COBL_MOUSE
ID COBL_MOUSE Reviewed; 1337 AA.
AC Q5NBX1; Q5NBX2; Q60859; Q6PAT4; Q7TQM9; Q80TV4; Q8C7Q0; Q8CE81; Q8CIM4;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Protein cordon-bleu;
GN Name=Cobl; Synonyms=Kiaa0633;
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 1), AND TISSUE SPECIFICITY.
RC STRAIN=CD-1; TISSUE=Brain;
RX PubMed=14512015; DOI=10.1016/s0012-1606(03)00323-3;
RA Carroll E.A., Gerrelli D., Gasca S., Berg E., Beier D.R., Copp A.J.,
RA Klingensmith J.;
RT "Cordon-bleu is a conserved gene involved in neural tube formation.";
RL Dev. Biol. 262:16-31(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 5).
RC STRAIN=C57BL/6J; TISSUE=Embryonic spinal cord, and Skin;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 734-1337.
RC STRAIN=C57BL/6J, and Czech II; TISSUE=Brain, and Mammary gland;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 64-448, AND TISSUE SPECIFICITY.
RC STRAIN=CD-1; TISSUE=Brain;
RX PubMed=7586755; DOI=10.1002/dvg.1020170206;
RA Gasca S., Hill D.P., Klingensmith J., Rossant J.;
RT "Characterization of a gene trap insertion into a novel gene, cordon-bleu,
RT expressed in axial structures of the gastrulating mouse embryo.";
RL Dev. Genet. 17:141-154(1995).
RN [7]
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 [8]
RP FUNCTION, ACTIN-BINDING, INTERACTION WITH PACSIN1 AND DBNL, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=17956734; DOI=10.1016/j.cell.2007.08.030;
RA Ahuja R., Pinyol R., Reichenbach N., Custer L., Klingensmith J.,
RA Kessels M.M., Qualmann B.;
RT "Cordon-bleu is an actin nucleation factor and controls neuronal
RT morphology.";
RL Cell 131:337-350(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47; SER-50; SER-272; THR-522
RP AND SER-1128, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, and Lung;
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).
RN [10]
RP FUNCTION, INTERACTION WITH DBNL, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=23223303; DOI=10.1523/jneurosci.0843-12.2012;
RA Haag N., Schwintzer L., Ahuja R., Koch N., Grimm J., Heuer H., Qualmann B.,
RA Kessels M.M.;
RT "The actin nucleator Cobl is crucial for Purkinje cell development and
RT works in close conjunction with the F-actin binding protein Abp1.";
RL J. Neurosci. 32:17842-17856(2012).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 1201-1332 IN COMPLEX WITH ACTA1;
RP GSN AND TMSB4X, AND SUBUNIT.
RX PubMed=23009842; DOI=10.1016/j.bpj.2012.07.030;
RA Durer Z.A., Kudryashov D.S., Sawaya M.R., Altenbach C., Hubbell W.,
RA Reisler E.;
RT "Structural states and dynamics of the D-loop in actin.";
RL Biophys. J. 103:930-939(2012).
CC -!- FUNCTION: Plays an important role in the reorganization of the actin
CC cytoskeleton. Binds to and sequesters actin monomers (G actin).
CC Nucleates actin polymerization by assembling three actin monomers in
CC cross-filament orientation and thereby promotes growth of actin
CC filaments at the barbed end. Can also mediate actin depolymerization at
CC barbed ends and severing of actin filaments. Promotes formation of cell
CC ruffles. Regulates neuron morphogenesis and increases branching of
CC axons and dendrites. Regulates dendrite branching in Purkinje cells.
CC {ECO:0000269|PubMed:17956734, ECO:0000269|PubMed:23223303}.
CC -!- SUBUNIT: Identified in a complex composed of COBL, PACSIN1 and WASL.
CC Interacts with PACSIN1, PACSIN2 and PACSIN3 (By similarity). Identified
CC in a complex composed of ACTA1, COBL, GSN AND TMSB4X. Interacts (via
CC WH2 domains) with actin monomers. Interacts with DBNL. {ECO:0000250,
CC ECO:0000269|PubMed:17956734, ECO:0000269|PubMed:23009842,
CC ECO:0000269|PubMed:23223303}.
