S6A19_MOUSE
ID S6A19_MOUSE Reviewed; 634 AA.
AC Q9D687;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Sodium-dependent neutral amino acid transporter B(0)AT1;
DE AltName: Full=Solute carrier family 6 member 19;
DE AltName: Full=System B(0) neutral amino acid transporter AT1;
GN Name=Slc6a19; Synonyms=B0at1, Xt3 {ECO:0000303|PubMed:17167413};
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], FUNCTION, TRANSPORTER ACTIVITY, TISSUE
RP SPECIFICITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=NMRI; TISSUE=Kidney;
RX PubMed=15044460; DOI=10.1074/jbc.m400904200;
RA Broeer A., Klingel K., Kowalczuk S., Rasko J.E.J., Cavanaugh J.A.,
RA Broeer S.;
RT "Molecular cloning of mouse amino acid transport system B(0), a neutral
RT amino acid transporter related to Hartnup disorder.";
RL J. Biol. Chem. 279:24467-24476(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Skin;
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 CHARACTERIZATION.
RX PubMed=15804236; DOI=10.1042/bj20050083;
RA Boehmer C., Broeer A., Munzinger M., Kowalczuk S., Rasko J.E.J., Lang F.,
RA Broeer S.;
RT "Characterization of mouse amino acid transporter B(0)AT1 (Slc6a19).";
RL Biochem. J. 389:745-751(2005).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17 AND SER-627, AND
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).
RN [5]
RP INTERACTION WITH CLTRN, FUNCTION, TRANSPORTER ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
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 [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=18424768; DOI=10.1096/fj.08-107300;
RA Kowalczuk S., Broeer A., Tietze N., Vanslambrouck J.M., Rasko J.E.,
RA Broeer S.;
RT "A protein complex in the brush-border membrane explains a Hartnup disorder
RT allele.";
RL FASEB J. 22:2880-2887(2008).
RN [7]
RP FUNCTION, INTERACTION WITH ACE2, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=19185582; DOI=10.1053/j.gastro.2008.10.055;
RA Camargo S.M., Singer D., Makrides V., Huggel K., Pos K.M., Wagner C.A.,
RA Kuba K., Danilczyk U., Skovby F., Kleta R., Penninger J.M., Verrey F.;
RT "Tissue-specific amino acid transporter partners ACE2 and collectrin
RT differentially interact with hartnup mutations.";
RL Gastroenterology 136:872-882(2009).
RN [8]
RP DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, FUNCTION, AND TISSUE
RP SPECIFICITY.
RX PubMed=21636576; DOI=10.1074/jbc.m111.241323;
RA Broeer A., Juelich T., Vanslambrouck J.M., Tietze N., Solomon P.S.,
RA Holst J., Bailey C.G., Rasko J.E., Broeer S.;
RT "Impaired nutrient signaling and body weight control in a Na+ neutral amino
RT acid cotransporter (Slc6a19)-deficient mouse.";
RL J. Biol. Chem. 286:26638-26651(2011).
RN [9]
RP INTERACTION WITH ANPEP, AND TISSUE SPECIFICITY.
RX PubMed=22677001; DOI=10.1042/bj20120307;
RA Fairweather S.J., Broeer A., O'Mara M.L., Broeer S.;
RT "Intestinal peptidases form functional complexes with the neutral amino
RT acid transporter B(0)AT1.";
RL Biochem. J. 446:135-148(2012).
RN [10]
RP FUNCTION.
RX PubMed=26240152; DOI=10.1074/jbc.m115.648519;
RA Fairweather S.J., Broeer A., Subramanian N., Tumer E., Cheng Q.,
RA Schmoll D., O'Mara M.L., Broeer S.;
RT "Molecular basis for the interaction of the mammalian amino acid
RT transporters B0AT1 and B0AT3 with their ancillary protein collectrin.";
RL J. Biol. Chem. 290:24308-24325(2015).
