S620A_MOUSE
ID S620A_MOUSE Reviewed; 592 AA.
AC Q8VDB9; Q3USE2;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Sodium- and chloride-dependent transporter XTRP3A;
DE AltName: Full=IMINO-B;
DE AltName: Full=Solute carrier family 6 member 20A;
DE AltName: Full=X transporter protein 3 similar 1;
GN Name=Slc6a20a {ECO:0000312|MGI:MGI:2143217};
GN Synonyms=Slc6a20 {ECO:0000312|EMBL:CAI80736.1},
GN Xt3s1 {ECO:0000303|PubMed:15689184}, Xtm3s1 {ECO:0000303|PubMed:12461651},
GN Xtrp3s1 {ECO:0000312|EMBL:CAD20989.1, ECO:0000312|MGI:MGI:2143217};
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] {ECO:0000312|EMBL:CAD20989.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ {ECO:0000312|EMBL:CAD20989.1};
RX PubMed=12461651; DOI=10.1007/s00335-002-3037-y;
RA Kiss H., Darai E., Kiss C., Kost-Alimova M., Klein G., Dumanski J.P.,
RA Imreh S.;
RT "Comparative human/murine sequence analysis of the common eliminated region
RT 1 from human 3p21.3.";
RL Mamm. Genome 13:646-655(2002).
RN [2] {ECO:0000305, ECO:0000312|EMBL:CAI80736.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:CAI80736.1};
RX PubMed=15689184; DOI=10.1042/bj20050100;
RA Kowalczuk S., Broeer A., Munzinger M., Tietze N., Klingel K., Broeer S.;
RT "Molecular cloning of the mouse IMINO system: an Na(+)- and Cl(-)-dependent
RT proline transporter.";
RL Biochem. J. 386:417-422(2005).
RN [3] {ECO:0000312|EMBL:BAE24391.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAE24391.1};
RC TISSUE=Medulla oblongata {ECO:0000312|EMBL:BAE24391.1};
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 [4] {ECO:0000312|EMBL:AAI18934.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [5] {ECO:0000305}
RP SUBCELLULAR LOCATION.
RX PubMed=16174864; DOI=10.1152/ajprenal.00286.2005;
RA Romeo E., Dave M.H., Bacic D., Ristic Z., Camargo S.M.R., Loffing J.,
RA Wagner C.A., Verrey F.;
RT "Luminal kidney and intestine SLC6 amino acid transporters of B0AT-cluster
RT and their tissue distribution in Mus musculus.";
RL Am. J. Physiol. 290:F376-F383(2006).
CC -!- FUNCTION: Mediates the calcium-dependent uptake of imino acids such as
CC L-proline, N-methyl-L-proline and pipecolate as well as N-methylated
CC amino acids. {ECO:0000269|PubMed:15689184}.
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000269|PubMed:16174864}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:16174864}. Note=Located in the apical brush border
CC membrane of kidney proximal tubule cells and in the apical membrane of
CC enterocytes lining the intestinal villi. {ECO:0000269|PubMed:16174864}.
CC -!- TISSUE SPECIFICITY: Expressed in brain, kidney, small intestine,
CC thymus, spleen and lung. In the brain, expressed in cerebellum, cortex
CC and brain stem. Not detected in liver, muscle or heart.
CC {ECO:0000269|PubMed:15689184}.
CC -!- SIMILARITY: Belongs to the sodium:neurotransmitter symporter (SNF) (TC
CC 2.A.22) family. SLC6A20 subfamily. {ECO:0000305}.
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DR EMBL; AJ428067; CAD20989.1; -; mRNA.
DR EMBL; AJ964961; CAI80736.1; -; mRNA.
DR EMBL; AK140445; BAE24391.1; -; mRNA.
DR EMBL; BC118933; AAI18934.1; -; mRNA.
DR CCDS; CCDS40817.1; -.
DR RefSeq; NP_631881.1; NM_139142.2.
DR AlphaFoldDB; Q8VDB9; -.
DR SMR; Q8VDB9; -.
DR STRING; 10090.ENSMUSP00000047690; -.
DR GlyGen; Q8VDB9; 1 site.
DR iPTMnet; Q8VDB9; -.
DR PhosphoSitePlus; Q8VDB9; -.
DR jPOST; Q8VDB9; -.
DR MaxQB; Q8VDB9; -.
DR PaxDb; Q8VDB9; -.
DR PRIDE; Q8VDB9; -.
DR ProteomicsDB; 253387; -.
DR DNASU; 102680; -.
DR Ensembl; ENSMUST00000040960; ENSMUSP00000047690; ENSMUSG00000036814.
DR GeneID; 102680; -.
