S15A1_CANLF
ID S15A1_CANLF Reviewed; 708 AA.
AC Q8WMX5;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 2.
DT 25-MAY-2022, entry version 95.
DE RecName: Full=Solute carrier family 15 member 1;
DE AltName: Full=Intestinal H(+)/peptide cotransporter {ECO:0000303|Ref.1};
DE AltName: Full=Oligopeptide transporter, small intestine isoform {ECO:0000303|Ref.1};
DE AltName: Full=Peptide transporter 1 {ECO:0000303|Ref.1};
GN Name=SLC15A1; Synonyms=PEPT1 {ECO:0000303|Ref.1};
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Cocker spaniel; TISSUE=Kidney;
RA Woods C.A., Etienne N.M.P., Matthews A.D., Davenport G.M., Matthews J.C.;
RT "Cloning, functional characterization, and substrate stimulation of canine
RT PepT1 using Madin-Darby canine kidney cells.";
RL Submitted (JUN-2002) 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 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:0000250|UniProtKB:P36836}; 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; AF461733; AAL67837.2; -; mRNA.
DR RefSeq; NP_001003036.1; NM_001003036.1.
DR AlphaFoldDB; Q8WMX5; -.
DR SMR; Q8WMX5; -.
DR STRING; 9615.ENSCAFP00000008446; -.
DR PaxDb; Q8WMX5; -.
DR GeneID; 403561; -.
DR KEGG; cfa:403561; -.
DR CTD; 6564; -.
DR eggNOG; KOG1237; Eukaryota.
DR InParanoid; Q8WMX5; -.
DR OrthoDB; 365203at2759; -.
DR Proteomes; UP000002254; Unplaced.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
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:0140206; P:dipeptide import across plasma membrane; ISS:UniProtKB.
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 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_0000064303"
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..585
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 117
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 495
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 499
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 527
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 539
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 708 AA; 78705 MW; F1AEAE54F89AC9BD CRC64;
MGMSKSYGCF GYPLSIFFIV VNEFCERFSY YGMRALLILY FRRFIGWDDN LSTAIYHTFV
ALCYLTPILG ALIADSWLGK FKTIVSLSIV YTIGQAVTAV SSINDLTDYN KDGTPDNLSV
HVALSMIGLA LIALGTGGIK PCVSAFGGDQ FEEGQEKQRN RFFSIFYLAI NAGSLISTIV
TPMLRVHECG IYSQKACYPL AFGVPAALMA VSLIVFVIGS GMYKKFQPQG NVMGKVVKCI
GFALKNRFRH RSKQFPKREH WLDWAKEKYD ERLISQIKMV TKVMFLYIPL PMFWALFDQQ
GSRWTLQATA MSGKIGLLEV QPDQMQTVNA ILIVVMVPIM DAVVYPLIAK CGFNFTSLKR
MTVGMFLASM AFVMAAIVQL EIDKTLPVFP KQNEVQIKVL NIGNGAMNVS FPGAVVTVSQ
MSQSDGFMTF DVDKLTSINI SSTGSPVIPV TYNFEQGHRH TLLVWAPNNY RVVKDGLNQK
PEKGENGIRF INSLNESLNI TMGDKVYVNV TSHNASEYQF FSLGTKNITI SSTQQISQNC
TKVLQSSNLE FGSAYTYVIG TQSTGCPELH MFEDISPNTV NMALQIPQYF LITCGEVVFS
VTGLEFSYSQ APSNMKSVLQ AGWLLTVAVG NIIVLIVAGA GQFSEQWAEY ILFAALLLVV
CVIFAIMARF YTYVNPAEIE AQFDDDEKKN LEKMNVYSTV TPVSQTQM
