PEPT1_CAEEL
ID PEPT1_CAEEL Reviewed; 835 AA.
AC Q21219; O76186;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Peptide transporter family 1;
DE AltName: Full=Di-/tri-peptide transporter CPTB;
DE AltName: Full=Oligopeptide transporter 1;
GN Name=pept-1 {ECO:0000312|WormBase:K04E7.2};
GN Synonyms=cptb {ECO:0000303|PubMed:9601088},
GN opt-2 {ECO:0000312|WormBase:K04E7.2}, pep-2 {ECO:0000312|WormBase:K04E7.2};
GN ORFNames=K04E7.2 {ECO:0000312|WormBase:K04E7.2};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DEVELOPMENTAL STAGE.
RC STRAIN=Bristol N2;
RX PubMed=9601088; DOI=10.1042/bj3320565;
RA Fei Y.-J., Fujita T., Lapp D.F., Ganapathy V., Leibach F.H.;
RT "Two oligopeptide transporters from Caenorhabditis elegans: molecular
RT cloning and functional expression.";
RL Biochem. J. 332:565-572(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=12939266; DOI=10.1074/jbc.m307351200;
RA Nehrke K.;
RT "A reduction in intestinal cell pHi due to loss of the Caenorhabditis
RT elegans Na+/H+ exchanger NHX-2 increases life span.";
RL J. Biol. Chem. 278:44657-44666(2003).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15155758; DOI=10.1074/jbc.m403415200;
RA Meissner B., Boll M., Daniel H., Baumeister R.;
RT "Deletion of the intestinal peptide transporter affects insulin and TOR
RT signaling in Caenorhabditis elegans.";
RL J. Biol. Chem. 279:36739-36745(2004).
RN [5]
RP DISRUPTION PHENOTYPE.
RX PubMed=18676815; DOI=10.1101/gad.1692008;
RA Kniazeva M., Euler T., Han M.;
RT "A branched-chain fatty acid is involved in post-embryonic growth control
RT in parallel to the insulin receptor pathway and its biosynthesis is
RT feedback-regulated in C. elegans.";
RL Genes Dev. 22:2102-2110(2008).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19621081; DOI=10.1371/journal.pone.0006279;
RA Spanier B., Lasch K., Marsch S., Benner J., Liao W., Hu H., Kienberger H.,
RA Eisenreich W., Daniel H.;
RT "How the intestinal peptide transporter PEPT-1 contributes to an obesity
RT phenotype in Caenorhabditits elegans.";
RL PLoS ONE 4:E6279-E6279(2009).
RN [7]
RP DISRUPTION PHENOTYPE.
RX PubMed=19844570; DOI=10.1371/journal.pone.0007545;
RA Brooks K.K., Liang B., Watts J.L.;
RT "The influence of bacterial diet on fat storage in C. elegans.";
RL PLoS ONE 4:E7545-E7545(2009).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20550516; DOI=10.1111/j.1474-9726.2010.00591.x;
RA Spanier B., Rubio-Aliaga I., Hu H., Daniel H.;
RT "Altered signalling from germline to intestine pushes daf-2;pept-1
RT Caenorhabditis elegans into extreme longevity.";
RL Aging Cell 9:636-646(2010).
RN [9]
RP FUNCTION.
RX PubMed=21275419; DOI=10.1021/pr100703a;
RA Martin F.P., Spanier B., Collino S., Montoliu I., Kolmeder C.,
RA Giesbertz P., Affolter M., Kussmann M., Daniel H., Kochhar S., Rezzi S.;
RT "Metabotyping of Caenorhabditis elegans and their culture media revealed
RT unique metabolic phenotypes associated to amino acid deficiency and
RT insulin-like signaling.";
RL J. Proteome Res. 10:990-1003(2011).
RN [10]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=21980510; DOI=10.1371/journal.pone.0025624;
RA Benner J., Daniel H., Spanier B.;
RT "A glutathione peroxidase, intracellular peptidases and the TOR complexes
RT regulate peptide transporter PEPT-1 in C. elegans.";
RL PLoS ONE 6:E25624-E25624(2011).
RN [11]
RP FUNCTION.