CC -!- FUNCTION: Transporter that mediates resorption of neutral amino acids
CC across the apical membrane of renal and intestinal epithelial cells
CC (PubMed:18424768, PubMed:17167413, PubMed:26240152, PubMed:19185582,
CC PubMed:15044460). This uptake is sodium-dependent and chloride-
CC independent (PubMed:18424768, PubMed:19185582, PubMed:15044460,
CC PubMed:21636576, PubMed:26240152). Requires CLTRN in kidney or ACE2 in
CC intestine for cell surface expression and amino acid transporter
CC activity (PubMed:18424768, PubMed:17167413, PubMed:19185582,
CC PubMed:22677001). {ECO:0000269|PubMed:15044460,
CC ECO:0000269|PubMed:17167413, ECO:0000269|PubMed:18424768,
CC ECO:0000269|PubMed:19185582, ECO:0000269|PubMed:21636576,
CC ECO:0000269|PubMed:22677001, ECO:0000269|PubMed:26240152}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-alanine(in) + Na(+)(in) = L-alanine(out) + Na(+)(out);
CC Xref=Rhea:RHEA:29283, ChEBI:CHEBI:29101, ChEBI:CHEBI:57972;
CC Evidence={ECO:0000250|UniProtKB:Q695T7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-cysteine(in) + Na(+)(in) = L-cysteine(out) + Na(+)(out);
CC Xref=Rhea:RHEA:68232, ChEBI:CHEBI:29101, ChEBI:CHEBI:35235;
CC Evidence={ECO:0000250|UniProtKB:Q695T7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-glutamine(in) + Na(+)(in) = L-glutamine(out) + Na(+)(out);
CC Xref=Rhea:RHEA:68236, ChEBI:CHEBI:29101, ChEBI:CHEBI:58359;
CC Evidence={ECO:0000269|PubMed:15044460};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glycine(in) + Na(+)(in) = glycine(out) + Na(+)(out);
CC Xref=Rhea:RHEA:68228, ChEBI:CHEBI:29101, ChEBI:CHEBI:57305;
CC Evidence={ECO:0000250|UniProtKB:Q695T7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-isoleucine(in) + Na(+)(in) = L-isoleucine(out) + Na(+)(out);
CC Xref=Rhea:RHEA:29275, ChEBI:CHEBI:29101, ChEBI:CHEBI:58045;
CC Evidence={ECO:0000269|PubMed:15044460, ECO:0000269|PubMed:17167413};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-leucine(in) + Na(+)(in) = L-leucine(out) + Na(+)(out);
CC Xref=Rhea:RHEA:29263, ChEBI:CHEBI:29101, ChEBI:CHEBI:57427;
CC Evidence={ECO:0000269|PubMed:15044460};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-methionine(in) + Na(+)(in) = L-methionine(out) + Na(+)(out);
CC Xref=Rhea:RHEA:68240, ChEBI:CHEBI:29101, ChEBI:CHEBI:57844;
CC Evidence={ECO:0000250|UniProtKB:Q695T7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-phenylalanine(in) + Na(+)(in) = L-phenylalanine(out) +
CC Na(+)(out); Xref=Rhea:RHEA:68244, ChEBI:CHEBI:29101,
CC ChEBI:CHEBI:58095; Evidence={ECO:0000269|PubMed:15044460};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-serine(in) + Na(+)(in) = L-serine(out) + Na(+)(out);
CC Xref=Rhea:RHEA:29575, ChEBI:CHEBI:29101, ChEBI:CHEBI:33384;
CC Evidence={ECO:0000250|UniProtKB:Q695T7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-tryptophan(in) + Na(+)(in) = L-tryptophan(out) + Na(+)(out);
CC Xref=Rhea:RHEA:68252, ChEBI:CHEBI:29101, ChEBI:CHEBI:57912;
CC Evidence={ECO:0000250|UniProtKB:Q695T7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-tyrosine(in) + Na(+)(in) = L-tyrosine(out) + Na(+)(out);
CC Xref=Rhea:RHEA:68248, ChEBI:CHEBI:29101, ChEBI:CHEBI:58315;
CC Evidence={ECO:0000250|UniProtKB:Q695T7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-valine(in) + Na(+)(in) = L-valine(out) + Na(+)(out);
CC Xref=Rhea:RHEA:29267, ChEBI:CHEBI:29101, ChEBI:CHEBI:57762;