CC -!- INTERACTION:
CC Q5NBX1; Q9Z0W5: Pacsin1; Xeno; NbExp=14; IntAct=EBI-1550138, EBI-1550185;
CC Q5NBX1; Q9QY17: Pacsin2; Xeno; NbExp=4; IntAct=EBI-1550138, EBI-491201;
CC Q5NBX1; Q5I2Z0: Pacsin3; Xeno; NbExp=3; IntAct=EBI-1550138, EBI-7003023;
CC Q5NBX1-1; P62161: Calm3; Xeno; NbExp=6; IntAct=EBI-16174243, EBI-397530;
CC Q5NBX1-1; Q9Z0W5: Pacsin1; Xeno; NbExp=2; IntAct=EBI-16174243, EBI-1550185;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasm,
CC cytoskeleton. Cell projection, ruffle. Cytoplasm. Note=Recruited to the
CC cell membrane via interaction with PACSIN1 (By similarity). Colocalizes
CC with the actin cytoskeleton. Detected throughout the neuron cell body,
CC as well as in axons and dendrites. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q5NBX1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5NBX1-2; Sequence=VSP_021615, VSP_021618;
CC Name=3;
CC IsoId=Q5NBX1-3; Sequence=VSP_021614;
CC Name=4;
CC IsoId=Q5NBX1-4; Sequence=VSP_021619, VSP_021620;
CC Name=5;
CC IsoId=Q5NBX1-5; Sequence=VSP_021616, VSP_021617;
CC -!- TISSUE SPECIFICITY: Detected in brain cortex and in the Purkinje cell
CC layer in the cerebellum. Detected in hippocampus neurons, and at lower
CC levels in testis, lung and spleen (at protein level). Detected in
CC embryonic neural tube. {ECO:0000269|PubMed:14512015,
CC ECO:0000269|PubMed:17956734, ECO:0000269|PubMed:23223303,
CC ECO:0000269|PubMed:7586755}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH23264.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAC65616.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY308745; AAP74341.1; -; mRNA.
DR EMBL; AK122334; BAC65616.1; ALT_INIT; mRNA.
DR EMBL; AK028833; BAC26144.1; -; mRNA.
DR EMBL; AK049730; BAC33896.1; -; mRNA.
DR EMBL; AL669822; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL713914; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC023264; AAH23264.1; ALT_FRAME; mRNA.
DR EMBL; BC060061; AAH60061.1; -; mRNA.
DR EMBL; U26967; AAA92362.1; -; mRNA.
DR CCDS; CCDS36113.1; -. [Q5NBX1-1]
DR RefSeq; NP_766084.3; NM_172496.3. [Q5NBX1-1]
DR RefSeq; XP_006514548.1; XM_006514485.3. [Q5NBX1-2]
DR PDB; 3TU5; X-ray; 3.00 A; B=1201-1332.
DR PDB; 4JHD; X-ray; 2.91 A; C/F=1176-1337.
DR PDB; 5YPU; X-ray; 2.00 A; B/D=1184-1204.
DR PDB; 6JBK; X-ray; 2.45 A; B/D/F/H=1184-1205.
DR PDB; 6JCU; X-ray; 2.30 A; B/D=1184-1205.
DR PDB; 6JH8; X-ray; 2.15 A; B=1183-1205.
DR PDB; 6JH9; X-ray; 1.74 A; B=1183-1205.
DR PDBsum; 3TU5; -.
DR PDBsum; 4JHD; -.
DR PDBsum; 5YPU; -.
DR PDBsum; 6JBK; -.
DR PDBsum; 6JCU; -.
DR PDBsum; 6JH8; -.
DR PDBsum; 6JH9; -.
DR AlphaFoldDB; Q5NBX1; -.
DR SMR; Q5NBX1; -.
DR BioGRID; 198800; 1.
DR DIP; DIP-39834N; -.
DR IntAct; Q5NBX1; 7.
DR MINT; Q5NBX1; -.
DR STRING; 10090.ENSMUSP00000045693; -.
DR iPTMnet; Q5NBX1; -.
DR PhosphoSitePlus; Q5NBX1; -.
DR MaxQB; Q5NBX1; -.