RX PubMed=30560135; DOI=10.3389/fmolb.2018.00109;
RA Spanier B., Wallwitz J., Zapoglou D., Idrissou B.M.G., Fischer C.,
RA Troll M., Petzold K., Daniel H.;
RT "The Reproduction Rate of Peptide Transporter PEPT-1 Deficient C. elegans
RT Is Dependent on Dietary Glutamate Supply.";
RL Front. Mol. Biosci. 5:109-109(2018).
CC -!- FUNCTION: Low-affinity peptide transporter that is necessary for
CC proton-dependent uptake of di- or tripeptides, and to a minor extent
CC tetrapeptides, in the intestine. Transport is independent of sodium and
CC chloride ions. Controls the uptake of dietary fatty acids, plays a role
CC in fatty acid synthesis and is responsible for dipeptide-induced
CC acidification of the intestine. Regulates cellular pH differences
CC together with the antiporter protein, nhx-2. Amino acid uptake and
CC absorption levels influence the insulin signaling/daf-2 and let-363/TOR
CC pathways, subsequently affecting the stress response and longevity of
CC the organism. It is required for the uptake of the L-enantiomers of
CC various amino acids, including L-glutamate (PubMed:30560135). In
CC response to the availability of amino acid nutrients, may play a role
CC in promoting reproduction and fertility (PubMed:30560135).
CC {ECO:0000269|PubMed:12939266, ECO:0000269|PubMed:15155758,
CC ECO:0000269|PubMed:19621081, ECO:0000269|PubMed:20550516,
CC ECO:0000269|PubMed:21275419, ECO:0000269|PubMed:21980510,
CC ECO:0000269|PubMed:30560135, ECO:0000269|PubMed:9601088}.
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000269|PubMed:12939266, ECO:0000269|PubMed:21980510}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:12939266,
CC ECO:0000269|PubMed:21980510}. Note=Colocalizes with nhx-2 along the
CC apical membrane of the intestinal cells.
CC -!- TISSUE SPECIFICITY: Expressed specifically in the intestine.
CC {ECO:0000269|PubMed:12939266}.
CC -!- DEVELOPMENTAL STAGE: Biphasic expression pattern observed. Gradual
CC increase in expression during development from embryo through to adult
CC with a decrease during larva stages 1 and 2.
CC {ECO:0000269|PubMed:9601088}.
CC -!- DISRUPTION PHENOTYPE: Mutant worms have decreased body size, high fat
CC stores, increased uptake of fatty acids, reduced brood size, retarded
CC postembryonic growth, extended reproductive life span and increased
CC resistance to stress. RNAi-mediated knockdown of the protein results in
CC impaired synthesis of long-chain and polyunsaturated fatty acids.
CC Pharyngeal pumping rate is similar to wild type but simultaneous
CC knockdown with nhx-2 results in reduced rate of pharyngeal pumping and
CC slightly higher acidic intestinal pH. {ECO:0000269|PubMed:12939266,
CC ECO:0000269|PubMed:15155758, ECO:0000269|PubMed:18676815,
CC ECO:0000269|PubMed:19621081, ECO:0000269|PubMed:19844570,
CC ECO:0000269|PubMed:20550516}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Proton-
CC dependent oligopeptide transporter (POT/PTR) (TC 2.A.17) family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC39119.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF000418; AAC39119.1; ALT_FRAME; mRNA.
DR EMBL; BX284606; CCD64583.1; -; Genomic_DNA.
DR PIR; E89551; E89551.
DR PIR; T37330; T37330.
DR RefSeq; NP_509087.1; NM_076686.5.
DR AlphaFoldDB; Q21219; -.
DR SMR; Q21219; -.
DR BioGRID; 45849; 5.
DR STRING; 6239.K04E7.2.1; -.
DR TCDB; 2.A.17.4.11; the proton-dependent oligopeptide transporter (pot/ptr) family.
DR iPTMnet; Q21219; -.
DR EPD; Q21219; -.
DR PaxDb; Q21219; -.
DR PeptideAtlas; Q21219; -.
DR EnsemblMetazoa; K04E7.2.1; K04E7.2.1; WBGene00003877.
DR GeneID; 180919; -.
DR KEGG; cel:CELE_K04E7.2; -.
DR UCSC; K04E7.2.2; c. elegans.
DR CTD; 180919; -.
DR WormBase; K04E7.2; CE25039; WBGene00003877; pept-1.
DR eggNOG; KOG1237; Eukaryota.
DR GeneTree; ENSGT00940000165486; -.
