S36A2_RAT
ID S36A2_RAT Reviewed; 481 AA.
AC Q8K415;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Proton-coupled amino acid transporter 2;
DE Short=Proton/amino acid transporter 2 {ECO:0000303|PubMed:12727219, ECO:0000303|PubMed:15644866};
DE Short=rPAT2 {ECO:0000303|PubMed:15644866};
DE AltName: Full=Solute carrier family 36 member 2 {ECO:0000312|RGD:620492};
DE AltName: Full=Transmembrane domain rich protein 1 {ECO:0000303|PubMed:12451123};
DE Short=Tramdorin-1 {ECO:0000303|PubMed:12451123};
GN Name=Slc36a2 {ECO:0000312|RGD:620492};
GN Synonyms=Pat2 {ECO:0000303|PubMed:12727219},
GN Tramd1 {ECO:0000303|PubMed:12451123};
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]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley;
RX PubMed=12451123; DOI=10.1523/jneurosci.22-23-10217.2002;
RA Bermingham J.R. Jr., Shumas S., Whisenhunt T., Sirkowski E.E.,
RA O'Connell S., Scherer S.S., Rosenfeld M.G.;
RT "Identification of genes that are downregulated in the absence of the POU
RT domain transcription factor pou3f1 (Oct-6, Tst-1, SCIP) in sciatic nerve.";
RL J. Neurosci. 22:10217-10231(2002).
RN [2]
RP FUNCTION, TRANSPORTER ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=12727219; DOI=10.1016/s0006-291x(03)00648-x;
RA Chen Z., Kennedy D.J., Wake K.A., Zhuang L., Ganapathy V., Thwaites D.T.;
RT "Structure, tissue expression pattern, and function of the amino acid
RT transporter rat PAT2.";
RL Biochem. Biophys. Res. Commun. 304:747-754(2003).
RN [3]
RP FUNCTION, TRANSPORTER ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP REGULATION, AND SUBCELLULAR LOCATION.
RX PubMed=15644866; DOI=10.1038/sj.bjp.0706029;
RA Kennedy D.J., Gatfield K.M., Winpenny J.P., Ganapathy V., Thwaites D.T.;
RT "Substrate specificity and functional characterisation of the H+/amino acid
RT transporter rat PAT2 (Slc36a2).";
RL Br. J. Pharmacol. 144:28-41(2005).
CC -!- FUNCTION: Electrogenic proton/amino acid symporter with a high
CC selectivity for the small side chains amino acids glycine, alanine and
CC proline, where both L- and D-enantiomers are transported. Extension of
CC the backbone length, as in beta-alanine and 4-aminobutanoate or
CC methylation of the amino group, as in sarcosine and N,N-
CC dimethylglycine, are also tolerated but decrease transport efficiency.
CC A free carboxyl group is preferred. {ECO:0000269|PubMed:12727219,
CC ECO:0000269|PubMed:15644866}.
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:12727219, ECO:0000269|PubMed:15644866};
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:12727219, ECO:0000269|PubMed:15644866};
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:15644866};
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:12727219, ECO:0000269|PubMed:15644866};
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:15644866};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-hydroxy-L-proline(in) + H(+)(in) = 4-hydroxy-L-proline(out)
CC + H(+)(out); Xref=Rhea:RHEA:70663, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58419; Evidence={ECO:0000269|PubMed:15644866};
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:12727219};
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:15644866};
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:12727219, ECO:0000269|PubMed:15644866};
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:0000250|UniProtKB:Q8BHK3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+)(in) + sarcosine(in) = H(+)(out) + sarcosine(out);
CC Xref=Rhea:RHEA:70655, ChEBI:CHEBI:15378, ChEBI:CHEBI:57433;
CC Evidence={ECO:0000269|PubMed:15644866};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+)(in) + N,N-dimethylglycine(in) = H(+)(out) + N,N-
CC dimethylglycine(out); Xref=Rhea:RHEA:70659, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58251; Evidence={ECO:0000269|PubMed:15644866};
CC -!- ACTIVITY REGULATION: Inhibited by L- and D-pipecolic acid, nipecotic
CC acid, isonipecotic acid, L- and D-cycloserine, and L-2-azetidine-
CC carboxylate. {ECO:0000269|PubMed:15644866}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.486 mM for glycine {ECO:0000269|PubMed:12727219};
CC KM=0.172 mM for proline {ECO:0000269|PubMed:15644866};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12727219,
CC ECO:0000269|PubMed:15644866}; Multi-pass membrane protein
CC {ECO:0000255}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q8BHK3}. Recycling endosome membrane
CC {ECO:0000250|UniProtKB:Q8BHK3}.
