S15A1_HUMAN
ID S15A1_HUMAN Reviewed; 708 AA.
AC P46059; Q5VW82;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Solute carrier family 15 member 1 {ECO:0000305};
DE AltName: Full=Intestinal H(+)/peptide cotransporter {ECO:0000303|PubMed:7896779};
DE AltName: Full=Oligopeptide transporter, small intestine isoform {ECO:0000303|PubMed:7896779};
DE AltName: Full=Peptide transporter 1 {ECO:0000303|PubMed:7896779};
GN Name=SLC15A1 {ECO:0000312|HGNC:HGNC:10920};
GN Synonyms=PEPT1 {ECO:0000303|PubMed:7896779};
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], FUNCTION, AND TRANSPORTER ACTIVITY.
RC TISSUE=Intestine;
RX PubMed=7896779; DOI=10.1074/jbc.270.12.6456;
RA Liang R., Fei Y.-J., Prasad P.D., Ramamoorthy S., Han H., Yang-Feng T.L.,
RA Hediger M.A., Ganapathy V., Leibach F.H.;
RT "Human intestinal H+/peptide cotransporter. Cloning, functional expression,
RT and chromosomal localization.";
RL J. Biol. Chem. 270:6456-6463(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [4]
RP FUNCTION, AND TRANSPORTER ACTIVITY.
RX PubMed=18367661; DOI=10.1152/ajprenal.00030.2008;
RA Sala-Rabanal M., Loo D.D., Hirayama B.A., Wright E.M.;
RT "Molecular mechanism of dipeptide and drug transport by the human renal
RT H+/oligopeptide cotransporter hPEPT2.";
RL Am. J. Physiol. 294:F1422-F1432(2008).
RN [5]
RP FUNCTION, TRANSPORTER ACTIVITY, AND MUTAGENESIS OF TYR-588; GLY-594 AND
RP GLU-595.
RX PubMed=19685173; DOI=10.1007/s11095-009-9952-9;
RA Xu L., Haworth I.S., Kulkarni A.A., Bolger M.B., Davies D.L.;
RT "Mutagenesis and cysteine scanning of transmembrane domain 10 of the human
RT dipeptide transporter.";
RL Pharm. Res. 26:2358-2366(2009).
RN [6]
RP VARIANTS ASN-117 AND ALA-419.
RX PubMed=12436193; DOI=10.1007/s100380200088;
RA Saito S., Iida A., Sekine A., Ogawa C., Kawauchi S., Higuchi S.,
RA Nakamura Y.;
RT "Catalog of 238 variations among six human genes encoding solute carriers
RT (hSLCs) in the Japanese population.";
RL J. Hum. Genet. 47:576-584(2002).
RN [7]
RP VARIANTS ILE-21; TYR-28; ASN-117; ARG-117; MET-122; ALA-419; ILE-450;
RP ASN-451 AND SER-537.
RX PubMed=16258023; DOI=10.1124/jpet.105.094615;
RA Anderle P., Nielsen C.U., Pinsonneault J., Krog P.L., Brodin B., Sadee W.;
RT "Genetic variants of the human dipeptide transporter PEPT1.";
RL J. Pharmacol. Exp. Ther. 316:636-646(2006).
