ID   E41L3_MOUSE             Reviewed;         929 AA.
AC   Q9WV92; Q69ZT8; Q9R102;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   24-JAN-2024, entry version 193.
DE   RecName: Full=Band 4.1-like protein 3;
DE   AltName: Full=4.1B;
DE   AltName: Full=Differentially expressed in adenocarcinoma of the lung protein 1;
DE            Short=DAL-1;
DE            Short=DAL1P;
DE            Short=mDAL-1;
DE   AltName: Full=Erythrocyte membrane protein band 4.1-like 3 {ECO:0000312|MGI:MGI:103008};
DE   Contains:
DE     RecName: Full=Band 4.1-like protein 3, N-terminally processed;
GN   Name=Epb41l3 {ECO:0000312|MGI:MGI:103008};
GN   Synonyms=Dal1 {ECO:0000312|MGI:MGI:103008}, Epb4.1l3
GN   {ECO:0000312|MGI:MGI:103008}, Kiaa0987;
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] (ISOFORMS 1; 2; 3; 4; 5 AND 6), SUBUNIT,
RP   SUBCELLULAR LOCATION, ACTIN-BINDING, AND TISSUE SPECIFICITY.
RC   TISSUE=Brain;
RX   PubMed=10652311; DOI=10.1074/jbc.275.5.3247;
RA   Parra M., Gascard P., Walensky L.D., Gimm J.A., Blackshaw S., Chan N.,
RA   Takakuwa Y., Berger T., Lee G., Chasis J.A., Snyder S.H., Mohandas N.,
RA   Conboy J.G.;
RT   "Molecular and functional characterization of protein 4.1B, a novel member
RT   of the protein 4.1 family with high level, focal expression in brain.";
RL   J. Biol. Chem. 275:3247-3255(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 6-929 (ISOFORM 7).
RC   STRAIN=BALB/cJ; TISSUE=Brain;
RA   Azam M., Andrabi S., Lin L., Newsham I., Chishti A.H.;
RT   "Mouse DAL-1 (mDAL-1) cDNA sequence.";
RL   Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 202-929 (ISOFORM 8).
RC   TISSUE=Fetal brain;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT   The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 719-929 (ISOFORMS 4/5/6/7).
RA   Marra M., Hillier L., Kucaba T., Martin J., Beck C., Wylie T.,
RA   Underwood K., Steptoe M., Theising B., Allen M., Bowers Y., Person B.,
RA   Swaller T., Gibbons M., Pape D., Harvey N., Schurk R., Ritter E., Kohn S.,
RA   Shin T., Jackson Y., Cardenas M., McCann R., Waterston R., Wilson R.;
RL   Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=15592455; DOI=10.1038/nbt1046;
RA   Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA   Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT   "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL   Nat. Biotechnol. 23:94-101(2005).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96 AND THR-923, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.m600046-mcp200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B.,
RA   Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in naive
RT   and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of electron
RT   capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-451; SER-486; THR-495;
RP   THR-518; SER-543; THR-545; SER-547; THR-725; SER-802 AND SER-804,
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-543 (ISOFORMS 3 AND 6),
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-525 (ISOFORM 7),
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-451 (ISOFORMS 7 AND 8), AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   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).
CC   -!- FUNCTION: Tumor suppressor that inhibits cell proliferation and
CC       promotes apoptosis. Modulates the activity of protein arginine N-
CC       methyltransferases, including PRMT3 and PRMT5 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Interacts (via FERM domain) with CADM1. Interacts (via FERM
CC       domain) with PRMT3; the interaction is direct and inhibits the protein-
CC       arginine N-methyltransferase activity of PRMT3. Interacts with PRMT5.
CC       Interacts with PRMT6. {ECO:0000250|UniProtKB:Q9Y2J2}.
CC   -!- SUBUNIT: [Isoform 2]: Has the complete spectrin--actin-binding (SAB)
CC       domain and fully interacts with spectrin and actin.