CC -!- TISSUE SPECIFICITY: Expressed in lung and spleen, and to a lower extent
CC in brain, heart, kidney and skeletal muscle.
CC {ECO:0000269|PubMed:12727219}.
CC -!- SIMILARITY: Belongs to the amino acid/polyamine transporter 2 family.
CC {ECO:0000305}.
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DR EMBL; AF512430; AAM44855.1; -; mRNA.
DR RefSeq; NP_647555.1; NM_139339.1.
DR AlphaFoldDB; Q8K415; -.
DR STRING; 10116.ENSRNOP00000016440; -.
DR iPTMnet; Q8K415; -.
DR PhosphoSitePlus; Q8K415; -.
DR PaxDb; Q8K415; -.
DR GeneID; 246235; -.
DR KEGG; rno:246235; -.
DR UCSC; RGD:620492; rat.
DR CTD; 153201; -.
DR RGD; 620492; Slc36a2.
DR eggNOG; KOG1304; Eukaryota.
DR InParanoid; Q8K415; -.
DR OrthoDB; 464614at2759; -.
DR PhylomeDB; Q8K415; -.
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:Q8K415; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0055038; C:recycling endosome membrane; ISS:UniProtKB.
DR GO; GO:0005280; F:amino acid:proton symporter activity; IDA:UniProtKB.
DR GO; GO:0015187; F:glycine transmembrane transporter activity; IDA: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:0005297; F:proline:proton symporter activity; IDA:UniProtKB.
DR GO; GO:0032973; P:amino acid export across plasma membrane; IDA: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:1900925; P:positive regulation of glycine import across plasma membrane; IDA:RGD.
DR GO; GO:0035524; P:proline transmembrane transport; IDA:RGD.
DR GO; GO:0015824; P:proline transport; ISO:RGD.
DR GO; GO:1902600; P:proton transmembrane transport; ISO:RGD.
DR GO; GO:0070881; P:regulation of proline transport; IDA:RGD.
DR GO; GO:0010155; P:regulation of proton transport; IDA:RGD.
DR InterPro; IPR013057; AA_transpt_TM.
DR Pfam; PF01490; Aa_trans; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Endoplasmic reticulum; Endosome; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..481
FT /note="Proton-coupled amino acid transporter 2"
FT /id="PRO_0000324821"
FT TOPO_DOM 1..56
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 57..77
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 78..79
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 80..100
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 101..146
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 147..167
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 168..195
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 196..216
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 217..220
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 221..241
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 242..262
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 263..283
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 284..295
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 296..316
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 317..343
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 344..364
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 365..377
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 378..398
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 399..402
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 403..423
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 424..444
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 445..465
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 466..481
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 26..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 481 AA; 52278 MW; FBCB4C32BCB0BB12 CRC64;
MSVTKSAGSP QVAATVKLDL VSFPESAKKV QSQDPNPVNG SSSESSEKTK GITGFQTLVH
LVKGNMGTGI LGLPLAVKNA GILMGPLSLL VMGLIACHCM HILVRCAQRF CHRLNKPFMD
YGDTVMHGLA SSPNTWLQSH AHWGRHAVSF FLIVTQLGFC CVYIVFLADN LKQVVEAVNS
TTISCHKNET VVLTPTIDSR LYMLAFLPVL GLLVFIRNLR VLTIFSLLAN VSMLVSLVII
GQYIIQGIPD PSQLPLVASW KTYPLFFGTA IFSFESIGVV LPLENKMKDA RRFPTILSLG
MSIITTLYIA IGALGYLRFG DDIKASITLN LPNCWLYQSV KLLYVVGILC THALQFYVPA
EIIIPLAVSQ VSKRWALPVD LSIRLALVCV TCMLAILIPR LDLVLSLVGS VSSSALALII
PPLLEVTTYY GEGMSPLTIT KDALISILGF MGFVVGTYQA LDELIRSGNS LPLSNSTMFI
Q
