RFOX2_MOUSE
ID RFOX2_MOUSE Reviewed; 449 AA.
AC Q8BP71; Q0R5Z7; Q0R5Z8; Q0VH84; Q537D4; Q537D5; Q8BRG0; Q8R2T5; Q8VI62;
AC Q923W8;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=RNA binding protein fox-1 homolog 2;
DE AltName: Full=Fox-1 homolog B;
DE AltName: Full=Fox-1 homolog Fxh;
DE AltName: Full=Hexaribonucleotide-binding protein 2;
DE AltName: Full=RNA-binding motif protein 9;
DE AltName: Full=RNA-binding protein 9;
GN Name=Rbfox2; Synonyms=Fox2, Fxh, Hrnbp2, Rbm9;
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 7), SUBCELLULAR LOCATION, INDUCTION,
RP AND TISSUE SPECIFICITY.
RX PubMed=11401487; DOI=10.1006/bbrc.2001.4617;
RA Lieberman A.P., Friedlich D.L., Harmison G., Howell B.W., Jordan C.L.,
RA Breedlove S.M., Fischbeck K.H.;
RT "Androgens regulate the mammalian homologues of invertebrate sex
RT determination genes tra-2 and fox-1.";
RL Biochem. Biophys. Res. Commun. 282:499-506(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 7; 8 AND 9), FUNCTION, AND SUBCELLULAR
RP LOCATION.
RC TISSUE=Brain, and Muscle;
RX PubMed=15824060; DOI=10.1093/nar/gki338;
RA Nakahata S., Kawamoto S.;
RT "Tissue-dependent isoforms of mammalian Fox-1 homologs are associated with
RT tissue-specific splicing activities.";
RL Nucleic Acids Res. 33:2078-2089(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 7), AND FUNCTION.
RX PubMed=16537540; DOI=10.1074/jbc.m511556200;
RA Ponthier J.L., Schluepen C., Chen W., Lersch R.A., Gee S.L., Hou V.C.,
RA Lo A.J., Short S.A., Chasis J.A., Winkelmann J.C., Conboy J.G.;
RT "Fox-2 splicing factor binds to a conserved intron motif to promote
RT inclusion of protein 4.1R alternative exon 16.";
RL J. Biol. Chem. 281:12468-12474(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3 AND 4), FUNCTION, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=C57BL/6J, and DBA/2J;
RX PubMed=17715393; DOI=10.1182/blood-2007-01-068940;
RA Yang G., Huang S.-C., Wu J.Y., Benz E.J. Jr.;
RT "Regulated Fox-2 isoform expression mediates protein 4.1R splicing during
RT erythroid differentiation.";
RL Blood 111:392-401(2008).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 6).
RC STRAIN=C57BL/6J; TISSUE=Embryo;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 7 AND 5).
RC STRAIN=Czech II; TISSUE=Mammary tumor;
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 [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=16260614; DOI=10.1128/mcb.25.22.10005-10016.2005;
RA Underwood J.G., Boutz P.L., Dougherty J.D., Stoilov P., Black D.L.;
RT "Homologues of the Caenorhabditis elegans Fox-1 protein are neuronal
RT splicing regulators in mammals.";
RL Mol. Cell. Biol. 25:10005-10016(2005).
RN [8]
RP FUNCTION.
RX PubMed=16449636; DOI=10.1128/mcb.26.4.1209-1222.2006;
RA Baraniak A.P., Chen J.R., Garcia-Blanco M.A.;
RT "Fox-2 mediates epithelial cell-specific fibroblast growth factor receptor
RT 2 exon choice.";
RL Mol. Cell. Biol. 26:1209-1222(2006).
RN [9]
RP FUNCTION.
RX PubMed=17101796; DOI=10.1128/mcb.01015-06;
RA Zhou H.-L., Baraniak A.P., Lou H.;
RT "Role for Fox-1/Fox-2 in mediating the neuronal pathway of
RT calcitonin/calcitonin gene-related peptide alternative RNA processing.";
RL Mol. Cell. Biol. 27:830-841(2007).
