ID   B3A2_MOUSE              Reviewed;        1237 AA.
AC   P13808; Q9ES09; Q9ES10; Q9ES11; Q9ES12; Q9ES13;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   08-NOV-2023, entry version 177.
DE   RecName: Full=Anion exchange protein 2;
DE            Short=AE 2;
DE            Short=Anion exchanger 2;
DE   AltName: Full=Band 3-related protein;
DE            Short=B3RP;
DE   AltName: Full=Non-erythroid band 3-like protein;
DE   AltName: Full=Solute carrier family 4 member 2;
GN   Name=Slc4a2; Synonyms=Ae2;
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 A).
RX   PubMed=3182834; DOI=10.1016/s0021-9258(18)37502-1;
RA   Alper S.L., Kopito R.R., Libresco S.M., Lodish H.F.;
RT   "Cloning and characterization of a murine band 3-related cDNA from kidney
RT   and from a lymphoid cell line.";
RL   J. Biol. Chem. 263:17092-17099(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING, AND TISSUE
RP   SPECIFICITY (ISOFORMS A; B1; B2; C1 AND C2).
RX   PubMed=11006093; DOI=10.1006/bbrc.2000.3439;
RA   Lecanda J., Urtasun R., Medina J.F.;
RT   "Molecular cloning and genomic organization of the mouse AE2 anion
RT   exchanger gene.";
RL   Biochem. Biophys. Res. Commun. 276:117-124(2000).
RN   [3]
RP   FUNCTION, TRANSPORTER ACTIVITY, ACTIVITY REGULATION, SUBCELLULAR LOCATION,
RP   AND TISSUE SPECIFICITY.
RX   PubMed=2371270; DOI=10.1073/pnas.87.14.5278;
RA   Lindsey A.E., Schneider K., Simmons D.M., Baron R., Lee B.S., Kopito R.R.;
RT   "Functional expression and subcellular localization of an anion exchanger
RT   cloned from choroid plexus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 87:5278-5282(1990).
RN   [4]
RP   FUNCTION (ISOFORMS A; B1 AND B2), DISRUPTION PHENOTYPE, AND TISSUE
RP   SPECIFICITY (ISOFORMS A; B1 AND B2).
RX   PubMed=14673081; DOI=10.1073/pnas.2536127100;
RA   Medina J.F., Recalde S., Prieto J., Lecanda J., Saez E., Funk C.D.,
RA   Vecino P., van Roon M.A., Ottenhoff R., Bosma P.J., Bakker C.T.,
RA   Elferink R.P.;
RT   "Anion exchanger 2 is essential for spermiogenesis in mice.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:15847-15852(2003).
RN   [5]
RP   FUNCTION, TRANSPORTER ACTIVITY, ACTIVITY REGULATION, SUBCELLULAR LOCATION,
RP   AND TISSUE SPECIFICITY.
RX   PubMed=12958022; DOI=10.1152/ajpgi.00158.2003;
RA   Nguyen H.V., Stuart-Tilley A., Alper S.L., Melvin J.E.;
RT   "Cl(-)/HCO(3)(-) exchange is acetazolamide sensitive and activated by a
RT   muscarinic receptor-induced [Ca(2+)](i) increase in salivary acinar
RT   cells.";
RL   Am. J. Physiol. 286:G312-G320(2004).
RN   [6]
RP   FUNCTION, SUBCELLULAR LOCATION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=18971331; DOI=10.1073/pnas.0808763105;
RA   Wu J., Glimcher L.H., Aliprantis A.O.;
RT   "HCO3-/Cl- anion exchanger SLC4A2 is required for proper osteoclast
RT   differentiation and function.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:16934-16939(2008).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-144; SER-170; SER-172 AND
RP   THR-253, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Kidney, Lung, Spleen, 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   [9]
RP   FUNCTION, TRANSPORTER ACTIVITY, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE,
RP   AND MUTAGENESIS OF ARG-1056.
RX   PubMed=23341620; DOI=10.1073/pnas.1206392110;
RA   Coury F., Zenger S., Stewart A.K., Stephens S., Neff L., Tsang K.,
RA   Shull G.E., Alper S.L., Baron R., Aliprantis A.O.;
RT   "SLC4A2-mediated Cl-/HCO3- exchange activity is essential for calpain-
RT   dependent regulation of the actin cytoskeleton in osteoclasts.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:2163-2168(2013).
RN   [10]
RP   FUNCTION, TRANSPORTER ACTIVITY, AND DISRUPTION PHENOTYPE.