CC -!- FUNCTION: Proton-coupled amino-acid transporter that transports
CC oligopeptides of 2 to 4 amino acids with a preference for dipeptides
CC (PubMed:7896779, PubMed:18367661, PubMed:19685173). Primarily
CC responsible for the absorption of dietary di- and tripeptides from the
CC small intestinal lumen (By similarity). {ECO:0000250|UniProtKB:P36836,
CC ECO:0000269|PubMed:18367661, ECO:0000269|PubMed:19685173,
CC ECO:0000269|PubMed:7896779}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a dipeptide(out) + H(+)(out) = a dipeptide(in) + H(+)(in);
CC Xref=Rhea:RHEA:64392, ChEBI:CHEBI:15378, ChEBI:CHEBI:90799;
CC Evidence={ECO:0000269|PubMed:18367661, ECO:0000269|PubMed:19685173,
CC ECO:0000269|PubMed:7896779};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64393;
CC Evidence={ECO:0000269|PubMed:18367661, ECO:0000269|PubMed:19685173,
CC ECO:0000269|PubMed:7896779};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an L-amino acid tripeptide(out) + H(+)(out) = an L-amino acid
CC tripeptide(in) + H(+)(in); Xref=Rhea:RHEA:64400, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:155837; Evidence={ECO:0000269|PubMed:7896779};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64401;
CC Evidence={ECO:0000269|PubMed:7896779};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glycyl-sarcosine(out) + H(+)(out) = glycyl-sarcosine(in) +
CC H(+)(in); Xref=Rhea:RHEA:64396, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:155838; Evidence={ECO:0000269|PubMed:18367661,
CC ECO:0000269|PubMed:7896779};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64397;
CC Evidence={ECO:0000269|PubMed:18367661, ECO:0000269|PubMed:7896779};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+)(out) + L-alanyl-L-proline(out) = H(+)(in) + L-alanyl-L-
CC proline(in); Xref=Rhea:RHEA:64420, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:155848; Evidence={ECO:0000269|PubMed:7896779};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64421;
CC Evidence={ECO:0000269|PubMed:7896779};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+)(out) + L-leucyl-L-proline(out) = H(+)(in) + L-leucyl-L-
CC proline(in); Xref=Rhea:RHEA:64424, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:155847; Evidence={ECO:0000269|PubMed:7896779};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64425;
CC Evidence={ECO:0000269|PubMed:7896779};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glycyl-L-proline(out) + H(+)(out) = glycyl-L-proline(in) +
CC H(+)(in); Xref=Rhea:RHEA:64428, ChEBI:CHEBI:15378, ChEBI:CHEBI:73779;
CC Evidence={ECO:0000269|PubMed:7896779};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64429;
CC Evidence={ECO:0000269|PubMed:7896779};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+)(out) + L-alanyl-L-prolylglycine(out) = H(+)(in) + L-
CC alanyl-L-prolylglycine(in); Xref=Rhea:RHEA:64432, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:155849; Evidence={ECO:0000269|PubMed:7896779};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64433;
CC Evidence={ECO:0000269|PubMed:7896779};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glycylglycyl-L-isoleucine(out) + H(+)(out) = glycylglycyl-L-
CC isoleucine(in) + H(+)(in); Xref=Rhea:RHEA:64436, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:155850; Evidence={ECO:0000269|PubMed:7896779};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64437;
CC Evidence={ECO:0000269|PubMed:7896779};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glycylglycyl-L-proline(out) + H(+)(out) = glycylglycyl-L-
CC proline(in) + H(+)(in); Xref=Rhea:RHEA:64440, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:155851; Evidence={ECO:0000269|PubMed:7896779};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64441;
CC Evidence={ECO:0000269|PubMed:7896779};
CC -!- SUBUNIT: Interacts (via extracellular domain region) with trypsin.
CC {ECO:0000250|UniProtKB:Q9JIP7}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q9JIP7}; Multi-
CC pass membrane protein {ECO:0000255}.
CC -!- DOMAIN: The extracellular domain (ECD) region specifically binds
CC trypsin. {ECO:0000250|UniProtKB:Q9JIP7}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Proton-
CC dependent oligopeptide transporter (POT/PTR) (TC 2.A.17) family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U13173; AAB61693.1; -; mRNA.
DR EMBL; U21936; AAA63797.1; -; mRNA.
DR EMBL; AL391670; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL353574; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC096328; AAH96328.1; -; mRNA.
DR EMBL; BC096329; AAH96329.1; -; mRNA.
DR CCDS; CCDS9489.1; -.
DR PIR; A56163; A56163.
DR RefSeq; NP_005064.1; NM_005073.3.
DR PDB; 7PMW; EM; 4.10 A; A=1-708.
DR PDB; 7PMX; EM; 3.50 A; A=1-708.
DR PDB; 7PN1; EM; 3.90 A; A=1-708.
DR PDBsum; 7PMW; -.
DR PDBsum; 7PMX; -.
DR PDBsum; 7PN1; -.
DR AlphaFoldDB; P46059; -.
DR SMR; P46059; -.
DR BioGRID; 112452; 81.
DR IntAct; P46059; 64.
DR STRING; 9606.ENSP00000365686; -.
DR BindingDB; P46059; -.
DR ChEMBL; CHEMBL4605; -.
DR DrugBank; DB00855; Aminolevulinic acid.
DR DrugBank; DB01060; Amoxicillin.