RN [10]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-340; ARG-356; ARG-388; ARG-440
RP AND ARG-445, METHYLATION [LARGE SCALE ANALYSIS] AT ARG-318 AND ARG-323
RP (ISOFORM 2), METHYLATION [LARGE SCALE ANALYSIS] AT ARG-236; ARG-241 AND
RP ARG-285 (ISOFORM 4), METHYLATION [LARGE SCALE ANALYSIS] AT ARG-336 AND
RP ARG-341 (ISOFORM 5), METHYLATION [LARGE SCALE ANALYSIS] AT ARG-268 AND
RP ARG-273 (ISOFORMS 6; 7 AND 8), METHYLATION [LARGE SCALE ANALYSIS] AT
RP ARG-317 (ISOFORM 8), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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).
CC -!- FUNCTION: RNA-binding protein that regulates alternative splicing
CC events by binding to 5'-UGCAUGU-3' elements. Prevents binding of U2AF2
CC to the 3'-splice site. Regulates alternative splicing of tissue-
CC specific exons and of differentially spliced exons during
CC erythropoiesis. Seems to act as a coregulatory factor of ER-alpha (By
CC similarity). {ECO:0000250, ECO:0000269|PubMed:15824060,
CC ECO:0000269|PubMed:16260614, ECO:0000269|PubMed:16449636,
CC ECO:0000269|PubMed:16537540, ECO:0000269|PubMed:17101796,
CC ECO:0000269|PubMed:17715393}.
CC -!- SUBUNIT: Interacts with ER-alpha N-terminal activation domain.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=9;
CC Name=1;
CC IsoId=Q8BP71-1; Sequence=Displayed;
CC Name=2; Synonyms=Fox-2A;
CC IsoId=Q8BP71-2; Sequence=VSP_030893, VSP_030897;
CC Name=3; Synonyms=1, Fox-2F;
CC IsoId=Q8BP71-3; Sequence=VSP_030892;
CC Name=4; Synonyms=2, Fox-2F-S;
CC IsoId=Q8BP71-4; Sequence=VSP_030892, VSP_030895, VSP_030896,
CC VSP_030897, VSP_030898;
CC Name=5;
CC IsoId=Q8BP71-5; Sequence=VSP_030897, VSP_030899;
CC Name=6;
CC IsoId=Q8BP71-6; Sequence=VSP_030892, VSP_030897, VSP_030900;
CC Name=7; Synonyms=1, F011;
CC IsoId=Q8BP71-7; Sequence=VSP_030892, VSP_030897;
CC Name=8; Synonyms=2, F411;
CC IsoId=Q8BP71-8; Sequence=VSP_030892, VSP_030897, VSP_030898;
CC Name=9; Synonyms=3, F402;
CC IsoId=Q8BP71-9; Sequence=VSP_030892, VSP_030894;
CC -!- TISSUE SPECIFICITY: Detected in brain neurons (at protein level).
CC Detected in heart, brain, embryo, lung, liver, kidney and ovary.
CC {ECO:0000269|PubMed:11401487, ECO:0000269|PubMed:16260614}.
CC -!- INDUCTION: Up-regulated by androgens in cultured motor neuron cells.
CC {ECO:0000269|PubMed:11401487}.
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DR EMBL; AF387322; AAK64287.1; -; mRNA.
DR EMBL; AY659951; AAV74334.1; -; mRNA.
DR EMBL; AY659952; AAV74335.1; -; mRNA.
DR EMBL; AY659953; AAV74336.1; -; mRNA.
DR EMBL; AF229055; AAL71902.1; -; mRNA.
DR EMBL; AY904025; AAX84842.1; -; mRNA.
DR EMBL; DQ017388; AAY78494.1; -; mRNA.
DR EMBL; DQ017389; AAY78495.1; -; mRNA.
