S15A2_DANRE
ID S15A2_DANRE Reviewed; 719 AA.
AC B0S6T2; Q08BT0; Q2F800;
DT 23-MAY-2018, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Solute carrier family 15 member 2 {ECO:0000303|PubMed:16317081};
DE AltName: Full=Peptide transporter 2 {ECO:0000303|PubMed:16317081};
DE Short=PEPT2 {ECO:0000303|PubMed:16317081};
GN Name=slc15a2 {ECO:0000303|PubMed:16317081,
GN ECO:0000312|ZFIN:ZDB-GENE-030131-5866};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955 {ECO:0000312|Proteomes:UP000000437};
RN [1] {ECO:0000312|EMBL:ABA86557.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TRANSPORTER ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP AND DEVELOPMENTAL STAGE.
RX PubMed=16317081; DOI=10.1152/physiolgenomics.00227.2005;
RA Romano A., Kottra G., Barca A., Tiso N., Maffia M., Argenton F., Daniel H.,
RA Storelli C., Verri T.;
RT "High-affinity peptide transporter PEPT2 (SLC15A2) of the zebrafish Danio
RT rerio: functional properties, genomic organization, and expression
RT analysis.";
RL Physiol. Genomics 24:207-217(2006).
RN [2] {ECO:0000312|Proteomes:UP000000437}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [3] {ECO:0000312|EMBL:AAI24582.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=AB {ECO:0000312|EMBL:AAI24582.1};
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (APR-2008) 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 {ECO:0000269|PubMed:16317081}.
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:0000269|PubMed:16317081};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64393;
CC Evidence={ECO:0000269|PubMed:16317081};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+)(out) + N-acetylmuramyl-L-alanyl-D-isoglutamine(out) =
CC H(+)(in) + N-acetylmuramyl-L-alanyl-D-isoglutamine(in);
CC Xref=Rhea:RHEA:64408, ChEBI:CHEBI:15378, ChEBI:CHEBI:155830;
CC Evidence={ECO:0000250|UniProtKB:Q9ES07};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64409;
CC Evidence={ECO:0000250|UniProtKB:Q9ES07};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=carnosine(out) + H(+)(out) = carnosine(in) + H(+)(in);
CC Xref=Rhea:RHEA:64404, ChEBI:CHEBI:15378, ChEBI:CHEBI:57485;
CC Evidence={ECO:0000250|UniProtKB:Q16348};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64405;
CC Evidence={ECO:0000250|UniProtKB:Q16348};
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:Q16348};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64397;
CC Evidence={ECO:0000250|UniProtKB:Q16348};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=97 uM for Gly-L-Gln (at pH 5.5 and -160 mV)
CC {ECO:0000269|PubMed:16317081};
CC KM=79 uM for Gly-L-Gln (at pH 6.5 and -160 mV)
CC {ECO:0000269|PubMed:16317081};
CC KM=48 uM for Gly-L-Gln (at pH 7.5 and -160 mV)
CC {ECO:0000269|PubMed:16317081};
CC KM=163 uM for Gly-L-Gln (at pH 8.5 and -160 mV)
CC {ECO:0000269|PubMed:16317081};
CC KM=82 uM for Gly-L-Gln (at pH 5.5 and -120 mV)
CC {ECO:0000269|PubMed:16317081};
CC KM=38 uM for Gly-L-Gln (at pH 6.5 and -120 mV)
CC {ECO:0000269|PubMed:16317081};
CC KM=18 uM for Gly-L-Gln (at pH 7.5 and -120 mV)
CC {ECO:0000269|PubMed:16317081};
CC KM=118 uM for Gly-L-Gln (at pH 8.5 and -120 mV)
CC {ECO:0000269|PubMed:16317081};
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:16317081};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:16317081};
CC Multi-pass membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=B0S6T2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=B0S6T2-2; Sequence=VSP_059583;
CC -!- TISSUE SPECIFICITY: Expressed in kidney, brain and gut. Also expressed
CC weakly in eye, gill and skeletal muscle. {ECO:0000269|PubMed:16317081}.
CC -!- DEVELOPMENTAL STAGE: Detected at 1 to 7 days post-fertilization (dpf).
CC Expressed in the forebrain and midbrain at 1 dpf, where it localizes to
CC the ependymal cell layer of the dicephalic ventricle and midbrain
CC ventricle. Expressed in the developing otic vesicle at 2-7 dpf, where
CC it shows particularly strong expression in the epithelium of the
CC semicircular canal projections. {ECO:0000269|PubMed:16317081}.
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; DQ192597; ABA86557.1; -; mRNA.
DR EMBL; BX548071; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC124581; AAI24582.1; -; mRNA.
DR EMBL; BC165646; AAI65646.1; -; mRNA.
DR RefSeq; NP_001034917.1; NM_001039828.1.
DR AlphaFoldDB; B0S6T2; -.
DR SMR; B0S6T2; -.
DR STRING; 7955.ENSDARP00000091395; -.
DR TCDB; 2.A.17.4.5; the proton-dependent oligopeptide transporter (pot/ptr) family.
DR PaxDb; B0S6T2; -.
DR Ensembl; ENSDART00000100622; ENSDARP00000091395; ENSDARG00000032010. [B0S6T2-1]
DR GeneID; 556684; -.
DR KEGG; dre:556684; -.
DR CTD; 6565; -.
