S15A1_RAT
ID S15A1_RAT Reviewed; 710 AA.
AC P51574; Q5EML1;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Solute carrier family 15 member 1;
DE AltName: Full=Intestinal H(+)/peptide cotransporter {ECO:0000303|PubMed:8605246};
DE AltName: Full=Oligopeptide transporter, small intestine isoform {ECO:0000303|PubMed:8605246};
DE AltName: Full=Peptide transporter 1 {ECO:0000303|PubMed:8605246};
DE AltName: Full=Proton-coupled dipeptide cotransporter;
GN Name=Slc15a1; Synonyms=Pept1 {ECO:0000303|PubMed:8605246};
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] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Small intestine;
RX PubMed=8605246; DOI=10.1016/0167-4781(95)00208-1;
RA Miyamoto K., Shiraga T., Morita K., Yamamoto H., Haga H., Taketani Y.,
RA Tamai I., Sai Y., Tsuji A., Takeda E.;
RT "Sequence, tissue distribution and developmental changes in rat intestinal
RT oligopeptide transporter.";
RL Biochim. Biophys. Acta 1305:34-38(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Kidney;
RX PubMed=8531138;
RA Saito H., Okuda M., Terada T., Sasaki S., Inui K.;
RT "Cloning and characterization of a rat H+/peptide cotransporter mediating
RT absorption of beta-lactam antibiotics in the intestine and kidney.";
RL J. Pharmacol. Exp. Ther. 275:1631-1637(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ALTERNATIVE PROMOTER USAGE,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=15684415; DOI=10.1074/jbc.m414587200;
RA Gaildrat P., Moller M., Mukda S., Humphries A., Carter D.A., Ganapathy V.,
RA Klein D.C.;
RT "A novel pineal-specific product of the oligopeptide transporter PepT1
RT gene: circadian expression mediated by cAMP activation of an intronic
RT promoter.";
RL J. Biol. Chem. 280:16851-16860(2005).
RN [4]
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=19103603; DOI=10.1074/jbc.m808394200;
RA Bailey M.J., Coon S.L., Carter D.A., Humphries A., Kim J.S., Shi Q.,
RA Gaildrat P., Morin F., Ganguly S., Hogenesch J.B., Weller J.L., Rath M.F.,
RA Moller M., Baler R., Sugden D., Rangel Z.G., Munson P.J., Klein D.C.;
RT "Night/day changes in pineal expression of >600 genes: central role of
RT adrenergic/cAMP signaling.";
RL J. Biol. Chem. 284:7606-7622(2009).
CC -!- FUNCTION: Proton-coupled amino-acid transporter that transports
CC oligopeptides of 2 to 4 amino acids with a preference for dipeptides.
CC Primarily responsible for the absorption of dietary di- and tripeptides
CC from the small intestinal lumen. {ECO:0000250|UniProtKB:P36836}.
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:0000250|UniProtKB:P46059};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64393;
CC Evidence={ECO:0000250|UniProtKB:P46059};
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:0000250|UniProtKB:P46059};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64401;
CC Evidence={ECO:0000250|UniProtKB:P46059};
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:0000250|UniProtKB:P46059};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64397;
CC Evidence={ECO:0000250|UniProtKB:P46059};
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:0000250|UniProtKB:P46059};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64421;
CC Evidence={ECO:0000250|UniProtKB:P46059};
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:0000250|UniProtKB:P46059};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64425;
CC Evidence={ECO:0000250|UniProtKB:P46059};
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:0000250|UniProtKB:P46059};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64429;
CC Evidence={ECO:0000250|UniProtKB:P46059};
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:0000250|UniProtKB:P46059};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64433;
CC Evidence={ECO:0000250|UniProtKB:P46059};
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:0000250|UniProtKB:P46059};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64437;
CC Evidence={ECO:0000250|UniProtKB:P46059};
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:0000250|UniProtKB:P46059};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64441;
CC Evidence={ECO:0000250|UniProtKB:P46059};
CC -!- SUBUNIT: Interacts (via extracellular domain region) with trypsin.
CC {ECO:0000250|UniProtKB:Q9JIP7}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:15684415}; Multi-
CC pass membrane protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage; Named isoforms=2;
CC Name=1;
CC IsoId=P51574-1; Sequence=Displayed;
CC Name=2; Synonyms=pgPepT1;
CC IsoId=P51574-2; Sequence=VSP_042081, VSP_042082;
CC -!- TISSUE SPECIFICITY: [Isoform 1]: Highly expressed in small intestine.
CC {ECO:0000269|PubMed:8531138, ECO:0000269|PubMed:8605246}.
CC -!- TISSUE SPECIFICITY: [Isoform 2]: Expression is restricted to
CC pinealocytes. {ECO:0000269|PubMed:15684415,
CC ECO:0000269|PubMed:19103603}.
CC -!- INDUCTION: [Isoform 2]: Exhibits night/day variations with close to
CC 100-fold increased expression at night (PubMed:15684415,
CC PubMed:19103603). Up-regulation is due to a large degree to the release
CC of norepinephrine from nerve terminals in the pineal gland and cAMP
CC signaling pathway, which activates an alternative promoter within
CC intron 20 resulting in isoform 2 production (PubMed:15684415,
CC PubMed:19103603). Levels rapidly decrease after exposure to daylight
CC and become undetectable at midday and late afternoon (PubMed:15684415,
CC PubMed:19103603). {ECO:0000269|PubMed:15684415,
CC ECO:0000269|PubMed:19103603}.
