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AT-rich interactive domain-containing protein 1A (ARID domain-containing protein 1A) (BRG1-associated factor 250) (BAF250) (BRG1-associated factor 250a) (BAF250A) (Osa homolog 1) (SWI-like protein) (SWI/SNF complex protein p270) (SWI/SNF-related, matrix-associated, actin-dependent regulator of chromatin subfamily F member 1)

 ARI1A_MOUSE             Reviewed;        2283 AA.
A2BH40; Q640Q1; Q925Q1;
09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
20-FEB-2007, sequence version 1.
25-OCT-2017, entry version 104.
RecName: Full=AT-rich interactive domain-containing protein 1A;
Short=ARID domain-containing protein 1A;
AltName: Full=BRG1-associated factor 250;
Short=BAF250;
AltName: Full=BRG1-associated factor 250a;
Short=BAF250A;
AltName: Full=Osa homolog 1;
AltName: Full=SWI-like protein;
AltName: Full=SWI/SNF complex protein p270;
AltName: Full=SWI/SNF-related, matrix-associated, actin-dependent regulator of chromatin subfamily F member 1;
Name=Arid1a; Synonyms=Baf250, Baf250a, Osa1, Smarcf1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ALTERNATIVE SPLICING (ISOFORM
3), TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=11318604; DOI=10.1006/geno.2001.6477;
Kozmik Z., Machon O., Kralova J., Kreslova J., Paces J., Vlcek C.;
"Characterization of mammalian orthologues of the Drosophila osa gene:
cDNA cloning, expression, chromosomal localization, and direct
physical interaction with Brahma chromatin-remodeling complex.";
Genomics 73:140-148(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
STRAIN=C57BL/6J; TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
FUNCTION OF THE NBAF AND NPBAF COMPLEXES, IDENTIFICATION BY MASS
SPECTROMETRY, IDENTIFICATION IN THE NBAF AND NPBAF COMPLEXES, AND
DEVELOPMENTAL STAGE.
PubMed=17640523; DOI=10.1016/j.neuron.2007.06.019;
Lessard J., Wu J.I., Ranish J.A., Wan M., Winslow M.M., Staahl B.T.,
Wu H., Aebersold R., Graef I.A., Crabtree G.R.;
"An essential switch in subunit composition of a chromatin remodeling
complex during neural development.";
Neuron 55:201-215(2007).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-697, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-365, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-365; SER-384; SER-697;
SER-699; SER-703; SER-731; SER-765; SER-773 AND THR-1874, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[8]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-431 AND ARG-1277, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, and Embryo;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
-!- FUNCTION: Involved in transcriptional activation and repression of
select genes by chromatin remodeling (alteration of DNA-nucleosome
topology). Binds DNA non-specifically. Belongs to the neural
progenitors-specific chromatin remodeling complex (npBAF complex)
and the neuron-specific chromatin remodeling complex (nBAF
complex). During neural development a switch from a
stem/progenitor to a post-mitotic chromatin remodeling mechanism
occurs as neurons exit the cell cycle and become committed to
their adult state. The transition from proliferating neural
stem/progenitor cells to post-mitotic neurons requires a switch in
subunit composition of the npBAF and nBAF complexes. As neural
progenitors exit mitosis and differentiate into neurons, npBAF
complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are
exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B
or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The
npBAF complex is essential for the self-renewal/proliferative
capacity of the multipotent neural stem cells. The nBAF complex
along with CREST plays a role regulating the activity of genes
essential for dendrite growth. {ECO:0000250,
ECO:0000269|PubMed:17640523}.
-!- SUBUNIT: Component of SWI/SNF chromatin remodeling complexes, in
some of which it can be mutually exclusive with ARID1B/BAF250B.
