S4A4_MOUSE
ID S4A4_MOUSE Reviewed; 1079 AA.
AC O88343; Q3USE4; Q8BUG0; Q8QZR9; Q9R1C4;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Electrogenic sodium bicarbonate cotransporter 1;
DE Short=Sodium bicarbonate cotransporter;
DE AltName: Full=Na(+)/HCO3(-) cotransporter;
DE AltName: Full=Solute carrier family 4 member 4;
GN Name=Slc4a4; Synonyms=Nbc1, Nbce1;
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] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC TISSUE=Pancreas;
RX PubMed=9651366; DOI=10.1074/jbc.273.28.17689;
RA Abuladze N., Lee I., Newman D., Hwang J., Boorer K., Pushkin A., Kurtz I.;
RT "Molecular cloning, chromosomal localization, tissue distribution, and
RT functional expression of the human pancreatic sodium bicarbonate
RT cotransporter.";
RL J. Biol. Chem. 273:17689-17695(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=C57BL/6J; TISSUE=Duodenum;
RX PubMed=11171615; DOI=10.1152/ajpgi.2001.280.3.g332;
RA Praetorius J., Hager H., Nielsen S., Aalkjaer C., Friis U.G.,
RA Ainsworth M.A., Johansen T.;
RT "Molecular and functional evidence for electrogenic and electroneutral
RT Na(+)-HCO(3)(-) cotransporters in murine duodenum.";
RL Am. J. Physiol. 280:G332-G343(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-400 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Kidney, and Medulla oblongata;
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]
RP PROTEIN SEQUENCE OF 1-9; 60-67; 168-174; 323-331; 343-359; 607-618;
RP 753-766; 857-869 AND 935-943, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 382-1079.
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 [6]
RP GLYCOSYLATION.
RX PubMed=12604466; DOI=10.1152/ajprenal.00131.2002;
RA Choi I., Hu L., Rojas J.D., Schmitt B.M., Boron W.F.;
RT "Role of glycosylation in the renal electrogenic Na+-HCO3-cotransporter
RT (NBCe1).";
RL Am. J. Physiol. 284:F1199-F1206(2003).
RN [7]
RP REGULATION BY CAMP, AND TISSUE SPECIFICITY.
RX PubMed=12388213; DOI=10.1152/ajpgi.00209.2002;
RA Bachmann O., Rossmann H., Berger U.V., Colledge W.H., Ratcliff R.,
RA Evans M.J., Gregor M., Seidler U.;
RT "cAMP-mediated regulation of murine intestinal/pancreatic Na+/HCO3-
RT cotransporter subtype pNBC1.";
RL Am. J. Physiol. 284:G37-G45(2003).
RN [8]
RP TISSUE SPECIFICITY.
RX PubMed=12727194; DOI=10.1016/s0006-291x(03)00632-6;
RA Kim Y.-B., Yang B.H., Piao Z.G., Oh S.B., Kim J.S., Park K.;
RT "Expression of Na+/HCO3- cotransporter and its role in pH regulation in
RT mouse parotid acinar cells.";
RL Biochem. Biophys. Res. Commun. 304:593-598(2003).
RN [9]
RP INTERACTION WITH CA4.
RX PubMed=14567693; DOI=10.1021/bi0353124;
RA Alvarez B.V., Loiselle F.B., Supuran C.T., Schwartz G.J., Casey J.R.;
RT "Direct extracellular interaction between carbonic anhydrase IV and the
RT human NBC1 sodium/bicarbonate co-transporter.";
RL Biochemistry 42:12321-12329(2003).
RN [10]
RP INTERACTION WITH CA2.
RX PubMed=15218065; DOI=10.1113/jphysiol.2004.065110;
RA Pushkin A., Abuladze N., Gross E., Newman D., Tatishchev S., Lee I.,
RA Fedotoff O., Bondar G., Azimov R., Ngyuen M., Kurtz I.;
RT "Molecular mechanism of kNBC1-carbonic anhydrase II interaction in proximal
RT tubule cells.";
RL J. Physiol. (Lond.) 559:55-65(2004).