DR EMBL; AK044929; BAC32147.1; -; mRNA.
DR EMBL; AK077594; BAC36885.1; -; mRNA.
DR EMBL; BC002124; AAH02124.1; -; mRNA.
DR EMBL; BC027263; AAH27263.1; -; mRNA.
DR CCDS; CCDS27598.1; -. [Q8BP71-5]
DR CCDS; CCDS49657.1; -. [Q8BP71-8]
DR CCDS; CCDS49658.1; -. [Q8BP71-3]
DR CCDS; CCDS49659.1; -. [Q8BP71-1]
DR CCDS; CCDS88795.1; -. [Q8BP71-9]
DR CCDS; CCDS88796.1; -. [Q8BP71-4]
DR CCDS; CCDS88798.1; -. [Q8BP71-7]
DR RefSeq; NP_001104297.1; NM_001110827.2.
DR RefSeq; NP_001104298.1; NM_001110828.2. [Q8BP71-3]
DR RefSeq; NP_001104299.1; NM_001110829.2. [Q8BP71-8]
DR RefSeq; NP_001104300.1; NM_001110830.2. [Q8BP71-7]
DR RefSeq; NP_001273346.1; NM_001286417.1.
DR RefSeq; NP_001273347.1; NM_001286418.1. [Q8BP71-9]
DR RefSeq; NP_001273348.1; NM_001286419.1. [Q8BP71-4]
DR RefSeq; NP_444334.3; NM_053104.6. [Q8BP71-1]
DR RefSeq; NP_780596.1; NM_175387.3. [Q8BP71-5]
DR AlphaFoldDB; Q8BP71; -.
DR SMR; Q8BP71; -.
DR BioGRID; 220236; 10.
DR IntAct; Q8BP71; 3.
DR MINT; Q8BP71; -.
DR STRING; 10090.ENSMUSP00000130739; -.
DR iPTMnet; Q8BP71; -.
DR PhosphoSitePlus; Q8BP71; -.
DR EPD; Q8BP71; -.
DR MaxQB; Q8BP71; -.
DR PaxDb; Q8BP71; -.
DR PeptideAtlas; Q8BP71; -.
DR PRIDE; Q8BP71; -.
DR ProteomicsDB; 255307; -. [Q8BP71-1]
DR ProteomicsDB; 255308; -. [Q8BP71-2]
DR ProteomicsDB; 255309; -. [Q8BP71-3]
DR ProteomicsDB; 255310; -. [Q8BP71-4]
DR ProteomicsDB; 255311; -. [Q8BP71-5]
DR ProteomicsDB; 255312; -. [Q8BP71-6]
DR ProteomicsDB; 255313; -. [Q8BP71-7]
DR ProteomicsDB; 255314; -. [Q8BP71-8]
DR ProteomicsDB; 255315; -. [Q8BP71-9]
DR Antibodypedia; 331; 259 antibodies from 27 providers.
DR DNASU; 93686; -.
DR Ensembl; ENSMUST00000048145; ENSMUSP00000048056; ENSMUSG00000033565. [Q8BP71-5]
DR Ensembl; ENSMUST00000166610; ENSMUSP00000130673; ENSMUSG00000033565. [Q8BP71-3]
DR Ensembl; ENSMUST00000171751; ENSMUSP00000130739; ENSMUSG00000033565. [Q8BP71-1]
DR Ensembl; ENSMUST00000227314; ENSMUSP00000154233; ENSMUSG00000033565. [Q8BP71-8]
DR Ensembl; ENSMUST00000227533; ENSMUSP00000154209; ENSMUSG00000033565. [Q8BP71-4]
DR Ensembl; ENSMUST00000227930; ENSMUSP00000154810; ENSMUSG00000033565. [Q8BP71-9]
DR Ensembl; ENSMUST00000228087; ENSMUSP00000153751; ENSMUSG00000033565. [Q8BP71-7]
DR GeneID; 93686; -.
