S36A1_HUMAN
ID S36A1_HUMAN Reviewed; 476 AA.
AC Q7Z2H8; C9JI34; Q1LZ56; Q7Z7C0; Q86YK4; Q96M74;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Proton-coupled amino acid transporter 1 {ECO:0000305|PubMed:12809675};
DE Short=Proton/amino acid transporter 1 {ECO:0000305|PubMed:12809675};
DE Short=hPAT1 {ECO:0000303|PubMed:12809675};
DE AltName: Full=Solute carrier family 36 member 1 {ECO:0000312|HGNC:HGNC:18761};
GN Name=SLC36A1 {ECO:0000312|HGNC:HGNC:18761};
GN Synonyms=PAT1 {ECO:0000303|PubMed:12527723};
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] (ISOFORM 1), FUNCTION, TRANSPORTER ACTIVITY, AND
RP SUBCELLULAR LOCATION.
RC TISSUE=Intestine;
RX PubMed=12809675; DOI=10.1016/s0888-7543(03)00099-5;
RA Boll M., Foltz M., Rubio-Aliaga I., Daniel H.;
RT "A cluster of proton/amino acid transporter genes in the human and mouse
RT genomes.";
RL Genomics 82:47-56(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TRANSPORTER ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBCELLULAR LOCATION.
RX PubMed=12527723; DOI=10.1113/jphysiol.2002.026500;
RA Chen Z., Fei Y.-J., Anderson C.M.H., Wake K.A., Miyauchi S., Huang W.,
RA Thwaites D.T., Ganapathy V.;
RT "Structure, function and immunolocalization of a proton-coupled amino acid
RT transporter (hPAT1) in the human intestinal cell line Caco-2.";
RL J. Physiol. (Lond.) 546:349-361(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), NUCLEOTIDE SEQUENCE [MRNA]
RP OF 164-476 (ISOFORM 1), AND ALTERNATIVE SPLICING.
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).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Endometrial tumor;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
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).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-356.
RC TISSUE=Testis;
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 [8]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC TISSUE=Placenta;
RX PubMed=17897319; DOI=10.1111/j.1600-0854.2007.00643.x;
RA Schroeder B., Wrocklage C., Pan C., Jaeger R., Koesters B., Schaefer H.,
RA Elsaesser H.-P., Mann M., Hasilik A.;
RT "Integral and associated lysosomal membrane proteins.";
RL Traffic 8:1676-1686(2007).
RN [9]
RP FUNCTION, TRANSPORTER ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP LOCATION, DISULFIDE BOND, TOPOLOGY MODEL, AND MUTAGENESIS OF CYS-180;
RP CYS-329 AND CYS-473.
RX PubMed=19549785; DOI=10.1074/jbc.m109.023713;
RA Dorn M., Weiwad M., Markwardt F., Laug L., Rudolph R., Brandsch M.,
RA Bosse-Doenecke E.;
RT "Identification of a disulfide bridge essential for transport function of
RT the human proton-coupled amino acid transporter hPAT1.";
RL J. Biol. Chem. 284:22123-22132(2009).
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:12809675,
CC PubMed:12527723, PubMed:19549785). May be involved in the efflux from
CC the lysosomal compartment of neutral amino acids resulting from
CC proteolysis (By similarity). May play a role in specifying sites for
CC exocytosis in neurons (By similarity). {ECO:0000250|UniProtKB:Q924A5,
CC ECO:0000269|PubMed:12527723, ECO:0000269|PubMed:12809675,
CC ECO:0000269|PubMed:19549785}.
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:12527723, ECO:0000269|PubMed:12809675,
CC ECO:0000269|PubMed:19549785};
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:12527723, ECO:0000269|PubMed:12809675};
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(+)(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:12527723, ECO:0000269|PubMed:12809675,
CC ECO:0000269|PubMed:19549785};
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: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:0000269|PubMed:12527723};
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=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:Q8K4D3};
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=2.3 mM for glycine {ECO:0000269|PubMed:12527723};
CC KM=11.4 mM for glycine (at pH 6.5) {ECO:0000269|PubMed:19549785};
CC pH dependence:
CC Optimum pH is 5.0-5.5. {ECO:0000269|PubMed:19549785};
CC -!- INTERACTION:
CC Q7Z2H8; P05067: APP; NbExp=3; IntAct=EBI-9978258, EBI-77613;
CC Q7Z2H8; A5PKU2: TUSC5; NbExp=3; IntAct=EBI-9978258, EBI-11988865;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12527723,
CC ECO:0000269|PubMed:12809675, ECO:0000269|PubMed:19549785}; Multi-pass
CC membrane protein {ECO:0000255}. Apical cell membrane
CC {ECO:0000269|PubMed:12527723}; Multi-pass membrane protein
CC {ECO:0000255}. Lysosome membrane {ECO:0000269|PubMed:17897319}; 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q7Z2H8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7Z2H8-3; Sequence=VSP_044392;
CC Name=3;
CC IsoId=Q7Z2H8-4; Sequence=VSP_044390, VSP_044391;
CC -!- SIMILARITY: Belongs to the amino acid/polyamine transporter 2 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB71435.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence={ECO:0000305};
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DR EMBL; AY162213; AAO11787.1; -; mRNA.
