S6A17_MOUSE
ID S6A17_MOUSE Reviewed; 727 AA.
AC Q8BJI1; B2RUH5; Q8C057; Q8CGQ9;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 135.
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;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J;
RA Liu Q.-R., Uhl G.R.;
RT "Sodium and chloride dependent mouse orphan neurotransmitter transporter
RT NTT4 cDNA.";
RL Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Olfactory bulb, and Spinal ganglion;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain cortex;
RX PubMed=17114649; DOI=10.1074/mcp.m600046-mcp200;
RA Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B.,
RA Panse C., Schlapbach R., Mansuy I.M.;
RT "Qualitative and quantitative analyses of protein phosphorylation in naive
RT and stimulated mouse synaptosomal preparations.";
RL Mol. Cell. Proteomics 6:283-293(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-377, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=18034455; DOI=10.1021/pr0701254;
RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT "Large-scale identification and evolution indexing of tyrosine
RT phosphorylation sites from murine brain.";
RL J. Proteome Res. 7:311-318(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13; SER-20 AND SER-665, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND SUBCELLULAR LOCATION.
RX PubMed=25704603; DOI=10.1016/j.ajhg.2015.01.010;
RA Iqbal Z., Willemsen M.H., Papon M.A., Musante L., Benevento M., Hu H.,
RA Venselaar H., Wissink-Lindhout W.M., Vulto-van Silfhout A.T., Vissers L.E.,
RA de Brouwer A.P., Marouillat S., Wienker T.F., Ropers H.H., Kahrizi K.,
RA Nadif Kasri N., Najmabadi H., Laumonnier F., Kleefstra T., van Bokhoven H.;
RT "Homozygous SLC6A17 mutations cause autosomal-recessive intellectual
RT disability with progressive tremor, speech impairment, and behavioral
RT problems.";
RL Am. J. Hum. Genet. 96:386-396(2015).
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 (By similarity).
CC {ECO:0000250|UniProtKB:P31662}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic
CC vesicle membrane {ECO:0000250|UniProtKB:P31662}; Multi-pass membrane
CC protein {ECO:0000250|UniProtKB:P31662}. Postsynapse
CC {ECO:0000269|PubMed:25704603}. Presynapse
CC {ECO:0000269|PubMed:25704603}. Note=Localizes at synaptic junctions
CC - at both pre- and post-synaptic sites - particularly in excitatory
CC glutamatergic terminals. {ECO:0000269|PubMed:25704603}.
CC -!- TISSUE SPECIFICITY: Expressed in the brain. The strongest expression
CC levels in embryonic, postnatal, and adult stages are found in both
CC cortical and hippocampal tissues. {ECO:0000269|PubMed:25704603}.
CC -!- DEVELOPMENTAL STAGE: Expressed during embryonic brain development and
CC the highest levels are observed postnatally.
CC {ECO:0000269|PubMed:25704603}.
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; AY155578; AAN75010.1; -; mRNA.
DR EMBL; AK083807; BAC39024.1; -; mRNA.
DR EMBL; AK032262; BAC27785.1; -; mRNA.
DR EMBL; BC141148; AAI41149.1; -; mRNA.
DR EMBL; BC171962; AAI71962.1; -; mRNA.
DR CCDS; CCDS79998.1; -.
DR PIR; C46027; C46027.
DR RefSeq; NP_001280618.1; NM_001293689.1.
DR RefSeq; NP_758475.1; NM_172271.2.
DR RefSeq; XP_006501469.1; XM_006501406.2.
DR RefSeq; XP_006501470.1; XM_006501407.2.
DR AlphaFoldDB; Q8BJI1; -.
DR SMR; Q8BJI1; -.
DR STRING; 10090.ENSMUSP00000029499; -.
DR GlyConnect; 2722; 3 N-Linked glycans (2 sites).
DR GlyGen; Q8BJI1; 2 sites, 3 N-linked glycans (2 sites).
DR iPTMnet; Q8BJI1; -.
DR PhosphoSitePlus; Q8BJI1; -.
DR MaxQB; Q8BJI1; -.
DR PaxDb; Q8BJI1; -.