DR KEGG; mmu:102680; -.
DR UCSC; uc009sgk.1; mouse.
DR CTD; 102680; -.
DR MGI; MGI:2143217; Slc6a20a.
DR VEuPathDB; HostDB:ENSMUSG00000036814; -.
DR eggNOG; KOG3659; Eukaryota.
DR GeneTree; ENSGT00940000155873; -.
DR HOGENOM; CLU_006855_7_2_1; -.
DR InParanoid; Q8VDB9; -.
DR OMA; FNNINHR; -.
DR OrthoDB; 547281at2759; -.
DR PhylomeDB; Q8VDB9; -.
DR TreeFam; TF343812; -.
DR Reactome; R-MMU-352230; Amino acid transport across the plasma membrane.
DR Reactome; R-MMU-442660; Na+/Cl- dependent neurotransmitter transporters.
DR BioGRID-ORCS; 102680; 5 hits in 74 CRISPR screens.
DR ChiTaRS; Slc6a20a; mouse.
DR PRO; PR:Q8VDB9; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q8VDB9; protein.
DR Bgee; ENSMUSG00000036814; Expressed in small intestine Peyer's patch and 120 other tissues.
DR ExpressionAtlas; Q8VDB9; baseline and differential.
DR Genevisible; Q8VDB9; MM.
DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0015171; F:amino acid transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0015199; F:amino-acid betaine transmembrane transporter activity; ISO:MGI.
DR GO; GO:0015193; F:L-proline transmembrane transporter activity; IDA:MGI.
DR GO; GO:0015175; F:neutral amino acid transmembrane transporter activity; IDA:ARUK-UCL.
DR GO; GO:0005298; F:proline:sodium symporter activity; ISO:MGI.
DR GO; GO:0089718; P:amino acid import across plasma membrane; ISO:MGI.
DR GO; GO:0006865; P:amino acid transport; IDA:UniProtKB.
DR GO; GO:0015838; P:amino-acid betaine transport; IDA:MGI.
DR GO; GO:0015816; P:glycine transport; ISO:MGI.
DR GO; GO:1904271; P:L-proline import across plasma membrane; ISO:MGI.
DR GO; GO:1905647; P:proline import across plasma membrane; IDA:ARUK-UCL.
DR GO; GO:0035524; P:proline transmembrane transport; IDA:MGI.
DR GO; GO:0015824; P:proline transport; ISO:MGI.
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 2: Evidence at transcript level;
KW Amino-acid transport; Cell membrane; Glycoprotein; Membrane;
KW Reference proteome; Symport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..592
FT /note="Sodium- and chloride-dependent transporter XTRP3A"
FT /id="PRO_0000343522"
FT TOPO_DOM 1..7
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 8..28
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 29..42
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 43..63
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 64..79
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 80..100
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 101..165
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 166..186
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 187..194
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 195..215
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 216..241
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 242..262
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 263..276
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 277..297
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 298..389
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 390..410
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 411..431
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 432..452
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 453..465
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 466..486
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 487..504
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 505..525
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 526..554
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 555..575
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 576..592
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 131
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 58
FT /note="L -> P (in Ref. 3; BAE24391)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 592 AA; 66178 MW; 547B9F8C0B7A99AA CRC64;
MEKARPQWGH PLQFVFACIS YAVGLGNVWR FPYLCQMYGG GSFLVPYIIM LIVEGMPLLY
LELAVGQRMR QGSIGAWRTI SPYLSGVGVA SVVVSFFLSM YYNVINAWGF WYLFHSFQDP
LPWSVCPLNS NHTGYDEECE KASSTQYFWY RKTLNISPSI QENGGVQWEP ALCLTLAWLM
VYLCILRGTE STGKVVYFTA SMPYCVLIIY LVRGLTLHGA TNGLMYMFTP KMEQLANPKA
WINAATQIFF SLGLGFGSLI AFASYNEPSN NCQKHAIIVS IINSSTSIFA SIVTFSIYGF
KATFNYENCL NKVILLLTNS FDLEDGFLTV SNLEEVKNYL ASTYPNKYSE VFPHIRNCSL
ESELDTAVQG TGLAFIVYTE AIKNMEVSQL WSVLYFFMLL MLGIGSMLGN TAAILTPLTD
SKVISSYLPK EAISGLVCLI NCAVGMVFTM EAGNYWFDIF NDYAATLSLL LIVLVETIAV
CYVYGLKRFE SDLRAMTGRT LSWYWKVMWA FVSPLLIVGL FIFYLSDYIL TGTLQYQAWD
ATQGQLVTKD YPPHALAVIG LLVASSTMCI PLVALGTFIR NRLKRGGSAP VA