DR EMBL; AF516142; AAP47194.1; -; mRNA.
DR EMBL; AY227111; AAO37091.1; -; mRNA.
DR EMBL; AY227112; AAO37092.1; -; mRNA.
DR EMBL; AY227113; AAO37093.1; -; mRNA.
DR EMBL; BX537963; CAD97927.1; -; mRNA.
DR EMBL; AC034205; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC136437; AAI36438.1; -; mRNA.
DR EMBL; BC136438; AAI36439.1; -; mRNA.
DR EMBL; AK057340; BAB71435.1; ALT_SEQ; mRNA.
DR EMBL; BK001052; DAA01126.1; -; mRNA.
DR CCDS; CCDS4316.1; -. [Q7Z2H8-1]
DR CCDS; CCDS78073.1; -. [Q7Z2H8-4]
DR CCDS; CCDS83035.1; -. [Q7Z2H8-3]
DR RefSeq; NP_001295079.1; NM_001308150.1. [Q7Z2H8-3]
DR RefSeq; NP_001295080.1; NM_001308151.1. [Q7Z2H8-4]
DR RefSeq; NP_510968.2; NM_078483.3. [Q7Z2H8-1]
DR RefSeq; XP_005268443.1; XM_005268386.1. [Q7Z2H8-1]
DR RefSeq; XP_011535883.1; XM_011537581.1. [Q7Z2H8-1]
DR RefSeq; XP_011535885.1; XM_011537583.2. [Q7Z2H8-1]
DR RefSeq; XP_011535886.1; XM_011537584.2. [Q7Z2H8-1]
DR RefSeq; XP_011535887.1; XM_011537585.1. [Q7Z2H8-1]
DR RefSeq; XP_011535888.1; XM_011537586.2. [Q7Z2H8-1]
DR RefSeq; XP_011535889.1; XM_011537587.2. [Q7Z2H8-1]
DR RefSeq; XP_011535890.1; XM_011537588.2.
DR RefSeq; XP_011535891.1; XM_011537589.2. [Q7Z2H8-1]
DR RefSeq; XP_011535892.1; XM_011537590.1. [Q7Z2H8-1]
DR RefSeq; XP_011535893.1; XM_011537591.1. [Q7Z2H8-1]
DR RefSeq; XP_011535894.1; XM_011537592.2. [Q7Z2H8-1]
DR RefSeq; XP_016864705.1; XM_017009216.1. [Q7Z2H8-1]
DR RefSeq; XP_016864709.1; XM_017009220.1. [Q7Z2H8-4]
DR AlphaFoldDB; Q7Z2H8; -.
DR SMR; Q7Z2H8; -.
DR BioGRID; 128503; 6.
DR IntAct; Q7Z2H8; 10.
DR STRING; 9606.ENSP00000243389; -.
DR BindingDB; Q7Z2H8; -.
DR ChEMBL; CHEMBL1914279; -.
DR DrugBank; DB00160; Alanine.
DR DrugBank; DB02853; D-Proline.
DR DrugBank; DB06554; Gaboxadol.
DR DrugBank; DB02530; gamma-Aminobutyric acid.
DR DrugBank; DB00145; Glycine.
DR DrugBank; DB08847; Hydroxyproline.
DR DrugBank; DB00563; Methotrexate.
DR DrugBank; DB08849; Nipecotic acid.
DR DrugBank; DB08835; Spaglumic acid.
DR DrugBank; DB01956; Taurine.
DR DrugBank; DB01080; Vigabatrin.
DR GuidetoPHARMACOLOGY; 1161; -.
DR TCDB; 2.A.18.8.7; the amino acid/auxin permease (aaap) family.