DR PaxDb; Q5NBX1; -.
DR PeptideAtlas; Q5NBX1; -.
DR PRIDE; Q5NBX1; -.
DR ProteomicsDB; 283337; -. [Q5NBX1-1]
DR ProteomicsDB; 283338; -. [Q5NBX1-2]
DR ProteomicsDB; 283339; -. [Q5NBX1-3]
DR ProteomicsDB; 283340; -. [Q5NBX1-4]
DR ProteomicsDB; 283341; -. [Q5NBX1-5]
DR Antibodypedia; 13730; 120 antibodies from 16 providers.
DR DNASU; 12808; -.
DR Ensembl; ENSMUST00000046755; ENSMUSP00000045693; ENSMUSG00000020173. [Q5NBX1-1]
DR Ensembl; ENSMUST00000109650; ENSMUSP00000105277; ENSMUSG00000020173. [Q5NBX1-2]
DR Ensembl; ENSMUST00000172919; ENSMUSP00000133669; ENSMUSG00000020173. [Q5NBX1-5]
DR GeneID; 12808; -.
DR KEGG; mmu:12808; -.
DR UCSC; uc007ibd.2; mouse. [Q5NBX1-1]
DR UCSC; uc007ibf.2; mouse. [Q5NBX1-4]
DR UCSC; uc011xrq.1; mouse. [Q5NBX1-5]
DR CTD; 23242; -.
DR MGI; MGI:105056; Cobl.
DR VEuPathDB; HostDB:ENSMUSG00000020173; -.
DR eggNOG; ENOG502QTAY; Eukaryota.
DR GeneTree; ENSGT00530000063608; -.
DR HOGENOM; CLU_045340_1_0_1; -.
DR InParanoid; Q5NBX1; -.
DR OMA; DSQHDSV; -.
DR OrthoDB; 986623at2759; -.
DR PhylomeDB; Q5NBX1; -.
DR TreeFam; TF333490; -.
DR BioGRID-ORCS; 12808; 1 hit in 72 CRISPR screens.
DR PRO; PR:Q5NBX1; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q5NBX1; protein.
DR Bgee; ENSMUSG00000020173; Expressed in hindlimb stylopod muscle and 211 other tissues.
DR ExpressionAtlas; Q5NBX1; baseline and differential.
DR Genevisible; Q5NBX1; MM.
DR GO; GO:0030424; C:axon; IDA:BHF-UCL.
DR GO; GO:0044295; C:axonal growth cone; IDA:BHF-UCL.
DR GO; GO:0005938; C:cell cortex; IDA:BHF-UCL.
DR GO; GO:0030425; C:dendrite; IDA:BHF-UCL.
DR GO; GO:0044294; C:dendritic growth cone; IDA:BHF-UCL.
DR GO; GO:0016020; C:membrane; IDA:BHF-UCL.
DR GO; GO:0043025; C:neuronal cell body; IDA:BHF-UCL.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:BHF-UCL.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0001726; C:ruffle; IDA:BHF-UCL.
DR GO; GO:1990357; C:terminal web; IBA:GO_Central.
DR GO; GO:0003785; F:actin monomer binding; IDA:BHF-UCL.
DR GO; GO:0051764; P:actin crosslink formation; NAS:BHF-UCL.
DR GO; GO:0030036; P:actin cytoskeleton organization; IMP:MGI.
DR GO; GO:0051639; P:actin filament network formation; IDA:BHF-UCL.
DR GO; GO:0030041; P:actin filament polymerization; IMP:BHF-UCL.
DR GO; GO:0048669; P:collateral sprouting in absence of injury; IMP:BHF-UCL.
DR GO; GO:0048565; P:digestive tract development; IEP:BHF-UCL.
DR GO; GO:0000578; P:embryonic axis specification; IEP:BHF-UCL.
DR GO; GO:0033504; P:floor plate development; IEP:BHF-UCL.
DR GO; GO:0001889; P:liver development; IEP:BHF-UCL.
DR GO; GO:0001843; P:neural tube closure; IGI:MGI.
DR GO; GO:0030903; P:notochord development; IEP:BHF-UCL.
DR GO; GO:1900006; P:positive regulation of dendrite development; IDA:BHF-UCL.
