S36A1_RAT
ID S36A1_RAT Reviewed; 475 AA.
AC Q924A5;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Proton-coupled amino acid transporter 1 {ECO:0000305|PubMed:11390972};
DE Short=Proton/amino acid transporter 1 {ECO:0000305|PubMed:11390972};
DE AltName: Full=Lysosomal amino acid transporter 1 {ECO:0000303|PubMed:11390972};
DE Short=LYAAT-1 {ECO:0000303|PubMed:11390972};
DE AltName: Full=Neutral amino acid/proton symporter;
DE AltName: Full=Solute carrier family 36 member 1 {ECO:0000312|RGD:619801};
GN Name=Slc36a1 {ECO:0000312|RGD:619801};
GN Synonyms=Lyaat1 {ECO:0000303|PubMed:11390972};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAK67316.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TRANSPORTER ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=Sprague-Dawley {ECO:0000312|EMBL:AAK67316.1};
RC TISSUE=Hippocampus {ECO:0000269|PubMed:11390972};
RX PubMed=11390972; DOI=10.1073/pnas.121183498;
RA Sagne C., Agulhon C., Ravassard P., Darmon M., Hamon M., El Mestikawy S.,
RA Gasnier B., Giros B.;
RT "Identification and characterization of a lysosomal transporter for small
RT neutral amino acids.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7206-7211(2001).
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TRANSPORTER ACTIVITY, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Brain {ECO:0000269|PubMed:12598615};
RX PubMed=12598615; DOI=10.1523/jneurosci.23-04-01265.2003;
RA Wreden C.C., Johnson J., Tran C., Seal R.P., Copenhagen D.R., Reimer R.J.,
RA Edwards R.H.;
RT "The H+-coupled electrogenic lysosomal amino acid transporter LYAAT1
RT localizes to the axon and plasma membrane of hippocampal neurons.";
RL J. Neurosci. 23:1265-1275(2003).
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:11390972,
CC PubMed:12598615). May be involved in the efflux from the lysosomal
CC compartment of neutral amino acids resulting from proteolysis
CC (PubMed:12598615). May play a role in specifying sites for exocytosis
CC in neurons (PubMed:12598615). {ECO:0000269|PubMed:11390972,
CC ECO:0000269|PubMed:12598615}.
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:0000250|UniProtKB:Q8K4D3};
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:12598615};
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:12598615};
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:12598615};
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:0000250|UniProtKB:Q8K4D3};
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:0000250|UniProtKB:Q8K4D3};
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:0000250|UniProtKB:Q8K4D3};
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:11390972,
CC ECO:0000269|PubMed:12598615};
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:0000250|UniProtKB:Q8K4D3};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=499 uM for 4-aminobutanoate {ECO:0000269|PubMed:11390972};
CC Vmax=2.5 pmol/min/ug enzyme with 4-aminobutanoate as substrate
CC {ECO:0000269|PubMed:11390972};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12598615};
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:0000269|PubMed:11390972,
CC ECO:0000269|PubMed:12598615}; Multi-pass membrane protein
CC {ECO:0000255}. Note=In neurons, colocalizes with the exocyst complex in
CC the axonal processes. {ECO:0000269|PubMed:12598615}.
CC -!- TISSUE SPECIFICITY: Widely expressed and predominantly expressed in
CC brain. Within the brain, expression restricted to neurons and not
CC detected in glial cells. Abundant in regions rich in neurons using
CC glutamate and GABA such as Purkinje cells in the cerebellum and
CC pyramidal cells in the hippocampus. {ECO:0000269|PubMed:11390972,
CC ECO:0000269|PubMed:12598615}.
CC -!- SIMILARITY: Belongs to the amino acid/polyamine transporter 2 family.
CC {ECO:0000305}.
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DR EMBL; AF361239; AAK67316.1; -; mRNA.
DR RefSeq; NP_569099.1; NM_130415.1.
DR RefSeq; XP_008765881.1; XM_008767659.1.
DR AlphaFoldDB; Q924A5; -.
DR SMR; Q924A5; -.