RN [11]
RP INTERACTION WITH AHCYL1.
RX PubMed=16769890; DOI=10.1073/pnas.0602250103;
RA Shirakabe K., Priori G., Yamada H., Ando H., Horita S., Fujita T.,
RA Fujimoto I., Mizutani A., Seki G., Mikoshiba K.;
RT "IRBIT, an inositol 1,4,5-trisphosphate receptor-binding protein,
RT specifically binds to and activates pancreas-type Na+/HCO3-cotransporter 1
RT (pNBC1).";
RL Proc. Natl. Acad. Sci. U.S.A. 103:9542-9547(2006).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-254; SER-257; SER-262;
RP SER-1029 AND SER-1034, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-30, 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 [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18630941; DOI=10.1021/pr800223m;
RA Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT "Specific phosphopeptide enrichment with immobilized titanium ion affinity
RT chromatography adsorbent for phosphoproteome analysis.";
RL J. Proteome Res. 7:3957-3967(2008).
RN [15]
RP FUNCTION, TISSUE SPECIFICITY, AND INTERACTION WITH AHCYL1.
RX PubMed=19033647; DOI=10.1172/jci36983;
RA Yang D., Shcheynikov N., Zeng W., Ohana E., So I., Ando H., Mizutani A.,
RA Mikoshiba K., Muallem S.;
RT "IRBIT coordinates epithelial fluid and HCO3- secretion by stimulating the
RT transporters pNBC1 and CFTR in the murine pancreatic duct.";
RL J. Clin. Invest. 119:193-202(2009).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-61; SER-65; SER-68; SER-223;
RP SER-232; SER-233; SER-245; THR-254; SER-256; SER-257; SER-262; SER-1026;
RP SER-1029; SER-1034 AND SER-1044, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT
RP SER-21 (ISOFORMS 2 AND 3), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
RP SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, and Testis;
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 [17]
RP INTERACTION WITH AHCYL1, SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
RX PubMed=21317537; DOI=10.1172/jci43475;
RA Yang D., Li Q., So I., Huang C.L., Ando H., Mizutani A., Seki G.,
RA Mikoshiba K., Thomas P.J., Muallem S.;
RT "IRBIT governs epithelial secretion in mice by antagonizing the WNK/SPAK
RT kinase pathway.";
RL J. Clin. Invest. 121:956-965(2011).
CC -!- FUNCTION: Electrogenic sodium/bicarbonate cotransporter with a
CC Na(+):HCO3(-) stoichiometry varying from 1:2 to 1:3. May regulate
CC bicarbonate influx/efflux at the basolateral membrane of cells and
CC regulate intracellular pH. {ECO:0000250|UniProtKB:Q9Y6R1,
CC ECO:0000269|PubMed:19033647}.
CC -!- FUNCTION: [Isoform 2]: May have a higher activity than isoform 1.
CC {ECO:0000250|UniProtKB:Q9Y6R1}.
CC -!- ACTIVITY REGULATION: Inhibited by stilbene derivatives and regulated by
CC cyclic AMP.
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with CA2/carbonic
CC anhydrase 2 and CA4/carbonic anhydrase 4 which may regulate transporter
CC activity (PubMed:14567693, PubMed:15218065). Isoform 1 but not isoform
CC 2 interacts with AHCYL1 (via PEST domain when phosphorylated); the
CC interaction increases SLC4A4 isoform 1 activity (PubMed:16769890,
CC PubMed:19033647, PubMed:21317537). Interacts with AHCYL2 (By
CC similarity). {ECO:0000250|UniProtKB:Q9GL77,
CC ECO:0000250|UniProtKB:Q9Y6R1, ECO:0000269|PubMed:14567693,
CC ECO:0000269|PubMed:15218065, ECO:0000269|PubMed:16769890,
CC ECO:0000269|PubMed:19033647, ECO:0000269|PubMed:21317537}.