Component of the BAF (SWI/SNF-A) complex, which includes at least
actin (ACTB), ARID1A, ARID1B/BAF250, SMARCA2,
SMARCA4/BRG1/BAF190A, ACTL6A/BAF53, ACTL6B/BAF53B, SMARCE1/BAF57,
SMARCC1/BAF155, SMARCC2/BAF170, SMARCB1/SNF5/INI1, and one or more
of SMARCD1/BAF60A, SMARCD2/BAF60B, or SMARCD3/BAF60C. In muscle
cells, the BAF complex also contains DPF3. Component of the
SWI/SNF-B (PBAF) complex, at least composed of
SMARCA4/BRG1/BAF190A, SMARCB1/BAF47, ACTL6A/BAF53A or
ACTL6B/BAF53B, SMARCE1/BAF57, SMARCD1/BAF60A, SMARCD2/BAF60B,
perhaps SMARCD3/BAF60C, SMARCC1/BAF155, SMARCC2/BAF170,
PB1/BAF180, ARID2/BAF200, ARID1A/BAF250A or ARID1B/BAF250B and
actin. Component of the SWI/SNF Brm complex, at least composed of
SMARCA2/BRM/BAF190B, SMARCB1/BAF47, ACTL6A/BAF53A or
ACTL6B/BAF53B, SMARCE1/BAF57, BAF60 (one or more of
SMARCD1/BAF60A, SMARCD2/BAF60B, or SMARCD3/BAF60C),
SMARCC1/BAF155, SMARCC2/BAF170, ARID1A/BAF250A, SIN3A, HDAC1,
HDAC2, and RBAP4. Component of the SWI/SNF complex Brg1(I), at
least composed of SMARCA4/BRG1/BAF190A, SMARCB1/BAF47,
ACTL6A/BAF53A or ACTL6B/BAF53B, SMARCE1/BAF57, BAF60 (one or more
of SMARCD1/BAF60A, SMARCD2/BAF60B, or SMARCD3/BAF60C),
SMARCC1/BAF155, SMARCC2/BAF170, ARID1A/BAF250A, SIN3A, and
probably HDAC2 and RBAP4. Component of the SWI/SNF Brg1(II), at
least composed of SMARCA4/BRG1/BAF190A, SMARCB1/BAF47,
ACTL6A/BAF53A or ACTL6B/BAF53B, SMARCE1/BAF57, SMARCC1/BAF155,
SMARCC2/BAF170, ARID1A/BAF250A and probably HDAC2 and RBAP4.
Component of a SWI/SNF-like EPAFa complex, at least composed of
SMARCA4/BRG1/BAF190A, SMARCB1/BAF47, ACTL6A/BAF53A, SMARCE1/BAF57,
SMARCD1/BAF60A, SMARCC1/BAF155, SMARCC2/BAF170, BAF250A and
MLLT1/ENL. Component of a SWI/SNF-like complex containing
ARID1A/BAF250A and ARID1B/BAF250B. Interacts through its C-
terminus with SMARCA2/BRM/BAF190B and SMARCA4/BRG1/BAF190A.
Interacts with SMARCC1/BAF155 (By similarity). Component of neural
progenitors-specific chromatin remodeling complex (npBAF complex)
composed of at least, ARID1A/BAF250A or ARID1B/BAF250B,
SMARCD1/BAF60A, SMARCD3/BAF60C, SMARCA2/BRM/BAF190B,
SMARCA4/BRG1/BAF190A, SMARCB1/BAF47, SMARCC1/BAF155,
SMARCE1/BAF57, SMARCC2/BAF170, PHF10/BAF45A, ACTL6A/BAF53A and
actin. Component of neuron-specific chromatin remodeling complex
(nBAF complex) composed of at least, ARID1A/BAF250A or
ARID1B/BAF250B, SMARCD1/BAF60A, SMARCD3/BAF60C,
SMARCA2/BRM/BAF190B, SMARCA4/BRG1/BAF190A, SMARCB1/BAF47,
SMARCC1/BAF155, SMARCE1/BAF57, SMARCC2/BAF170, DPF1/BAF45B,
DPF3/BAF45C, ACTL6B/BAF53B and actin. {ECO:0000250,
ECO:0000269|PubMed:17640523}.
-!- INTERACTION:
O35845:Smarca4; NbExp=2; IntAct=EBI-371499, EBI-371515;
Q3TKT4:Smarca4; NbExp=7; IntAct=EBI-371499, EBI-1210244;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
ProRule:PRU00355}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=A2BH40-1; Sequence=Displayed;
Name=2;
IsoId=A2BH40-2; Sequence=VSP_038737, VSP_038739;
Name=3;
IsoId=A2BH40-3; Sequence=VSP_038740;
Name=4;
IsoId=A2BH40-4; Sequence=VSP_038737, VSP_038738, VSP_038739;
-!- TISSUE SPECIFICITY: Widely expressed. Expressed at high levels in
the testis. {ECO:0000269|PubMed:11318604}.
