S15A2_HUMAN
ID S15A2_HUMAN Reviewed; 729 AA.
AC Q16348; A8K1A5; B4E2A7;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 2.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Solute carrier family 15 member 2 {ECO:0000305};
DE AltName: Full=Kidney H(+)/peptide cotransporter {ECO:0000250|UniProtKB:P46029};
DE AltName: Full=Oligopeptide transporter, kidney isoform {ECO:0000250|UniProtKB:P46029};
DE AltName: Full=Peptide transporter 2 {ECO:0000303|PubMed:7756356};
GN Name=SLC15A2 {ECO:0000312|HGNC:HGNC:10921};
GN Synonyms=PEPT2 {ECO:0000303|PubMed:7756356};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Kidney;
RX PubMed=7756356; DOI=10.1016/0005-2736(95)80036-f;
RA Liu W., Liang R., Ramamoorthy S., Fei Y.J., Ganapathy M.E., Hediger M.A.,
RA Ganapathy V., Leibach F.H.;
RT "Molecular cloning of PEPT 2, a new member of the H+/peptide cotransporter
RT family, from human kidney.";
RL Biochim. Biophys. Acta 1235:461-466(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Trachea;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, AND TRANSPORTER ACTIVITY.
RX PubMed=18367661; DOI=10.1152/ajprenal.00030.2008;
RA Sala-Rabanal M., Loo D.D., Hirayama B.A., Wright E.M.;
RT "Molecular mechanism of dipeptide and drug transport by the human renal
RT H+/oligopeptide cotransporter hPEPT2.";
RL Am. J. Physiol. 294:F1422-F1432(2008).
RN [6]
RP FUNCTION, AND TRANSPORTER ACTIVITY.
RX PubMed=31073693; DOI=10.1007/s00726-019-02739-w;
RA Oppermann H., Heinrich M., Birkemeyer C., Meixensberger J., Gaunitz F.;
RT "The proton-coupled oligopeptide transporters PEPT2, PHT1 and PHT2 mediate
RT the uptake of carnosine in glioblastoma cells.";
RL Amino Acids 51:999-1008(2019).
CC -!- FUNCTION: Proton-coupled amino-acid transporter that transports
CC oligopeptides of 2 to 4 amino acids with a preference for dipeptides
CC (PubMed:7756356, PubMed:18367661). Transports the dipeptide-like
CC aminopeptidase inhibitor bestatin (By similarity). Can also transport
CC the aminocephalosporin antibiotic cefadroxil (By similarity). Also able
CC to transport carnosine (PubMed:31073693). Involved in innate immunity
CC by promoting the detection of microbial pathogens by NOD-like receptors
CC (NLRs) (By similarity). Probably acts by mediating transport of
CC bacterial peptidoglycans across the plasma membrane: catalyzes the
CC transport of certain bacterial peptidoglycans, such as muramyl
CC dipeptide (MDP), the NOD2 ligand (By similarity).
CC {ECO:0000250|UniProtKB:P46029, ECO:0000250|UniProtKB:Q63424,
CC ECO:0000250|UniProtKB:Q9ES07, ECO:0000269|PubMed:18367661,
CC ECO:0000269|PubMed:31073693, ECO:0000269|PubMed:7756356}.
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:18367661};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64393;
CC Evidence={ECO:0000269|PubMed:18367661};
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:0000269|PubMed:31073693};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64405;
CC Evidence={ECO:0000269|PubMed:31073693};
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:0000269|PubMed:18367661};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64397;
CC Evidence={ECO:0000269|PubMed:18367661};
CC -!- SUBUNIT: Interacts (via extracellular domain region) with trypsin.
CC {ECO:0000250|UniProtKB:Q63424}.
