S6A17_RAT
ID S6A17_RAT Reviewed; 727 AA.
AC P31662;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Sodium-dependent neutral amino acid transporter SLC6A17;
DE AltName: Full=Sodium-dependent neurotransmitter transporter NTT4;
DE AltName: Full=Solute carrier family 6 member 17;
GN Name=Slc6a17; Synonyms=Ntt4, Rxt1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=8093354; DOI=10.1016/0014-5793(93)81145-p;
RA Liu Q.-R., Mandiyan S., Lopez-Corcuera B., Nelson H., Nelson N.;
RT "A rat brain cDNA encoding the neurotransmitter transporter with an unusual
RT structure.";
RL FEBS Lett. 315:114-118(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8294906; DOI=10.1046/j.1471-4159.1994.62020445.x;
RA el Mestikawy S., Giros B., Pohl M., Hamon M., Kingsmore S.F., Seldin M.F.,
RA Caron M.G.;
RT "Characterization of an atypical member of the Na+/Cl(-)-dependent
RT transporter family: chromosomal localization and distribution in GABAergic
RT and glutamatergic neurons in the rat brain.";
RL J. Neurochem. 62:445-455(1994).
RN [3]
RP IDENTIFICATION, AND TISSUE SPECIFICITY.
RX PubMed=16125675; DOI=10.1016/j.bbrc.2005.08.048;
RA Hoglund P.J., Adzic D., Scicluna S.J., Lindblom J., Fredriksson R.;
RT "The repertoire of solute carriers of family 6: identification of new human
RT and rodent genes.";
RL Biochem. Biophys. Res. Commun. 336:175-189(2005).
RN [4]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, AND
RP SUBCELLULAR LOCATION.
RX PubMed=18768736; DOI=10.1124/mol.108.050005;
RA Parra L.A., Baust T., El Mestikawy S., Quiroz M., Hoffman B., Haflett J.M.,
RA Yao J.K., Torres G.E.;
RT "The orphan transporter Rxt1/NTT4 (SLC6A17) functions as a synaptic vesicle
RT amino acid transporter selective for proline, glycine, leucine, and
RT alanine.";
RL Mol. Pharmacol. 74:1521-1532(2008).
RN [5]
RP SUBCELLULAR LOCATION, AND PH DEPENDENCE.
RX PubMed=19147495; DOI=10.1074/jbc.m806407200;
RA Zaia K.A., Reimer R.J.;
RT "Synaptic vesicle protein NTT4/XT1 (SLC6A17) catalyzes Na+-coupled neutral
RT amino acid transport.";
RL J. Biol. Chem. 284:8439-8448(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-665 AND SER-701, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Functions as a sodium-dependent vesicular transporter
CC selective for proline, glycine, leucine and alanine. In contrast to
CC other members of this neurotransmitter transporter family, does not
CC appear to be chloride-dependent. {ECO:0000269|PubMed:18768736}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.72 mM for glycine {ECO:0000269|PubMed:18768736};
CC KM=0.86 mM for proline {ECO:0000269|PubMed:18768736};
CC Vmax=199 pmol/min/mg enzyme for glycine
CC {ECO:0000269|PubMed:18768736};
CC Vmax=172 pmol/min/mg enzyme for proline
CC {ECO:0000269|PubMed:18768736};
CC pH dependence:
CC Optimum pH is 8.5. {ECO:0000269|PubMed:18768736,
CC ECO:0000269|PubMed:19147495};
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic
CC vesicle membrane {ECO:0000269|PubMed:18768736,
CC ECO:0000269|PubMed:19147495}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:18768736, ECO:0000269|PubMed:19147495}. Postsynapse
CC {ECO:0000250|UniProtKB:Q8BJI1}. Presynapse
CC {ECO:0000250|UniProtKB:Q8BJI1}. Note=Localizes at synaptic junctions
CC - at both pre- and post-synaptic sites - particularly in excitatory
CC glutamatergic terminals. {ECO:0000250|UniProtKB:Q8BJI1}.
CC -!- TISSUE SPECIFICITY: Found exclusively in the central nervous system and
CC is more abundant in the cerebellum and the cerebral cortex. Expressed
CC in PC-12 cell line. {ECO:0000269|PubMed:16125675,
CC ECO:0000269|PubMed:18768736}.
CC -!- SIMILARITY: Belongs to the sodium:neurotransmitter symporter (SNF) (TC
CC 2.A.22) family. SLC6A17 subfamily. {ECO:0000305}.
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DR EMBL; L06434; AAB24776.1; -; mRNA.
DR EMBL; S68944; AAC60673.1; -; mRNA.
DR PIR; I56506; I56506.
DR PIR; S27043; S27043.
DR RefSeq; NP_001028251.1; NM_001033079.1.
DR AlphaFoldDB; P31662; -.
DR SMR; P31662; -.
DR BioGRID; 565981; 1.
DR STRING; 10116.ENSRNOP00000065179; -.
DR TCDB; 2.A.22.6.2; the neurotransmitter:sodium symporter (nss) family.
DR GlyGen; P31662; 2 sites.
DR iPTMnet; P31662; -.
DR PhosphoSitePlus; P31662; -.
DR SwissPalm; P31662; -.
DR PaxDb; P31662; -.
DR PRIDE; P31662; -.
DR Ensembl; ENSRNOT00000075653; ENSRNOP00000065179; ENSRNOG00000050090.
DR GeneID; 613226; -.
DR KEGG; rno:613226; -.