DR STRING; 10116.ENSRNOP00000016755; -.
DR GlyGen; Q924A5; 3 sites.
DR PaxDb; Q924A5; -.
DR Ensembl; ENSRNOT00000016755; ENSRNOP00000016755; ENSRNOG00000012356.
DR GeneID; 155205; -.
DR KEGG; rno:155205; -.
DR UCSC; RGD:619801; rat.
DR CTD; 206358; -.
DR RGD; 619801; Slc36a1.
DR eggNOG; KOG1304; Eukaryota.
DR GeneTree; ENSGT00940000156583; -.
DR HOGENOM; CLU_009646_0_2_1; -.
DR InParanoid; Q924A5; -.
DR OMA; AMYVPNF; -.
DR OrthoDB; 464614at2759; -.
DR PhylomeDB; Q924A5; -.
DR TreeFam; TF314873; -.
DR Reactome; R-RNO-352230; Amino acid transport across the plasma membrane.
DR Reactome; R-RNO-428559; Proton-coupled neutral amino acid transporters.
DR PRO; PR:Q924A5; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000012356; Expressed in jejunum and 18 other tissues.
DR Genevisible; Q924A5; RN.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
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; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0022858; F:alanine transmembrane transporter activity; ISO:RGD.
DR GO; GO:0005280; F:amino acid:proton symporter activity; IDA:UniProtKB.
DR GO; GO:0015187; F:glycine transmembrane transporter activity; ISO:RGD.
DR GO; GO:0015180; F:L-alanine transmembrane transporter activity; ISO:RGD.
DR GO; GO:0015179; F:L-amino acid transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015193; F:L-proline transmembrane transporter activity; ISO:RGD.
DR GO; GO:0015175; F:neutral amino acid transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0005297; F:proline:proton symporter activity; IDA:UniProtKB.
DR GO; GO:0015078; F:proton transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0005368; F:taurine transmembrane transporter activity; ISO:RGD.
DR GO; GO:0032328; P:alanine transport; ISO:RGD.
DR GO; GO:0089718; P:amino acid import across plasma membrane; ISO:RGD.
DR GO; GO:0003333; P:amino acid transmembrane transport; IBA:GO_Central.
DR GO; GO:0015816; P:glycine transport; ISO:RGD.
DR GO; GO:0015808; P:L-alanine transport; ISO:RGD.
DR GO; GO:0015804; P:neutral amino acid transport; IDA:UniProtKB.
DR GO; GO:0035524; P:proline transmembrane transport; IBA:GO_Central.
DR GO; GO:0015824; P:proline transport; ISO:RGD.
DR GO; GO:1902600; P:proton transmembrane transport; IDA:UniProtKB.
DR GO; GO:0015734; P:taurine transport; ISO:RGD.
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_0000093827"
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 108
FT /note="L -> M (in Ref. 2; no nucleotide entry)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 475 AA; 52569 MW; D3D04A489AD1D23C CRC64;
MSTQRLRNED YHDYSSTDVS PEESPSEGLG SFSPGSYQRL GENSSMTWFQ TLIHLLKGNI
GTGLLGLPLA VKNAGLLLGP LSLLVIGIVA VHCMGILVKC AHHLCRRLNK PFLDYGDTVM
YGLECSPSTW IRNHSHWGRR IVDFFLVVTQ LGFCCVYFVF LADNFKQVIE AANGTTTNCN
NNETVILTPT MDSRLYMLTF LPFLVLLSFI RNLRILSIFS LLANISMFVS LIMIYQFIVQ
RIPDPSHLPL VAPWKTYPLF FGTAIFAFEG IGVVLPLENK MKDSQKFPLI LYLGMAIITV
LYISLGSLGY LQFGADIKGS ITLNLPNCWL YQSVKLLYSI GIFFTYALQF YVAAEIIIPA
IVSRVPERFE LVVDLSARTA MVCVTCVLAV LIPRLDLVIS LVGSVSSSAL ALIIPPLLEV
TTYYGEGISP LTITKDALIS ILGFVGFVVG TYESLWELIQ PSHSDSSTNS TSAFI
