ID   NFAT5_MOUSE             Reviewed;        1534 AA.
AC   Q9WV30; E9Q0P3; E9Q6U2; G5E8N9; Q91WY0; Q9JLA1;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   16-OCT-2013, sequence version 2.
DT   27-MAR-2024, entry version 166.
DE   RecName: Full=Nuclear factor of activated T-cells 5;
DE            Short=NF-AT5;
DE   AltName: Full=Rel domain-containing transcription factor NFAT5;
DE   AltName: Full=T-cell transcription factor NFAT5;
GN   Name=Nfat5;
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 4).
RA   Lu J., Xu H., Olson E.N.;
RT   "Identification of NFAT5, a new rel-like transcription factor.";
RL   Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 3-1534 (ISOFORM 3), ALTERNATIVE SPLICING,
RP   FUNCTION, DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION, AND INDUCTION.
RC   TISSUE=Brain;
RX   PubMed=11934689; DOI=10.1152/ajprenal.00123.2001;
RA   Maouyo D., Kim J.Y., Lee S.D., Wu Y., Woo S.K., Kwon H.M.;
RT   "Mouse TonEBP-NFAT5: expression in early development and alternative
RT   splicing.";
RL   Am. J. Physiol. 282:F802-F809(2002).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 13-1534 (ISOFORM 2).
RC   TISSUE=Skeletal muscle;
RX   PubMed=11233530; DOI=10.1101/sqb.1999.64.517;
RA   Lopez-Rodriguez C., Aramburu J., Rakeman A.S., Copeland N.G., Gilbert D.J.,
RA   Thomas S., Disteche C., Jenkins N.A., Rao A.;
RT   "NFAT5: the NF-AT family of transcription factors expands in a new
RT   direction.";
RL   Cold Spring Harb. Symp. Quant. Biol. 64:517-526(1999).
RN   [6]
RP   SUBCELLULAR LOCATION, AND ALTERNATIVE SPLICING.
RX   PubMed=10377394; DOI=10.1073/pnas.96.13.7214;
RA   Lopez-Rodriguez C., Aramburu J., Rakeman A.S., Rao A.;
RT   "NFAT5, a constitutively nuclear NFAT protein that does not cooperate with
RT   Fos and Jun.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:7214-7219(1999).
RN   [7]
RP   FUNCTION IN RENAL HOMEOSTASIS, DISRUPTION PHENOTYPE, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=14983020; DOI=10.1073/pnas.0308703100;
RA   Lopez-Rodriguez C., Antos C.L., Shelton J.M., Richardson J.A., Lin F.,
RA   Novobrantseva T.I., Bronson R.T., Igarashi P., Rao A., Olson E.N.;
RT   "Loss of NFAT5 results in renal atrophy and lack of tonicity-responsive
RT   gene expression.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:2392-2397(2004).
RN   [8]
RP   TISSUE SPECIFICITY, AND INDUCTION BY OSMOTIC STRESS.
RX   PubMed=23233732; DOI=10.1194/jlr.m033365;
RA   Ueno M., Shen W.J., Patel S., Greenberg A.S., Azhar S., Kraemer F.B.;
RT   "Fat-specific protein 27 modulates nuclear factor of activated T cells 5
RT   and the cellular response to stress.";
RL   J. Lipid Res. 54:734-743(2013).
RN   [9]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-122, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA   Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA   Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT   "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT   pathways.";
RL   Mol. Cell 50:919-930(2013).
CC   -!- FUNCTION: Transcription factor involved, among others, in the
CC       transcriptional regulation of osmoprotective and inflammatory genes
CC       (PubMed:11934689, PubMed:14983020). Binds the DNA consensus sequence
CC       5'-[ACT][AG]TGGAAA[CAT]A[TA][ATC][CA][ATG][GT][GAC][CG][CT]-3' (By
CC       similarity). Mediates the transcriptional response to hypertonicity (By
CC       similarity). Positively regulates the transcription of LCN2 and S100A4
CC       genes; optimal transactivation of these genes requires the presence of
CC       DDX5/DDX17 (By similarity). Also involved in the DNA damage response by
CC       preventing formation of R-loops; R-loops are composed of a DNA:RNA
CC       hybrid and the associated non-template single-stranded DNA (By
CC       similarity). {ECO:0000250|UniProtKB:O94916,
CC       ECO:0000269|PubMed:11934689, ECO:0000269|PubMed:14983020}.