DR GlyGen; Q7Z2H8; 3 sites.
DR iPTMnet; Q7Z2H8; -.
DR PhosphoSitePlus; Q7Z2H8; -.
DR BioMuta; SLC36A1; -.
DR DMDM; 51316800; -.
DR EPD; Q7Z2H8; -.
DR jPOST; Q7Z2H8; -.
DR MassIVE; Q7Z2H8; -.
DR MaxQB; Q7Z2H8; -.
DR PaxDb; Q7Z2H8; -.
DR PeptideAtlas; Q7Z2H8; -.
DR PRIDE; Q7Z2H8; -.
DR ProteomicsDB; 10285; -.
DR ProteomicsDB; 68959; -. [Q7Z2H8-1]
DR TopDownProteomics; Q7Z2H8-1; -. [Q7Z2H8-1]
DR Antibodypedia; 49166; 84 antibodies from 17 providers.
DR DNASU; 206358; -.
DR Ensembl; ENST00000243389.8; ENSP00000243389.3; ENSG00000123643.13. [Q7Z2H8-1]
DR Ensembl; ENST00000429484.6; ENSP00000395640.2; ENSG00000123643.13. [Q7Z2H8-4]
DR Ensembl; ENST00000520701.5; ENSP00000428140.1; ENSG00000123643.13. [Q7Z2H8-1]
DR Ensembl; ENST00000616007.4; ENSP00000480948.1; ENSG00000123643.13. [Q7Z2H8-3]
DR GeneID; 206358; -.
DR KEGG; hsa:206358; -.
DR MANE-Select; ENST00000243389.8; ENSP00000243389.3; NM_078483.4; NP_510968.2.
DR UCSC; uc003luc.4; human. [Q7Z2H8-1]
DR CTD; 206358; -.
DR DisGeNET; 206358; -.
DR GeneCards; SLC36A1; -.
DR HGNC; HGNC:18761; SLC36A1.
DR HPA; ENSG00000123643; Tissue enhanced (brain, parathyroid gland).
DR MIM; 606561; gene.
DR neXtProt; NX_Q7Z2H8; -.
DR OpenTargets; ENSG00000123643; -.
DR PharmGKB; PA134870308; -.
DR VEuPathDB; HostDB:ENSG00000123643; -.
DR eggNOG; KOG1304; Eukaryota.
DR GeneTree; ENSGT00940000156583; -.
DR HOGENOM; CLU_009646_0_2_1; -.
DR InParanoid; Q7Z2H8; -.
DR OMA; AMYVPNF; -.
DR OrthoDB; 464614at2759; -.
DR PhylomeDB; Q7Z2H8; -.
DR TreeFam; TF314873; -.
DR PathwayCommons; Q7Z2H8; -.
DR Reactome; R-HSA-352230; Amino acid transport across the plasma membrane.
DR Reactome; R-HSA-428559; Proton-coupled neutral amino acid transporters.
DR SignaLink; Q7Z2H8; -.
DR SIGNOR; Q7Z2H8; -.
DR BioGRID-ORCS; 206358; 11 hits in 1075 CRISPR screens.
DR ChiTaRS; SLC36A1; human.
DR GeneWiki; SLC36A1; -.
DR GenomeRNAi; 206358; -.
DR Pharos; Q7Z2H8; Tchem.
DR PRO; PR:Q7Z2H8; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q7Z2H8; protein.
DR Bgee; ENSG00000123643; Expressed in jejunal mucosa and 187 other tissues.
DR ExpressionAtlas; Q7Z2H8; baseline and differential.
DR Genevisible; Q7Z2H8; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:LIFEdb.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005765; C:lysosomal membrane; HDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0022858; F:alanine transmembrane transporter activity; IDA:ARUK-UCL.
DR GO; GO:0015171; F:amino acid transmembrane transporter activity; TAS:Reactome.
DR GO; GO:0005280; F:amino acid:proton symporter activity; IDA:UniProtKB.
DR GO; GO:0015187; F:glycine transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015180; F:L-alanine transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015179; F:L-amino acid transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015193; F:L-proline transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0005297; F:proline:proton symporter activity; IDA:UniProtKB.
DR GO; GO:0005368; F:taurine transmembrane transporter activity; IDA:ARUK-UCL.
DR GO; GO:0032328; P:alanine transport; IDA:ARUK-UCL.