RX   PubMed=24515893; DOI=10.1002/eji.201344218;
RA   Concepcion A.R., Salas J.T., Sarvide S., Saez E., Ferrer A., Lopez M.,
RA   Portu A., Banales J.M., Hervas-Stubbs S., Oude Elferink R.P., Prieto J.,
RA   Medina J.F.;
RT   "Anion exchanger 2 is critical for CD8(+) T cells to maintain pHi
RT   homeostasis and modulate immune responses.";
RL   Eur. J. Immunol. 44:1341-1351(2014).
CC   -!- FUNCTION: Sodium-independent anion exchanger which mediates the
CC       electroneutral exchange of chloride for bicarbonate ions across the
CC       cell membrane (PubMed:2371270, PubMed:12958022, PubMed:18971331,
CC       PubMed:23341620, PubMed:24515893). Plays an important role in
CC       osteoclast differentiation and function (PubMed:18971331,
CC       PubMed:23341620). Regulates bone resorption and calpain-dependent actin
CC       cytoskeleton organization in osteoclasts via anion exchange-dependent
CC       control of pH (PubMed:23341620). Essential for intracellular pH
CC       regulation in CD8(+) T-cells upon CD3 stimulation, modulating CD8(+) T-
CC       cell responses (PubMed:24515893). {ECO:0000269|PubMed:12958022,
CC       ECO:0000269|PubMed:18971331, ECO:0000269|PubMed:23341620,
CC       ECO:0000269|PubMed:2371270, ECO:0000269|PubMed:24515893}.
CC   -!- FUNCTION: [Isoform A]: Plays a critical role in male fertility and
CC       spermiogenesis. {ECO:0000269|PubMed:14673081}.
CC   -!- FUNCTION: [Isoform B1]: Plays a critical role in male fertility and
CC       spermiogenesis. {ECO:0000269|PubMed:14673081}.
CC   -!- FUNCTION: [Isoform B2]: Plays a critical role in male fertility and
CC       spermiogenesis. {ECO:0000269|PubMed:14673081}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=chloride(out) + hydrogencarbonate(in) = chloride(in) +
CC         hydrogencarbonate(out); Xref=Rhea:RHEA:72363, ChEBI:CHEBI:17544,
CC         ChEBI:CHEBI:17996; Evidence={ECO:0000269|PubMed:12958022,
CC         ECO:0000269|PubMed:23341620, ECO:0000269|PubMed:2371270,
CC         ECO:0000269|PubMed:24515893};
CC   -!- ACTIVITY REGULATION: Inhibited by 4,4'-diisothiocyanatostilbene-2,2'-
CC       disulfonic acid (DIDS) and acetazolamide (PubMed:2371270,
CC       PubMed:12958022). Muscarinic receptor stimulation enhances activity
CC       through a Ca(2+)-dependent mechanism (PubMed:12958022).
CC       {ECO:0000269|PubMed:12958022, ECO:0000269|PubMed:2371270}.
CC   -!- SUBCELLULAR LOCATION: Apical cell membrane
CC       {ECO:0000250|UniProtKB:P04920}; Multi-pass membrane protein
CC       {ECO:0000255}. Basolateral cell membrane {ECO:0000269|PubMed:12958022,
CC       ECO:0000269|PubMed:18971331, ECO:0000269|PubMed:23341620,
CC       ECO:0000269|PubMed:2371270}; Multi-pass membrane protein {ECO:0000255}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=A;
CC         IsoId=P13808-1; Sequence=Displayed;
CC       Name=B1;
CC         IsoId=P13808-2; Sequence=VSP_000458;
CC       Name=B2;
CC         IsoId=P13808-3; Sequence=VSP_000457;
CC       Name=C1;
CC         IsoId=P13808-4; Sequence=VSP_000460;
CC       Name=C2;
CC         IsoId=P13808-5; Sequence=VSP_000459, VSP_000461;
CC   -!- TISSUE SPECIFICITY: Expressed in the choroid plexus epithelium (at
CC       protein level) (PubMed:2371270). Expressed in the parotid gland and
CC       sublingual salivary gland acinar cells (at protein level)
CC       (PubMed:12958022). {ECO:0000269|PubMed:12958022,
CC       ECO:0000269|PubMed:2371270}.
CC   -!- TISSUE SPECIFICITY: [Isoform A]: Widely expressed at similar levels in
CC       all tissues examined (PubMed:11006093). Expressed in the testis
CC       (PubMed:14673081). {ECO:0000269|PubMed:11006093,
CC       ECO:0000269|PubMed:14673081}.
