ID RFOX3_MOUSE Reviewed; 374 AA.
AC Q8BIF2; A2A4W7; A2A4W8; B7ZC12; B7ZC13; D1GI07; Q3TUE0; Q7TQI4;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 2.
DT 24-JAN-2024, entry version 147.
DE RecName: Full=RNA binding protein fox-1 homolog 3;
DE AltName: Full=Fox-1 homolog C;
DE AltName: Full=Hexaribonucleotide-binding protein 3;
DE Short=Fox-3;
DE AltName: Full=Neuronal nuclei antigen;
DE Short=NeuN antigen;
GN Name=Rbfox3; Synonyms=D11Bwg0517e, Hrnbp3;
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 AND 5), PROTEIN SEQUENCE OF 139-153;
RP 156-166 AND 320-360, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP AND INDUCTION BY RETINOIC ACID.
RC TISSUE=Brain;
RX PubMed=19713214; DOI=10.1074/jbc.m109.052969;
RA Kim K.K., Adelstein R.S., Kawamoto S.;
RT "Identification of neuronal nuclei (NeuN) as Fox-3, a new member of the
RT Fox-1 gene family of splicing factors.";
RL J. Biol. Chem. 284:31052-31061(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Diencephalon, and Head;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PROTEIN SEQUENCE OF 102-135; 139-153; 192-201; 239-250 AND 319-337,
RP FUNCTION, SUBCELLULAR LOCATION, ALTERNATIVE SPLICING, TISSUE SPECIFICITY,
RP INDUCTION BY RETINOIC ACID, AND IDENTIFICATION BY MASS SPECTROMETRY
RP (ISOFORMS 1; 4 AND 5).
RX PubMed=21747913; DOI=10.1371/journal.pone.0021585;
RA Dredge B.K., Jensen K.B.;
RT "NeuN/Rbfox3 nuclear and cytoplasmic isoforms differentially regulate
RT alternative splicing and nonsense-mediated decay of Rbfox2.";
RL PLoS ONE 6:E21585-E21585(2011).
RN [7]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=1483388; DOI=10.1242/dev.116.1.201;
RA Mullen R.J., Buck C.R., Smith A.M.;
RT "NeuN, a neuronal specific nuclear protein in vertebrates.";
RL Development 116:201-211(1992).
RN [8]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND PHOSPHORYLATION.
RX PubMed=15605376; DOI=10.1002/jnr.20354;
RA Lind D., Franken S., Kappler J., Jankowski J., Schilling K.;
RT "Characterization of the neuronal marker NeuN as a multiply phosphorylated
RT antigen with discrete subcellular localization.";
RL J. Neurosci. Res. 79:295-302(2005).
RN [9]
RP ALTERNATIVE SPLICING.
RX PubMed=20042473; DOI=10.1261/rna.1838210;
RA Damianov A., Black D.L.;
RT "Autoregulation of Fox protein expression to produce dominant negative
RT splicing factors.";
RL RNA 16:405-416(2010).
RN [10]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-223 AND ARG-319, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [11]
RP DISRUPTION PHENOTYPE.
RX PubMed=26619789; DOI=10.1038/srep17383;
RA Wang H.Y., Hsieh P.F., Huang D.F., Chin P.S., Chou C.H., Tung C.C.,
RA Chen S.Y., Lee L.J., Gau S.S., Huang H.S.;
RT "RBFOX3/NeuN is required for hippocampal circuit balance and function.";
RL Sci. Rep. 5:17383-17383(2015).
CC -!- FUNCTION: Pre-mRNA alternative splicing regulator. Regulates
CC alternative splicing of RBFOX2 to enhance the production of mRNA
CC species that are targeted for nonsense-mediated decay (NMD).
CC {ECO:0000269|PubMed:19713214, ECO:0000269|PubMed:21747913}.
CC -!- INTERACTION:
CC Q8BIF2; Q61221: Hif1a; NbExp=2; IntAct=EBI-4567146, EBI-298954;
CC Q8BIF2; Q16665: HIF1A; Xeno; NbExp=2; IntAct=EBI-4567146, EBI-447269;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Nucleus.
CC -!- SUBCELLULAR LOCATION: [Isoform 4]: Cytoplasm.
CC -!- SUBCELLULAR LOCATION: [Isoform 5]: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1; Synonyms=Fox3v1, Fox-3-L;
CC IsoId=Q8BIF2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BIF2-2; Sequence=VSP_035220;
CC Name=3;
CC IsoId=Q8BIF2-3; Sequence=VSP_035219, VSP_035220;
CC Name=4; Synonyms=Fox3v3;
CC IsoId=Q8BIF2-4; Sequence=VSP_043949, VSP_035220;
CC Name=5; Synonyms=Fox3v2, Fox-3-S;
CC IsoId=Q8BIF2-5; Sequence=VSP_043949;
CC -!- TISSUE SPECIFICITY: Widely expressed in brain, including in cerebral
CC cortex, hippocampus, thalamus, caudate/putamen, cerebellum, as well as
CC in the spinal cord (at protein level). Not expressed in all neuronal
CC cells within a region, in cerebellum, expression is absent in Purkinje
CC cells (at protein level). Expressed in the retina in the ganglion cells
CC and some cells in the inner nuclear layer, but absent from the
CC photoreceptor cells and most cells in the inner nuclear layer (at
CC protein level). {ECO:0000269|PubMed:1483388,
CC ECO:0000269|PubMed:15605376, ECO:0000269|PubMed:19713214,
CC ECO:0000269|PubMed:21747913}.