CC       {ECO:0000269|PubMed:10652311}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cell
CC       membrane {ECO:0000269|PubMed:10652311}; Peripheral membrane protein
CC       {ECO:0000269|PubMed:10652311}; Cytoplasmic side
CC       {ECO:0000269|PubMed:10652311}. Cytoplasm {ECO:0000250}. Cell junction
CC       {ECO:0000269|PubMed:10652311}. Note=Detected in the cytoplasm of
CC       actively dividing cells.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=8;
CC         Comment=Experimental confirmation may be lacking for some isoforms.;
CC       Name=1; Synonyms=4.1B-brain;
CC         IsoId=Q9WV92-1; Sequence=Displayed;
CC       Name=2; Synonyms=4.1B-heart;
CC         IsoId=Q9WV92-2; Sequence=VSP_000490, VSP_000489;
CC       Name=3; Synonyms=4.1B-kidney;
CC         IsoId=Q9WV92-3; Sequence=VSP_000490;
CC       Name=4; Synonyms=4.1b-brain;
CC         IsoId=Q9WV92-4; Sequence=VSP_000491;
CC       Name=5; Synonyms=4.1B-heart;
CC         IsoId=Q9WV92-5; Sequence=VSP_000490, VSP_000489, VSP_000491;
CC       Name=6; Synonyms=4.1B-kidney;
CC         IsoId=Q9WV92-6; Sequence=VSP_000490, VSP_000491;
CC       Name=7;
CC         IsoId=Q9WV92-7; Sequence=VSP_000487, VSP_000490, VSP_000488,
CC                                  VSP_000491;
CC       Name=8;
CC         IsoId=Q9WV92-8; Sequence=VSP_000487, VSP_023063, VSP_000491;
CC   -!- TISSUE SPECIFICITY: Detected in brain (at protein level). Highest
CC       expression in brain, lower in testis, adrenal gland, heart and kidney.
CC       Also present in muscle and epithelial cells. Isoform 1 is expressed in
CC       brain, isoform 2 is expressed in heart and isoform 3 is mostly
CC       expressed in kidney but also in heart and brain. Isoform 6 seems to be
CC       most abundant in kidney while isoform 4 and isoform 5 are predominantly
CC       expressed in heart and brain. {ECO:0000269|PubMed:10652311}.
CC   -!- MISCELLANEOUS: The complete SAB domain is present only in the heart-
CC       specific isoforms (isoform 2 and isoform 5).
CC   -!- MISCELLANEOUS: [Isoform 7]: Inferred from the cDNA sequence of Ref.2.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD51365.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AF152247; AAD38048.1; -; mRNA.
DR   EMBL; AF177146; AAD51365.1; ALT_INIT; mRNA.
DR   EMBL; AK173080; BAD32358.1; -; mRNA.
DR   CCDS; CCDS28952.1; -. [Q9WV92-1]
DR   RefSeq; NP_038841.1; NM_013813.1. [Q9WV92-1]
DR   RefSeq; XP_011244586.1; XM_011246284.1.
DR   RefSeq; XP_011244591.1; XM_011246289.1.
DR   RefSeq; XP_017172724.1; XM_017317235.1.
DR   RefSeq; XP_017172725.1; XM_017317236.1.
DR   AlphaFoldDB; Q9WV92; -.
DR   SMR; Q9WV92; -.
DR   BioGRID; 199461; 35.
DR   IntAct; Q9WV92; 16.
DR   STRING; 10090.ENSMUSP00000079098; -.
DR   GlyGen; Q9WV92; 10 sites, 1 O-linked glycan (10 sites).
DR   iPTMnet; Q9WV92; -.
DR   PhosphoSitePlus; Q9WV92; -.
DR   SwissPalm; Q9WV92; -.
DR   EPD; Q9WV92; -.
DR   jPOST; Q9WV92; -.
DR   MaxQB; Q9WV92; -.
DR   PaxDb; 10090-ENSMUSP00000108300; -.
DR   PeptideAtlas; Q9WV92; -.
DR   ProteomicsDB; 277738; -. [Q9WV92-1]
DR   ProteomicsDB; 277739; -. [Q9WV92-2]
DR   ProteomicsDB; 277740; -. [Q9WV92-3]
DR   ProteomicsDB; 277741; -. [Q9WV92-4]
DR   ProteomicsDB; 277742; -. [Q9WV92-5]
DR   ProteomicsDB; 277743; -. [Q9WV92-6]
DR   ProteomicsDB; 277744; -. [Q9WV92-7]
DR   ProteomicsDB; 277745; -. [Q9WV92-8]
DR   Pumba; Q9WV92; -.