CC -!- INTERACTION:
CC Q16348; O43184-4: ADAM12; NbExp=3; IntAct=EBI-12806032, EBI-12006944;
CC Q16348; Q49AR9: ANKS1A; NbExp=3; IntAct=EBI-12806032, EBI-11954519;
CC Q16348; P29972: AQP1; NbExp=3; IntAct=EBI-12806032, EBI-745213;
CC Q16348; Q6NUJ2: C11orf87; NbExp=3; IntAct=EBI-12806032, EBI-6660291;
CC Q16348; Q9H2X0: CHRD; NbExp=3; IntAct=EBI-12806032, EBI-947551;
CC Q16348; Q9H0I2: ENKD1; NbExp=3; IntAct=EBI-12806032, EBI-744099;
CC Q16348; Q2WGJ6: KLHL38; NbExp=3; IntAct=EBI-12806032, EBI-6426443;
CC Q16348; Q5T749: KPRP; NbExp=3; IntAct=EBI-12806032, EBI-10981970;
CC Q16348; O76011: KRT34; NbExp=3; IntAct=EBI-12806032, EBI-1047093;
CC Q16348; P59991: KRTAP12-2; NbExp=3; IntAct=EBI-12806032, EBI-10176379;
CC Q16348; P60328: KRTAP12-3; NbExp=3; IntAct=EBI-12806032, EBI-11953334;
CC Q16348; Q3LI76: KRTAP15-1; NbExp=3; IntAct=EBI-12806032, EBI-11992140;
CC Q16348; Q6PEX3: KRTAP26-1; NbExp=3; IntAct=EBI-12806032, EBI-3957672;
CC Q16348; P61968: LMO4; NbExp=3; IntAct=EBI-12806032, EBI-2798728;
CC Q16348; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-12806032, EBI-741158;
CC Q16348; P32242: OTX1; NbExp=3; IntAct=EBI-12806032, EBI-740446;
CC Q16348; P78337: PITX1; NbExp=3; IntAct=EBI-12806032, EBI-748265;
CC Q16348; Q9NRQ2: PLSCR4; NbExp=3; IntAct=EBI-12806032, EBI-769257;
CC Q16348; Q92922: SMARCC1; NbExp=3; IntAct=EBI-12806032, EBI-355653;
CC Q16348; Q96A09: TENT5B; NbExp=3; IntAct=EBI-12806032, EBI-752030;
CC Q16348; O43711: TLX3; NbExp=3; IntAct=EBI-12806032, EBI-3939165;
CC Q16348; O95231: VENTX; NbExp=3; IntAct=EBI-12806032, EBI-10191303;
CC Q16348; Q9NZC7-5: WWOX; NbExp=3; IntAct=EBI-12806032, EBI-12040603;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:7756356};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q16348-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q16348-2; Sequence=VSP_043084;
CC -!- TISSUE SPECIFICITY: Expressed in kidney (PubMed:7756356). Not detected
CC in intestine (PubMed:7756356). {ECO:0000269|PubMed:7756356}.
CC -!- DOMAIN: The extracellular domain (ECD) region specifically binds
CC trypsin. {ECO:0000250|UniProtKB:Q63424}.
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; S78203; AAB34388.1; -; mRNA.
DR EMBL; AK289820; BAF82509.1; -; mRNA.
DR EMBL; AK304189; BAG65069.1; -; mRNA.
DR EMBL; AC072031; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471052; EAW79496.1; -; Genomic_DNA.
DR CCDS; CCDS3007.1; -. [Q16348-1]
DR CCDS; CCDS54631.1; -. [Q16348-2]
DR PIR; I52481; I52481.
DR RefSeq; NP_001139470.1; NM_001145998.1. [Q16348-2]
DR RefSeq; NP_066568.3; NM_021082.3. [Q16348-1]
DR PDB; 6EZI; X-ray; 1.50 A; B=720-729.
DR PDB; 7PMY; EM; 3.80 A; A=1-729.
DR PDBsum; 6EZI; -.
DR PDBsum; 7PMY; -.
DR AlphaFoldDB; Q16348; -.
DR SMR; Q16348; -.
DR BioGRID; 112453; 27.
DR IntAct; Q16348; 26.
DR MINT; Q16348; -.
DR STRING; 9606.ENSP00000417085; -.
DR BindingDB; Q16348; -.
DR ChEMBL; CHEMBL1743125; -.
DR DrugBank; DB00855; Aminolevulinic acid.
DR DrugBank; DB01060; Amoxicillin.
DR DrugBank; DB00415; Ampicillin.
DR DrugBank; DB08795; Azidocillin.
DR DrugBank; DB00542; Benazepril.
DR DrugBank; DB01053; Benzylpenicillin.
DR DrugBank; DB00833; Cefaclor.
DR DrugBank; DB01140; Cefadroxil.
DR DrugBank; DB00456; Cefalotin.
DR DrugBank; DB00535; Cefdinir.
DR DrugBank; DB01413; Cefepime.
DR DrugBank; DB00671; Cefixime.
DR DrugBank; DB00274; Cefmetazole.
DR DrugBank; DB00493; Cefotaxime.
DR DrugBank; DB01333; Cefradine.
DR DrugBank; DB01415; Ceftibuten.
DR DrugBank; DB01212; Ceftriaxone.
DR DrugBank; DB01112; Cefuroxime.
DR DrugBank; DB00567; Cephalexin.
DR DrugBank; DB00672; Chlorpropamide.
DR DrugBank; DB01340; Cilazapril.
DR DrugBank; DB01147; Cloxacillin.
DR DrugBank; DB01000; Cyclacillin.
DR DrugBank; DB00485; Dicloxacillin.