CC -!- INTERACTION:
CC O88343; Q64444: Ca4; NbExp=2; IntAct=EBI-771342, EBI-6859308;
CC -!- SUBCELLULAR LOCATION: Basolateral cell membrane
CC {ECO:0000269|PubMed:11171615}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:11171615}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=pNBC;
CC IsoId=O88343-1; Sequence=Displayed;
CC Name=2; Synonyms=kNBC;
CC IsoId=O88343-2; Sequence=VSP_016709, VSP_016710;
CC Name=3;
CC IsoId=O88343-3; Sequence=VSP_016709, VSP_016710, VSP_016711,
CC VSP_016712;
CC -!- TISSUE SPECIFICITY: Isoform 1 is specifically expressed in pancreatic
CC ducts and acini (PubMed:19033647). Also expressed in parotid acinar
CC cells and in the colonic crypts. {ECO:0000269|PubMed:11171615,
CC ECO:0000269|PubMed:12388213, ECO:0000269|PubMed:12727194,
CC ECO:0000269|PubMed:19033647, ECO:0000269|PubMed:9651366}.
CC -!- PTM: Phosphorylation of Ser-1026 by PKA increases the binding of CA2
CC and changes the Na(+):HCO3(-) stoichiometry of the transporter from 3:1
CC to 2:1. Phosphorylated in presence of STK39 and dephosphorylated in
CC presence of PP1 phosphatase; phosphorylation seems to inhibit SLC4A4
CC activity (PubMed:21317537). {ECO:0000250|UniProtKB:Q9Y6R1,
CC ECO:0000269|PubMed:21317537}.
CC -!- PTM: N-glycosylated. May not be necessary for the transporter basic
CC functions. {ECO:0000269|PubMed:12604466}.
CC -!- SIMILARITY: Belongs to the anion exchanger (TC 2.A.31) family.
CC {ECO:0000305}.
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DR EMBL; AF020195; AAC40160.1; -; mRNA.
DR EMBL; AF141934; AAD31036.3; -; mRNA.
DR EMBL; AK085387; BAC39437.1; -; mRNA.
DR EMBL; AK140443; BAE24389.1; -; mRNA.
DR EMBL; BC026592; AAH26592.1; -; mRNA.
DR CCDS; CCDS19406.1; -. [O88343-1]
DR CCDS; CCDS89936.1; -. [O88343-2]
DR PIR; T14031; T14031.
DR RefSeq; NP_001129732.1; NM_001136260.1.
DR RefSeq; NP_061230.2; NM_018760.2. [O88343-1]
DR AlphaFoldDB; O88343; -.
DR SMR; O88343; -.
DR BioGRID; 207650; 6.
DR IntAct; O88343; 6.
DR MINT; O88343; -.
DR STRING; 10090.ENSMUSP00000121744; -.
DR GlyGen; O88343; 2 sites.
DR iPTMnet; O88343; -.
DR PhosphoSitePlus; O88343; -.
DR SwissPalm; O88343; -.
DR jPOST; O88343; -.
DR MaxQB; O88343; -.
DR PaxDb; O88343; -.
DR PeptideAtlas; O88343; -.
DR PRIDE; O88343; -.
DR ProteomicsDB; 260907; -. [O88343-1]
DR ProteomicsDB; 260908; -. [O88343-2]
DR ProteomicsDB; 260909; -. [O88343-3]
DR Antibodypedia; 24400; 202 antibodies from 28 providers.
DR DNASU; 54403; -.
DR Ensembl; ENSMUST00000113216; ENSMUSP00000108842; ENSMUSG00000060961. [O88343-3]
DR Ensembl; ENSMUST00000130041; ENSMUSP00000118413; ENSMUSG00000060961. [O88343-2]
DR Ensembl; ENSMUST00000148750; ENSMUSP00000119325; ENSMUSG00000060961. [O88343-1]
DR GeneID; 54403; -.