CC   -!- TISSUE SPECIFICITY: [Isoform B1]: Predominantly expressed in stomach
CC       although they are also detected at lower levels in other tissues
CC       (PubMed:11006093). Expressed in the testis (PubMed:14673081).
CC       {ECO:0000269|PubMed:11006093, ECO:0000269|PubMed:14673081}.
CC   -!- TISSUE SPECIFICITY: [Isoform B2]: Predominantly expressed in stomach
CC       although they are also detected at lower levels in other tissues
CC       (PubMed:11006093). Expressed in the testis (PubMed:14673081).
CC       {ECO:0000269|PubMed:11006093, ECO:0000269|PubMed:14673081}.
CC   -!- TISSUE SPECIFICITY: [Isoform C1]: Stomach-specific.
CC       {ECO:0000269|PubMed:11006093}.
CC   -!- TISSUE SPECIFICITY: [Isoform C2]: Expressed at slightly higher levels
CC       in lung and stomach than in other tissues.
CC       {ECO:0000269|PubMed:11006093}.
CC   -!- INDUCTION: Up-regulated during osteoclast differentiation.
CC       {ECO:0000269|PubMed:18971331}.
CC   -!- DISRUPTION PHENOTYPE: Male mice are infertile and the size and weight
CC       of the testis is reduced by 40-60%. Spermiogenesis is interrupted after
CC       stage VII, with only a few late spermatids and a complete absence of
CC       spermatozoa in the seminiferous tubules. The number of apoptotic bodies
CC       is increased in the seminiferous tubules and in the epididymis, which
CC       also shows squamous metaplasia of the epididymal epithelium
CC       (PubMed:14673081). CD8(+) T-cells exhibit increased intracellular pH
CC       and enhanced cell proliferation and activation after CD3 stimulation
CC       (PubMed:24515893). Mice display osteopetrosis with osteoclasts showing
CC       abnormal differentiation and increased apoptosis (PubMed:18971331).
CC       Conditional knockout in osteoclasts (OCs) result in dysfunctional OCs
CC       which exhibit altered intracellular pH and actin cytoskeletal dynamics
CC       and an impaired bone resorption capacity owing to a dysregulation of
CC       calpain-dependent podosomal disassembly (PubMed:23341620).
CC       {ECO:0000269|PubMed:14673081, ECO:0000269|PubMed:18971331,
CC       ECO:0000269|PubMed:23341620, ECO:0000269|PubMed:24515893}.
CC   -!- SIMILARITY: Belongs to the anion exchanger (TC 2.A.31) family.
CC       {ECO:0000305}.
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DR   EMBL; J04036; AAA65505.1; -; mRNA.
DR   EMBL; AF255774; AAG23154.1; -; Genomic_DNA.
DR   EMBL; AF255774; AAG23155.1; -; Genomic_DNA.
DR   EMBL; AF255774; AAG23156.1; -; Genomic_DNA.
DR   EMBL; AF255774; AAG23158.1; -; Genomic_DNA.
DR   EMBL; AF255774; AAG23157.1; -; Genomic_DNA.
DR   CCDS; CCDS19119.1; -. [P13808-1]
DR   PIR; A31789; A31789.
DR   RefSeq; NP_001240821.1; NM_001253892.1.
DR   RefSeq; NP_033233.2; NM_009207.3.
DR   RefSeq; XP_006535713.1; XM_006535650.1.
DR   RefSeq; XP_006535714.1; XM_006535651.3.
DR   RefSeq; XP_006535718.1; XM_006535655.3.
DR   RefSeq; XP_006535719.1; XM_006535656.3.
DR   AlphaFoldDB; P13808; -.
DR   SMR; P13808; -.
DR   BioGRID; 203314; 7.
DR   STRING; 10090.ENSMUSP00000078972; -.
DR   GlyCosmos; P13808; 3 sites, No reported glycans.
DR   GlyGen; P13808; 3 sites.
DR   iPTMnet; P13808; -.
DR   PhosphoSitePlus; P13808; -.
DR   EPD; P13808; -.
DR   jPOST; P13808; -.
DR   MaxQB; P13808; -.
DR   PaxDb; 10090-ENSMUSP00000078972; -.
DR   PeptideAtlas; P13808; -.
DR   ProteomicsDB; 273516; -. [P13808-1]
DR   ProteomicsDB; 273517; -. [P13808-2]
DR   ProteomicsDB; 273518; -. [P13808-3]
DR   ProteomicsDB; 273519; -. [P13808-4]
DR   ProteomicsDB; 273520; -. [P13808-5]
DR   Pumba; P13808; -.