DR GO; GO:0089718; P:amino acid import across plasma membrane; IDA:ARUK-UCL.
DR GO; GO:0003333; P:amino acid transmembrane transport; IBA:GO_Central.
DR GO; GO:0006865; P:amino acid transport; TAS:Reactome.
DR GO; GO:0015816; P:glycine transport; IBA:GO_Central.
DR GO; GO:0006811; P:ion transport; TAS:Reactome.
DR GO; GO:0015808; P:L-alanine transport; IBA:GO_Central.
DR GO; GO:0035524; P:proline transmembrane transport; IBA:GO_Central.
DR GO; GO:0015824; P:proline transport; IEA:Ensembl.
DR GO; GO:1902600; P:proton transmembrane transport; IBA:GO_Central.
DR GO; GO:0015734; P:taurine transport; IDA:ARUK-UCL.
DR InterPro; IPR013057; AA_transpt_TM.
DR Pfam; PF01490; Aa_trans; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Amino-acid transport; Cell membrane; Disulfide bond;
KW Glycoprotein; Lysosome; Membrane; Reference proteome; Symport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..476
FT /note="Proton-coupled amino acid transporter 1"
FT /id="PRO_0000093825"
FT TOPO_DOM 1..51
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 52..72
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 73..78
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 79..99
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 100..141
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 142..162
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 163..190
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 191..211
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 212..215
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 216..236
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 237..257
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 258..278
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 279..289
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 290..310
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 311..342
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 343..363
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 364..372
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 373..393
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 394..397
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 398..418
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 419..439
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 440..460
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 461..476
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 174
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 183
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 470
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 180..329
FT /evidence="ECO:0000269|PubMed:19549785"
FT VAR_SEQ 242..243
FT /note="RI -> IL (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15058382"
FT /id="VSP_044390"
FT VAR_SEQ 244..476
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15058382"
FT /id="VSP_044391"
FT VAR_SEQ 387..476
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15058382"
FT /id="VSP_044392"
FT VARIANT 362
FT /note="F -> L (in dbSNP:rs9687945)"
FT /id="VAR_048122"
FT MUTAGEN 180
FT /note="C->A,S: Loss amino acid:proton symporter activity.
FT No effect on localization to the plasma membrane."
FT /evidence="ECO:0000269|PubMed:19549785"
FT MUTAGEN 329
FT /note="C->A,S: Loss amino acid:proton symporter activity.
FT No effect on localization to the plasma membrane."
FT /evidence="ECO:0000269|PubMed:19549785"
FT MUTAGEN 473
FT /note="C->A,S: No effect on amino acid:proton symporter
FT activity. No effect on localization to the plasma
FT membrane."
FT /evidence="ECO:0000269|PubMed:19549785"
FT CONFLICT 72
FT /note="V -> A (in Ref. 7; BAB71435)"
FT /evidence="ECO:0000305"
FT CONFLICT 394
FT /note="P -> L (in Ref. 2; AAP47194)"
FT /evidence="ECO:0000305"
FT CONFLICT 446
FT /note="V -> G (in Ref. 2; AAP47194)"
FT /evidence="ECO:0000305"
FT CONFLICT 449..450
FT /note="VV -> GG (in Ref. 2; AAP47194)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 476 AA; 53076 MW; 628AE7FC7A6559F0 CRC64;
MSTQRLRNED YHDYSSTDVS PEESPSEGLN NLSSPGSYQR FGQSNSTTWF QTLIHLLKGN
IGTGLLGLPL AVKNAGIVMG PISLLIIGIV AVHCMGILVK CAHHFCRRLN KSFVDYGDTV
MYGLESSPCS WLRNHAHWGR RVVDFFLIVT QLGFCCVYFV FLADNFKQVI EAANGTTNNC
HNNETVILTP TMDSRLYMLS FLPFLVLLVF IRNLRALSIF SLLANITMLV SLVMIYQFIV
QRIPDPSHLP LVAPWKTYPL FFGTAIFSFE GIGMVLPLEN KMKDPRKFPL ILYLGMVIVT
ILYISLGCLG YLQFGANIQG SITLNLPNCW LYQSVKLLYS IGIFFTYALQ FYVPAEIIIP
FFVSRAPEHC ELVVDLFVRT VLVCLTCILA ILIPRLDLVI SLVGSVSSSA LALIIPPLLE
VTTFYSEGMS PLTIFKDALI SILGFVGFVV GTYEALYELI QPSNAPIFIN STCAFI
