ESPN_MOUSE
ID ESPN_MOUSE Reviewed; 871 AA.
AC Q9ET47; A2AK06; A2AK09; A2AK13; B1AWP3; B1AWP6; B1AWQ2; Q6GYS0; Q6GYS1;
AC Q80ZC0; Q80ZC1; Q80ZC2; Q80ZC3; Q9QY27;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Espin;
DE AltName: Full=Ectoplasmic specialization protein;
GN Name=Espn;
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 TISSUE=Testis;
RX PubMed=10975527; DOI=10.1016/s0092-8674(00)00042-8;
RA Zheng L., Sekerkova G., Vranich K., Tilney L.G., Mugnaini E., Bartles J.R.;
RT "The deaf jerker mouse has a mutation in the gene encoding the espin actin-
RT bundling proteins of hair cell stereocilia and lacks espins.";
RL Cell 102:377-385(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3; 4 AND 5), TISSUE SPECIFICITY,
RP SUBCELLULAR LOCATION, AND INTERACTION WITH BAIAP2.
RC STRAIN=CBA/CaJ; TISSUE=Cerebellum;
RX PubMed=12598619; DOI=10.1523/jneurosci.23-04-01310.2003;
RA Sekerkova G., Loomis P.A., Changyaleket B., Zheng L., Eytan R., Chen B.,
RA Mugnaini E., Bartles J.R.;
RT "Novel espin actin-bundling proteins are localized to Purkinje cell
RT dendritic spines and bind the Src homology 3 adapter protein insulin
RT receptor substrate p53.";
RL J. Neurosci. 23:1310-1319(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 6 AND 7), FUNCTION, INTERACTION WITH
RP PFN2, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=CD-1;
RX PubMed=15190118; DOI=10.1523/jneurosci.1279-04.2004;
RA Sekerkova G., Zheng L., Loomis P.A., Changyaleket B., Whitlon D.S.,
RA Mugnaini E., Bartles J.R.;
RT "Espins are multifunctional actin cytoskeletal regulatory proteins in the
RT microvilli of chemosensory and mechanosensory cells.";
RL J. Neurosci. 24:5445-5456(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 8), AND SUBUNIT.
RC STRAIN=129/SvJ;
RX PubMed=10588661; DOI=10.1091/mbc.10.12.4327;
RA Chen B., Li A., Wang D., Wang M., Zheng L., Bartles J.R.;
RT "Espin contains an additional actin-binding site in its N terminus and is a
RT major actin-bundling protein of the Sertoli cell-spermatid ectoplasmic
RT specialization junctional plaque.";
RL Mol. Biol. Cell 10:4327-4339(1999).
RN [5]
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 [6]
RP FUNCTION.
RX PubMed=14657236; DOI=10.1083/jcb.200309093;
RA Loomis P.A., Zheng L., Sekerkova G., Changyaleket B., Mugnaini E.,
RA Bartles J.R.;
RT "Espin cross-links cause the elongation of microvillus-type parallel actin
RT bundles in vivo.";
RL J. Cell Biol. 163:1045-1055(2003).
RN [7]
RP DOMAIN.
RX PubMed=16569662; DOI=10.1242/jcs.02869;
RA Loomis P.A., Kelly A.E., Zheng L., Changyaleket B., Sekerkova G.,
RA Mugnaini E., Ferreira A., Mullins R.D., Bartles J.R.;
RT "Targeted wild-type and jerker espins reveal a novel, WH2-domain-dependent
RT way to make actin bundles in cells.";
RL J. Cell Sci. 119:1655-1665(2006).
RN [8]
RP FUNCTION.
RX PubMed=19287378; DOI=10.1038/ncb1851;
RA Salles F.T., Merritt R.C. Jr., Manor U., Dougherty G.W., Sousa A.D.,
RA Moore J.E., Yengo C.M., Dose A.C., Kachar B.;
RT "Myosin IIIa boosts elongation of stereocilia by transporting espin 1 to
RT the plus ends of actin filaments.";
RL Nat. Cell Biol. 11:443-450(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-342; SER-665; SER-704 AND
RP SER-708, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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).
RN [10]
RP FUNCTION.
RX PubMed=21455486; DOI=10.1371/journal.pgen.1002032;
RA Sekerkova G., Richter C.P., Bartles J.R.;
RT "Roles of the espin actin-bundling proteins in the morphogenesis and
RT stabilization of hair cell stereocilia revealed in CBA/CaJ congenic jerker
RT mice.";
RL PLoS Genet. 7:E1002032-E1002032(2011).
RN [11]
RP FUNCTION.
RX PubMed=22264607; DOI=10.1016/j.cub.2011.12.053;
RA Merritt R.C., Manor U., Salles F.T., Grati M., Dose A.C., Unrath W.C.,
RA Quintero O.A., Yengo C.M., Kachar B.;
RT "Myosin IIIB uses an actin-binding motif in its espin-1 cargo to reach the
RT tips of actin protrusions.";
RL Curr. Biol. 22:320-325(2012).
RN [12]
RP SUBCELLULAR LOCATION.