DR   DNASU; 20535; -.
DR   GeneID; 20535; -.
DR   KEGG; mmu:20535; -.
DR   UCSC; uc008wrm.2; mouse. [P13808-1]
DR   AGR; MGI:109351; -.
DR   CTD; 6522; -.
DR   MGI; MGI:109351; Slc4a2.
DR   eggNOG; KOG1172; Eukaryota.
DR   InParanoid; P13808; -.
DR   OrthoDB; 1013180at2759; -.
DR   PhylomeDB; P13808; -.
DR   TreeFam; TF313630; -.
DR   Reactome; R-MMU-425381; Bicarbonate transporters.
DR   BioGRID-ORCS; 20535; 2 hits in 76 CRISPR screens.
DR   ChiTaRS; Slc4a2; mouse.
DR   PRO; PR:P13808; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; P13808; Protein.
DR   GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
DR   GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB.
DR   GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0015108; F:chloride transmembrane transporter activity; IDA:UniProtKB.
DR   GO; GO:0140900; F:chloride:bicarbonate antiporter activity; IDA:UniProtKB.
DR   GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR   GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0097186; P:amelogenesis; IDA:ARUK-UCL.
DR   GO; GO:0015701; P:bicarbonate transport; IBA:GO_Central.
DR   GO; GO:0006821; P:chloride transport; IDA:UniProtKB.
DR   GO; GO:0043377; P:negative regulation of CD8-positive, alpha-beta T cell differentiation; IMP:UniProtKB.
DR   GO; GO:2000565; P:negative regulation of CD8-positive, alpha-beta T cell proliferation; IMP:UniProtKB.
DR   GO; GO:0030316; P:osteoclast differentiation; IMP:UniProtKB.
DR   GO; GO:0070175; P:positive regulation of enamel mineralization; IDA:ARUK-UCL.
DR   GO; GO:0032956; P:regulation of actin cytoskeleton organization; IMP:UniProtKB.
DR   GO; GO:0045124; P:regulation of bone resorption; IMP:UniProtKB.
DR   GO; GO:0051453; P:regulation of intracellular pH; ISO:MGI.
DR   GO; GO:0007283; P:spermatogenesis; IMP:UniProtKB.
DR   GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR   Gene3D; 1.10.287.570; Helical hairpin bin; 1.
DR   InterPro; IPR001717; Anion_exchange.
DR   InterPro; IPR002978; Anion_exchange_2.
DR   InterPro; IPR018241; Anion_exchange_CS.
DR   InterPro; IPR013769; Band3_cytoplasmic_dom.
DR   InterPro; IPR011531; HCO3_transpt-like_TM_dom.
DR   InterPro; IPR003020; HCO3_transpt_euk.
DR   InterPro; IPR016152; PTrfase/Anion_transptr.
DR   NCBIfam; TIGR00834; ae; 1.
DR   PANTHER; PTHR11453; ANION EXCHANGE PROTEIN; 1.
DR   PANTHER; PTHR11453:SF14; ANION EXCHANGE PROTEIN 2; 1.
DR   Pfam; PF07565; Band_3_cyto; 1.
DR   Pfam; PF00955; HCO3_cotransp; 1.
DR   PRINTS; PR00165; ANIONEXCHNGR.
DR   PRINTS; PR01188; ANIONEXHNGR2.
DR   PRINTS; PR01231; HCO3TRNSPORT.
DR   SUPFAM; SSF55804; Phoshotransferase/anion transport protein; 1.
DR   PROSITE; PS00219; ANION_EXCHANGER_1; 1.