DR KEGG; mmu:54403; -.
DR UCSC; uc008yak.1; mouse. [O88343-1]
DR CTD; 8671; -.
DR MGI; MGI:1927555; Slc4a4.
DR VEuPathDB; HostDB:ENSMUSG00000060961; -.
DR eggNOG; KOG1172; Eukaryota.
DR GeneTree; ENSGT00940000156290; -.
DR HOGENOM; CLU_002289_5_2_1; -.
DR InParanoid; O88343; -.
DR OMA; LCMAPAN; -.
DR OrthoDB; 265068at2759; -.
DR PhylomeDB; O88343; -.
DR Reactome; R-MMU-425381; Bicarbonate transporters.
DR BioGRID-ORCS; 54403; 4 hits in 74 CRISPR screens.
DR ChiTaRS; Slc4a4; mouse.
DR PRO; PR:O88343; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; O88343; protein.
DR Bgee; ENSMUSG00000060961; Expressed in ciliary body and 244 other tissues.
DR ExpressionAtlas; O88343; baseline and differential.
DR Genevisible; O88343; MM.
DR GO; GO:0016323; C:basolateral plasma membrane; ISS:UniProtKB.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:MGI.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0005452; F:inorganic anion exchanger activity; IEA:InterPro.
DR GO; GO:0008510; F:sodium:bicarbonate symporter activity; ISS:UniProtKB.
DR GO; GO:0015293; F:symporter activity; ISO:MGI.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015701; P:bicarbonate transport; IGI:MGI.
DR GO; GO:0051649; P:establishment of localization in cell; IGI:MGI.
DR GO; GO:0050801; P:ion homeostasis; IBA:GO_Central.
DR GO; GO:0045821; P:positive regulation of glycolytic process; IMP:ARUK-UCL.
DR GO; GO:0051453; P:regulation of intracellular pH; IMP:ARUK-UCL.
DR GO; GO:0042391; P:regulation of membrane potential; IMP:ARUK-UCL.
DR GO; GO:0006885; P:regulation of pH; TAS:MGI.
DR GO; GO:0036376; P:sodium ion export across plasma membrane; ISO:MGI.
DR GO; GO:0035725; P:sodium ion transmembrane transport; ISO:MGI.
DR GO; GO:0006814; P:sodium ion transport; IDA:MGI.
DR GO; GO:0055085; P:transmembrane transport; ISO:MGI.
DR Gene3D; 3.40.930.10; -; 1.
DR InterPro; IPR013769; Band3_cytoplasmic_dom.
DR InterPro; IPR011531; HCO3_transpt-like_TM_dom.
DR InterPro; IPR003020; HCO3_transpt_euk.
DR InterPro; IPR003024; Na/HCO3_transpt.
DR InterPro; IPR016152; PTrfase/Anion_transptr.
DR PANTHER; PTHR11453; PTHR11453; 1.
DR Pfam; PF07565; Band_3_cyto; 1.
DR Pfam; PF00955; HCO3_cotransp; 1.
DR PRINTS; PR01231; HCO3TRNSPORT.
DR PRINTS; PR01232; NAHCO3TRSPRT.
DR SUPFAM; SSF55804; SSF55804; 1.