DR PeptideAtlas; Q8BJI1; -.
DR PRIDE; Q8BJI1; -.
DR ProteomicsDB; 255448; -.
DR Antibodypedia; 1942; 86 antibodies from 19 providers.
DR DNASU; 229706; -.
DR Ensembl; ENSMUST00000169449; ENSMUSP00000129379; ENSMUSG00000027894.
DR GeneID; 229706; -.
DR KEGG; mmu:229706; -.
DR UCSC; uc008qxb.1; mouse.
DR CTD; 388662; -.
DR MGI; MGI:2442535; Slc6a17.
DR VEuPathDB; HostDB:ENSMUSG00000027894; -.
DR eggNOG; KOG3659; Eukaryota.
DR GeneTree; ENSGT00940000156542; -.
DR InParanoid; Q8BJI1; -.
DR OrthoDB; 250396at2759; -.
DR PhylomeDB; Q8BJI1; -.
DR TreeFam; TF352709; -.
DR BioGRID-ORCS; 229706; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Slc6a17; mouse.
DR PRO; PR:Q8BJI1; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q8BJI1; protein.
DR Bgee; ENSMUSG00000027894; Expressed in primary visual cortex and 148 other tissues.
DR ExpressionAtlas; Q8BJI1; baseline and differential.
DR Genevisible; Q8BJI1; MM.
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; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
DR GO; GO:0030285; C:integral component of synaptic vesicle membrane; ISO:MGI.
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; ISS:UniProtKB.
DR GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR GO; GO:0032328; P:alanine transport; ISS:UniProtKB.
DR GO; GO:0007420; P:brain development; IDA:UniProtKB.
DR GO; GO:0015816; P:glycine transport; ISS:UniProtKB.
DR GO; GO:0015820; P:leucine transport; ISS:UniProtKB.
DR GO; GO:0006836; P:neurotransmitter transport; IEA:UniProtKB-KW.
DR GO; GO:0015804; P:neutral amino acid transport; ISS:UniProtKB.
DR GO; GO:0015824; P:proline transport; ISS: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_0000214804"
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..715
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 20
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 377
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18034455"
FT MOD_RES 665
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 701
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P31662"
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 434..436
FT /note="Missing (in Ref. 1; AAN75010)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 727 AA; 81071 MW; 0EAA2B192E77D7FA CRC64;
MPKNSKVTQR EHSNEHVTES VADLLALEEP VDYKQSVLNV AGETGGKQKV AEEELDTEDR
PAWNSKLQYI LAQIGFSVGL GNIWRFPYLC QKNGGGAYLV PYLVLLIIIG IPLFFLELAV
GQRIRRGSIG VWHYVCPRLG GIGFSSCIVC LFVGLYYNVI IGWSVFYFFK SFQYPLPWSE
CPVIRNGTVA VVEPECEKSS ATTYFWYREA LDISNSISES GGLNWKMTLC LLVAWSIVGM
AVVKGIQSSG KVMYFSSLFP YVVLACFLVR GLLLRGAVDG ILHMFTPKLD KMLDPQVWRE
AATQVFFALG LGFGGVIAFS SYNKQDNNCH FDAALVSFIN FFTSVLATLV VFAVLGFKAN
IMNEKCVVEN AEKILGYLNS NVLSRDLIPP HVNFSHLTTK DYSEMYSVIM TVKEKQFPAL
GLDPCLLEDE LDKSVQGTGL AFIAFTEAMT HFPASPFWSV MFFLMLINLG LGSMIGTMAG
ITTPIIDTFK VPKEMFTVGC CVFAFFVGLL FVQRSGNYFV TMFDDYSATL PLTVIVILEN
IAVAWIYGTK KFMQELTEML GFQPYRFYFY MWKFVSPLCM AVLTTASIIQ LGVSPPGYSA
WIKEEAAERY LYFPNWAMAL LITLIAVATL PIPVVFILRH FHLLSDGSNT LSVSYKKGRM
MKDISNLEEN DETRFILSKV PSEAPSPMPT HRSYLGPGST SPLDNSNNPN GRYGSGYLLA
STPESEL