-!- DEVELOPMENTAL STAGE: Expressed ubiquitously throughout the
developing spinal cord, brain and other embryonic tissues at
E10.5-E16.5. In the earlier stages at E9.5 and E10.5, is fairly
ubiquitous though with clearly elevated expression in the progress
zone and lateral mesoderm of limb buds, optic and otic vesicle,
neural tube, and brain. Later on at E11.5 and E12.5, expression
becomes more restricted and is confined to the interdigital area
of limbs, dorsal mes/metencephalon, neocortex, and neural tube.
Expression is seen in the eye lens from E10.5 until E12.5.
{ECO:0000269|PubMed:11318604, ECO:0000269|PubMed:17640523}.
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EMBL; AF268912; AAK54504.1; -; mRNA.
EMBL; CR751606; CAM20580.1; -; Genomic_DNA.
EMBL; BX537327; CAM20580.1; JOINED; Genomic_DNA.
EMBL; CR925752; CAM20580.1; JOINED; Genomic_DNA.
EMBL; BX537327; CAM25151.1; -; Genomic_DNA.
EMBL; CR751606; CAM25151.1; JOINED; Genomic_DNA.
EMBL; CR925752; CAM25151.1; JOINED; Genomic_DNA.
EMBL; CR925752; CAM27607.1; -; Genomic_DNA.
EMBL; BX537327; CAM27607.1; JOINED; Genomic_DNA.
EMBL; CR751606; CAM27607.1; JOINED; Genomic_DNA.
EMBL; BC082554; AAH82554.1; -; mRNA.
CCDS; CCDS38908.1; -. [A2BH40-1]
RefSeq; NP_001074288.1; NM_001080819.1. [A2BH40-1]
RefSeq; XP_006539390.1; XM_006539327.3. [A2BH40-2]
UniGene; Mm.22478; -.
ProteinModelPortal; A2BH40; -.
SMR; A2BH40; -.
BioGrid; 220298; 20.
DIP; DIP-58952N; -.
IntAct; A2BH40; 22.
MINT; MINT-4123278; -.
STRING; 10090.ENSMUSP00000101517; -.
iPTMnet; A2BH40; -.
PhosphoSitePlus; A2BH40; -.
EPD; A2BH40; -.
MaxQB; A2BH40; -.
PaxDb; A2BH40; -.
PeptideAtlas; A2BH40; -.
PRIDE; A2BH40; -.
Ensembl; ENSMUST00000008024; ENSMUSP00000008024; ENSMUSG00000007880. [A2BH40-4]
Ensembl; ENSMUST00000105897; ENSMUSP00000101517; ENSMUSG00000007880. [A2BH40-1]
GeneID; 93760; -.
KEGG; mmu:93760; -.
UCSC; uc008vdh.1; mouse. [A2BH40-1]
UCSC; uc008vdj.1; mouse. [A2BH40-4]
CTD; 8289; -.
MGI; MGI:1935147; Arid1a.
eggNOG; KOG2510; Eukaryota.
eggNOG; ENOG410Y034; LUCA.
GeneTree; ENSGT00550000074575; -.
HOGENOM; HOG000232161; -.
HOVERGEN; HBG058196; -.
InParanoid; A2BH40; -.
KO; K11653; -.
PhylomeDB; A2BH40; -.
Reactome; R-MMU-3214858; RMTs methylate histone arginines.
Reactome; R-MMU-8939243; RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known.
ChiTaRS; Arid1a; mouse.
PRO; PR:A2BH40; -.
Proteomes; UP000000589; Chromosome 4.
Bgee; ENSMUSG00000007880; -.
ExpressionAtlas; A2BH40; baseline and differential.
Genevisible; A2BH40; MM.
GO; GO:0090544; C:BAF-type complex; IDA:MGI.
GO; GO:0071565; C:nBAF complex; IDA:UniProtKB.
GO; GO:0071564; C:npBAF complex; IDA:UniProtKB.
GO; GO:0000790; C:nuclear chromatin; IDA:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0016514; C:SWI/SNF complex; IDA:MGI.
GO; GO:0003677; F:DNA binding; ISO:MGI.
GO; GO:0016922; F:ligand-dependent nuclear receptor binding; ISO:MGI.
GO; GO:0030521; P:androgen receptor signaling pathway; ISS:UniProtKB.
GO; GO:0043044; P:ATP-dependent chromatin remodeling; IDA:MGI.
GO; GO:0003205; P:cardiac chamber development; IMP:MGI.
GO; GO:0055007; P:cardiac muscle cell differentiation; IMP:MGI.