DR ZFIN; ZDB-GENE-030131-5866; slc15a2.
DR eggNOG; KOG1237; Eukaryota.
DR GeneTree; ENSGT00940000156507; -.
DR HOGENOM; CLU_004790_3_0_1; -.
DR InParanoid; B0S6T2; -.
DR OMA; YGHELET; -.
DR OrthoDB; 365203at2759; -.
DR PhylomeDB; B0S6T2; -.
DR TreeFam; TF330897; -.
DR Reactome; R-DRE-427975; Proton/oligopeptide cotransporters.
DR PRO; PR:B0S6T2; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 9.
DR Bgee; ENSDARG00000032010; Expressed in intestine and 24 other tissues.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0071916; F:dipeptide transmembrane transporter activity; IDA:ZFIN.
DR GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR GO; GO:0140206; P:dipeptide import across plasma membrane; ISS:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0015835; P:peptidoglycan transport; ISS:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0070424; P:regulation of nucleotide-binding oligomerization domain containing signaling pathway; ISS:UniProtKB.
DR GO; GO:0001878; P:response to yeast; IDA:ZFIN.
DR Gene3D; 1.20.1250.20; -; 2.
DR InterPro; IPR036259; MFS_trans_sf.
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 PROSITE; PS01022; PTR2_1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Glycoprotein; Immunity;
KW Innate immunity; Membrane; Peptide transport; Protein transport;
KW Reference proteome; Symport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..719
FT /note="Solute carrier family 15 member 2"
FT /id="PRO_0000444319"
FT TOPO_DOM 1..43
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 44..61
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 62..69
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 70..90
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 91..99
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 100..120
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 121..125
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 126..146
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 147..169
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 170..190
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 191..201
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 202..222
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 223..280
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 281..301
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 302..334
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 335..355
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 356..367
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 368..388
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 389..594
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 595..615
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 616..626
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 627..647
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 648..657
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 658..678
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 679..719
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 389..594
FT /note="Extracellular domain (ECD)"
FT /evidence="ECO:0000250|UniProtKB:Q63424"
FT REGION 695..719
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 66
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 481
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 513
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 532
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT VAR_SEQ 280..304
FT /note="Missing (in isoform 2)"
FT /id="VSP_059583"
FT CONFLICT 456..459
FT /note="MNYQ -> VNYE (in Ref. 1; ABA86557 and 3; AAI24582/
FT AAI65646)"
FT /evidence="ECO:0000305"
FT CONFLICT 477..481
FT /note="TAQHN -> PAQSG (in Ref. 1; ABA86557 and 3; AAI24582/
FT AAI65646)"
FT /evidence="ECO:0000305"
FT CONFLICT 549
FT /note="T -> S (in Ref. 1; ABA86557 and 3; AAI24582/
FT AAI65646)"
FT /evidence="ECO:0000305"
FT CONFLICT 572
FT /note="A -> T (in Ref. 1; ABA86557 and 3; AAI24582/
FT AAI65646)"
FT /evidence="ECO:0000305"
FT CONFLICT 578
FT /note="V -> I (in Ref. 1; ABA86557 and 3; AAI24582/
FT AAI65646)"
FT /evidence="ECO:0000305"
FT CONFLICT 694
FT /note="D -> E (in Ref. 1; ABA86557 and 3; AAI24582/
FT AAI65646)"
FT /evidence="ECO:0000305"
FT CONFLICT 712..713
FT /note="DM -> EI (in Ref. 1; ABA86557 and 3; AAI24582/
FT AAI65646)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 719 AA; 79690 MW; 7026718548852604 CRC64;
MGKMKDKDVD AEKYEKAQRS PKLCGTNYPV SIAFIVVNEF CERFSYYGMK AVLTLYFMNY
LHWDKNLSTA IYHAFSGLCY FTPLLGALIA DSWLGKFKTI IYLSIVYVIG HVVKSVGAIP
DVGDSTVHIA LSMVGLGLIA LGTGGIKPCV AAFGGDQFDE DNIDERRKFF SIFYMSINAG
SVLSTIITPI LRGDVQCFGG DCYALAFGVP AALMVIALVV FISGSGLYKK SPPEGNVLVR
VCKCIGFAIS NRWTNSKKSP KRSHWLDWAE EKYSKRLIQE IKMVCRVLVL YIPLPMFWAL
FDQQGSRWTL QATRMNMDFG GGFIIKPDQM QMLNALLILV FIPIFDMGIY PLVGLCRIKL
TPLKKMATGM ILAALAFCAA TAVEVYVIKT VVEPPPAKES LVQVYNLMDS DVTVQFPAHN
VFSEPLKPYE EPSGYSSLPL TGESQLQNVV VSHNGMNYQC RLTFTERMAY SLLLHPTAQH
NGSVCNLVKD HITKSETGAA YIRFINTHTE NINVTVGTEE VHASANYGIS RNISVPRGEY
NKAVCVTDTK EYEINLGLLD FGAFYTVILS EAGNNLAVKK MEDIQANNIH IGWQIPQYVF
LTAGEVMFSI TGLEFSYSQA PASMKSVLQA GWLMTVAFGN VIVLIVAEGA GMEQWVEFLL
FAALLVAVSI IFSIMAYFYT YVDPDQLDKL FKEDGDGGKV ESSKKDELSL GDMPKQTKM