CC Evidence={ECO:0000250|UniProtKB:Q695T7};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=630 uM for leucine {ECO:0000269|PubMed:15044460};
CC KM=522 uM for glutamine {ECO:0000269|PubMed:15044460};
CC KM=589 uM for phenylalanine {ECO:0000269|PubMed:15044460};
CC KM=0.99 mM for L-isoleucine {ECO:0000269|PubMed:17167413};
CC KM=0.78 mM for L-isoleucine (in presence of CLTRN)
CC {ECO:0000269|PubMed:17167413};
CC Note=Vmax for leucine is about twice the value of Vmax for glutamine,
CC and three times the value of Vmax for phenylalanine. KM and Vmax
CC values are complex functions of the concentration of substrate (L-
CC amino acid) and cosubstrate (Na(+)) and the membrane potential.;
CC -!- SUBUNIT: Interacts in a tissue-specific manner with ACE2 in small
CC intestine and with CLTRN in the kidney (PubMed:19185582,
CC PubMed:17167413). Interacts with CLTRN; this interaction is required
CC for trafficking of SLC6A19 to the plasma membrane and for its catalytic
CC activation in kidneys (PubMed:17167413). Interacts with ACE2; this
CC interaction is required for trafficking of SLC6A19 to the plasma
CC membrane and for its catalytic activation in intestine
CC (PubMed:19185582). Interacts with ANPEP; the interaction positively
CC regulates its amino acid transporter activity (PubMed:22677001).
CC {ECO:0000269|PubMed:17167413, ECO:0000269|PubMed:19185582,
CC ECO:0000269|PubMed:22677001}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18424768};
CC Multi-pass membrane protein {ECO:0000255}. Note=Localizes in small
CC intestine brush border membranes (at protein level).
CC {ECO:0000269|PubMed:19185582}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in kidney and small
CC intestine (at protein level) (PubMed:15044460, PubMed:19185582).
CC Expressed in the intestinal brush border (at protein level)
CC (PubMed:22677001). Expression not observed in other organs, such as
CC lung, skeletal muscle, brain, liver and pancreas. In kidney, expression
CC is localized in the renal cortex but not in the medulla. Substantial
CC amounts of expression in the proximal tubules. The distal nephron
CC segments and the glomeruli are consistently negative. In the small
CC intestine, expression is exclusively localized in villus enterocytes.
CC High resolution of the hybridization-positive villi reveals a gradient
CC of expression with the highest levels in apical cells. Not detected in
CC crypt cells or in any other cell types of the small intestine.
CC {ECO:0000269|PubMed:15044460, ECO:0000269|PubMed:19185582,
CC ECO:0000269|PubMed:22677001}.
CC -!- DISRUPTION PHENOTYPE: Deficient mice exhibit reduced growth, impaired
CC body weight control, insulin response and amino acid absorption and
CC excretion. {ECO:0000269|PubMed:21636576}.
CC -!- SIMILARITY: Belongs to the sodium:neurotransmitter symporter (SNF) (TC
CC 2.A.22) family. SLC6A19 subfamily. {ECO:0000305}.
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DR EMBL; AJ633679; CAG17898.1; -; mRNA.
DR EMBL; AK014544; BAB29422.1; -; mRNA.
DR EMBL; AK028784; BAC26119.1; -; mRNA.
DR CCDS; CCDS26634.1; -.
DR RefSeq; NP_083154.1; NM_028878.3.
DR AlphaFoldDB; Q9D687; -.
DR SMR; Q9D687; -.
DR DIP; DIP-38102N; -.
DR IntAct; Q9D687; 2.
DR STRING; 10090.ENSMUSP00000022048; -.
DR TCDB; 2.A.22.6.3; the neurotransmitter:sodium symporter (nss) family.
DR GlyGen; Q9D687; 6 sites.
DR iPTMnet; Q9D687; -.
DR PhosphoSitePlus; Q9D687; -.
DR jPOST; Q9D687; -.
DR MaxQB; Q9D687; -.
DR PaxDb; Q9D687; -.