DR   Antibodypedia; 21920; 284 antibodies from 31 providers.
DR   DNASU; 13823; -.
DR   Ensembl; ENSMUST00000080208.7; ENSMUSP00000079098.6; ENSMUSG00000024044.20. [Q9WV92-1]
DR   Ensembl; ENSMUST00000112680.8; ENSMUSP00000108300.2; ENSMUSG00000024044.20. [Q9WV92-2]
DR   GeneID; 13823; -.
DR   KEGG; mmu:13823; -.
DR   UCSC; uc008dkp.1; mouse. [Q9WV92-1]
DR   UCSC; uc008dkq.1; mouse. [Q9WV92-7]
DR   UCSC; uc008dkr.1; mouse. [Q9WV92-8]
DR   AGR; MGI:103008; -.
DR   CTD; 23136; -.
DR   MGI; MGI:103008; Epb41l3.
DR   VEuPathDB; HostDB:ENSMUSG00000024044; -.
DR   eggNOG; KOG3527; Eukaryota.
DR   GeneTree; ENSGT00940000157047; -.
DR   HOGENOM; CLU_003623_3_1_1; -.
DR   InParanoid; Q9WV92; -.
DR   OMA; RCKENGH; -.
DR   OrthoDB; 5319111at2759; -.
DR   PhylomeDB; Q9WV92; -.
DR   TreeFam; TF351626; -.
DR   Reactome; R-MMU-6794361; Neurexins and neuroligins.
DR   BioGRID-ORCS; 13823; 6 hits in 46 CRISPR screens.
DR   ChiTaRS; Epb41l3; mouse.
DR   PRO; PR:Q9WV92; -.
DR   Proteomes; UP000000589; Chromosome 17.
DR   RNAct; Q9WV92; Protein.
DR   Bgee; ENSMUSG00000024044; Expressed in small intestine Peyer's patch and 242 other cell types or tissues.
DR   ExpressionAtlas; Q9WV92; baseline and differential.
DR   GO; GO:0030054; C:cell junction; ISO:MGI.
DR   GO; GO:0005911; C:cell-cell junction; ISS:HGNC-UCL.
DR   GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0044224; C:juxtaparanode region of axon; IDA:BHF-UCL.
DR   GO; GO:0033270; C:paranode region of axon; IDA:BHF-UCL.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0014069; C:postsynaptic density; IDA:MGI.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0106006; F:cytoskeletal protein-membrane anchor activity; TAS:BHF-UCL.
DR   GO; GO:0005200; F:structural constituent of cytoskeleton; TAS:BHF-UCL.
DR   GO; GO:0031032; P:actomyosin structure organization; IBA:GO_Central.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0061564; P:axon development; IMP:MGI.
DR   GO; GO:0030866; P:cortical actin cytoskeleton organization; IEA:InterPro.
DR   GO; GO:0030865; P:cortical cytoskeleton organization; TAS:BHF-UCL.
DR   GO; GO:0043217; P:myelin maintenance; IMP:BHF-UCL.
DR   GO; GO:0048812; P:neuron projection morphogenesis; IMP:BHF-UCL.
DR   GO; GO:0030913; P:paranodal junction assembly; IMP:BHF-UCL.
DR   GO; GO:1990227; P:paranodal junction maintenance; IMP:MGI.
DR   GO; GO:0071205; P:protein localization to juxtaparanode region of axon; IMP:BHF-UCL.
DR   GO; GO:0002175; P:protein localization to paranode region of axon; IMP:BHF-UCL.
DR   GO; GO:0072659; P:protein localization to plasma membrane; IMP:BHF-UCL.
DR   GO; GO:0008360; P:regulation of cell shape; IMP:BHF-UCL.
DR   CDD; cd14473; FERM_B-lobe; 1.
DR   CDD; cd13184; FERM_C_4_1_family; 1.
DR   CDD; cd17203; FERM_F1_EPB41L3; 1.
DR   Gene3D; 1.20.80.10; -; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   InterPro; IPR030691; Band4.1-L3_FERM_F1.