DR CTD; 388662; -.
DR RGD; 1587185; Slc6a17.
DR eggNOG; KOG3659; Eukaryota.
DR GeneTree; ENSGT00940000156542; -.
DR HOGENOM; CLU_006855_7_1_1; -.
DR InParanoid; P31662; -.
DR OMA; WSECPIV; -.
DR OrthoDB; 250396at2759; -.
DR PhylomeDB; P31662; -.
DR PRO; PR:P31662; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000050090; Expressed in frontal cortex and 15 other tissues.
DR Genevisible; P31662; RN.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0098982; C:GABA-ergic synapse; IDA:SynGO.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
DR GO; GO:0030285; C:integral component of synaptic vesicle membrane; IDA:SynGO.
DR GO; GO:0031224; C:intrinsic component of membrane; IBA:GO_Central.
DR GO; GO:0098794; C:postsynapse; IEA:UniProtKB-SubCell.
DR GO; GO:0008021; C:synaptic vesicle; IDA:UniProtKB.
DR GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR GO; GO:0032328; P:alanine transport; IDA:UniProtKB.
DR GO; GO:0007420; P:brain development; ISS:UniProtKB.
DR GO; GO:0015816; P:glycine transport; IDA:UniProtKB.
DR GO; GO:0015820; P:leucine transport; IDA:UniProtKB.
DR GO; GO:0006836; P:neurotransmitter transport; IEA:UniProtKB-KW.
DR GO; GO:0015804; P:neutral amino acid transport; IDA:UniProtKB.
DR GO; GO:0015824; P:proline transport; IDA:UniProtKB.
DR GO; GO:0035725; P:sodium ion transmembrane transport; IBA:GO_Central.
DR InterPro; IPR000175; Na/ntran_symport.
DR InterPro; IPR002438; Neutral_aa_SLC6.
DR InterPro; IPR037272; SNS_sf.
DR PANTHER; PTHR11616; PTHR11616; 1.
DR Pfam; PF00209; SNF; 1.
DR PRINTS; PR00176; NANEUSMPORT.
DR PRINTS; PR01206; ORPHTRNSPORT.
DR SUPFAM; SSF161070; SSF161070; 1.
DR PROSITE; PS00610; NA_NEUROTRAN_SYMP_1; 1.
DR PROSITE; PS00754; NA_NEUROTRAN_SYMP_2; 1.
DR PROSITE; PS50267; NA_NEUROTRAN_SYMP_3; 1.
PE 1: Evidence at protein level;
KW Cell projection; Cytoplasmic vesicle; Glycoprotein; Membrane;
KW Neurotransmitter transport; Phosphoprotein; Reference proteome; Symport;
KW Synapse; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..727
FT /note="Sodium-dependent neutral amino acid transporter
FT SLC6A17"
FT /id="PRO_0000214805"
FT TOPO_DOM 1..68
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 69..89
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 90..96
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 97..116
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 117..140
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 141..161
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 162..224
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 225..243
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 244..251
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 252..269
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 270..304
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 305..322
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 323..333
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 334..355
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 356..451
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 452..471
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 472..494
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 495..513
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 514..528
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 529..549
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 550..569
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 570..591
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 592..618
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 619..641
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 642..727
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 680..727
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 693..712
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BJI1"
FT MOD_RES 20
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BJI1"
FT MOD_RES 377
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q8BJI1"
FT MOD_RES 665
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 701
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CARBOHYD 186
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 393
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 261
FT /note="Y -> C (in Ref. 2; AAC60673)"
FT /evidence="ECO:0000305"
FT CONFLICT 499
FT /note="G -> S (in Ref. 2; AAC60673)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 727 AA; 81055 MW; C676048C0A6BDF7C CRC64;
MPKNSKVTQR EHSNEHVTES VADLLALEEP VDYKQSVLNV AGETGGKQKV AEEELDAEDR
PAWNSKLQYI LAQIGFSVGL GNIWRFPYLC QKNGGGAYLV PYLVLLIIIG IPLFFLELAV
GQRIRRGSIG VWHYVCPRLG GIGFSSCIVC LFVGLYYNVI IGWSVFYFFK SFQYPLPWSE
CPVIRNGTVA VVEPECEKSS ATTYFWYREA LDISNSISES GGLNWKMTVC LLVAWSIVGM
AVVKGIQSSG KVMYFSSLFP YVVLACFLVR GLLLRGAVDG ILHMFTPKLD KMLDPQVWRE
AATQVFFALG LGFGGVIAFS SYNKQDNNCH FDAALVSFIN FFTSVLATLV VFAVLGFKAN
IMNEKCVVEN AEKILGYLNS NVLSRDLIPP HVNFSHLTTK DYSEMYNVIM TVKEKQFSAL
GLDPCLLEDE LDKSVQGTGL AFIAFTEAMT HFPASPFWSV MFFLMLINLG LGSMIGTMAG
ITTPIIDTFK VPKEMFTVGC CVFAFFVGLL FVQRSGNYFV TMFDDYSATL PLTVIVILEN
IAVAWIYGTK KFMQELTEML GFRPYRFYFY MWKFVSPLCM AVLTTASIIQ LGVSPPGYSA
WIKEEAAERY LYFPNWAMAL LITLIAVATL PIPVVFILRH FHLLSDGSNT LSVSYKKGRM
MKDISNLEEN DETRFILSKV PSEAPSPMPT HRSYLGPGST SPLESSSHPN GRYGSGYLLA
STPESEL
