PEPT1_DROME
ID PEPT1_DROME Reviewed; 743 AA.
AC P91679; A9UNA2; A9UNE6; O77281; O77282; Q7K7E7; Q7KVX8; Q8IRT2; Q95TX0;
AC Q9TY25; Q9TY26; Q9W4P7; Q9W4P8;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 2.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Peptide transporter family 1;
DE AltName: Full=Oligopeptide transporter 1;
DE AltName: Full=Protein YIN;
GN Name=yin; Synonyms=opt1; ORFNames=CG44402;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), AND TISSUE SPECIFICITY.
RX PubMed=9038337; DOI=10.1016/s0092-8674(00)81886-3;
RA Amrein H., Axel R.;
RT "Genes expressed in neurons of adult male Drosophila.";
RL Cell 88:459-469(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORMS A AND B),
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=Canton-S; TISSUE=Head;
RX PubMed=9730971; DOI=10.1152/ajpcell.1998.275.3.c857;
RA Roman G., Meller V., Wu K.H., Davis R.L.;
RT "The opt1 gene of Drosophila melanogaster encodes a proton-dependent
RT dipeptide transporter.";
RL Am. J. Physiol. 275:C857-C869(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [4]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=Oregon-R;
RX PubMed=10731137; DOI=10.1126/science.287.5461.2220;
RA Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., Barrell B.G.,
RA Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Borkova D., Minana B., Kafatos F.C.,
RA Louis C., Siden-Kiamos I., Bolshakov S., Papagiannakis G., Spanos L.,
RA Cox S., Madueno E., de Pablos B., Modolell J., Peter A., Schoettler P.,
RA Werner M., Mourkioti F., Beinert N., Dowe G., Schaefer U., Jaeckle H.,
RA Bucheton A., Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S.,
RA McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C.,
RA Glover D.M.;
RT "From sequence to chromosome: the tip of the X chromosome of D.
RT melanogaster.";
RL Science 287:2220-2222(2000).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS B AND C).
RC STRAIN=Berkeley; TISSUE=Embryo, and Head;
RA Stapleton M., Carlson J.W., Frise E., Kapadia B., Park S., Wan K.H., Yu C.,
RA Celniker S.E.;
RL Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 359-743.
RC STRAIN=Berkeley; TISSUE=Head;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
CC -!- FUNCTION: Important role in absorption of dietary peptides. High-
CC affinity transporter of alanylalanine. Dipeptide transport activity is
CC proton dependent. {ECO:0000269|PubMed:9730971}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=48.8 uM for alanylalanine {ECO:0000269|PubMed:9730971};
CC pH dependence:
CC Optimum pH is 6. {ECO:0000269|PubMed:9730971};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:9730971}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:9730971}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=A; Synonyms=Long;
CC IsoId=P91679-1; Sequence=Displayed;
CC Name=B; Synonyms=Short;
CC IsoId=P91679-2; Sequence=VSP_015662;
CC Name=C;
CC IsoId=P91679-3; Sequence=VSP_015663;
CC -!- TISSUE SPECIFICITY: Expressed in thorax and abdomen of females: apical
CC epithelial membranes of midgut, rectum, and reproductive tract. Also
CC expressed in neuropil of the central nervous system, with elevated
CC expression within the alpha- and beta-lobes of the mushroom bodies.
CC {ECO:0000269|PubMed:9038337, ECO:0000269|PubMed:9730971}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC {ECO:0000269|PubMed:9730971}.
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=AAL13696.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=ABY21723.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U85982; AAC47465.1; -; mRNA.
DR EMBL; U97114; AAD04200.1; -; Genomic_DNA.
DR EMBL; U97114; AAD04201.1; -; Genomic_DNA.
DR EMBL; AE014298; AAF45899.1; -; Genomic_DNA.
DR EMBL; AE014298; AAF45900.2; -; Genomic_DNA.
DR EMBL; AE014298; AAN09110.1; -; Genomic_DNA.
DR EMBL; AL031130; CAA20014.1; -; Genomic_DNA.
DR EMBL; AL031130; CAA20015.1; -; Genomic_DNA.
DR EMBL; BT031266; ABY20507.1; -; mRNA.
DR EMBL; BT031310; ABY21723.1; ALT_INIT; mRNA.
DR EMBL; AY058467; AAL13696.1; ALT_INIT; mRNA.
DR PIR; T13673; T13673.
DR PIR; T13674; T13674.
DR RefSeq; NP_477147.2; NM_057799.4. [P91679-1]
DR RefSeq; NP_477148.2; NM_057800.4. [P91679-2]
DR RefSeq; NP_726894.1; NM_166993.2. [P91679-3]
DR AlphaFoldDB; P91679; -.
DR SMR; P91679; -.
DR BioGRID; 57859; 8.
DR IntAct; P91679; 3.
DR STRING; 7227.FBpp0070601; -.
DR TCDB; 2.A.17.4.2; the proton-dependent oligopeptide transporter (pot/ptr) family.
DR PaxDb; P91679; -.
DR PRIDE; P91679; -.
DR DNASU; 31340; -.
DR EnsemblMetazoa; FBtr0340204; FBpp0309179; FBgn0265575. [P91679-1]
DR EnsemblMetazoa; FBtr0340205; FBpp0309180; FBgn0265575. [P91679-2]
DR EnsemblMetazoa; FBtr0340206; FBpp0309181; FBgn0265575. [P91679-3]
DR GeneID; 31340; -.