GO; GO:0006325; P:chromatin organization; IPI:MGI.
GO; GO:0006338; P:chromatin remodeling; IMP:MGI.
GO; GO:0016569; P:covalent chromatin modification; IEA:UniProtKB-KW.
GO; GO:0007566; P:embryo implantation; IMP:MGI.
GO; GO:0030900; P:forebrain development; IMP:MGI.
GO; GO:0001704; P:formation of primary germ layer; IMP:MGI.
GO; GO:0007369; P:gastrulation; IMP:MGI.
GO; GO:0042921; P:glucocorticoid receptor signaling pathway; ISO:MGI.
GO; GO:0030520; P:intracellular estrogen receptor signaling pathway; ISS:UniProtKB.
GO; GO:0006344; P:maintenance of chromatin silencing; IMP:MGI.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:MGI.
GO; GO:0001843; P:neural tube closure; IMP:MGI.
GO; GO:0006337; P:nucleosome disassembly; ISO:MGI.
GO; GO:0003408; P:optic cup formation involved in camera-type eye development; IMP:MGI.
GO; GO:0060674; P:placenta blood vessel development; IMP:MGI.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0019827; P:stem cell population maintenance; IMP:MGI.
GO; GO:1901998; P:toxin transport; IMP:MGI.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 1.10.150.60; -; 1.
Gene3D; 1.25.10.10; -; 1.
InterPro; IPR001606; ARID_dom.
InterPro; IPR036431; ARID_dom_sf.
InterPro; IPR011989; ARM-like.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR021906; BAF250/Osa.
InterPro; IPR033388; BAF250_C.
InterPro; IPR030094; BAF250a.
PANTHER; PTHR12656; PTHR12656; 1.
PANTHER; PTHR12656:SF12; PTHR12656:SF12; 1.
Pfam; PF01388; ARID; 1.
Pfam; PF12031; BAF250_C; 1.
SMART; SM00501; BRIGHT; 1.
SUPFAM; SSF46774; SSF46774; 1.
SUPFAM; SSF48371; SSF48371; 1.
PROSITE; PS51011; ARID; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Chromatin regulator;
Complete proteome; DNA-binding; Methylation; Neurogenesis; Nucleus;
Phosphoprotein; Reference proteome; Transcription;
Transcription regulation.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:O14497}.
CHAIN 2 2283 AT-rich interactive domain-containing
protein 1A.
/FTId=PRO_0000391619.
DOMAIN 1018 1109 ARID. {ECO:0000255|PROSITE-
ProRule:PRU00355}.
MOTIF 296 300 LXXLL.
MOTIF 1369 1388 Nuclear localization signal.
{ECO:0000250|UniProtKB:O14497}.
MOTIF 1710 1714 LXXLL.
MOTIF 1965 1969 LXXLL.
MOTIF 2083 2087 LXXLL.
COMPBIAS 16 20 Poly-Pro.
COMPBIAS 38 43 Poly-Ala.
COMPBIAS 53 425 Gly-rich.
COMPBIAS 331 350 Ala-rich.
COMPBIAS 405 612 Gln-rich.
COMPBIAS 999 1002 Poly-Ser.
COMPBIAS 1328 1500 Gln-rich.
COMPBIAS 1545 1644 Pro-rich.
COMPBIAS 1761 1766 Poly-Glu.
COMPBIAS 1773 1778 Poly-Glu.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000250|UniProtKB:O14497}.
MOD_RES 56 56 Phosphoserine.
{ECO:0000250|UniProtKB:O14497}.
MOD_RES 77 77 Phosphoserine.
{ECO:0000250|UniProtKB:O14497}.
MOD_RES 234 234 Phosphoserine.
{ECO:0000250|UniProtKB:O14497}.
MOD_RES 287 287 Phosphothreonine.
{ECO:0000250|UniProtKB:O14497}.
MOD_RES 302 302 Phosphoserine.
{ECO:0000250|UniProtKB:O14497}.
MOD_RES 365 365 Phosphoserine.
{ECO:0000244|PubMed:19144319,
ECO:0000244|PubMed:21183079}.
MOD_RES 384 384 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 431 431 Asymmetric dimethylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 605 605 Phosphoserine.
{ECO:0000250|UniProtKB:O14497}.
MOD_RES 697 697 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 699 699 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 703 703 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 731 731 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 765 765 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 773 773 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1185 1185 Phosphoserine.