DR PRIDE; Q9D687; -.
DR ProteomicsDB; 260808; -.
DR Antibodypedia; 22313; 75 antibodies from 22 providers.
DR DNASU; 74338; -.
DR Ensembl; ENSMUST00000022048; ENSMUSP00000022048; ENSMUSG00000021565.
DR GeneID; 74338; -.
DR KEGG; mmu:74338; -.
DR UCSC; uc007rdy.1; mouse.
DR CTD; 340024; -.
DR MGI; MGI:1921588; Slc6a19.
DR VEuPathDB; HostDB:ENSMUSG00000021565; -.
DR eggNOG; KOG3659; Eukaryota.
DR GeneTree; ENSGT00940000154896; -.
DR HOGENOM; CLU_006855_7_2_1; -.
DR InParanoid; Q9D687; -.
DR OMA; SAKIQMS; -.
DR OrthoDB; 547281at2759; -.
DR PhylomeDB; Q9D687; -.
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; 74338; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Slc6a19; mouse.
DR PRO; PR:Q9D687; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q9D687; protein.
DR Bgee; ENSMUSG00000021565; Expressed in small intestine Peyer's patch and 64 other tissues.
DR ExpressionAtlas; Q9D687; baseline and differential.
DR Genevisible; Q9D687; MM.
DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR GO; GO:0031526; C:brush border membrane; IDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISS:MGI.
DR GO; GO:0015175; F:neutral amino acid transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR GO; GO:0015804; P:neutral amino acid transport; IDA:MGI.
DR GO; GO:0007584; P:response to nutrient; IEA:Ensembl.
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; PS50267; NA_NEUROTRAN_SYMP_3; 1.
PE 1: Evidence at protein level;
KW Amino-acid transport; Cell membrane; Glycoprotein; Membrane;
KW Phosphoprotein; Reference proteome; Symport; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..634
FT /note="Sodium-dependent neutral amino acid transporter
FT B(0)AT1"
FT /id="PRO_0000214810"
FT TOPO_DOM 1..41
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 42..62
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 63..67
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 68..88
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 89..119
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 120..140
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 141..192
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 193..213
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 214..221
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 222..242
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 243..268
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 269..289
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 290..304
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 305..325
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 326..413
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 414..434
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 435..456
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 457..477
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 478..487
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 488..508
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 509..531
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 532..552
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 553..581
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 582..602
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 603..634
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 627
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 158
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 182
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 258
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 354
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 368
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 555
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 634 AA; 71367 MW; 433EB23C97E9FE5B CRC64;
MVRLVLPNPG LEERIPSLDE LEVIEKEEAG SRPKWDNKAQ YMLTCVGFCV GLGNVWRFPY
LCQSHGGGAF MIPFLILLVF EGIPLLYLEF AIGQRLRKGS MGVWSSIHPA LKGIGIASMF
VSFMVGLYYN TIIAWVMWYF FNSFQEPLPW SECPLNQNQT GYVEECAKSS SVDYFWYRET
LNISTSISDS GSIQWWILLC LTCAWSVLYV CIIRGIETTG KAVYITSTLP YVVLTIFLIR
GLTLKGATNG IVFLFTPNIT ELSNPNTWLD AGAQVFYSFS LAFGGLISFS SYNSVHNNCE
MDSVIVSVIN GFTSVYAATV VYSIIGFRAT ERFDDCVNTN ILTLINGFDL PEGNVTSENF
EAYQQWCNAT NPQAYAQLKF QTCDINSFLS EGVEGTGLAF IVFTEAITKM PVSPLWSVLF
FIMLFCLGLS SMFGNMEGVV VPLQDLNITP KKWPKELLTG LICLGTYLIA FIFTLNSGQY
WLSLLDSFAG SIPLLIIAFC EMFAVVYVYG VDRFNKDIEF MIGHKPNIFW QVTWRVVSPL
IMLVIFLFFF VIEVNKTLMY SIWDPNYEEF PKSQKIPYPN WVYAVVVTVA GVPCLSIPCF
AIYKFIRNCC QKSDDHHGLV NTLSTASVNG DLKN
