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2.A.17.4.1
Peptide:H+ symporter (transports cationic, neutral and anionic dipeptides including glycylsarcosine (gly-sar) (Søndergaard et al., 2008) as well as anserine (β-alanyl-1-N-methyl-L-histidine) and carnosine (β-alanyl-L-histidine) (Geissler et al., 2010); also transports β-lactam antibiotics, the antitumor agent, bestatin, and various protease inhibitors). It is competitively inhibited by L-4,4'-biphenylalanyl-L-proline (Bip-Pro) with ~10-20µM affinity. Inhibitors/substrates include cefadroxil, Ala-4-nitroanilide and δ-aminolevulinic acid (Knutter et al., 2007). The intracellular loop linking transmembrane domains 6 and 7 of the human dipeptide transporter hPEPT1 includes two amphipathic alpha-helices, with net positive and negative charges which interact and influence conformational changes of hPEPT1 during and after glycylsarcosine transport (Xu et al., 2010).  The rabbit orthologue provides the main pathway for dietary nitrogen uptake. Five tyrosyl residues are important for function and/or substrate binding (Pieri et al. 2009).  Human PepT1 is modified by N-glycosylation, and all six asparagine residues in the large extracellular loop between transmembrane domains 9 and 10 are subject to N-glycosylation (Chan et al. 2016).

Accession Number:P51574
Protein Name:PET1 aka PepT1 aka SLC15A1
Length:710
Molecular Weight:78929.00
Species:Rattus norvegicus (Rat) [10116]
Number of TMSs:11
Location1 / Topology2 / Orientation3: Membrane1 / Multi-pass membrane protein2
Substrate peptides, H+

Cross database links:

Genevestigator: P51574
eggNOG: roNOG04902
RefSeq: NP_476462.1   
Entrez Gene ID: 117261   
Pfam: PF00854   

Gene Ontology

GO:0016021 C:integral to membrane
GO:0005624 C:membrane fraction
GO:0016248 F:channel inhibitor activity
GO:0015293 F:symporter activity
GO:0051956 P:negative regulation of amino acid transport
GO:0015031 P:protein transport

References (2)

[1] “Sequence, tissue distribution and developmental changes in rat intestinal oligopeptide transporter.”  Miyamoto K.et.al.   8605246
[2] “Cloning and characterization of a rat H+/peptide cotransporter mediating absorption of beta-lactam antibiotics in the intestine and kidney.”  Saito H.et.al.   8531138

External Searches:

  • Search: DB with
  • BLAST ExPASy (Swiss Institute of Bioinformatics (SIB) BLAST)
  • CDD Search (Conserved Domain Database)
  • Search COGs (Clusters of Orthologous Groups of proteins)
  • 2° Structure (Network Protein Sequence Analysis)

Analyze:

Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MGMSKSRGCF GYPLSIFFIV VNEFCERFSY YGMRALLVLY FRNFLGWDDD LSTAIYHTFV 
61:	ALCYLTPILG ALIADSWLGK FKTIVSLSIV YTIGQAVISV SSINDLTDHD HDGSPNNLPL 
121:	HVALSMIGLA LIALGTGGIK PCVSAFGGDQ FEEGQEKQRN RFFSIFYLAI NAGSLLSTII 
181:	TPILRVQQCG IHSQQACYPL AFGVPAALMA VALIVFVLGS GMYKKFQPQG NIMGKVAKCI 
241:	RFAIKNRFRH RSKAFPKRNH WLDWAKEKYD ERLISQIKIM TKVMFLYIPL PMFWALFDQQ 
301:	GSRWTLQATT MTGKIGTIEI QPDQMQTVNA ILIVIMVPIV DAVVYPLIAK CGFNFTSLKK 
361:	MTVGMFLASM AFVVAAIVQV EIDKTLPVFP SGNQVQIKVL NIGNNDMAVY FPGKNVTVAQ 
421:	MSQTDTFMTF DVDQLTSINV SSPGSPGVTT VAHEFEPGHR HTLLVWGPNL YRVVKDGLNQ 
481:	KPEKGENGIR FVSTLNEMIT IKMSGKVYEN VTSHSASNYQ FFPSGQKDYT INTTEIAPNC 
541:	SSDFKSSNLD FGSAYTYVIR SRASDGCLEV KEFEDIPPNT VNMALQIPQY FLLTCGEVVF 
601:	SVTGLEFSYS QAPSNMKSVL QAGWLLTVAI GNIIVLIVAE AGHFDKQWAE YVLFASLLLV 
661:	VCIIFAIMAR FYTYINPAEI EAQFDEDEKK KGVGKENPYS SLEPVSQTNM