DR GO; GO:1900029; P:positive regulation of ruffle assembly; IDA:BHF-UCL.
DR GO; GO:0001757; P:somite specification; IEP:BHF-UCL.
DR InterPro; IPR039895; COBL-like.
DR InterPro; IPR019025; Cordon-bleu_ubiquitin_domain.
DR InterPro; IPR003124; WH2_dom.
DR PANTHER; PTHR47008; PTHR47008; 1.
DR Pfam; PF09469; Cobl; 1.
DR Pfam; PF02205; WH2; 3.
DR SMART; SM00246; WH2; 3.
DR PROSITE; PS51082; WH2; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Actin-binding; Alternative splicing; Cell membrane;
KW Cell projection; Cytoplasm; Cytoskeleton; Membrane; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..1337
FT /note="Protein cordon-bleu"
FT /id="PRO_0000260492"
FT DOMAIN 1185..1205
FT /note="WH2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00406"
FT DOMAIN 1225..1245
FT /note="WH2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00406"
FT DOMAIN 1313..1333
FT /note="WH2 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00406"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 260..556
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 647..768
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 892..923
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 967..991
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1070..1094
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1113..1133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1145..1168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1192..1221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1262..1310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 323..328
FT /note="KKRRAP 1"
FT MOTIF 356..361
FT /note="KKRRAP 2"
FT COMPBIAS 284..316
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..375
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 402..427
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 479..498
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 499..513
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 529..548
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 647..664
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 680..709
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 715..732
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1070..1092
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1196..1221
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1273..1292
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1293..1310
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 47
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 50
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 212
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:D3ZUI5"
FT MOD_RES 235
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:D3ZUI5"
FT MOD_RES 272
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 294
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75128"
FT MOD_RES 346
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:D3ZUI5"
FT MOD_RES 349
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75128"
FT MOD_RES 372
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75128"
FT MOD_RES 522
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 649
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75128"
FT MOD_RES 816
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75128"
FT MOD_RES 1038
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75128"
FT MOD_RES 1128
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1303
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75128"
FT VAR_SEQ 1..16
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12693553"
