PEPT3_CAEEL
ID PEPT3_CAEEL Reviewed; 701 AA.
AC O01840; Q9NJH8;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Peptide transporter 3;
DE AltName: Full=Oligopeptide transporter 3;
GN Name=pept-3; Synonyms=opt-3; ORFNames=F56F4.5;
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, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RC STRAIN=Bristol N2;
RX PubMed=10734106; DOI=10.1074/jbc.275.13.9563;
RA Fei Y.J., Romero M.F., Krause M., Liu J.C., Huang W., Ganapathy V.,
RA Leibach F.H.;
RT "A novel H(+)-coupled oligopeptide transporter (OPT3) from Caenorhabditis
RT elegans with a predominant function as a H(+) channel and an exclusive
RT expression in neurons.";
RL J. Biol. Chem. 275:9563-9571(2000).
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 GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-391 AND ASN-432, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Bristol N2;
RX PubMed=17761667; DOI=10.1074/mcp.m600392-mcp200;
RA Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T.,
RA Taoka M., Takahashi N., Isobe T.;
RT "Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis
RT elegans and suggests an atypical translocation mechanism for integral
RT membrane proteins.";
RL Mol. Cell. Proteomics 6:2100-2109(2007).
CC -!- FUNCTION: Neuron-specific, H(+)-coupled oligopeptide transporter with
CC broad specificity towards di- and tripeptides in a Na(+) and Cl(-)-
CC independent manner. Shows H(+) channel activity in the absence of
CC peptide substrates. {ECO:0000269|PubMed:10734106}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in the AVA interneuron.
CC {ECO:0000269|PubMed:10734106}.
CC -!- DEVELOPMENTAL STAGE: Expression is detected as early as the larval L1
CC stage and continues into the adult stage.
CC {ECO:0000269|PubMed:10734106}.
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; AF142441; AAF66614.1; -; mRNA.
DR EMBL; FO081494; CCD71980.1; -; Genomic_DNA.
DR PIR; T15235; T15235.
DR RefSeq; NP_491767.3; NM_059366.5.
DR AlphaFoldDB; O01840; -.
DR SMR; O01840; -.
DR BioGRID; 37751; 1.
DR DIP; DIP-26802N; -.
DR STRING; 6239.F56F4.5; -.
DR TCDB; 2.A.17.4.10; the proton-dependent oligopeptide transporter (pot/ptr) family.
DR iPTMnet; O01840; -.
DR EPD; O01840; -.
DR PaxDb; O01840; -.
DR PeptideAtlas; O01840; -.
DR EnsemblMetazoa; F56F4.5.1; F56F4.5.1; WBGene00003878.
DR GeneID; 172298; -.
DR KEGG; cel:CELE_F56F4.5; -.
DR UCSC; F56F4.5; c. elegans.
DR CTD; 172298; -.
DR WormBase; F56F4.5; CE11268; WBGene00003878; pept-3.
DR eggNOG; KOG1237; Eukaryota.
DR HOGENOM; CLU_004790_3_0_1; -.
DR InParanoid; O01840; -.
DR OMA; PPAVFFM; -.
DR OrthoDB; 365203at2759; -.
DR PhylomeDB; O01840; -.
DR PRO; PR:O01840; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00003878; Expressed in larva and 3 other tissues.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0071916; F:dipeptide transmembrane transporter activity; IDA:WormBase.
DR GO; GO:0015252; F:proton channel activity; IDA:WormBase.
DR GO; GO:0042938; P:dipeptide transport; IDA:WormBase.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:1902600; P:proton transmembrane transport; IDA:WormBase.
DR Gene3D; 1.20.1250.20; -; 2.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR004768; Oligopep_transport.
DR InterPro; IPR031124; Pept-3.
DR InterPro; IPR000109; POT_fam.
DR InterPro; IPR018456; PTR2_symporter_CS.
DR PANTHER; PTHR11654; PTHR11654; 1.
DR PANTHER; PTHR11654:SF289; PTHR11654:SF289; 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 1: Evidence at protein level;
KW Glycoprotein; Membrane; Peptide transport; Protein transport;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..701
FT /note="Peptide transporter 3"
FT /id="PRO_0000064315"
FT TRANSMEM 29..49
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 55..75
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 91..111
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 119..139
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 154..174
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 188..208
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 269..289
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 318..338
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 351..371
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 575..595
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 611..631
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 641..661
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 391
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT CARBOHYD 432
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT CONFLICT 205
FT /note="L -> Q (in Ref. 1; AAF66614)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 701 AA; 77967 MW; A1D260CD57A82C1F CRC64;
MEEKSLLQKL RSYPPAVFFM LGNEFCERFS FYGMKTILFI YLITEHEFSP SKATFIYHLF
TCIAYLTPLI GSIMADSVFG RFKVILYGSS IYVVGHVLLS LGAVPFLSYP IRSSLDFSGL
FVIAFATGCI KPCVSAFAAD QFTEDQKDLR SQFFSFFYFA INGGSLFAII ITPILRGRVQ
CFGNAHCFPL AFGVPGVLML LALILFLMGW SMYKKHPPSK ENVGSKVVAV IYTSLRKMVG
GASRDKPVTH WLDHAAPEHS QKMIDSTRGL LNVAVIFCPL IFFWALFDQQ GSTWVLQARR
LDGRVGHFSI LPEQIHAINP VCVLILVPIF EGWVYPALRK ITRVTPLRKM AVGGLLTAFS
FAIAGVLQLK VNETMEFPPS LGRIYLQRVG NESLISDFRY KSDGRLIGDG MLPKGRTELD
AGIYTFNTGL KNESQEIDIS TPNKGYVMAV FRLKDAVEVV KFDYKVEKTD NGATRVFVVT
AREDADTLVY AINKKGKILS SCELKSGSYV DVIPGIISDP NVRLYWGPKN SCSGVDCPNT
VTLNAQMGAV HVLHIHPSTT EGDFNLLVRP NSVSILWSLP QYIIITLGEV LLSVTGLEFA
YSQAAPNMKS VLTAMWLLTV FAGNLIDMMI SGTRLIPHPA LEFFFYSTLM VIVMGVFILL
AMQYTYVEDN DDEITITESE KKDVIALTEI ESGTATSDKK E