DR DrugBank; DB00415; Ampicillin.
DR DrugBank; DB08795; Azidocillin.
DR DrugBank; DB00542; Benazepril.
DR DrugBank; DB03793; Benzoic acid.
DR DrugBank; DB01053; Benzylpenicillin.
DR DrugBank; DB01197; Captopril.
DR DrugBank; DB00833; Cefaclor.
DR DrugBank; DB01140; Cefadroxil.
DR DrugBank; DB00456; Cefalotin.
DR DrugBank; DB00535; Cefdinir.
DR DrugBank; DB01413; Cefepime.
DR DrugBank; DB00671; Cefixime.
DR DrugBank; DB00274; Cefmetazole.
DR DrugBank; DB00493; Cefotaxime.
DR DrugBank; DB01333; Cefradine.
DR DrugBank; DB01415; Ceftibuten.
DR DrugBank; DB01332; Ceftizoxime.
DR DrugBank; DB01212; Ceftriaxone.
DR DrugBank; DB01112; Cefuroxime.
DR DrugBank; DB00567; Cephalexin.
DR DrugBank; DB00672; Chlorpropamide.
DR DrugBank; DB01340; Cilazapril.
DR DrugBank; DB01147; Cloxacillin.
DR DrugBank; DB01000; Cyclacillin.
DR DrugBank; DB09213; Dexibuprofen.
DR DrugBank; DB00485; Dicloxacillin.
DR DrugBank; DB00584; Enalapril.
DR DrugBank; DB01095; Fluvastatin.
DR DrugBank; DB00492; Fosinopril.
DR DrugBank; DB01016; Glyburide.
DR DrugBank; DB01235; Levodopa.
DR DrugBank; DB01255; Lisdexamfetamine.
DR DrugBank; DB00722; Lisinopril.
DR DrugBank; DB00447; Loracarbef.
DR DrugBank; DB00563; Methotrexate.
DR DrugBank; DB00968; Methyldopa.
DR DrugBank; DB00211; Midodrine.
DR DrugBank; DB00691; Moexipril.
DR DrugBank; DB00731; Nateglinide.
DR DrugBank; DB00198; Oseltamivir.
DR DrugBank; DB00713; Oxacillin.
DR DrugBank; DB00790; Perindopril.
DR DrugBank; DB00417; Phenoxymethylpenicillin.
DR DrugBank; DB00881; Quinapril.
DR DrugBank; DB00178; Ramipril.
DR DrugBank; DB01348; Spirapril.
DR DrugBank; DB01956; Taurine.
DR DrugBank; DB08836; Temocapril.
DR DrugBank; DB01124; Tolbutamide.
DR DrugBank; DB00519; Trandolapril.
DR DrugBank; DB03424; Ubenimex.
DR DrugBank; DB00577; Valaciclovir.
DR DrugBank; DB01610; Valganciclovir.
DR DrugCentral; P46059; -.
DR GuidetoPHARMACOLOGY; 984; -.
DR TCDB; 2.A.17.4.9; the proton-dependent oligopeptide transporter (pot/ptr) family.
DR GlyGen; P46059; 7 sites.
DR iPTMnet; P46059; -.
DR PhosphoSitePlus; P46059; -.
DR BioMuta; SLC15A1; -.
DR DMDM; 1172435; -.
DR MassIVE; P46059; -.
DR PaxDb; P46059; -.
DR PeptideAtlas; P46059; -.
DR PRIDE; P46059; -.
DR ProteomicsDB; 55711; -.
DR Antibodypedia; 10820; 230 antibodies from 31 providers.
DR DNASU; 6564; -.
DR Ensembl; ENST00000376503.10; ENSP00000365686.4; ENSG00000088386.17.
DR GeneID; 6564; -.
DR KEGG; hsa:6564; -.
DR MANE-Select; ENST00000376503.10; ENSP00000365686.4; NM_005073.4; NP_005064.1.
DR UCSC; uc001vno.4; human.
DR CTD; 6564; -.
DR DisGeNET; 6564; -.
DR GeneCards; SLC15A1; -.
DR HGNC; HGNC:10920; SLC15A1.
DR HPA; ENSG00000088386; Tissue enriched (intestine).
DR MIM; 600544; gene.
DR neXtProt; NX_P46059; -.
DR OpenTargets; ENSG00000088386; -.