CC   -!- SUBUNIT: Homodimer when bound to DNA, completely encircles its DNA
CC       target (By similarity). Interacts with CIDEC; this interaction is
CC       direct and retains NFAT5 in the cytoplasm (By similarity). Does not
CC       bind with Fos and Jun transcription factors. Interacts with DDX5 and
CC       DDX17; this interaction leads to DDX5/DDX17 recruitment to LNC2 and
CC       S100A4 promoters and NFAT5-mediated DDX5/DDX17-enhanced transactivation
CC       (By similarity). {ECO:0000250|UniProtKB:D3ZGB1,
CC       ECO:0000250|UniProtKB:O94916}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10377394,
CC       ECO:0000269|PubMed:11934689}. Cytoplasm {ECO:0000269|PubMed:11934689}.
CC       Chromosome {ECO:0000250|UniProtKB:O94916}. Note=Nuclear distribution
CC       increases under hypertonic conditions (PubMed:11934689). Recruited to
CC       sites of R-loop-associated DNA damage following poly-ADP-ribosylation
CC       by PARP1 (By similarity). {ECO:0000250|UniProtKB:O94916,
CC       ECO:0000269|PubMed:11934689}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1; Synonyms=C;
CC         IsoId=Q9WV30-1; Sequence=Displayed;
CC       Name=2; Synonyms=D;
CC         IsoId=Q9WV30-2; Sequence=VSP_058790;
CC       Name=3; Synonyms=B;
CC         IsoId=Q9WV30-3; Sequence=VSP_058790, VSP_058791, VSP_058789;
CC       Name=4;
CC         IsoId=Q9WV30-4; Sequence=VSP_058792, VSP_058793;
CC   -!- TISSUE SPECIFICITY: Detected in white and brown adipose tissue, muscle,
CC       heart, liver and kidney. Expressed in lymphocytes (at protein level).
CC       {ECO:0000269|PubMed:14983020, ECO:0000269|PubMed:23233732}.
CC   -!- DEVELOPMENTAL STAGE: At 10.5 dpc, expressed in brain and developing
CC       lens. At 12.5 dpc, the expression is extended to liver. By 17.5 dpc,
CC       expressed abundantly in brain, spinal cord, heart end liver and
CC       moderately in salivary gland, lung, kidney, gut and bladder (at protein
CC       level). {ECO:0000269|PubMed:11934689}.
CC   -!- INDUCTION: Up-regulated upon hypertonic conditions, this up-regulation
CC       in not observed in ES cells. {ECO:0000269|PubMed:11934689,
CC       ECO:0000269|PubMed:23233732}.
CC   -!- PTM: Phosphorylated at Thr-135 by CDK5 in response to osmotic stress;
CC       this phosphorylation mediates its rapid nuclear localization.
CC       {ECO:0000250|UniProtKB:O94916}.
CC   -!- PTM: Poly-ADP-ribosylated by PARP1 in response to DNA damage, promoting
CC       recruitment to sites of R-loop-associated DNA damage.
CC       {ECO:0000250|UniProtKB:O94916}.
CC   -!- DISRUPTION PHENOTYPE: Embryonic and perinatal lethality with incomplete
CC       penetrance. At 17.5 dpc, 50% of the expected Mendelian rate with only
CC       3.4% of the expected number living past 21 days after birth. The few
CC       survivors to adulthood fail to thrive and their weight is half compared
CC       to the wild-type. At 3 weeks old, kidney hypoplasia and an altered
CC       medullary morphology are observed with an increased apoptosis in the
CC       kidney inner medulla. Under osmotic stress, the transcriptional
CC       regulation of osmoprotective genes is altered in the kidney medulla.
CC       {ECO:0000269|PubMed:14983020}.
CC   -!- MISCELLANEOUS: [Isoform 1]: May have longer half-life and is more
CC       efficient in stimulation of transcription than isoform 3.
CC   -!- MISCELLANEOUS: [Isoform 3]: The transcript encoding this isoform
CC       contains an alternative coding exon 4 which contains 2 stop codons and
CC       could target the transcript to nonsense-mediated mRNA decay after the
CC       pioneer round of translation, as suggested by decreased NFAT5 protein
CC       levels when the number of exon 4-containing transcripts increases. The
CC       insertion of exon 4 is stimulated in the presence of DDX5 and DDX17.
CC       {ECO:0000269|PubMed:10377394}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF31405.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAK97603.1; Type=Erroneous translation; Evidence={ECO:0000305};
CC       Sequence=EDL11405.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AF162853; AAD44343.1; -; mRNA.