CC -!- DEVELOPMENTAL STAGE: In the neural tube, expressed as early as 9.5 dpc
CC and expression is confined to the nervous system. By 12.5 dpc, can be
CC found in the developing ventral horns and is also detected in the
CC developing dorsal horns as well as in the dorsal root ganglion. Not
CC detected in the ventricular zone, roof plate, floor plate or marginal
CC zone (developing white matter). It is expressed from embryonic stage to
CC adulthood. {ECO:0000269|PubMed:1483388}.
CC -!- INDUCTION: By retinoic acid. Expression is up-regulated in P19 cells
CC during neural differentiation upon retinoic acid treatment (at the
CC protein level). {ECO:0000269|PubMed:19713214,
CC ECO:0000269|PubMed:21747913}.
CC -!- PTM: Phosphorylated. {ECO:0000305|PubMed:15605376}.
CC -!- DISRUPTION PHENOTYPE: Knockout mice have significantly reduced brain
CC weight, impaired neurofilament expression and decreased white matter
CC volume, but normal total body mass. They show increased susceptibility
CC to seizures and reduced anxiety-related behaviors compared with wild
CC type littermates, as well as defective hippocampal gene expression and
CC deficits in synaptic transmission and plasticity in the dentate gyrus.
CC {ECO:0000269|PubMed:26619789}.
CC -!- CAUTION: Initial characterization was derived from usage of a
CC monoclonal antibody (A60) directed to an unknown protein called NeuN
CC (PubMed:15605376, PubMed:1483388), but later identified as RBFOX3.
CC {ECO:0000305|PubMed:21747913}.
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DR EMBL; FJ958310; ACY91937.1; -; mRNA.
DR EMBL; FJ958311; ACY91938.1; -; mRNA.
DR EMBL; AK079086; BAC37531.1; -; mRNA.
DR EMBL; AK160816; BAE36031.1; -; mRNA.
DR EMBL; AL591514; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL591544; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL591075; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466558; EDL34674.1; -; Genomic_DNA.
DR EMBL; BC054403; AAH54403.1; -; mRNA.
DR CCDS; CCDS25705.1; -. [Q8BIF2-4]
DR CCDS; CCDS25706.1; -. [Q8BIF2-1]
DR CCDS; CCDS70358.1; -. [Q8BIF2-3]
DR CCDS; CCDS70360.1; -. [Q8BIF2-2]
DR RefSeq; NP_001020102.2; NM_001024931.2. [Q8BIF2-4]
DR RefSeq; NP_001034256.1; NM_001039167.1. [Q8BIF2-1]
DR RefSeq; NP_001034257.1; NM_001039168.1.
DR RefSeq; NP_001272365.1; NM_001285436.1. [Q8BIF2-2]
DR RefSeq; NP_001272366.1; NM_001285437.1. [Q8BIF2-3]
DR RefSeq; NP_001272367.1; NM_001285438.1. [Q8BIF2-4]
DR RefSeq; XP_006533785.1; XM_006533722.3. [Q8BIF2-1]
DR RefSeq; XP_006533788.1; XM_006533725.3. [Q8BIF2-1]
DR RefSeq; XP_006533790.1; XM_006533727.3. [Q8BIF2-5]
DR RefSeq; XP_017170150.1; XM_017314661.1. [Q8BIF2-1]
DR RefSeq; XP_017170151.1; XM_017314662.1. [Q8BIF2-1]
DR RefSeq; XP_017170152.1; XM_017314663.1. [Q8BIF2-2]
DR AlphaFoldDB; Q8BIF2; -.
DR SMR; Q8BIF2; -.
DR BioGRID; 206871; 3.
DR IntAct; Q8BIF2; 4.
DR MINT; Q8BIF2; -.
DR STRING; 10090.ENSMUSP00000017576; -.
DR GlyGen; Q8BIF2; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; Q8BIF2; -.
DR PhosphoSitePlus; Q8BIF2; -.
DR SwissPalm; Q8BIF2; -.
DR MaxQB; Q8BIF2; -.
DR PaxDb; 10090-ENSMUSP00000017576; -.
DR PeptideAtlas; Q8BIF2; -.
DR ProteomicsDB; 255181; -. [Q8BIF2-1]
DR ProteomicsDB; 255182; -. [Q8BIF2-2]
DR ProteomicsDB; 255183; -. [Q8BIF2-3]
DR ProteomicsDB; 255184; -. [Q8BIF2-4]
DR ProteomicsDB; 255185; -. [Q8BIF2-5]
DR Antibodypedia; 32645; 598 antibodies from 38 providers.