{ECO:0000250|UniProtKB:O14497}.
MOD_RES 1236 1236 Phosphoserine.
{ECO:0000250|UniProtKB:O14497}.
MOD_RES 1277 1277 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 1605 1605 Phosphoserine.
{ECO:0000250|UniProtKB:O14497}.
MOD_RES 1613 1613 N6-acetyllysine.
{ECO:0000250|UniProtKB:O14497}.
MOD_RES 1874 1874 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1886 1886 Phosphothreonine.
{ECO:0000250|UniProtKB:O14497}.
MOD_RES 1903 1903 N6-acetyllysine.
{ECO:0000250|UniProtKB:O14497}.
MOD_RES 1927 1927 Phosphoserine.
{ECO:0000250|UniProtKB:O14497}.
MOD_RES 1942 1942 Phosphoserine.
{ECO:0000250|UniProtKB:O14497}.
VAR_SEQ 1 385 Missing (in isoform 2 and isoform 4).
{ECO:0000303|PubMed:11318604,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_038737.
VAR_SEQ 1181 1181 Missing (in isoform 4).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_038738.
VAR_SEQ 1336 1336 Q -> QQQQQR (in isoform 2 and isoform 4).
{ECO:0000303|PubMed:11318604,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_038739.
VAR_SEQ 1367 1583 Missing (in isoform 3). {ECO:0000305}.
/FTId=VSP_038740.
CONFLICT 697 697 S -> F (in Ref. 1; AAK54504).
{ECO:0000305}.
CONFLICT 750 750 D -> E (in Ref. 1; AAK54504).
{ECO:0000305}.
CONFLICT 758 758 P -> S (in Ref. 1; AAK54504).
{ECO:0000305}.
CONFLICT 833 833 M -> I (in Ref. 1; AAK54504).
{ECO:0000305}.
CONFLICT 1011 1011 K -> Q (in Ref. 1; AAK54504).
{ECO:0000305}.
CONFLICT 1148 1148 P -> H (in Ref. 1; AAK54504).
{ECO:0000305}.
CONFLICT 1181 1182 SR -> G (in Ref. 1; AAK54504).
{ECO:0000305}.
CONFLICT 1635 1635 M -> I (in Ref. 1; AAK54504).
{ECO:0000305}.
CONFLICT 1755 1755 Y -> S (in Ref. 1; AAK54504).
{ECO:0000305}.
CONFLICT 1795 1795 S -> P (in Ref. 1; AAK54504).
{ECO:0000305}.
CONFLICT 1799 1799 N -> S (in Ref. 1; AAK54504).
{ECO:0000305}.
CONFLICT 1929 1929 E -> D (in Ref. 1; AAK54504).
{ECO:0000305}.
CONFLICT 1956 1956 E -> D (in Ref. 1; AAK54504).
{ECO:0000305}.
CONFLICT 1974 1974 S -> P (in Ref. 1; AAK54504).
{ECO:0000305}.
CONFLICT 2233 2233 A -> P (in Ref. 1; AAK54504).
{ECO:0000305}.
SEQUENCE 2283 AA; 242092 MW; 0F14BB1372CC4268 CRC64;
MAAQVAPAAA SSLGNPPPPP SELKKAEQQQ REEAGGEAAA AAAERGEMKA AAGQESEGPA
VGPPQPLGKE LQDGAESNGG GGGGGAGSGG GPGAEPDLKN SNGNAGPRPA LNNNLPEPPG
GGGGGGSSSS DGVGAPPHSA AAALPPPAYG FGQAYGRSPS AVAAAAAAVF HQQHGGQQSP
GLAALQSGGG GGLEPYAGPQ QNSHDHGFPN HQYNSYYPNR SAYPPPPQAY ALSSPRGGTP
