S36A1_MOUSE
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 03-AUG-2022, entry version 137.
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=7.0 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 GlyGen; Q8K4D3; 3 sites.
DR iPTMnet; Q8K4D3; -.
DR PhosphoSitePlus; Q8K4D3; -.
DR MaxQB; Q8K4D3; -.
DR PaxDb; Q8K4D3; -.
DR PRIDE; Q8K4D3; -.
DR ProteomicsDB; 256889; -.
DR Antibodypedia; 49166; 84 antibodies from 17 providers.
DR DNASU; 215335; -.
DR Ensembl; ENSMUST00000020499; ENSMUSP00000020499; ENSMUSG00000020261.
DR Ensembl; ENSMUST00000108867; ENSMUSP00000104495; ENSMUSG00000020261.
DR Ensembl; ENSMUST00000108872; ENSMUSP00000104500; ENSMUSG00000020261.
DR GeneID; 215335; -.
DR KEGG; mmu:215335; -.
DR UCSC; uc007izd.1; mouse.
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; AMYVPNF; -.
DR OrthoDB; 464614at2759; -.
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 75 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 205 other tissues.
DR ExpressionAtlas; Q8K4D3; baseline and differential.
DR Genevisible; Q8K4D3; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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: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:0015179; F:L-amino acid transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015193; F:L-proline transmembrane transporter activity; IDA:MGI.
DR GO; GO:0015175; F:neutral 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:0003333; P:amino acid transmembrane transport; IBA:GO_Central.
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 Pfam; PF01490; Aa_trans; 1.
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