RX PubMed=26754646; DOI=10.1083/jcb.201509017;
RA Lelli A., Michel V., Boutet de Monvel J., Cortese M., Bosch-Grau M.,
RA Aghaie A., Perfettini I., Dupont T., Avan P., El-Amraoui A., Petit C.;
RT "Class III myosins shape the auditory hair bundles by limiting microvilli
RT and stereocilia growth.";
RL J. Cell Biol. 212:231-244(2016).
RN [13]
RP FUNCTION, INTERACTION WITH MYO3A AND MYO3B, AND TISSUE SPECIFICITY.
RX PubMed=26926603; DOI=10.1038/ncomms10833;
RA Ebrahim S., Avenarius M.R., Grati M., Krey J.F., Windsor A.M., Sousa A.D.,
RA Ballesteros A., Cui R., Millis B.A., Salles F.T., Baird M.A.,
RA Davidson M.W., Jones S.M., Choi D., Dong L., Raval M.H., Yengo C.M.,
RA Barr-Gillespie P.G., Kachar B.;
RT "Stereocilia-staircase spacing is influenced by myosin III motors and their
RT cargos espin-1 and espin-like.";
RL Nat. Commun. 7:10833-10833(2016).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 1-352, AND INTERACTION WITH
RP MYO3B.
RX PubMed=26785147; DOI=10.7554/elife.12856;
RA Liu H., Li J., Raval M.H., Yao N., Deng X., Lu Q., Nie S., Feng W., Wan J.,
RA Yengo C.M., Liu W., Zhang M.;
RT "Myosin III-mediated cross-linking and stimulation of actin bundling
RT activity of Espin.";
RL Elife 5:0-0(2016).
CC -!- FUNCTION: Multifunctional actin-bundling protein. Plays a major role in
CC regulating the organization, dimension, dynamics and signaling
CC capacities of the actin filament-rich microvilli in the mechanosensory
CC and chemosensory cells (PubMed:14657236, PubMed:15190118). Required for
CC the assembly and stabilization of the stereociliary parallel actin
CC bundles. Plays a crucial role in the formation and maintenance of inner
CC ear hair cell stereocilia (PubMed:21455486). Involved in the elongation
CC of actin in stereocilia (PubMed:19287378, PubMed:22264607). In
CC extrastriolar hair cells, required for targeting MYO3B to stereocilia
CC tips, and for regulation of stereocilia diameter and staircase
CC formation (PubMed:26926603). {ECO:0000269|PubMed:14657236,
CC ECO:0000269|PubMed:15190118, ECO:0000269|PubMed:19287378,
CC ECO:0000269|PubMed:21455486, ECO:0000269|PubMed:22264607,
CC ECO:0000269|PubMed:26926603}.
CC -!- SUBUNIT: Monomer (Probable). Binds F-actin in a Ca(2+)-resistant
CC fashion (PubMed:10588661). Interacts (via N-terminus) with BAIAP2 (via
CC SH3-domain) (PubMed:12598619). Interacts with PFN2 (PubMed:15190118).
CC Interacts with MYO3A (via C-terminus) (PubMed:26926603). Interacts with
CC MYO3B (via C-terminus) (PubMed:26926603, PubMed:26785147).
CC {ECO:0000269|PubMed:10588661, ECO:0000269|PubMed:12598619,
CC ECO:0000269|PubMed:15190118, ECO:0000269|PubMed:26785147,
CC ECO:0000269|PubMed:26926603, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cell projection,
CC stereocilium {ECO:0000269|PubMed:26754646}. Cell projection,
CC microvillus. Cell junction.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm, cytoskeleton. Cell
CC projection, dendritic spine.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm, cytoskeleton. Cell
CC projection, dendritic spine.
CC -!- SUBCELLULAR LOCATION: [Isoform 4]: Cytoplasm, cytoskeleton. Cell
CC projection, dendritic spine.
CC -!- SUBCELLULAR LOCATION: [Isoform 5]: Cytoplasm, cytoskeleton. Cell
CC projection, dendritic spine.
CC -!- SUBCELLULAR LOCATION: [Isoform 8]: Cytoplasm, cytoskeleton. Cell
CC junction. Note=Isoform 8 localizes to parallel actin bundles of
CC ectoplasmic specializations between neighboring Sertoli cells and at
CC sites where Sertoli cells contact the heads of elongate spermatids.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=8;
CC Name=1;
CC IsoId=Q9ET47-1; Sequence=Displayed;
CC Name=2; Synonyms=Purkinje cell espin isoform 1;
CC IsoId=Q9ET47-2; Sequence=VSP_033733, VSP_033734, VSP_033736,
CC VSP_033739;
CC Name=3; Synonyms=Purkinje cell espin isoform 1+;
CC IsoId=Q9ET47-3; Sequence=VSP_033733, VSP_033734, VSP_033736;
CC Name=4; Synonyms=Purkinje cell espin isoform 2+;
CC IsoId=Q9ET47-4; Sequence=VSP_033733, VSP_033734, VSP_033735;
CC Name=5; Synonyms=Purkinje cell espin isoform 2;
CC IsoId=Q9ET47-5; Sequence=VSP_033733, VSP_033734, VSP_033735,
CC VSP_033739;
CC Name=6; Synonyms=3B;
CC IsoId=Q9ET47-6; Sequence=VSP_033732, VSP_033737, VSP_033739;
CC Name=7; Synonyms=3A;
CC IsoId=Q9ET47-7; Sequence=VSP_033731, VSP_033739;
CC Name=8; Synonyms=small;
CC IsoId=Q9ET47-8; Sequence=VSP_033730, VSP_033738, VSP_033740;
CC -!- TISSUE SPECIFICITY: Expressed at high concentration in the microvillar
CC parallel actin bundle (PAB) of hair cells stereocilia in the cochlea
CC and vestibular system. Detected also at high levels of a number of
CC other sensory cell types, including taste receptor cells, solitary
CC chemoreceptor cells, vomeronasal sensory neurons and Merkel cells.