DR KEGG; mmu:93686; -.
DR UCSC; uc007wnc.3; mouse. [Q8BP71-5]
DR UCSC; uc007wnd.2; mouse. [Q8BP71-7]
DR UCSC; uc007wne.2; mouse. [Q8BP71-8]
DR UCSC; uc007wnf.2; mouse. [Q8BP71-4]
DR UCSC; uc007wng.2; mouse. [Q8BP71-1]
DR UCSC; uc007wni.2; mouse. [Q8BP71-2]
DR UCSC; uc011zvf.1; mouse. [Q8BP71-3]
DR UCSC; uc011zvg.2; mouse. [Q8BP71-9]
DR CTD; 23543; -.
DR MGI; MGI:1933973; Rbfox2.
DR VEuPathDB; HostDB:ENSMUSG00000033565; -.
DR eggNOG; KOG0125; Eukaryota.
DR GeneTree; ENSGT00940000157534; -.
DR HOGENOM; CLU_048440_0_1_1; -.
DR InParanoid; Q8BP71; -.
DR OMA; TYIPLIX; -.
DR OrthoDB; 871288at2759; -.
DR PhylomeDB; Q8BP71; -.
DR TreeFam; TF315942; -.
DR Reactome; R-MMU-6803529; FGFR2 alternative splicing.
DR BioGRID-ORCS; 93686; 10 hits in 73 CRISPR screens.
DR ChiTaRS; Rbfox2; mouse.
DR PRO; PR:Q8BP71; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q8BP71; protein.
DR Bgee; ENSMUSG00000033565; Expressed in cortical plate and 225 other tissues.
DR ExpressionAtlas; Q8BP71; baseline and differential.
DR Genevisible; Q8BP71; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISS:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IDA:MGI.
DR GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR GO; GO:0003714; F:transcription corepressor activity; ISS:UniProtKB.
DR GO; GO:0048813; P:dendrite morphogenesis; IMP:MGI.
DR GO; GO:0030520; P:intracellular estrogen receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0007399; P:nervous system development; IBA:GO_Central.
DR GO; GO:0050885; P:neuromuscular process controlling balance; IGI:MGI.
DR GO; GO:0021942; P:radial glia guided migration of Purkinje cell; IMP:MGI.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IMP:BHF-UCL.
DR GO; GO:0010724; P:regulation of definitive erythrocyte differentiation; IDA:BHF-UCL.
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; RNA-bd_Fox-1.
DR InterPro; IPR000504; RRM_dom.
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; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Methylation; mRNA processing;
KW mRNA splicing; Nucleus; Reference proteome; RNA-binding.
FT CHAIN 1..449
FT /note="RNA binding protein fox-1 homolog 2"
FT /id="PRO_0000317115"
FT DOMAIN 180..256
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..91
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..107
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..182
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 181
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT SITE 189
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT SITE 190
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT SITE 214
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT SITE 219
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT SITE 223
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT SITE 247
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT SITE 257
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT MOD_RES 340
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 356
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 388
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 440
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 440
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 445
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 445
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT VAR_SEQ 1..76
FT /note="MAEGGQAQQQPPQLGPGAAARGMKRESEVELPVPGAGADGPEPGLSKRPRTE
FT EAADGGMQNEPLTPGYHGFPARDG -> MEKKKMVT (in isoform 3, isoform