DR HOGENOM; CLU_004790_3_0_1; -.
DR InParanoid; Q21219; -.
DR OMA; YGHELET; -.
DR OrthoDB; 365203at2759; -.
DR PhylomeDB; Q21219; -.
DR PRO; PR:Q21219; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00003877; Expressed in larva and 4 other tissues.
DR GO; GO:0016324; C:apical plasma membrane; IDA:WormBase.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0071916; F:dipeptide transmembrane transporter activity; IMP:WormBase.
DR GO; GO:0080144; P:amino acid homeostasis; IMP:UniProtKB.
DR GO; GO:0008340; P:determination of adult lifespan; IGI:WormBase.
DR GO; GO:0042938; P:dipeptide transport; IMP:WormBase.
DR GO; GO:0015807; P:L-amino acid transport; IMP:UniProtKB.
DR GO; GO:0019915; P:lipid storage; IMP:WormBase.
DR GO; GO:2000192; P:negative regulation of fatty acid transport; IMP:WormBase.
DR GO; GO:0002119; P:nematode larval development; IMP:WormBase.
DR GO; GO:0040010; P:positive regulation of growth rate; IMP:WormBase.
DR GO; GO:0040018; P:positive regulation of multicellular organism growth; IMP:WormBase.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0060378; P:regulation of brood size; IMP:UniProtKB.
DR GO; GO:1900101; P:regulation of endoplasmic reticulum unfolded protein response; IMP:WormBase.
DR GO; GO:0006885; P:regulation of pH; IGI:WormBase.
DR GO; GO:0032006; P:regulation of TOR signaling; IMP:WormBase.
DR GO; GO:0000003; P:reproduction; IMP:WormBase.
DR GO; GO:0009408; P:response to heat; IMP:WormBase.
DR GO; GO:0006979; P:response to oxidative stress; IMP:WormBase.
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 Cell membrane; Membrane; Peptide transport; Protein transport;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..835
FT /note="Peptide transporter family 1"
FT /id="PRO_0000064314"
FT TRANSMEM 86..106
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 113..133
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 150..170
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 183..203
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 222..242
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 325..345
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 368..388
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 401..421
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 697..717
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 738..758
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 765..785
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 814..835
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 835 AA; 94109 MW; 5CC84A90800ED617 CRC64;
MGYSESRSES VSSKGKTSYG HELETVPLPE KKIYTTWPDM IRHWPKTTLC IVSNEFCERF
SYYGMRTVLT FYLLNVLKFT DSQSTIFFNG FTVLCYTTPL LGSIVADGYI GKFWTIFSVS
ILYAIGQVVL ALASTKNFQS SVHPWMDLSG LLIIAFGTGG IKPCVSAFGG DQFELGQERM
LSLFFSMFYF SINAGSMIST FISPIFRSQP CLGQDSCYPM AFGIPAILMI VATLVFMGGS
FWYKKNPPKD NVFGEVSRLM FRAVGNKMKS GSTPKEHWLL HYLTTHDCAL DAKCLELQAE
KRNKNLCQKK KFIDDVRSLL RVLVMFLPVP MFWALYDQQG SVWLIQAIQM DCRLSDTLLL
LPDQMQTLNA VLILLFIPLF QVIIYPVAAK CVRLTPLRKM VTGGLLASLA FLITGFVQLQ
VNTTLPTLPE EGEASISFWN QFETDCTITV MSGIHKRVLP HDKYLHEDKK NKSGIYNLFT
TKSPAKGNGD WTLTYDLSYD GACGDTSKLE KTVKVTAKSK KIIYVGVGSF GYYQNTANTD
KPTDGTGEFS MGIVTVFNSS YGGNFAMCRQ NTSDFDVNHP CNPRHPADFY FWETDYNSHT
DDRDQNATIT GSLSSQPAVT YKQKSVKPGY WQLYYLLNTP KDVDRQTYNK TATLVAPTNY
GFHRVKQGGV FIYALTGTYE NPKIHELQIV QSNSVSILWQ IPQIVVITAA EILFSITGYE
FAYSQSAPSM KALVQALWLL TTAAGDSIIV VITILNLFEN MAVEFFVYAA AMFVVIAIFA
LLSIFYYTYN YYTTDEEDGE IGVDDEEEIE DHNPRYSIDN KGFHPDEKDT FDMHF