DR   PROSITE; PS00220; ANION_EXCHANGER_2; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Anion exchange; Antiport; Cell membrane;
KW   Differentiation; Glycoprotein; Ion transport; Lipoprotein; Membrane;
KW   Methylation; Palmitate; Phosphoprotein; Reference proteome;
KW   Spermatogenesis; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..1237
FT                   /note="Anion exchange protein 2"
FT                   /id="PRO_0000079216"
FT   TOPO_DOM        1..703
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        704..727
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        733..770
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        790..812
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        822..843
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        844..896
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        897..914
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        915..929
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        930..950
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        984..1006
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1032..1053
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1087..1132
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1159..1195
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..238
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          285..316
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          445..466
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          704..1237
FT                   /note="Membrane (anion exchange)"
FT   COMPBIAS        32..54
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        61..98
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        302..316
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         112
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P04920"
FT   MOD_RES         131
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P04920"
FT   MOD_RES         144
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19144319"
FT   MOD_RES         170
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19144319"
FT   MOD_RES         172
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19144319"
FT   MOD_RES         239
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P04920"
FT   MOD_RES         253
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:19144319"
FT   MOD_RES         270
FT                   /note="N6-methyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P04920"
FT   MOD_RES         439
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P04920"
FT   LIPID           1169
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        855
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        866
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        878
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         1..198
FT                   /note="Missing (in isoform C1)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_000460"
FT   VAR_SEQ         1..166
FT                   /note="Missing (in isoform C2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_000459"
FT   VAR_SEQ         1..17
FT                   /note="MSSAPRRPASGADSLHT -> MTQ (in isoform B1)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_000458"
FT   VAR_SEQ         1..17
FT                   /note="MSSAPRRPASGADSLHT -> MDFLLRPQ (in isoform B2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_000457"
FT   VAR_SEQ         167..193
FT                   /note="ERTSPSPPTQTPHQEAAPRASKGAQTG -> MPAFQEWKSGGLREEAVFGAH
FT                   GCSVCR (in isoform C2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_000461"
FT   MUTAGEN         1056
FT                   /note="R->A: Loss of activity but no effect on localization
FT                   to basolateral cell membrane."
FT                   /evidence="ECO:0000269|PubMed:23341620"
FT   CONFLICT        205
FT                   /note="A -> G (in Ref. 2;
FT                   AAG23154/AAG23155/AAG23156/AAG23158/AAG23157)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1237 AA;  136814 MW;  1A0782C0071782EE CRC64;
     MSSAPRRPAS GADSLHTPEP ESLSPGTPGF PEQEEDELRT LGVERFEEIL QEAGSRGGEE
     PGRSYGEEDF EYHRQSSHHI HHPLSTHLPP DARRRKTPQG PGRKPRRRPG ASPTGETPTI
     EEGEEDEEEA SEAEGFRAPP QQPSPATTPS AVQFFLQEDE GAERKPERTS PSPPTQTPHQ
     EAAPRASKGA QTGTLVEEMV AVASATAGGD DGGAAGRPLT KAQPGHRSYN LQERRRIGSM
     TGVEQALLPR VPTDESEAQT LATADLDLMK SHRFEDVPGV RRHLVRKNAK GSTQAAREGR
     EPGPTPRARP RAPHKPHEVF VELNELLLDK NQEPQWRETA RWIKFEEDVE EETERWGKPH
     VASLSFRSLL ELRRTLAHGA VLLDLDQQTL PGVAHQVVEQ MVISDQIKAE DRANVLRALL
     LKHSHPSDEK EFSFPRNISA GSLGSLLGHH HAQGTESDPH VTEPLIGGVP ETRLEVDRER
     ELPPPAPPAG ITRSKSKHEL KLLEKIPENA EATVVLVGCV EFLSRPTMAF VRLREAVELD
     AVLEVPVPVR FLFLLLGPSS ANMDYHEIGR SISTLMSDKQ FHEAAYLADE RDDLLTAINA
     FLDCSVVLPP SEVQGEELLR SVAHFQRQML KKREEQGRLL PPGAGLEPKS AQDKALLQMV
     EVAGAAEDDP LRRTGRPFGG LIRDVRRRYP HYLSDFRDAL DPQCLAAVIF IYFAALSPAI
     TFGGLLGEKT KDLIGVSELI MSTALQGVVF CLLGAQPLLV IGFSGPLLVF EEAFFSFCSS
     NELEYLVGRV WIGFWLVFLA LLMVALEGSF LVRFVSRFTQ EIFAFLISLI FIYETFYKLI
     KIFQEHPLHG CSGSNDSEAG SSSSSNMTWA TTILVPDNSS ASGQSGQEKP RGQPNTALLS
     LVLMAGTFFI AFFLRKFKNS RFFPGRIRRV IGDFGVPIAI LIMVLVDYSI EDTYTQKLSV
     PSGFSVTAPD KRGWVINPLG EKTPFPVWMM VASLLPAVLV FILIFMETQI TTLIISKKER
     MLQKGSGFHL DLLLIVAMGG ICALFGLPWL AAATVRSVTH ANALTVMSKA VAPGDKPKIQ
     EVKEQRVTGL LVALLVGLSM VIGDLLRQIP LAVLFGIFLY MGVTSLNGIQ FYERLHLLLM
     PPKHHPDVTY VKKVRTMRMH LFTALQLLCL ALLWAVMSTA ASLAFPFILI LTVPLRMVVL
     TRIFTEREMK CLDANEAEPV FDECEGVDEY NEMPMPV
//