DR TIGRFAMs; TIGR00834; ae; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Ion transport; Membrane; Phosphoprotein;
KW Reference proteome; Sodium; Sodium transport; Symport; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..1079
FT /note="Electrogenic sodium bicarbonate cotransporter 1"
FT /id="PRO_0000079228"
FT TOPO_DOM 1..466
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R1"
FT TRANSMEM 467..491
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R1"
FT TOPO_DOM 492..501
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R1"
FT TRANSMEM 502..520
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R1"
FT TOPO_DOM 521
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R1"
FT TRANSMEM 522..542
FT /note="Discontinuously helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R1"
FT TOPO_DOM 543..550
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R1"
FT TRANSMEM 551..571
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R1"
FT TOPO_DOM 572..585
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R1"
FT TRANSMEM 586..609
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R1"
FT TOPO_DOM 610..692
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R1"
FT TRANSMEM 693..710
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R1"
FT TOPO_DOM 711..725
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R1"
FT TRANSMEM 726..745
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R1"
FT TOPO_DOM 746..779
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R1"
FT TRANSMEM 780..807
FT /note="Helical; Name=8"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R1"
FT TOPO_DOM 808..819
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R1"
FT TRANSMEM 820..836
FT /note="Helical; Name=9"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R1"
FT TOPO_DOM 837
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R1"
FT TRANSMEM 838..855
FT /note="Discontinuously helical; Name=10"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R1"
FT TOPO_DOM 856..877
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R1"
FT TRANSMEM 878..894
FT /note="Helical; Name=11"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R1"
FT TOPO_DOM 895..901
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R1"
FT TRANSMEM 902..918
FT /note="Helical; Name=12"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R1"
FT TOPO_DOM 919..960
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R1"
FT INTRAMEM 961..986
FT /note="Discontinuously helical"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R1"
FT TOPO_DOM 987..1079
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R1"
FT REGION 1..62
FT /note="Required for interaction with AHCYL1"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R1"
FT REGION 39..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 235..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 748..779
FT /note="Interaction with CA4"
FT /evidence="ECO:0000250"
FT REGION 1002..1004
FT /note="CA2-binding"
FT /evidence="ECO:0000250"
FT REGION 1012..1079
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1030..1033
FT /note="CA2-binding"
FT /evidence="ECO:0000250"
FT REGION 1057..1059
FT /note="Required for basolateral targeting"
FT /evidence="ECO:0000250"
FT COMPBIAS 39..53
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..73
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..260
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1012..1039
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1060..1079
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 30
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18034455"
FT MOD_RES 61
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 65
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 68
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 223
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 232
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 233
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 245
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 249
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9JI66"
FT MOD_RES 254