DR   InterPro; IPR008379; Band_4.1_C.
DR   InterPro; IPR019749; Band_41_domain.
DR   InterPro; IPR000798; Ez/rad/moesin-like.
DR   InterPro; IPR014847; FA.
DR   InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
DR   InterPro; IPR035963; FERM_2.
DR   InterPro; IPR019748; FERM_central.
DR   InterPro; IPR019747; FERM_CS.
DR   InterPro; IPR000299; FERM_domain.
DR   InterPro; IPR018979; FERM_N.
DR   InterPro; IPR018980; FERM_PH-like_C.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR007477; SAB_dom.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   PANTHER; PTHR23280; 4.1 G PROTEIN; 1.
DR   PANTHER; PTHR23280:SF20; BAND 4.1-LIKE PROTEIN 3; 1.
DR   Pfam; PF05902; 4_1_CTD; 1.
DR   Pfam; PF08736; FA; 1.
DR   Pfam; PF09380; FERM_C; 1.
DR   Pfam; PF00373; FERM_M; 1.
DR   Pfam; PF09379; FERM_N; 1.
DR   Pfam; PF04382; SAB; 1.
DR   PIRSF; PIRSF002304; Membrane_skeletal_4_1; 1.
DR   PRINTS; PR00935; BAND41.
DR   PRINTS; PR00661; ERMFAMILY.
DR   SMART; SM00295; B41; 1.
DR   SMART; SM01195; FA; 1.
DR   SMART; SM01196; FERM_C; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF47031; Second domain of FERM; 1.
DR   SUPFAM; SSF54236; Ubiquitin-like; 1.
DR   PROSITE; PS00660; FERM_1; 1.
DR   PROSITE; PS00661; FERM_2; 1.
DR   PROSITE; PS50057; FERM_3; 1.
DR   Genevisible; Q9WV92; MM.
PE   1: Evidence at protein level;
KW   Acetylation; Actin-binding; Alternative splicing; Apoptosis; Cell junction;
KW   Cell membrane; Cytoplasm; Cytoskeleton; Membrane; Phosphoprotein;
KW   Reference proteome; Tumor suppressor.
FT   CHAIN           1..929
FT                   /note="Band 4.1-like protein 3"
FT                   /id="PRO_0000423195"
FT   INIT_MET        1
FT                   /note="Removed; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y2J2"
FT   CHAIN           2..929
FT                   /note="Band 4.1-like protein 3, N-terminally processed"
FT                   /id="PRO_0000219400"
FT   DOMAIN          118..399
FT                   /note="FERM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00084"
FT   REGION          1..72
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          402..528
FT                   /note="Hydrophilic"
FT   REGION          490..554
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          559..602
FT                   /note="Spectrin--actin-binding"
FT   REGION          608..630
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          665..689
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          705..807
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          777..929
FT                   /note="C-terminal (CTD)"
FT   COMPBIAS        496..539
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        705..756
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        758..781
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y2J2"
FT   MOD_RES         2
FT                   /note="N-acetylthreonine; in Band 4.1-like protein 3, N-
FT                   terminally processed"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y2J2"
FT   MOD_RES         96
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:16452087,
FT                   ECO:0007744|PubMed:19131326"
FT   MOD_RES         428
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y2J2"
FT   MOD_RES         451
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         486
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         495
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         518
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         543
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         545
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         547
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         725
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         802
