S15A1_RABIT
ID S15A1_RABIT Reviewed; 707 AA.
AC P36836;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Solute carrier family 15 member 1;
DE AltName: Full=Intestinal H(+)/peptide cotransporter {ECO:0000303|PubMed:8139693};
DE AltName: Full=Oligopeptide transporter, small intestine isoform {ECO:0000303|PubMed:8139693};
DE AltName: Full=Peptide transporter 1 {ECO:0000303|PubMed:8139693};
GN Name=SLC15A1; Synonyms=PEPT1 {ECO:0000303|PubMed:8139693};
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TRANSPORTER ACTIVITY.
RC TISSUE=Small intestine;
RX PubMed=8139693; DOI=10.1038/368563a0;
RA Fei Y.-J., Kanai Y., Nussberger S., Ganapathy V., Leibach F.H.,
RA Romero M.F., Singh S.K., Boron W.F., Hediger M.A.;
RT "Expression cloning of a mammalian proton-coupled oligopeptide
RT transporter.";
RL Nature 368:563-566(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Small intestine;
RA Boll M., Markovich D., Weber M., Korte H., Daniel H., Murer H.;
RL Submitted (AUG-1994) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Proton-coupled amino-acid transporter that transports
CC oligopeptides of 2 to 4 amino acids with a preference for dipeptides
CC (PubMed:8139693). Primarily responsible for the absorption of dietary
CC di- and tripeptides from the small intestinal lumen (PubMed:8139693).
CC {ECO:0000269|PubMed:8139693}.
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:8139693};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64393;
CC Evidence={ECO:0000269|PubMed:8139693};
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:8139693};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64401;
CC Evidence={ECO:0000269|PubMed:8139693};
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:8139693}; Multi-pass
CC membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Intestine, kidney, liver and low in brain.
CC {ECO:0000269|PubMed:8139693}.
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; U06467; AAA17721.1; -; mRNA.
DR EMBL; U13707; AAA21335.1; -; mRNA.
DR PIR; S43297; S43297.
DR RefSeq; NP_001075806.1; NM_001082337.1.
DR AlphaFoldDB; P36836; -.
DR SMR; P36836; -.
DR STRING; 9986.ENSOCUP00000010337; -.
DR BindingDB; P36836; -.
DR ChEMBL; CHEMBL3509595; -.
DR PRIDE; P36836; -.
DR GeneID; 100009186; -.
DR KEGG; ocu:100009186; -.
DR CTD; 6564; -.
DR eggNOG; KOG1237; Eukaryota.
DR InParanoid; P36836; -.
DR OrthoDB; 365203at2759; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0089717; C:spanning component of membrane; IDA:ARUK-UCL.
DR GO; GO:0071916; F:dipeptide transmembrane transporter activity; IDA:ARUK-UCL.
DR GO; GO:0015333; F:peptide:proton symporter activity; IDA:ARUK-UCL.
DR GO; GO:0042937; F:tripeptide transmembrane transporter activity; IDA:ARUK-UCL.
DR GO; GO:0140206; P:dipeptide import across plasma membrane; IDA:ARUK-UCL.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0140207; P:tripeptide import across plasma membrane; IDA: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 2: Evidence at transcript level;
KW Glycoprotein; Membrane; Peptide transport; Protein transport;
KW Reference proteome; Symport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..707
FT /note="Solute carrier family 15 member 1"
FT /id="PRO_0000064306"
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..583
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 584..604
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 605..618
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 619..639
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 640..644
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 645..665
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 666..707
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 383..583
FT /note="Extracellular domain (ECD)"
FT /evidence="ECO:0000250|UniProtKB:Q9JIP7"
FT REGION 682..707
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 50
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 498
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 513
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 619..620
FT /note="AG -> DR (in Ref. 2; AAA21335)"
FT /evidence="ECO:0000305"
FT CONFLICT 699
FT /note="L -> V (in Ref. 2; AAA21335)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 707 AA; 78927 MW; 9186B3282981B5B4 CRC64;
MGMSKSLSCF GYPLSIFFIV VNEFCERFSY YGMRALLILY FRNFIGWDDN LSTVIYHTFV
ALCYLTPILG ALIADAWLGK FKTIVWLSIV YTIGQAVTSL SSVNELTDNN HDGTPDSLPV
HVAVCMIGLL LIALGTGGIK PCVSAFGGDQ FEEGQEKQRN RFFSIFYLAI NAGSLLSTII
TPMVRVQQCG IHVKQACYPL AFGIPAILMA VSLIVFIIGS GMYKKFKPQG NILSKVVKCI
CFAIKNRFRH RSKQFPKRAH WLDWAKEKYD ERLIAQIKMV TRVLFLYIPL PMFWALFDQQ
GSRWTLQATT MSGRIGILEI QPDQMQTVNT ILIIILVPIM DAVVYPLIAK CGLNFTSLKK
MTIGMFLASM AFVAAAILQV EIDKTLPVFP KANEVQIKVL NVGSENMIIS LPGQTVTLNQ
MSQTNEFMTF NEDTLTSINI TSGSQVTMIT PSLEAGQRHT LLVWAPNNYR VVNDGLTQKS
DKGENGIRFV NTYSQPINVT MSGKVYEHIA SYNASEYQFF TSGVKGFTVS SAGISEQCRR
DFESPYLEFG SAYTYLITSQ ATGCPQVTEF EDIPPNTMNM AWQIPQYFLI TSGEVVFSIT
GLEFSYSQAP SNMKSVLQAG WLLTVAVGNI IVLIVAGAGQ INKQWAEYIL FAALLLVVCV
IFAIMARFYT YVNPAEIEAQ FEEDEKKKNP EKNDLYPSLA PVSQTQM