DR   EMBL; AC125207; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC158364; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH466525; EDL11404.1; -; Genomic_DNA.
DR   EMBL; CH466525; EDL11405.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AF369980; AAK97603.1; ALT_SEQ; mRNA.
DR   EMBL; AF200687; AAF31405.1; ALT_INIT; mRNA.
DR   CCDS; CCDS22648.2; -. [Q9WV30-2]
DR   CCDS; CCDS72168.1; -. [Q9WV30-4]
DR   RefSeq; NP_001273189.1; NM_001286260.1. [Q9WV30-4]
DR   RefSeq; NP_061293.2; NM_018823.2. [Q9WV30-2]
DR   RefSeq; NP_598718.2; NM_133957.3.
DR   RefSeq; XP_006531255.1; XM_006531192.3. [Q9WV30-1]
DR   RefSeq; XP_017168393.1; XM_017312904.1.
DR   AlphaFoldDB; Q9WV30; -.
DR   SMR; Q9WV30; -.
DR   BioGRID; 207661; 4.
DR   IntAct; Q9WV30; 2.
DR   MINT; Q9WV30; -.
DR   STRING; 10090.ENSMUSP00000127784; -.
DR   GlyGen; Q9WV30; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9WV30; -.
DR   PhosphoSitePlus; Q9WV30; -.
DR   EPD; Q9WV30; -.
DR   jPOST; Q9WV30; -.
DR   MaxQB; Q9WV30; -.
DR   PaxDb; 10090-ENSMUSP00000127784; -.
DR   ProteomicsDB; 293539; -. [Q9WV30-1]
DR   ProteomicsDB; 293540; -. [Q9WV30-2]
DR   ProteomicsDB; 293541; -. [Q9WV30-3]
DR   ProteomicsDB; 293542; -. [Q9WV30-4]
DR   Pumba; Q9WV30; -.
DR   Antibodypedia; 29866; 373 antibodies from 30 providers.
DR   DNASU; 54446; -.
DR   Ensembl; ENSMUST00000075922.11; ENSMUSP00000075311.5; ENSMUSG00000003847.17. [Q9WV30-4]
DR   Ensembl; ENSMUST00000125721.8; ENSMUSP00000116094.2; ENSMUSG00000003847.17. [Q9WV30-1]
DR   Ensembl; ENSMUST00000133026.8; ENSMUSP00000116631.2; ENSMUSG00000003847.17. [Q9WV30-3]
DR   Ensembl; ENSMUST00000151114.8; ENSMUSP00000119370.2; ENSMUSG00000003847.17. [Q9WV30-2]
DR   Ensembl; ENSMUST00000169453.8; ENSMUSP00000127784.2; ENSMUSG00000003847.17. [Q9WV30-2]
DR   GeneID; 54446; -.
DR   KEGG; mmu:54446; -.
DR   UCSC; uc009nhl.2; mouse. [Q9WV30-2]
DR   UCSC; uc009nhm.3; mouse. [Q9WV30-4]
DR   UCSC; uc009nhp.1; mouse. [Q9WV30-1]
DR   AGR; MGI:1859333; -.
DR   CTD; 10725; -.
DR   MGI; MGI:1859333; Nfat5.
DR   VEuPathDB; HostDB:ENSMUSG00000003847; -.
DR   eggNOG; ENOG502QSVE; Eukaryota.
DR   GeneTree; ENSGT00940000155213; -.
DR   HOGENOM; CLU_004396_0_0_1; -.
DR   InParanoid; Q9WV30; -.
DR   OMA; PYQNQVI; -.
DR   OrthoDB; 5405363at2759; -.
DR   TreeFam; TF326480; -.
DR   BioGRID-ORCS; 54446; 1 hit in 79 CRISPR screens.
DR   ChiTaRS; Nfat5; mouse.
DR   PRO; PR:Q9WV30; -.
DR   Proteomes; UP000000589; Chromosome 8.
DR   RNAct; Q9WV30; Protein.
DR   Bgee; ENSMUSG00000003847; Expressed in humerus cartilage element and 252 other cell types or tissues.
DR   ExpressionAtlas; Q9WV30; baseline and differential.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0005667; C:transcription regulator complex; IBA:GO_Central.
DR   GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; IDA:MGI.
DR   GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:MGI.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; TAS:MGI.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:MGI.
DR   GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR   GO; GO:0033173; P:calcineurin-NFAT signaling cascade; IBA:GO_Central.