GSGAAAAAGS KPPPSSSASA SSSSSSFAQQ RFGAMGGGGP SAAGGGTPQP TATPTLNQLL
TSPSSARGYQ GYPGGDYGGG PQDGGAGKGP ADMASQCWGA AAAAAAAAAA VSGGAQQRSH
HAPMSPGSSG GGGQPLARTP QSSSPMDQMG KMRPQPYGGT NPYSQQQGPP SGPQQGHGYP
GQPYGSQTPQ RYPMTMQGRA QSAMGSLSYA QQIPPYGQQG PSAYGQQGQT PYYNQQSPHP
QQQPPYAQQP PSQTPHAQPS YQQQPQTQQP QLQSSQPPYS QQPSQPPHQQ SPTPYPSQQS
TTQQHPQSQP PYSQPQAQSP YQQQQPQQPA SSSLSQQAAY PQPQPQQSQQ TAYSQQRFPP
PQELSQDSFG SQASSAPSMT SSKGGQEDMN LSLQSRPSSL PDLSGSIDDL PMGTEGALSP
GVSTSGISSS QGEQSNPAQS PFSPHTSPHL PGIRGPSPSP VGSPASVAQS RSGPLSPAAV
PGNQMPPRPP SGQSDSIMHP SMNQSSIAQD RGYMQRNPQM PQYTSPQPGS ALSPRQPSGG
QMHSGVGSYQ QNSMGSYGPQ GSQYGPQGGY PRQPNYNALP NANYPNAGMA GSMNPMGAGG
QMHGQPGIPP YGTLPPGRMA HASMGNRPYG PNMANMPPQV GSGMCPPPGG MNRKTQESAV
AMHVAANSIQ NRPPGYPNMN QGGMMGTGPP YGQGINSMAG MINPQGPPYP MGGTMANNSA
GMAASPEMMG LGDVKLTPAT KMNNKADGTP KTESKSKKSS SSTTTNEKIT KLYELGGEPE
RKMWVDRYLA FTEEKAMGMT NLPAVGRKPL DLYRLYVSVK EIGGLTQVNK NKKWRELATN
LNVGTSSSAA SSLKKQYIQC LYAFECKIER GEDPPPDIFA AADSKKSQPK IQPPSPAGSG
SMQGPQTPQS TSSSMAEGGD LKPPTPASTP HSQIPPLPGM SRSNSVGIQD AFPDGSDPTF
QKRNSMTPNP GYQPSMNTSD MMGRMSYEPN KDPYGSMRKA PGSDPFMSSG QGPNGGMGDP
YSRAAGPGLG SVAMGPRQHY PYGGPYDRVR TEPGIGPEGN MGTGAPQPNL MPSTPDSGMY
SPSRYPPQQQ QQQQQQHDSY GNQFSTQGTP SSSPFPSQQT TMYQQQQQNY KRPMDGTYGP
PAKRHEGEMY SVPYSAGQGQ PQQQQLPAAQ SQPASQPQAA QPSPQQDVYN QYSNAYPASA
TAATDRRPAG GPQNQFPFQF GRDRVSAPPG SSAQQNMPPQ MMGGPIQASA EVAQQGTMWQ
GRNDMTYNYA NRQNTGSATQ GPAYHGVNRT DEMLHTDQRA NHEGPWPSHG TRQPPYGPSA
PVPPMTRPPP SNYQPPPSMP NHIPQVSSPA PLPRPMENRT SPSKSPFLHS GMKMQKAGPP
VPASHIAPTP VQPPMIRRDI TFPPGSVEAT QPVLKQRRRL TMKDIGTPEA WRVMMSLKSG
LLAESTWALD TINILLYDDN SIMTFNLSQL PGLLELLVEY FRRCLIEIFG ILKEYEVGDP
GQRTLLDPGR FTKVYSPAHT EEEEEEHLDP KLEEEEEEGV GNDEEMAFLG KDKPSSENNE
EKLVSKFDKL PVKIVQRNDP FVVDCSDKLG RVQEFDSGLL HWRIGGGDTT EHIQTHFESK
IELLPSRPYV PCPTPPRKHL TTVEGTPGTT EQEGPPPDGL PEKRITATMD DMLSTRSSTL
TDEGAKSAEA TKESSKFPFG ISPAQSHRNI KILEDEPHSK DETPLCTLLD WQDSLAKRCV
CVSNTIRSLS FVPGNDFEMS KHPGLLLILG KLILLHHKHP ERKQAPLTYE KEEEQDQGVS
CDKVEWWWDC LEMLRENTLV TLANISGQLD LSPYPESICL PVLDGLLHWA VCPSAEAQDP
FSTLGPNAVL SPQRLVLETL SKLSIQDNNV DLILATPPFS RLEKLYSTMV RFLSDRKNPV
CREMAVVLLA NLAQGDSLAA RAIAVQKGSI GNLLGFLEDS LAATQFQQSQ ASLLHMQNPP
FEPTSVDMMR RAARALLALA KVDENHSEFT LYESRLLDIS VSPLMNSLVS QVICDVLFLI
GQS


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