DR PharmGKB; PA323; -.
DR VEuPathDB; HostDB:ENSG00000088386; -.
DR eggNOG; KOG1237; Eukaryota.
DR GeneTree; ENSGT00940000155995; -.
DR HOGENOM; CLU_004790_3_0_1; -.
DR InParanoid; P46059; -.
DR OMA; YNASEYQ; -.
DR OrthoDB; 925637at2759; -.
DR PhylomeDB; P46059; -.
DR TreeFam; TF330897; -.
DR PathwayCommons; P46059; -.
DR Reactome; R-HSA-427975; Proton/oligopeptide cotransporters.
DR SignaLink; P46059; -.
DR BioGRID-ORCS; 6564; 11 hits in 1062 CRISPR screens.
DR ChiTaRS; SLC15A1; human.
DR GeneWiki; Peptide_transporter_1; -.
DR GenomeRNAi; 6564; -.
DR Pharos; P46059; Tchem.
DR PRO; PR:P46059; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; P46059; protein.
DR Bgee; ENSG00000088386; Expressed in duodenum and 105 other tissues.
DR ExpressionAtlas; P46059; baseline and differential.
DR Genevisible; P46059; HS.
DR GO; GO:0016324; C:apical plasma membrane; ISS:ARUK-UCL.
DR GO; GO:0005903; C:brush border; IEA:Ensembl.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:ARUK-UCL.
DR GO; GO:0089717; C:spanning component of membrane; ISS:ARUK-UCL.
DR GO; GO:0071916; F:dipeptide transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0015333; F:peptide:proton symporter activity; IDA:UniProtKB.
DR GO; GO:0005427; F:proton-dependent oligopeptide secondary active transmembrane transporter activity; IEA:Ensembl.
DR GO; GO:0042937; F:tripeptide transmembrane transporter activity; ISS:ARUK-UCL.
DR GO; GO:0140206; P:dipeptide import across plasma membrane; IDA:UniProtKB.
DR GO; GO:0006811; P:ion transport; TAS:Reactome.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0140207; P:tripeptide import across plasma membrane; ISS:ARUK-UCL.
DR Gene3D; 1.20.1250.20; -; 2.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR004768; Oligopep_transport.
DR InterPro; IPR000109; POT_fam.
DR InterPro; IPR018456; PTR2_symporter_CS.
DR PANTHER; PTHR11654; PTHR11654; 1.
DR Pfam; PF00854; PTR2; 2.
DR SUPFAM; SSF103473; SSF103473; 1.
DR TIGRFAMs; TIGR00926; 2A1704; 1.
DR PROSITE; PS01022; PTR2_1; 1.
DR PROSITE; PS01023; PTR2_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Glycoprotein; Membrane; Peptide transport; Protein transport;
KW Reference proteome; Symport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..708
FT /note="Solute carrier family 15 member 1"
FT /id="PRO_0000064304"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 22..53
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 54..74
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 75..82
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 83..103
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 104..118
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 119..139
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 140..161
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 162..182
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 183..198
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 199..219
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 220..276
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 277..297
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 298..327
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 328..348
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 349..361
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 362..382
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 383..584
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 585..605
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 606..619
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 620..640
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 641..645
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 646..666
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 667..708
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 383..584
FT /note="Extracellular domain (ECD)"
FT /evidence="ECO:0000250|UniProtKB:Q9JIP7"
FT CARBOHYD 50
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 404
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 408
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 439
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 509
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 514
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 562
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 21
FT /note="V -> I (in dbSNP:rs8187818)"
FT /evidence="ECO:0000269|PubMed:16258023"
FT /id="VAR_029321"
FT VARIANT 28
FT /note="F -> Y (in dbSNP:rs8187817)"
FT /evidence="ECO:0000269|PubMed:16258023"
FT /id="VAR_029322"
FT VARIANT 117
FT /note="S -> N (in dbSNP:rs2297322)"
FT /evidence="ECO:0000269|PubMed:12436193,
FT ECO:0000269|PubMed:16258023"
FT /id="VAR_022147"
FT VARIANT 117
FT /note="S -> R (in dbSNP:rs8187821)"
FT /evidence="ECO:0000269|PubMed:16258023"
FT /id="VAR_029323"
FT VARIANT 122
FT /note="V -> M (in dbSNP:rs8187820)"
FT /evidence="ECO:0000269|PubMed:16258023"
FT /id="VAR_020456"
FT VARIANT 419
FT /note="G -> A (in dbSNP:rs4646227)"
FT /evidence="ECO:0000269|PubMed:12436193,
FT ECO:0000269|PubMed:16258023"
FT /id="VAR_020457"
FT VARIANT 450
FT /note="V -> I (in dbSNP:rs2274828)"
FT /evidence="ECO:0000269|PubMed:16258023"
FT /id="VAR_022148"
FT VARIANT 451
FT /note="T -> N (in dbSNP:rs8187838)"
FT /evidence="ECO:0000269|PubMed:16258023"
FT /id="VAR_020458"
FT VARIANT 459
FT /note="R -> C (in dbSNP:rs2274827)"
FT /id="VAR_022149"
FT VARIANT 537
FT /note="P -> S (in dbSNP:rs8187830)"
FT /evidence="ECO:0000269|PubMed:16258023"
FT /id="VAR_029324"
FT MUTAGEN 588
FT /note="Y->C: Reduced transmembrane transport of
FT dipeptides."