DR   GO; GO:0071345; P:cellular response to cytokine stimulus; ISO:MGI.
DR   GO; GO:0006974; P:DNA damage response; ISS:UniProtKB.
DR   GO; GO:0006351; P:DNA-templated transcription; TAS:MGI.
DR   GO; GO:0035811; P:negative regulation of urine volume; TAS:BHF-UCL.
DR   GO; GO:0043123; P:positive regulation of canonical NF-kappaB signal transduction; ISO:MGI.
DR   GO; GO:0010628; P:positive regulation of gene expression; IDA:MGI.
DR   GO; GO:1904996; P:positive regulation of leukocyte adhesion to vascular endothelial cell; ISO:MGI.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
DR   GO; GO:0062176; P:R-loop processing; ISS:UniProtKB.
DR   GO; GO:0070884; P:regulation of calcineurin-NFAT signaling cascade; IDA:MGI.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0003091; P:renal water homeostasis; TAS:BHF-UCL.
DR   GO; GO:0009414; P:response to water deprivation; TAS:BHF-UCL.
DR   CDD; cd01178; IPT_NFAT; 1.
DR   CDD; cd07882; RHD-n_TonEBP; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   Gene3D; 2.60.40.340; Rel homology domain (RHD), DNA-binding domain; 1.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR014756; Ig_E-set.
DR   InterPro; IPR002909; IPT_dom.
DR   InterPro; IPR008366; NFAT.
DR   InterPro; IPR015646; NFAT5_RHD_DNA-bd.
DR   InterPro; IPR008967; p53-like_TF_DNA-bd_sf.
DR   InterPro; IPR032397; RHD_dimer.
DR   InterPro; IPR011539; RHD_DNA_bind_dom.
DR   InterPro; IPR037059; RHD_DNA_bind_dom_sf.
DR   PANTHER; PTHR12533; NFAT; 1.
DR   PANTHER; PTHR12533:SF10; NUCLEAR FACTOR OF ACTIVATED T-CELLS 5; 1.
DR   Pfam; PF16179; RHD_dimer; 1.
DR   Pfam; PF00554; RHD_DNA_bind; 1.
DR   PRINTS; PR01789; NUCFACTORATC.
DR   SMART; SM00429; IPT; 1.
DR   SUPFAM; SSF81296; E set domains; 1.
DR   SUPFAM; SSF49417; p53-like transcription factors; 1.
DR   PROSITE; PS50254; REL_2; 1.
DR   Genevisible; Q9WV30; MM.
PE   1: Evidence at protein level;
KW   Acetylation; Activator; ADP-ribosylation; Alternative splicing; Chromosome;
KW   Cytoplasm; DNA damage; DNA-binding; Isopeptide bond; Nucleus;
KW   Phosphoprotein; Reference proteome; Transcription;
KW   Transcription regulation; Ubl conjugation.
FT   CHAIN           1..1534
FT                   /note="Nuclear factor of activated T-cells 5"
FT                   /id="PRO_0000205184"
FT   DOMAIN          264..443
FT                   /note="RHD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00265"
FT   DNA_BIND        293..300
FT                   /evidence="ECO:0000250|UniProtKB:O94916"
FT   REGION          34..89
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          175..220
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          241..265
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          607..666
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          845..885
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          953..993
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1241..1369
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1478..1510
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        42..56
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        68..89
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        175..195
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        241..261
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        862..885
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         120
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O94916"
FT   MOD_RES         122
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         134
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O94916"