DR KEGG; dme:Dmel_CG44402; -.
DR CTD; 31340; -.
DR FlyBase; FBgn0265575; yin.
DR VEuPathDB; VectorBase:FBgn0265575; -.
DR eggNOG; KOG1237; Eukaryota.
DR GeneTree; ENSGT00940000165486; -.
DR HOGENOM; CLU_004790_3_0_1; -.
DR InParanoid; P91679; -.
DR OMA; YNASEYQ; -.
DR PhylomeDB; P91679; -.
DR Reactome; R-DME-427975; Proton/oligopeptide cotransporters.
DR SignaLink; P91679; -.
DR BioGRID-ORCS; 31340; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 31340; -.
DR PRO; PR:P91679; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0265575; Expressed in oocyte and 43 other tissues.
DR ExpressionAtlas; P91679; baseline and differential.
DR Genevisible; P91679; DM.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:FlyBase.
DR GO; GO:0030670; C:phagocytic vesicle membrane; IGI:FlyBase.
DR GO; GO:0071916; F:dipeptide transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0035673; F:oligopeptide transmembrane transporter activity; IGI:FlyBase.
DR GO; GO:0005427; F:proton-dependent oligopeptide secondary active transmembrane transporter activity; IDA:FlyBase.
DR GO; GO:0035442; P:dipeptide transmembrane transport; IGI:FlyBase.
DR GO; GO:0006857; P:oligopeptide transport; IDA:FlyBase.
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 1: Evidence at protein level;
KW Alternative splicing; Membrane; Peptide transport; Protein transport;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..743
FT /note="Peptide transporter family 1"
FT /id="PRO_0000064312"
FT TRANSMEM 74..94
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 104..124
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 132..152
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 173..193
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 207..227
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 334..354
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 364..384
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 597..619
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 629..649
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 659..679
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..27
FT /note="MASEITNGKNGQNGKNGQKEESDSQIA -> MAFVSNAIVGPENCKSVTVSL
FT (in isoform B)"
FT /evidence="ECO:0000303|PubMed:9038337, ECO:0000303|Ref.6"
FT /id="VSP_015662"
FT VAR_SEQ 1..27
FT /note="MASEITNGKNGQNGKNGQKEESDSQIA -> MAFVSNAIVGPENCKSVT
FT (in isoform C)"
FT /evidence="ECO:0000303|Ref.6"
FT /id="VSP_015663"
FT CONFLICT 145
FT /note="T -> N (in Ref. 1; AAC47465)"
FT /evidence="ECO:0000305"
FT CONFLICT 149
FT /note="K -> N (in Ref. 1; AAC47465)"
FT /evidence="ECO:0000305"
FT CONFLICT 154
FT /note="A -> P (in Ref. 1; AAC47465)"
FT /evidence="ECO:0000305"
FT CONFLICT 158
FT /note="D -> E (in Ref. 1; AAC47465)"
FT /evidence="ECO:0000305"
FT CONFLICT 371
FT /note="L -> F (in Ref. 1; AAC47465)"
FT /evidence="ECO:0000305"
FT CONFLICT 462
FT /note="I -> T (in Ref. 5; CAA20015)"
FT /evidence="ECO:0000305"
FT CONFLICT 588
FT /note="L -> P (in Ref. 1; AAC47465, 2; AAD04200/AAD04201
FT and 5; CAA20015)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 743 AA; 82245 MW; A382230B0DFE3107 CRC64;
MASEITNGKN GQNGKNGQKE ESDSQIAPPI PYPKSVAFII SNEFCERFNY YGMRTILVLY
LTNKLGYNEE TATVLFHTFT MLVYIFPLIG ALIADGWLGK YKTILYLSLV YSLGAMVVSF
GAVPLSGMPT KAVTVVGLLL IAIGTGGIKP CVSAFGGDQF SLPAQSFQLA KFFSLFYFAI
NAGSLISTTF TPILRADVHC FGDQDCFSLA FGVPAILMIF SVIIFMAGKR LYRCQPPAGN
MIFGVSRCIA DAFKGWQKRR HSEPMESFLD YAKPTVGSRM VQETKCLGRI LRLFLPFPVF
WALFDQQGSR WTFQATRMDG NVLGFQIKPD QMQVVNPLLI LGFLPLFDYI IYPALARCGI
RRPLQKLTLG LLLAALGFFL SAGLEMKMEQ AAYRATPIEP DMTHLRIYNG MPCRYEISSA
VVQTPRVIEP LNVWEDLSLQ MTESKEYTFN AQPVSGECPS IIDKLRLQPG KSVSYFLAQD
KLVEFADGLQ MAATDTGRTS VRALLNTPDG EGPVLLSTES ATSQEPPLTL DKGNVPQLHR
ITPGFARVDI NGKKVASFEA KEGRLYSILV TGSARDGYQH NVIEVVALST VSILWQLPQI
VVMTAAEVMF SVTGLEFSYS QSPPSMKSVL QACWLLSVAI GNMLVVVIAE FKFTSSQSGE
FTLFASLMLV DMMIFLWLAR SYQYKDQRED FEDDDDATID SVMQSKPKAT TVDTTARKTN
GIEAEPGYGA YRNHAYDNDF SEA