FT /evidence="ECO:0000269|PubMed:19685173"
FT MUTAGEN 594
FT /note="G->A: Does not affect transmembrane transport of
FT dipeptides."
FT /evidence="ECO:0000269|PubMed:19685173"
FT MUTAGEN 594
FT /note="G->C: Nearly abolished transmembrane transport of
FT dipeptides."
FT /evidence="ECO:0000269|PubMed:19685173"
FT MUTAGEN 594
FT /note="G->V: Abolished transmembrane transport of
FT dipeptides."
FT /evidence="ECO:0000269|PubMed:19685173"
FT MUTAGEN 595
FT /note="E->C: Nearly abolished transmembrane transport of
FT dipeptides."
FT /evidence="ECO:0000269|PubMed:19685173"
FT MUTAGEN 595
FT /note="E->D: Does not affect transmembrane transport of
FT dipeptides."
FT /evidence="ECO:0000269|PubMed:19685173"
FT MUTAGEN 595
FT /note="E->K,R: Abolished transmembrane transport of
FT dipeptides."
FT /evidence="ECO:0000269|PubMed:19685173"
FT HELIX 13..44
FT /evidence="ECO:0007829|PDB:7PMX"
FT HELIX 51..55
FT /evidence="ECO:0007829|PDB:7PMX"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:7PMX"
FT TURN 59..61
FT /evidence="ECO:0007829|PDB:7PMX"
FT HELIX 62..65
FT /evidence="ECO:0007829|PDB:7PMX"
FT HELIX 67..74
FT /evidence="ECO:0007829|PDB:7PMX"
FT TURN 75..78
FT /evidence="ECO:0007829|PDB:7PMX"
FT HELIX 79..107
FT /evidence="ECO:0007829|PDB:7PMX"
FT HELIX 118..148
FT /evidence="ECO:0007829|PDB:7PMX"
FT HELIX 156..184
FT /evidence="ECO:0007829|PDB:7PMX"
FT HELIX 198..218
FT /evidence="ECO:0007829|PDB:7PMX"
FT TURN 219..222
FT /evidence="ECO:0007829|PDB:7PMX"
FT HELIX 232..248
FT /evidence="ECO:0007829|PDB:7PMX"
FT HELIX 262..265
FT /evidence="ECO:0007829|PDB:7PMX"
FT TURN 266..268
FT /evidence="ECO:0007829|PDB:7PMX"
FT HELIX 271..285
FT /evidence="ECO:0007829|PDB:7PMX"
FT HELIX 290..292
FT /evidence="ECO:0007829|PDB:7PMX"
FT HELIX 293..297
FT /evidence="ECO:0007829|PDB:7PMX"
FT HELIX 299..310
FT /evidence="ECO:0007829|PDB:7PMX"
FT HELIX 322..326
FT /evidence="ECO:0007829|PDB:7PMX"
FT HELIX 327..342
FT /evidence="ECO:0007829|PDB:7PMX"
FT HELIX 344..350
FT /evidence="ECO:0007829|PDB:7PMX"
FT HELIX 357..383
FT /evidence="ECO:0007829|PDB:7PMX"
FT STRAND 394..401
FT /evidence="ECO:0007829|PDB:7PMX"
FT STRAND 403..405
FT /evidence="ECO:0007829|PDB:7PMX"
FT STRAND 407..411
FT /evidence="ECO:0007829|PDB:7PMX"