DR Ensembl; ENSMUST00000017576.11; ENSMUSP00000017576.5; ENSMUSG00000025576.18. [Q8BIF2-1]
DR Ensembl; ENSMUST00000069343.12; ENSMUSP00000069598.6; ENSMUSG00000025576.18. [Q8BIF2-3]
DR Ensembl; ENSMUST00000103023.8; ENSMUSP00000099312.2; ENSMUSG00000025576.18. [Q8BIF2-4]
DR Ensembl; ENSMUST00000106278.9; ENSMUSP00000101885.3; ENSMUSG00000025576.18. [Q8BIF2-4]
DR Ensembl; ENSMUST00000117731.8; ENSMUSP00000113636.2; ENSMUSG00000025576.18. [Q8BIF2-2]
DR Ensembl; ENSMUST00000120061.8; ENSMUSP00000113987.2; ENSMUSG00000025576.18. [Q8BIF2-5]
DR GeneID; 52897; -.
DR KEGG; mmu:52897; -.
DR UCSC; uc007mpl.1; mouse. [Q8BIF2-4]
DR UCSC; uc007mpm.1; mouse. [Q8BIF2-5]
DR UCSC; uc007mpn.1; mouse. [Q8BIF2-1]
DR UCSC; uc007mpp.1; mouse. [Q8BIF2-3]
DR AGR; MGI:106368; -.
DR CTD; 146713; -.
DR MGI; MGI:106368; Rbfox3.
DR VEuPathDB; HostDB:ENSMUSG00000025576; -.
DR eggNOG; KOG0125; Eukaryota.
DR GeneTree; ENSGT00940000159924; -.
DR HOGENOM; CLU_048440_0_0_1; -.
DR InParanoid; Q8BIF2; -.
DR OMA; AAEPYHH; -.
DR OrthoDB; 5406502at2759; -.
DR PhylomeDB; Q8BIF2; -.
DR TreeFam; TF315942; -.
DR BioGRID-ORCS; 52897; 3 hits in 76 CRISPR screens.
DR ChiTaRS; Rbfox3; mouse.
DR PRO; PR:Q8BIF2; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8BIF2; Protein.
DR Bgee; ENSMUSG00000025576; Expressed in piriform cortex and 138 other cell types or tissues.
DR ExpressionAtlas; Q8BIF2; baseline and differential.
DR Genevisible; Q8BIF2; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0043204; C:perikaryon; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0007399; P:nervous system development; IBA:GO_Central.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR CDD; cd12407; RRM_FOX1_like; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR025670; Fox-1_C_dom.
DR InterPro; IPR034237; FOX1_RRM.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR017325; RBFOX1-3.
DR InterPro; IPR047131; RBFOX1-like.
DR InterPro; IPR000504; RRM_dom.
DR PANTHER; PTHR15597; ATAXIN 2-BINDING PROTEIN 1-RELATED; 1.
DR PANTHER; PTHR15597:SF25; RNA BINDING PROTEIN FOX-1 HOMOLOG 3; 1.
DR Pfam; PF12414; Fox-1_C; 1.
DR Pfam; PF00076; RRM_1; 1.
DR PIRSF; PIRSF037932; Ataxin_2_bd_A2BP; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Direct protein sequencing; Methylation;
KW mRNA processing; mRNA splicing; Nucleus; Reference proteome; RNA-binding.
FT CHAIN 1..374
FT /note="RNA binding protein fox-1 homolog 3"
FT /id="PRO_0000349208"
FT DOMAIN 99..175
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..34
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..92
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 100
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT SITE 108
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT SITE 109
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT SITE 133
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT SITE 138
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT SITE 142
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT SITE 166
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT SITE 176
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT MOD_RES 223
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 223
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 319
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT VAR_SEQ 139..169
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_035219"
FT VAR_SEQ 253..299
FT /note="Missing (in isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:19713214"
FT /id="VSP_043949"
FT VAR_SEQ 361..374
FT /note="Missing (in isoform 2, isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_035220"
FT CONFLICT 266
FT /note="A -> V (in Ref. 1; BAC37531)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 374 AA; 40610 MW; AC1454ADBCD2B810 CRC64;
MAQPYPPAQY PPPPQNGIPA EYAPPPPHPT QDYSGQTPVP PEHGMTLYTP AQTHPEQPGT
EASTQPIAGT QTVPQADEAA QTDNQQLHPS DPTEKQQPKR LHVSNIPFRF RDPDLRQMFG
QFGKILDVEI IFNERGSKGF GFVTFETSSD ADRAREKLNG TIVEGRKIEV NNATARVMTN
KKPGNPYANG WKLNPVVGTV YGPEFYAVTS FPYPTTGTAV AYRGAHLRGR GRAVYNTFRA
APPPPPIPTY GAALEQTLVK MPVPWAGLAP CPLPPQQTPE PAYPTSPAFP PLSCPFASRV
VYQDGFYGAE IYGGYAAYRY AQPAAATAAA YSDSYGRVYA AADPYHHTIG PTATYSIGTM
ASLCRGGYSR FTPY
//
