E41L3_MOUSE
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 03-AUG-2022, entry version 185.
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},
GN Epb4.1l3 {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, Spleen, and
RC 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. [Q9WV92-8]
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; 25.
DR IntAct; Q9WV92; 15.
DR STRING; 10090.ENSMUSP00000108300; -.
DR iPTMnet; Q9WV92; -.
DR PhosphoSitePlus; Q9WV92; -.
DR SwissPalm; Q9WV92; -.
DR EPD; Q9WV92; -.
DR jPOST; Q9WV92; -.
DR MaxQB; Q9WV92; -.
DR PaxDb; Q9WV92; -.
DR PeptideAtlas; Q9WV92; -.
DR PRIDE; 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 Antibodypedia; 21920; 253 antibodies from 31 providers.
DR DNASU; 13823; -.
DR Ensembl; ENSMUST00000080208; ENSMUSP00000079098; ENSMUSG00000024044. [Q9WV92-1]
DR Ensembl; ENSMUST00000112680; ENSMUSP00000108300; ENSMUSG00000024044. [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 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; NDYVSEF; -.
DR OrthoDB; 193911at2759; -.
DR PhylomeDB; Q9WV92; -.
DR TreeFam; TF351626; -.
DR Reactome; R-MMU-6794361; Neurexins and neuroligins.
DR BioGRID-ORCS; 13823; 6 hits in 41 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 239 other tissues.
DR ExpressionAtlas; Q9WV92; baseline and differential.
DR Genevisible; Q9WV92; MM.
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:0001558; P:regulation of cell growth; IEA:InterPro.
DR GO; GO:0008360; P:regulation of cell shape; IMP:BHF-UCL.
DR CDD; cd14473; FERM_B-lobe; 1.
DR Gene3D; 1.20.80.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR030691; Band4.1-L3.
DR InterPro; IPR008379; Band_4.1_C.
DR InterPro; IPR019749; Band_41_domain.
DR InterPro; IPR000798; Ez/rad/moesin-like.
DR InterPro; IPR014847; FERM-adjacent.
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:SF20; PTHR23280:SF20; 2.
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 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; SSF47031; SSF47031; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS00660; FERM_1; 1.
DR PROSITE; PS00661; FERM_2; 1.
DR PROSITE; PS50057; FERM_3; 1.
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