FT STRAND 414..418
FT /evidence="ECO:0007829|PDB:7PMX"
FT STRAND 428..431
FT /evidence="ECO:0007829|PDB:7PMX"
FT HELIX 432..434
FT /evidence="ECO:0007829|PDB:7PMX"
FT STRAND 439..441
FT /evidence="ECO:0007829|PDB:7PMX"
FT STRAND 458..466
FT /evidence="ECO:0007829|PDB:7PMX"
FT STRAND 469..474
FT /evidence="ECO:0007829|PDB:7PMX"
FT HELIX 482..484
FT /evidence="ECO:0007829|PDB:7PMX"
FT STRAND 486..492
FT /evidence="ECO:0007829|PDB:7PMX"
FT STRAND 494..496
FT /evidence="ECO:0007829|PDB:7PMX"
FT STRAND 498..502
FT /evidence="ECO:0007829|PDB:7PMX"
FT STRAND 505..510
FT /evidence="ECO:0007829|PDB:7PMX"
FT STRAND 519..521
FT /evidence="ECO:0007829|PDB:7PMX"
FT STRAND 527..535
FT /evidence="ECO:0007829|PDB:7PMX"
FT STRAND 542..544
FT /evidence="ECO:0007829|PDB:7PMX"
FT STRAND 553..560
FT /evidence="ECO:0007829|PDB:7PMX"
FT STRAND 566..574
FT /evidence="ECO:0007829|PDB:7PMX"
FT HELIX 581..584
FT /evidence="ECO:0007829|PDB:7PMX"
FT HELIX 585..609
FT /evidence="ECO:0007829|PDB:7PMX"
FT HELIX 615..636
FT /evidence="ECO:0007829|PDB:7PMX"
FT HELIX 644..650
FT /evidence="ECO:0007829|PDB:7PMX"
FT TURN 651..655
FT /evidence="ECO:0007829|PDB:7PMX"
FT HELIX 656..667
FT /evidence="ECO:0007829|PDB:7PMX"
FT HELIX 671..673
FT /evidence="ECO:0007829|PDB:7PMX"
FT HELIX 676..679
FT /evidence="ECO:0007829|PDB:7PMX"
FT HELIX 680..682
FT /evidence="ECO:0007829|PDB:7PMX"
SQ SEQUENCE 708 AA; 78806 MW; A75475789177A907 CRC64;
MGMSKSHSFF GYPLSIFFIV VNEFCERFSY YGMRAILILY FTNFISWDDN LSTAIYHTFV
ALCYLTPILG ALIADSWLGK FKTIVSLSIV YTIGQAVTSV SSINDLTDHN HDGTPDSLPV
HVVLSLIGLA LIALGTGGIK PCVSAFGGDQ FEEGQEKQRN RFFSIFYLAI NAGSLLSTII
TPMLRVQQCG IHSKQACYPL AFGVPAALMA VALIVFVLGS GMYKKFKPQG NIMGKVAKCI
GFAIKNRFRH RSKAFPKREH WLDWAKEKYD ERLISQIKMV TRVMFLYIPL PMFWALFDQQ
GSRWTLQATT MSGKIGALEI QPDQMQTVNA ILIVIMVPIF DAVLYPLIAK CGFNFTSLKK
MAVGMVLASM AFVVAAIVQV EIDKTLPVFP KGNEVQIKVL NIGNNTMNIS LPGEMVTLGP
MSQTNAFMTF DVNKLTRINI SSPGSPVTAV TDDFKQGQRH TLLVWAPNHY QVVKDGLNQK
PEKGENGIRF VNTFNELITI TMSGKVYANI SSYNASTYQF FPSGIKGFTI SSTEIPPQCQ
PNFNTFYLEF GSAYTYIVQR KNDSCPEVKV FEDISANTVN MALQIPQYFL LTCGEVVFSV
TGLEFSYSQA PSNMKSVLQA GWLLTVAVGN IIVLIVAGAG QFSKQWAEYI LFAALLLVVC
VIFAIMARFY TYINPAEIEA QFDEDEKKNR LEKSNPYFMS GANSQKQM