FT 4, isoform 6, isoform 7, isoform 8 and isoform 9)"
FT /evidence="ECO:0000303|PubMed:11401487,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:15824060,
FT ECO:0000303|PubMed:16141072, ECO:0000303|PubMed:16537540,
FT ECO:0000303|PubMed:17715393"
FT /id="VSP_030892"
FT VAR_SEQ 19..36
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17715393"
FT /id="VSP_030893"
FT VAR_SEQ 153..250
FT /note="Missing (in isoform 9)"
FT /evidence="ECO:0000303|PubMed:15824060,
FT ECO:0000303|PubMed:17715393"
FT /id="VSP_030894"
FT VAR_SEQ 153
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:17715393"
FT /id="VSP_030895"
FT VAR_SEQ 220..250
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:17715393"
FT /id="VSP_030896"
FT VAR_SEQ 320..324
FT /note="SLPLV -> I (in isoform 2, isoform 4, isoform 5,
FT isoform 6, isoform 7 and isoform 8)"
FT /evidence="ECO:0000303|PubMed:11401487,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:15824060,
FT ECO:0000303|PubMed:16141072, ECO:0000303|PubMed:16537540,
FT ECO:0000303|PubMed:17715393"
FT /id="VSP_030897"
FT VAR_SEQ 369..381
FT /note="VVYQDGFYGADLY -> IVLQEPIISAKIPQ (in isoform 4 and
FT isoform 8)"
FT /evidence="ECO:0000303|PubMed:15824060,
FT ECO:0000303|PubMed:17715393"
FT /id="VSP_030898"
FT VAR_SEQ 370..449
FT /note="VYQDGFYGADLYGGYAAYRYAQPATATAATAAAAAAAAYSDGYGRVYTADPY
FT HALAPAASYGVGAVASLYRGGYSRFAPY -> DMQPTDMHSLLLQPQPQLLQPLQPLTA
FT TVTAGCTQLTPTMPSPLPPAMELALWRVCTEVATADLPPTEVT (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_030899"
FT VAR_SEQ 373..449
FT /note="DGFYGADLYGGYAAYRYAQPATATAATAAAAAAAAYSDGYGRVYTADPYHAL
FT APAASYGVGAVASLYRGGYSRFAPY -> DMQPTDMHSLLLQPQPQLLQPLQPLTATVT
FT AGCTQLTPTMPSPLPPAMELAL (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_030900"
FT CONFLICT 88
FT /note="A -> G (in Ref. 5; BAC32147)"
FT /evidence="ECO:0000305"
FT CONFLICT 306
FT /note="L -> M (in Ref. 3; AAL71902)"
FT /evidence="ECO:0000305"
FT CONFLICT 342
FT /note="A -> D (in Ref. 5; BAC36885)"
FT /evidence="ECO:0000305"
FT MOD_RES Q8BP71-2:318
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES Q8BP71-2:323
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES Q8BP71-4:236
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES Q8BP71-4:241
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES Q8BP71-4:285
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES Q8BP71-5:336
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES Q8BP71-5:341
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES Q8BP71-6:268
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES Q8BP71-6:273
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES Q8BP71-7:268
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES Q8BP71-7:273
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES Q8BP71-8:268
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES Q8BP71-8:273
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES Q8BP71-8:317
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
SQ SEQUENCE 449 AA; 47330 MW; C4B01F814B3C8F5A CRC64;
MAEGGQAQQQ PPQLGPGAAA RGMKRESEVE LPVPGAGADG PEPGLSKRPR TEEAADGGMQ
NEPLTPGYHG FPARDGQGNQ EPTTTPDAMV QPFTTIPFPP PPQNGIPTEY GVPHTQDYAG
QTSEHNLTLY GSTQPHGEQS SNSPSNQNGS LTQTEGGAQT DGQQSQTQSS ENSESKSTPK
RLHVSNIPFR FRDPDLRQMF GQFGKILDVE IIFNERGSKG FGFVTFENSA DADRAREKLH
GTVVEGRKIE VNNATARVMT NKKMVTPYAN GWKLSPVVGA VYGPELYAAS SFQADVSLGN
EAAVPLSGRG GINTYIPLIS LPLVPGFPYP TAATTAAAFR GAHLRGRGRT VYGAVRAVPP
TAIPAYPGVV YQDGFYGADL YGGYAAYRYA QPATATAATA AAAAAAAYSD GYGRVYTADP
YHALAPAASY GVGAVASLYR GGYSRFAPY