FT   MOD_RES         135
FT                   /note="Phosphothreonine; by CDK5"
FT                   /evidence="ECO:0000250|UniProtKB:O94916"
FT   MOD_RES         155
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O94916"
FT   MOD_RES         560
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O94916"
FT   CROSSLNK        555
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO1); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:O94916"
FT   CROSSLNK        555
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:O94916"
FT   CROSSLNK        602
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:O94916"
FT   VAR_SEQ         24
FT                   /note="R -> RDSLKLHPSQTFHRAGLLE (in isoform 2 and isoform
FT                   3)"
FT                   /evidence="ECO:0000303|PubMed:11233530,
FT                   ECO:0000305|PubMed:11934689"
FT                   /id="VSP_058790"
FT   VAR_SEQ         67..81
FT                   /note="DASSAPSSSSMGGAC -> GFASEAGSVCIKNDL (in isoform 3)"
FT                   /evidence="ECO:0000305|PubMed:11934689"
FT                   /id="VSP_058791"
FT   VAR_SEQ         82..1534
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000305|PubMed:11934689"
FT                   /id="VSP_058789"
FT   VAR_SEQ         1213..1225
FT                   /note="VALGSLPPNPMPQ -> ESLHSHITPDACK (in isoform 4)"
FT                   /evidence="ECO:0000303|Ref.1"
FT                   /id="VSP_058792"
FT   VAR_SEQ         1226..1534
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|Ref.1"
FT                   /id="VSP_058793"
FT   CONFLICT        108
FT                   /note="C -> G (in Ref. 4; AAK97603)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1534 AA;  165800 MW;  996904A84D3A7AFE CRC64;
     MPSDFISLLS ADLDLESPKS LYSRESVYDL LPKELQLPPP RETSVASMSQ TSGGEAGSPP
     PAVVAADASS APSSSSMGGA CSSFTTSSSP TIYSTSVTDS KAMQVESCSS AVGVSNRGVS
     EKQLTGNTVQ QHPSTPKRHT VLYISPPPED LLDNSRMSCQ DEGCGLESEQ SCSMWMEDSP
     SNFSNMSTSS YNDNTEVPRK SRKRNPKQRP GVKRRDCEES NMDIFDADSA KAPHYVLSQL
     TTDNKGNSKA GNGTLDSQKG TGVKKSPMLC GQYPVKSEGK ELKIVVQPET QHRARYLTEG
     SRGSVKDRTQ QGFPTVKLEG HNEPVVLQVF VGNDSGRVKP HGFYQACRVT GRNTTPCKEV
     DIEGTTVIEV GLDPSNNMTL AVDCVGILKL RNADVEARIG IAGSKKKSTR ARLVFRVNIT
     RKDGSTLTLQ TPSSPILCTQ PAGVPEILKK SLHSCSVKGE EEVFLIGKNF LKGTKVIFQE
     NVSDENSWKS EAEIDMELFH QNHLIVKVPP YHDQHITLPV SVGIYVVTNA GRSHDVQPFT
     YTPDPAAGAL NVNVKKEISS PARPCSFEEA MKAMKTTGCN VDKVTILPNA LITPLISSSM
     IKTEDVTPME VTSEKRSSPI FQTTKSIGST QQTLETISNI AGGAPFSSPS SSSHLTPESE
     NQQQLQPKAY NPETLTTIQT QDISQPGTFP AVSAASQLPS SDALLQQATQ FQTREAQSRD
     TIQSDTVVNL SQLTEASQQQ QSPLQEQAQT LQQQIPSNIF PSPSSVSQLQ STIQQLQAGS
     FTGSAAGGRS GSVDLVQQVL EAQQQLSSVL FSTPDGNENV QEQLNADIFQ VSQIQNSVSP
     GMFSSAESAV HTRPDNLLPG RADSVHQQTE NTLSNQQQQQ QQQQQVMESS AAMVMEMQQS
     ICQAAAQIQS ELFPSAASAS GSLQQSPVYQ QPSHMMSALP TNEDMQMQCE LFSSPPAASG
     NETSTTTTPQ VATPGSTMFQ TPSSGDGEET GAQAKQIQNS VFQTMVQMQR SGDSQPQVNL
     FSSTKNIMSV QNNGTQQQGN SLFQQGSEMM SLQSGNFLQQ SSHSQAQLFH PQNPIADAQN
     LSQETQGSIF HSPNPIVHSQ TSTASSEQLQ PSMFHSQNTI AVLQGSSVPQ DQQSPNIFLS
     QSSINNLQTN TVAQEEQISF FAAQNSISPL QSTSNTEQQA AFQQQPPISH IQTPILSQEQ
     AQPSQQGLFQ PQVALGSLPP NPMPQNQQGP IFQTQRPIVG MQSNSPSQEQ QQQQQQQQQQ
     QQQQQQQQQS ILFSNQNAMA TMASQKQPPP NMMFSPNQNP MASQEQQNQS IFHQQSNMAP
     MNQEQQPMQF QNQPTVSSLQ NPGPTQSESP QTSLFHSSPQ IQLVQGSPSS QDQQVTLFLS
     PASMSALQTS INQPDMQQSP LYSPQNNIPG IQGSTSSPQP QATLFHNTTG GTINQIQNSP
     GSSQQTSGMF LFGIQNNCSQ LLTSGPATLP DQLMAINQQG QPQNEGQSSV TTLLSQQMPE
     TSPLASSVNS SQNMEKIDLL VSLQSQGNNL TGSF
//