central.
DR   GO; GO:0022858; F:alanine transmembrane transporter activity; ISO:MGI.
DR   GO; GO:0005280; F:amino acid:proton symporter activity; IDA:MGI.
DR   GO; GO:0015187; F:glycine transmembrane transporter activity; IDA:MGI.
DR   GO; GO:0015180; F:L-alanine transmembrane transporter activity; IDA:MGI.
DR   GO; GO:0015193; F:L-proline transmembrane transporter activity; IDA:MGI.
DR   GO; GO:0015175; F:neutral L-amino acid transmembrane transporter activity; ISO:MGI.
DR   GO; GO:0005297; F:proline:proton symporter activity; ISO:MGI.
DR   GO; GO:0015078; F:proton transmembrane transporter activity; ISO:MGI.
DR   GO; GO:0005368; F:taurine transmembrane transporter activity; ISO:MGI.
DR   GO; GO:0032328; P:alanine transport; ISO:MGI.
DR   GO; GO:0089718; P:amino acid import across plasma membrane; ISO:MGI.
DR   GO; GO:0015816; P:glycine transport; IDA:MGI.
DR   GO; GO:0015808; P:L-alanine transport; IDA:MGI.
DR   GO; GO:0015804; P:neutral amino acid transport; ISO:MGI.
DR   GO; GO:0035524; P:proline transmembrane transport; IBA:GO_Central.
DR   GO; GO:0015824; P:proline transport; IDA:MGI.
DR   GO; GO:1902600; P:proton transmembrane transport; IDA:MGI.
DR   GO; GO:0015734; P:taurine transport; ISO:MGI.
DR   InterPro; IPR013057; AA_transpt_TM.
DR   PANTHER; PTHR22950; AMINO ACID TRANSPORTER; 1.
DR   PANTHER; PTHR22950:SF188; PROTON-COUPLED AMINO ACID TRANSPORTER 1; 1.
DR   Pfam; PF01490; Aa_trans; 1.
DR   Genevisible; Q8K4D3; MM.
PE   1: Evidence at protein level;
KW   Amino-acid transport; Cell membrane; Disulfide bond; Glycoprotein;
KW   Lysosome; Membrane; Reference proteome; Symport; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..475
FT                   /note="Proton-coupled amino acid transporter 1"
FT                   /id="PRO_0000093826"
FT   TOPO_DOM        1..50
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        51..71
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        72..77
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        78..98
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        99..140
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        141..161
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        162..189
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        190..210
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        211..214
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        215..235
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        236..256
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        257..277
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        278..288
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        289..309
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        310..341
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        342..362
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        363..371
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        372..392
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        393..396
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        397..417
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        418..438
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        439..459
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        460..475
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   REGION          1..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..17
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        18..32
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        173
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        182
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        469
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        179..328
FT                   /evidence="ECO:0000250"
FT   CONFLICT        43
FT                   /note="N -> S (in Ref. 2; AAO37090)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        198
FT                   /note="L -> P (in Ref. 2; AAO37090)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   475 AA;  52466 MW;  113C23309F2B51F1 CRC64;
     MSTQRLRNED YHDYSSTDVS PEESPSEGLG SFSPGSYQRL GENSSMTWFQ TLIHLLKGNI
     GTGLLGLPLA VKNAGLLLGP LSLLVIGIVA VHCMGILVKC AHHLCRRLNK PFLDYGDTVM
     YGLECSPSTW VRNHSHWGRR IVDFFLIVTQ LGFCCVYFVF LADNFKQVIE AANGTTTNCN
     NNVTVIPTPT MDSRLYMLSF LPFLVLLSFI RNLRVLSIFS LLANISMFVS LIMIYQFIVQ
     RIPDPSHLPL VAPWKTYPLF FGTAIFAFEG IGVVLPLENK MKDSQKFPLI LYLGMAIITV
     LYISLGSLGY LQFGANIKGS ITLNLPNCWL YQSVKLLYSI GIFFTYALQF YVAAEIIIPA
     IVSRVPEHFE LMVDLCVRTA MVCVTCVLAI LIPRLDLVIS LVGSVSSSAL ALIIPPLLEV
     VTYYGEGISP LTVTKDALIS ILGFVGFVVG TYESLCELIQ PSHSDSSTNS TSAFI
//