DR DrugBank; DB00492; Fosinopril.
DR DrugBank; DB01016; Glyburide.
DR DrugBank; DB00722; Lisinopril.
DR DrugBank; DB00447; Loracarbef.
DR DrugBank; DB00691; Moexipril.
DR DrugBank; DB00731; Nateglinide.
DR DrugBank; DB00713; Oxacillin.
DR DrugBank; DB00790; Perindopril.
DR DrugBank; DB00781; Polymyxin B.
DR DrugBank; DB00881; Quinapril.
DR DrugBank; DB00178; Ramipril.
DR DrugBank; DB01348; Spirapril.
DR DrugBank; DB01124; Tolbutamide.
DR DrugBank; DB00519; Trandolapril.
DR DrugBank; DB03424; Ubenimex.
DR DrugBank; DB00577; Valaciclovir.
DR DrugBank; DB01610; Valganciclovir.
DR DrugCentral; Q16348; -.
DR GuidetoPHARMACOLOGY; 985; -.
DR TCDB; 2.A.17.4.8; the proton-dependent oligopeptide transporter (pot/ptr) family.
DR GlyGen; Q16348; 5 sites.
DR iPTMnet; Q16348; -.
DR PhosphoSitePlus; Q16348; -.
DR BioMuta; SLC15A2; -.
DR DMDM; 209572672; -.
DR EPD; Q16348; -.
DR MassIVE; Q16348; -.
DR PaxDb; Q16348; -.
DR PeptideAtlas; Q16348; -.
DR PRIDE; Q16348; -.
DR ProteomicsDB; 60859; -. [Q16348-1]
DR ProteomicsDB; 60860; -. [Q16348-2]
DR Antibodypedia; 32862; 74 antibodies from 22 providers.
DR DNASU; 6565; -.
DR Ensembl; ENST00000295605.6; ENSP00000295605.2; ENSG00000163406.11. [Q16348-2]
DR Ensembl; ENST00000489711.6; ENSP00000417085.1; ENSG00000163406.11. [Q16348-1]
DR GeneID; 6565; -.
DR KEGG; hsa:6565; -.
DR MANE-Select; ENST00000489711.6; ENSP00000417085.1; NM_021082.4; NP_066568.3.
DR UCSC; uc003eep.3; human. [Q16348-1]
DR CTD; 6565; -.
DR DisGeNET; 6565; -.
DR GeneCards; SLC15A2; -.
DR HGNC; HGNC:10921; SLC15A2.
DR HPA; ENSG00000163406; Tissue enhanced (cervix, epididymis, prostate).
DR MIM; 602339; gene.
DR neXtProt; NX_Q16348; -.
DR OpenTargets; ENSG00000163406; -.
DR PharmGKB; PA35812; -.
DR VEuPathDB; HostDB:ENSG00000163406; -.
DR eggNOG; KOG1237; Eukaryota.
DR GeneTree; ENSGT00940000156507; -.
DR HOGENOM; CLU_004790_3_0_1; -.
DR InParanoid; Q16348; -.
DR OMA; YGHELET; -.
DR OrthoDB; 365203at2759; -.
DR PhylomeDB; Q16348; -.
DR TreeFam; TF330897; -.
DR PathwayCommons; Q16348; -.
DR Reactome; R-HSA-427975; Proton/oligopeptide cotransporters.
DR SignaLink; Q16348; -.
DR BioGRID-ORCS; 6565; 10 hits in 1067 CRISPR screens.
DR ChiTaRS; SLC15A2; human.
DR GeneWiki; SLC15A2; -.
DR GenomeRNAi; 6565; -.
DR Pharos; Q16348; Tchem.
DR PRO; PR:Q16348; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q16348; protein.
DR Bgee; ENSG00000163406; Expressed in nasal cavity epithelium and 161 other tissues.
DR ExpressionAtlas; Q16348; baseline and differential.
DR Genevisible; Q16348; HS.
DR GO; GO:0016324; C:apical plasma membrane; ISS:ARUK-UCL.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:ARUK-UCL.
DR GO; GO:0044214; C:spanning component of plasma membrane; IC:ARUK-UCL.
DR GO; GO:0071916; F:dipeptide transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0015333; F:peptide:proton symporter activity; IDA:ARUK-UCL.
DR GO; GO:0140206; P:dipeptide import across plasma membrane; IDA:UniProtKB.
DR GO; GO:0042938; P:dipeptide transport; ISS:ARUK-UCL.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0006811; P:ion transport; TAS:Reactome.
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:0070293; P:renal absorption; ISS:ARUK-UCL.
DR GO; GO:0150104; P:transport across blood-brain barrier; NAS:ARUK-UCL.