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 256
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 257
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 262
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1026
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1029
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1034
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1044
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1069
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JI66"
FT CARBOHYD 641
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT CARBOHYD 661
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT DISULFID 627..629
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R1"
FT DISULFID 674..686
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R1"
FT VAR_SEQ 1..44
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:11171615,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_016709"
FT VAR_SEQ 45..85
FT /note="HKRKAGHKEKKEKERISENYSDKSDVENADESSSSILKPLI -> MSTENVE
FT GKPNNLGERGRARSSTFLRVFQPMFNHSIFTSAV (in isoform 2 and
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:11171615,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_016710"
FT VAR_SEQ 185..201
FT /note="MIADHQIETGLLKPDLK -> LLGESRKVIRPAGFIRP (in isoform
FT 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_016711"
FT VAR_SEQ 202..1079
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_016712"
FT CONFLICT 388
FT /note="T -> A (in Ref. 1; AAC40160)"
FT /evidence="ECO:0000305"
FT CONFLICT 546
FT /note="H -> N (in Ref. 1; AAC40160)"
FT /evidence="ECO:0000305"
FT CONFLICT 560
FT /note="W -> R (in Ref. 1; AAC40160)"
FT /evidence="ECO:0000305"
FT CONFLICT 564
FT /note="M -> L (in Ref. 1; AAC40160)"
FT /evidence="ECO:0000305"
FT CONFLICT 567
FT /note="V -> I (in Ref. 1; AAC40160)"
FT /evidence="ECO:0000305"
FT CONFLICT 589
FT /note="S -> P (in Ref. 1; AAC40160)"
FT /evidence="ECO:0000305"
FT CONFLICT 740
FT /note="C -> G (in Ref. 1; AAC40160)"
FT /evidence="ECO:0000305"
FT CONFLICT 775
FT /note="G -> E (in Ref. 1; AAC40160)"
FT /evidence="ECO:0000305"
FT CONFLICT 814
FT /note="K -> Q (in Ref. 1; AAC40160)"
FT /evidence="ECO:0000305"
FT CONFLICT 832
FT /note="V -> I (in Ref. 1; AAC40160)"
FT /evidence="ECO:0000305"
FT CONFLICT 835
FT /note="F -> L (in Ref. 1; AAC40160)"
FT /evidence="ECO:0000305"
FT CONFLICT 848
FT /note="S -> F (in Ref. 2; AAD31036)"
FT /evidence="ECO:0000305"
FT CONFLICT 876
FT /note="Q -> P (in Ref. 2; AAD31036)"
FT /evidence="ECO:0000305"
FT CONFLICT 884
FT /note="F -> L (in Ref. 1; AAC40160)"
FT /evidence="ECO:0000305"
FT CONFLICT 901
FT /note="P -> R (in Ref. 2; AAD31036)"
FT /evidence="ECO:0000305"
FT CONFLICT 909..910
FT /note="FL -> SW (in Ref. 2; AAD31036)"
FT /evidence="ECO:0000305"
FT MOD_RES O88343-2:21
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES O88343-3:21
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 1079 AA; 121484 MW; DBC7C3DEBE10BE97 CRC64;
MEDEAVLDRG ASFLKHVCDE EEVEGHHTIY IGVHVPKSYR RRRRHKRKAG HKEKKEKERI
SENYSDKSDV ENADESSSSI LKPLISPAAE RIRFILGEED DSPAPPQLFT ELDELLAVDG
QEMEWKETAR WIKFEEKVEQ GGERWSKPHV ATLSLHSLFE LRTCMEKGSI MLDREASSLP
QLVEMIADHQ IETGLLKPDL KDKVTYTLLR KHRHQTKKSN LRSLADIGKT VSSASRMFSN
PDNGSPAMTH RNLTSSSLND ISDKPEKDQL KNKFMKKLPR DAEASNVLVG EVDFLDTPFI
AFVRLQQAVM LGALTEVPVP TRFLFILLGP KGKAKSYHEI GRAIATLMSD EVFHDIAYKA
KDRHDLIAGI DEFLDEVIVL PPGEWDPTIR IEPPKSLPSS DKRKNMYSGG ENVQMNGDTP
HDGGHGGGGH GDCEELQRTG RFCGGLIKDI KRKAPFFASD FYDALNIQAL SAILFIYLAT
VTNAITFGGL LGDATDNMQG VLESFLGTAV SGAIFCLFAG QPLTILSSTG PVLVFERLLF
NFSKDHNFDY LEFRLWIGLW SAFMCLVLVA TDASFLVQYF TRFTEEGFSS LISFIFIYDA
FKKMIKLADY YPINSDFKVG YNTHFSCACL PPDPVNLSVS NDTTLAPEDL PTISSTDMYH
NVTFDWAYLS KKECVKYGGK LVGNNCDFVP DITLMSFILF LGTYTSSMAM KKFKTSRYFP
TTARKLISDF AIILSILIFC VIDALVGVDT PKLIVPSEFK PTSPNRGWFV PPFGGNPWWV
CLAAAIPALL VTILIFMDQQ ITAVIVNRKE HKLKKGAGYH LDLFWVAILM VVCSFMALPW
YVAATVISIA HIDSLKMETE TSAPGEQPKF LGVREQRVTG TLVFILTGLS VFMAPILKFI
PMPVLYGVFL YMGVASLNGV QFMDRLKLLL MPLKHQPDFI YLRHVPLRRV HLFTFLQVLC
LALLWILKST VAAIIFPVMI LALVAVRKGM DYLFSQHDLS FLDDVIPEKD KKKKEDEKKK
KKKKGSLDSD NDDSDCPYSE KVPSIKIPMD IMEQQPFLSD NKPLDRERSS TFLERHTSC