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}.
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DR EMBL; D50664; BAA09318.1; -; mRNA.
DR EMBL; D50306; BAA08844.1; -; mRNA.
DR EMBL; AY860424; AAW80389.1; -; mRNA.
DR PIR; S72497; S72497.
DR RefSeq; NP_001073307.1; NM_001079838.1. [P51574-2]
DR RefSeq; NP_476462.1; NM_057121.1. [P51574-1]
DR AlphaFoldDB; P51574; -.
DR SMR; P51574; -.
DR STRING; 10116.ENSRNOP00000015890; -.
DR BindingDB; P51574; -.
DR ChEMBL; CHEMBL2073691; -.
DR TCDB; 2.A.17.4.1; the proton-dependent oligopeptide transporter (pot/ptr) family.
DR GlyGen; P51574; 5 sites.
DR PaxDb; P51574; -.
DR PRIDE; P51574; -.
DR GeneID; 117261; -.
DR KEGG; rno:117261; -.
DR CTD; 6564; -.
DR RGD; 621736; Slc15a1.
DR eggNOG; KOG1237; Eukaryota.
DR InParanoid; P51574; -.
DR OrthoDB; 365203at2759; -.
DR PhylomeDB; P51574; -.
DR Reactome; R-RNO-427975; Proton/oligopeptide cotransporters.
DR PRO; PR:P51574; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0016324; C:apical plasma membrane; IDA:ARUK-UCL.
DR GO; GO:0005903; C:brush border; ISO:RGD.
DR GO; GO:0016021; C:integral component of membrane; ISO:RGD.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0016248; F:channel inhibitor activity; IDA:RGD.
DR GO; GO:0071916; F:dipeptide transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0015333; F:peptide:proton symporter activity; ISS:UniProtKB.
DR GO; GO:0005427; F:proton-dependent oligopeptide secondary active transmembrane transporter activity; ISO:RGD.
DR GO; GO:0140206; P:dipeptide import across plasma membrane; ISS:UniProtKB.
DR GO; GO:0051956; P:negative regulation of amino acid transport; IDA:RGD.
DR GO; GO:0006857; P:oligopeptide transport; ISO:RGD.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
KW Alternative promoter usage; Glycoprotein; Membrane; Peptide transport;
KW Protein transport; Reference proteome; Symport; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..710
FT /note="Solute carrier family 15 member 1"
FT /id="PRO_0000064307"
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..586
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 587..607
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 608..621
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 622..642
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 643..647
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 648..668
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 669..710
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 383..586
FT /note="Extracellular domain (ECD)"
FT /evidence="ECO:0000250|UniProtKB:Q9JIP7"
FT REGION 687..710
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 415
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 510
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 532
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 539
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..560
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15684415"
FT /id="VSP_042081"
FT VAR_SEQ 561..563
FT /note="SRA -> MVQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15684415"
FT /id="VSP_042082"
FT CONFLICT 241
FT /note="R -> G (in Ref. 2; BAA08844)"
FT /evidence="ECO:0000305"
FT CONFLICT 259
FT /note="N -> E (in Ref. 2; BAA08844)"
FT /evidence="ECO:0000305"
FT CONFLICT 279..280
FT /note="IM -> MV (in Ref. 2; BAA08844)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 710 AA; 78929 MW; 435727A6C76F2D7B CRC64;
MGMSKSRGCF GYPLSIFFIV VNEFCERFSY YGMRALLVLY FRNFLGWDDD LSTAIYHTFV
ALCYLTPILG ALIADSWLGK FKTIVSLSIV YTIGQAVISV SSINDLTDHD HDGSPNNLPL
HVALSMIGLA LIALGTGGIK PCVSAFGGDQ FEEGQEKQRN RFFSIFYLAI NAGSLLSTII
TPILRVQQCG IHSQQACYPL AFGVPAALMA VALIVFVLGS GMYKKFQPQG NIMGKVAKCI
RFAIKNRFRH RSKAFPKRNH WLDWAKEKYD ERLISQIKIM TKVMFLYIPL PMFWALFDQQ
GSRWTLQATT MTGKIGTIEI QPDQMQTVNA ILIVIMVPIV DAVVYPLIAK CGFNFTSLKK
MTVGMFLASM AFVVAAIVQV EIDKTLPVFP SGNQVQIKVL NIGNNDMAVY FPGKNVTVAQ
MSQTDTFMTF DVDQLTSINV SSPGSPGVTT VAHEFEPGHR HTLLVWGPNL YRVVKDGLNQ
KPEKGENGIR FVSTLNEMIT IKMSGKVYEN VTSHSASNYQ FFPSGQKDYT INTTEIAPNC
SSDFKSSNLD FGSAYTYVIR SRASDGCLEV KEFEDIPPNT VNMALQIPQY FLLTCGEVVF
SVTGLEFSYS QAPSNMKSVL QAGWLLTVAI GNIIVLIVAE AGHFDKQWAE YVLFASLLLV
VCIIFAIMAR FYTYINPAEI EAQFDEDEKK KGVGKENPYS SLEPVSQTNM