DR GO; GO:1990961; P:xenobiotic detoxification by transmembrane export across the plasma membrane; NAS:UniProtKB.
DR GO; GO:0042908; P:xenobiotic transport; ISS:ARUK-UCL.
DR Gene3D; 1.20.1250.20; -; 2.
DR InterPro; IPR029028; Alpha/beta_knot_MTases.
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 SUPFAM; SSF75217; SSF75217; 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 3D-structure; Alternative splicing; Cell membrane; Glycoprotein; Immunity;
KW Innate immunity; Membrane; Peptide transport; Phosphoprotein;
KW Protein transport; Reference proteome; Symport; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..729
FT /note="Solute carrier family 15 member 2"
FT /id="PRO_0000064308"
FT TOPO_DOM 1..57
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 58..78
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 79..83
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 84..104
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 105..113
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 114..134
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 135..139
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 140..160
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 161..183
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 184..204
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 205..217
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 218..238
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 239..295
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 296..316
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 317..343
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 344..364
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 365..380
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 381..401
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 402..611
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 612..632
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 633..643
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 644..664
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 665..674
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 675..695
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 696..729
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 402..611
FT /note="Extracellular domain (ECD)"
FT /evidence="ECO:0000250|UniProtKB:Q63424"
FT COMPBIAS 20..34
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ES07"
FT MOD_RES 12
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9ES07"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63424"
FT CARBOHYD 435
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 472
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 528
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 567
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 587
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT VAR_SEQ 113..143
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043084"
FT VARIANT 57
FT /note="R -> H (in dbSNP:rs1920305)"
FT /id="VAR_047001"
FT VARIANT 73
FT /note="Y -> C (in dbSNP:rs1143667)"
FT /id="VAR_047002"
FT VARIANT 350
FT /note="L -> F (in dbSNP:rs2257212)"
FT /id="VAR_047003"
FT VARIANT 409
FT /note="P -> S (in dbSNP:rs1143671)"
FT /id="VAR_047004"
FT VARIANT 509
FT /note="R -> K (in dbSNP:rs1143672)"
FT /id="VAR_047005"
FT VARIANT 609
FT /note="A -> G (in dbSNP:rs1143668)"
FT /id="VAR_047006"
FT VARIANT 704
FT /note="M -> L (in dbSNP:rs1920314)"
FT /id="VAR_047008"
FT CONFLICT 278..279
FT /note="QH -> HD (in Ref. 1; AAB34388)"
FT /evidence="ECO:0000305"
FT CONFLICT 396
FT /note="A -> R (in Ref. 1; AAB34388)"
FT /evidence="ECO:0000305"
FT CONFLICT 609
FT /note="A -> R (in Ref. 1; AAB34388)"
FT /evidence="ECO:0000305"
FT STRAND 724..728
FT /evidence="ECO:0007829|PDB:6EZI"
SQ SEQUENCE 729 AA; 81783 MW; 0169DC150BD35BC3 CRC64;
MNPFQKNESK ETLFSPVSIE EVPPRPPSPP KKPSPTICGS NYPLSIAFIV VNEFCERFSY
YGMKAVLILY FLYFLHWNED TSTSIYHAFS SLCYFTPILG AAIADSWLGK FKTIIYLSLV
YVLGHVIKSL GALPILGGQV VHTVLSLIGL SLIALGTGGI KPCVAAFGGD QFEEKHAEER
TRYFSVFYLS INAGSLISTF ITPMLRGDVQ CFGEDCYALA FGVPGLLMVI ALVVFAMGSK
IYNKPPPEGN IVAQVFKCIW FAISNRFKNR SGDIPKRQHW LDWAAEKYPK QLIMDVKALT
RVLFLYIPLP MFWALLDQQG SRWTLQAIRM NRNLGFFVLQ PDQMQVLNPL LVLIFIPLFD
FVIYRLVSKC GINFSSLRKM AVGMILACLA FAVAAAVEIK INEMAPAQPG PQEVFLQVLN
LADDEVKVTV VGNENNSLLI ESIKSFQKTP HYSKLHLKTK SQDFHFHLKY HNLSLYTEHS
VQEKNWYSLV IREDGNSISS MMVKDTESRT TNGMTTVRFV NTLHKDVNIS LSTDTSLNVG
EDYGVSAYRT VQRGEYPAVH CRTEDKNFSL NLGLLDFGAA YLFVITNNTN QGLQAWKIED
IPANKMSIAW QLPQYALVTA GEVMFSVTGL EFSYSQAPSS MKSVLQAAWL LTIAVGNIIV
LVVAQFSGLV QWAEFILFSC LLLVICLIFS IMGYYYVPVK TEDMRGPADK HIPHIQGNMI
KLETKKTKL
