S620B_MOUSE
ID S620B_MOUSE Reviewed; 635 AA.
AC O88575; E9QNK3; Q3TP52; Q91WT6;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Sodium- and chloride-dependent transporter XTRP3B;
DE AltName: Full=IMINO-K;
DE AltName: Full=Solute carrier family 6 member 20B;
GN Name=Slc6a20b; Synonyms=Slc6a20, Xt3, Xtrp3;
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], AND TISSUE SPECIFICITY.
RC TISSUE=Kidney;
RX PubMed=9932288;
RA Nash S.R., Giros B., Kingsmore S.F., Kim K.M., El-Mestikawy S., Dong Q.,
RA Fumagalli F., Seldin M.F., Caron M.G.;
RT "Cloning, gene structure, and genomic localization of an orphan transporter
RT from mouse kidney with six alternatively-spliced isoforms.";
RL Recept. Channels 6:113-128(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Kidney;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Kidney;
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]
RP FUNCTION, AND TISSUE SPECIFICITY.
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 [6]
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).
RN [7]
RP INTERACTION WITH CLTRN.
RX PubMed=17167413; DOI=10.1038/nature05475;
RA Danilczyk U., Sarao R., Remy C., Benabbas C., Stange G., Richter A.,
RA Arya S., Pospisilik J.A., Singer D., Camargo S.M., Makrides V., Ramadan T.,
RA Verrey F., Wagner C.A., Penninger J.M.;
RT "Essential role for collectrin in renal amino acid transport.";
RL Nature 444:1088-1091(2006).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney;
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).
CC -!- FUNCTION: Does not show transporter activity with a range of tested
CC amino acids including proline, glutamine, glutamic acid, leucine,
CC alanine, histidine, glycine and arginine.
CC {ECO:0000269|PubMed:15689184}.
CC -!- SUBUNIT: Interacts with CLTRN. {ECO:0000269|PubMed:17167413}.
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.
CC -!- TISSUE SPECIFICITY: Detected only in kidney and lung.
CC {ECO:0000269|PubMed:15689184, ECO:0000269|PubMed:9932288}.
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; AF075261; AAC27756.1; -; mRNA.
DR EMBL; AK144038; BAE25668.1; -; mRNA.
DR EMBL; AK164706; BAE37885.1; -; mRNA.
DR EMBL; AC132852; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC013484; AAH13484.1; -; mRNA.
DR CCDS; CCDS23661.1; -.
DR RefSeq; NP_035861.2; NM_011731.3.
DR AlphaFoldDB; O88575; -.
DR SMR; O88575; -.
DR DIP; DIP-60422N; -.
DR IntAct; O88575; 1.
DR STRING; 10090.ENSMUSP00000026273; -.
DR GlyGen; O88575; 2 sites.
DR iPTMnet; O88575; -.
DR PhosphoSitePlus; O88575; -.
DR jPOST; O88575; -.
DR MaxQB; O88575; -.
DR PaxDb; O88575; -.
DR PRIDE; O88575; -.
DR ProteomicsDB; 256907; -.
DR DNASU; 22599; -.
DR GeneID; 22599; -.
DR KEGG; mmu:22599; -.
DR UCSC; uc009sgi.2; mouse.
DR CTD; 22599; -.
DR MGI; MGI:1336891; Slc6a20b.
DR VEuPathDB; HostDB:ENSMUSG00000025243; -.
DR eggNOG; KOG3659; Eukaryota.
DR HOGENOM; CLU_006855_7_2_1; -.
DR InParanoid; O88575; -.
DR OrthoDB; 547281at2759; -.
DR PhylomeDB; O88575; -.
DR TreeFam; TF343812; -.
DR BioGRID-ORCS; 22599; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Slc6a20b; mouse.
DR PRO; PR:O88575; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; O88575; protein.
DR ExpressionAtlas; O88575; baseline and differential.
DR Genevisible; O88575; MM.
DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR GO; GO:0031526; C:brush border membrane; IDA:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0015171; F:amino acid transmembrane transporter activity; ISO:MGI.
DR GO; GO:0015199; F:amino-acid betaine transmembrane transporter activity; ISO:MGI.
DR GO; GO:0015193; F:L-proline transmembrane transporter activity; ISO:MGI.
DR GO; GO:0015175; F:neutral amino acid transmembrane transporter activity; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0015838; P:amino-acid betaine transport; ISO: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; ISO: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 1: Evidence at protein level;
KW Cell membrane; Glycoprotein; Membrane; Reference proteome; Symport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..635
FT /note="Sodium- and chloride-dependent transporter XTRP3B"
FT /id="PRO_0000214813"
FT TOPO_DOM 1..56
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 57..77
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 78..85
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 86..106
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 107..127
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 128..148
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 149..208
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 209..229
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 230..237
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 238..258
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 259..284
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 285..305
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 306..319
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 320..340
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 341..432
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 433..453
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 454..474
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 475..495
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 496..508
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 509..529
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 530..547
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 548..568
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 569..597
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 598..618
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 619..635
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 174
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 400
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 85
FT /note="N -> S (in Ref. 1; AAC27756, 2; BAE25668/BAE37885
FT and 4; AAH13484)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 635 AA; 70687 MW; 465AD54AA807EBE3 CRC64;
MESPSAHAVS LPEDEELQPW GGAGGPGQHP GRPRSTECAH PGVVEKVRPK WDNPLQFLLV
CISYAVGLGN VWRFPYLCQM YGGGNFLVPY IIMLIVEGMP LLYLELAVGQ RMRQGSIGAW
RTISPYLSGV GIASLVVSFL ASVYFNVINT WALWYLFHSF QDPLPWSVCP LNSNHTGYDE
ECEKASSTQY FWYRKTLNIS PSIQENGGVQ WEPALCLTLA WLMVYLCILR GTESTGKVVY
FTTSLPYFVL IIYLVRGLTL HGATNGLAYM FTPKIEQLAN PKAWINAATQ IFFSLGLGCG
GLIAFASYNE PSNDCQKHAL IVSVINSTTA IFSSIVTFSI YGFKATFNYE NCLNKVILLL
TNSFDLEDGF LTVSNLEEVK NYLASTYPNK YSEVFPHIRN CSLESELDTA VQGTGLAFIV
YTEAIKNMEV SQLWSVLYFF MLLTLGMGSM VGTGTAILTP LTDSKIISSY LPKEAISGLV
CLLNCAIGMV FTMEAGNYWF DLFNDYTATL SLLLIVLVET IAVCYVYGLK RFESDLRAMT
GRTLSWYWKV MWAFVSPLLI VGLFIFYLSD YILTGTLQYQ AWDATQGHVV TKDYPTYALA
VIGLLVASST MCIPLVALGT FVTRHFKIRE QFSAA