FT /id="VSP_021614"
FT VAR_SEQ 262..286
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_021615"
FT VAR_SEQ 345..349
FT /note="ASLSS -> VPLLV (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_021616"
FT VAR_SEQ 350..1337
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_021617"
FT VAR_SEQ 391..448
FT /note="GVGRQVPQKPPRGTARGPPQLVLPPPPPYPPPDTDVTEPVTFPGEGAGSETS
FT ELRPKL -> V (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_021618"
FT VAR_SEQ 448..469
FT /note="LSLPLGPGSHCSMGGVSQVPAE -> RTCLLLPFQLCVDHLSFWSLLV (in
FT isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_021619"
FT VAR_SEQ 470..1337
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_021620"
FT CONFLICT 10
FT /note="K -> Q (in Ref. 3; BAC33896)"
FT /evidence="ECO:0000305"
FT CONFLICT 18
FT /note="K -> R (in Ref. 3; BAC33896)"
FT /evidence="ECO:0000305"
FT CONFLICT 45
FT /note="L -> M (in Ref. 3; BAC26144)"
FT /evidence="ECO:0000305"
FT CONFLICT 112
FT /note="T -> N (in Ref. 1; AAP74341)"
FT /evidence="ECO:0000305"
FT CONFLICT 128
FT /note="N -> S (in Ref. 3; BAC26144)"
FT /evidence="ECO:0000305"
FT CONFLICT 801
FT /note="L -> F (in Ref. 1; AAP74341)"
FT /evidence="ECO:0000305"
FT CONFLICT 914
FT /note="Q -> R (in Ref. 4; BAC65616)"
FT /evidence="ECO:0000305"
FT CONFLICT 1010
FT /note="V -> I (in Ref. 5; AAH23264)"
FT /evidence="ECO:0000305"
FT CONFLICT 1112
FT /note="L -> V (in Ref. 5; AAH23264)"
FT /evidence="ECO:0000305"
FT CONFLICT 1205
FT /note="T -> V (in Ref. 1; AAP74341)"
FT /evidence="ECO:0000305"
FT CONFLICT 1285
FT /note="P -> T (in Ref. 1; AAP74341 and 5; AAH23264)"
FT /evidence="ECO:0000305"
FT HELIX 1185..1194
FT /evidence="ECO:0007829|PDB:6JH9"
FT TURN 1195..1197
FT /evidence="ECO:0007829|PDB:4JHD"
FT HELIX 1198..1201
FT /evidence="ECO:0007829|PDB:6JH9"
FT STRAND 1202..1205
FT /evidence="ECO:0007829|PDB:4JHD"
FT HELIX 1222..1235
FT /evidence="ECO:0007829|PDB:4JHD"
FT TURN 1248..1250
FT /evidence="ECO:0007829|PDB:4JHD"
FT HELIX 1251..1254
FT /evidence="ECO:0007829|PDB:4JHD"
SQ SEQUENCE 1337 AA; 143865 MW; F4A8D3250294A277 CRC64;
MDAPRALAAK PPTGRKMKAR APPPPGKPAA QNVHSEQKLP HDATLGSQQS LVYMKEALQN
STLDITVVLP SGLEKQSVVS GSHAMMDLLV ELCLQNHLNP SHHVLEIWSS ETQQPLSFKP
NTLIGSLNVH TVLLKEKVPE ERVKPGLTKA PEKSVRLVVN YLRTQKAVVR VSPEVPLQNI
LPVICAKCEV NPEHVILLRD NVAGEELELS KSLNELGIKE LYAWDNRREM FRKSSLGNDE
TDKEKKKFLG FFKANKRSNS KAEHLGLSGA DSDEDPAKSA SGGDLNGCVT TPNSPSLHSR
SLTLGPSLSL GNISGVSMKS DMKKRRAPPP PSPKLLGQDK VSEKASLSSQ ADLQKKKRRA
PAPPPPQQPP PSPVVPNRKE DKEENRKSTV GVGRQVPQKP PRGTARGPPQ LVLPPPPPYP
PPDTDVTEPV TFPGEGAGSE TSELRPKLSL PLGPGSHCSM GGVSQVPAES EETASEDTTE
DSGVMSSPSD AISLDSQQDS MRSKDKWSTD QEDGSDQDLA GTPELGPQKS PSWGKSGSGS
SILRTEKATM PTNDDEDLFI TGHLHQTLAE LDEDLEGMEE NYETDTSSLT NSVNGVSNHS
LQEAIIPDSG VDDIPVTFIG EVSDEPFDSG LFSSRCNNAT TFNTGSIASQ RSHLSPSQTE
HSQPFVRTSR KEPDPSPPSQ DNRKRNQPTL ANTSENENPV ETDPTVTSLV SKLLIDDPKA
KDKGKVHGSS HSEKTQAGHG INSLRVNPRD GKDESSNSAP PPWSHHGQAL GGSYGLKYGL
TTYKIVPPKS EMRCYDRDVS LSTGAIKIDE LGNLVSPHMN GSRTISPPSA VVETDTPPIG
KVKEFWRRNS MEKYLNGPAE CTIKRAPSTT ITATPEKPQQ DNGMKAAFTV TTPQQQPASQ
EYGAHLEEER SRPQSAVSCS VKVPASNPTD ITFLKPQRRT SSQYVASAIA KKMGPPKVHA
DVVRPHKATT EQCHEEAKLA RSPPTRKDDA APNLHSEARQ HEHGTNQSSV CLPSNPGVQL
PAGGHPKVEV NSTYGKSSTQ DYPAAVHRNS YFLPGRSSHR DRVSVGQSCG FNEKQTTSNQ
KANSTSNFSQ ALDKAHPPPL LLAEARDSGR ILMNGSARTP GNCEPPHSPK ESTLTSYIIL
QTEEKPSSLS TDGQDADDTL PSSIFGPKKK FKPVIQRPLP KDVSLHSALM EAIHSSGGRE
KLRKTAEQTS EGRPKKPSYV EAESERSALL AAIRGHSGTL SLRKVSSLAS EELQSFRNAA
LGAPGLDKPQ QEDLGLPPPP ALPPPPAPAP QAPSASVTVS RFSTGTPSNS VNARQALMDA
IRSGTGAARL RKVPLLV