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         804
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         923
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:16452087"
FT   VAR_SEQ         455..472
FT                   /note="Missing (in isoform 7 and isoform 8)"
FT                   /evidence="ECO:0000303|PubMed:15368895, ECO:0000303|Ref.2"
FT                   /id="VSP_000487"
FT   VAR_SEQ         528
FT                   /note="K -> KSPPGHGAADSCPPSPPSAHPDPPPPTELRRRCKEKERAEPSSLESE
FT                   AQGKAYLGDQDVAFSYRQPAGKGTTLFSFSLQLPESFPSLLDEDGYLSFPNLSETNLLP
FT                   QSWQHFLPIRSPSLLPCFLFIFFFLLSASFSVPYALTLSFPLALCLCYLEPKAASLSAS
FT                   LDNDPSDSSEEE (in isoform 8)"
FT                   /evidence="ECO:0000303|PubMed:15368895"
FT                   /id="VSP_023063"
FT   VAR_SEQ         547..558
FT                   /note="Missing (in isoform 2, isoform 3, isoform 5, isoform
FT                   6 and isoform 7)"
FT                   /evidence="ECO:0000303|PubMed:10652311, ECO:0000303|Ref.2"
FT                   /id="VSP_000490"
FT   VAR_SEQ         559
FT                   /note="D -> NSLIKRIKGENVYVKHSNLMLED (in isoform 2 and
FT                   isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:10652311"
FT                   /id="VSP_000489"
FT   VAR_SEQ         623..663
FT                   /note="Missing (in isoform 7)"
FT                   /evidence="ECO:0000303|Ref.2"
FT                   /id="VSP_000488"
FT   VAR_SEQ         894..929
FT                   /note="ALAQAIKEAKEQHPDMSVTKVVVHKETEITPEDGED -> E (in
FT                   isoform 4, isoform 5, isoform 6, isoform 7 and isoform 8)"
FT                   /evidence="ECO:0000303|PubMed:10652311,
FT                   ECO:0000303|PubMed:15368895, ECO:0000303|Ref.2"
FT                   /id="VSP_000491"
FT   CONFLICT        6..10
FT                   /note="GSDSE -> RIRLR (in Ref. 2; AAD51365)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        28
FT                   /note="Q -> R (in Ref. 2; AAD51365)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        288
FT                   /note="A -> V (in Ref. 2; AAD51365)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        306
FT                   /note="V -> G (in Ref. 2; AAD51365)"
FT                   /evidence="ECO:0000305"
FT   MOD_RES         Q9WV92-3:543
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         Q9WV92-6:543
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         Q9WV92-7:451
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         Q9WV92-7:525
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         Q9WV92-8:451
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
SQ   SEQUENCE   929 AA;  103338 MW;  F4975FF405DA44AE CRC64;
     MTTESGSDSE SKPDQEAEPQ EAAGPQGQAG AQPGPEPAGG NGSLNGEKQQ PALEQFPEAA
     AHSTPVKREI GDKDRDFAAA AAKQLEYQQF EDDKLSQRSS SSKLSRSPLK IVKRPKSMQC
     KVTLLDGSEY GCDVDKRSRG QVLFDKVCEH LNLLEKDYFG LTYRDAENQK NWLDPAKEIK
     KQIRSGAWHF SFNVKFYPPD PAQLSEDITR YYLCLQLRDD IVSGRLPCSF VTLALLGSYT
     VQSELGDYDP DECGNDYISE FRFAPNHTKE LEDKVIELHK SHRGMTPAEA EMHFLENAKK
     LSMYGVDLHH AKDSEGVEIM LGVCASGLLI YRDRLRINRF AWPKVLKISY KRNNFYIKIR
     PGEFEQFEST IGFKLPNHRA AKRLWKVCVE HHTFFRLLLP EAPPKKFLTL GSKFRYSGRT
     QAQTRRASAL IDRPAPYFER SSSKRYTMSR SLDGASVSEN HEIYMKDSVS AAEVGTGQYA
     TTKGISQTNL ITTVTPEKKA EEERVEEEDR RKKAEEATPV TALRHEGKTD SERTDTAADG
     ETSATESDQE EDAEIKAQDL DKTQDELMKH QTNISELKRT FLETSTETAL TNEWEKRLST
     SPVRLAARQE DAPMIEPLVP EETKQSSGEK LMDGSEILSL LESARKPTEF IGGVSSTTQS
     WVQKLETKTE PVEAEVESTP HPQPLSTEKV LQETILVEER HVMSVHASGD ASHTARDEVD
     AAESTPTDRR HTGKGKEGSS VTEAAKEQRG EEVDQSAPEQ EQPATVSHEE EQASTIRTSE
     GLEQKSHFES STVRVESTSV GSISPGGAKL EISTKEVPVV HTETKTITYE SSQVDPGADL
     EPGVLMSAQT ITSETTSTTT TTHITKTVKG GISETRIEKR IVITGDADID HDQALAQAIK
     EAKEQHPDMS VTKVVVHKET EITPEDGED
//