CC Isoforms 2, 3, 4 and 5 are expressed in Purkinje cells dendritic
CC spines. Expressed in utricle hair bundles (at protein level)
CC (PubMed:26926603). {ECO:0000269|PubMed:10975527,
CC ECO:0000269|PubMed:12598619, ECO:0000269|PubMed:15190118,
CC ECO:0000269|PubMed:26926603}.
CC -!- DOMAIN: The WH2-domain binds actin monomer and mediates actin bundle
CC assembly. {ECO:0000269|PubMed:16569662}.
CC -!- MISCELLANEOUS: Jerker mice have a frameshift mutation that affect the
CC espin C-terminus. This mutation cause deafness, vestibular dysfunction
CC and hair cell degeneration. {ECO:0000269|PubMed:10975527}.
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DR EMBL; AF239886; AAF98134.1; -; mRNA.
DR EMBL; AF540942; AAO50326.1; -; mRNA.
DR EMBL; AF540943; AAO50327.1; -; mRNA.
DR EMBL; AF540944; AAO50328.1; -; mRNA.
DR EMBL; AF540945; AAO50329.1; -; mRNA.
DR EMBL; AY587570; AAT46472.1; -; mRNA.
DR EMBL; AY587571; AAT46473.1; -; mRNA.
DR EMBL; AF134858; AAF18322.1; -; Genomic_DNA.
DR EMBL; AL772240; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS18989.1; -. [Q9ET47-1]
DR CCDS; CCDS18990.1; -. [Q9ET47-3]
DR CCDS; CCDS18991.1; -. [Q9ET47-4]
DR CCDS; CCDS18992.1; -. [Q9ET47-5]
DR CCDS; CCDS18993.1; -. [Q9ET47-2]
DR CCDS; CCDS18994.1; -. [Q9ET47-8]
DR RefSeq; NP_997570.1; NM_207687.2. [Q9ET47-1]
DR RefSeq; NP_997571.1; NM_207688.2. [Q9ET47-3]
DR RefSeq; NP_997572.1; NM_207689.2. [Q9ET47-4]
DR RefSeq; NP_997573.1; NM_207690.2. [Q9ET47-5]
DR RefSeq; NP_997574.2; NM_207691.2. [Q9ET47-2]
DR PDB; 5ET0; X-ray; 2.30 A; A/C=1-352.
DR PDB; 5ET1; X-ray; 1.65 A; A/B=1-352.
DR PDBsum; 5ET0; -.
DR PDBsum; 5ET1; -.
DR AlphaFoldDB; Q9ET47; -.
DR SMR; Q9ET47; -.
DR BioGRID; 207859; 8.
DR IntAct; Q9ET47; 9.
DR MINT; Q9ET47; -.
DR STRING; 10090.ENSMUSP00000030785; -.
DR iPTMnet; Q9ET47; -.
DR PhosphoSitePlus; Q9ET47; -.
DR EPD; Q9ET47; -.
DR MaxQB; Q9ET47; -.
DR PaxDb; Q9ET47; -.
DR PRIDE; Q9ET47; -.
DR ProteomicsDB; 275545; -. [Q9ET47-1]
DR ProteomicsDB; 275546; -. [Q9ET47-2]
DR ProteomicsDB; 275547; -. [Q9ET47-3]
DR ProteomicsDB; 275548; -. [Q9ET47-4]
DR ProteomicsDB; 275549; -. [Q9ET47-5]
DR ProteomicsDB; 275550; -. [Q9ET47-6]
DR ProteomicsDB; 275551; -. [Q9ET47-7]
DR ProteomicsDB; 275552; -. [Q9ET47-8]
DR ABCD; Q9ET47; 22 sequenced antibodies.
DR Antibodypedia; 27332; 88 antibodies from 22 providers.
DR Ensembl; ENSMUST00000030785; ENSMUSP00000030785; ENSMUSG00000028943. [Q9ET47-1]
DR Ensembl; ENSMUST00000070018; ENSMUSP00000065545; ENSMUSG00000028943. [Q9ET47-2]
DR Ensembl; ENSMUST00000080042; ENSMUSP00000078951; ENSMUSG00000028943. [Q9ET47-4]
DR Ensembl; ENSMUST00000084114; ENSMUSP00000081131; ENSMUSG00000028943. [Q9ET47-3]
DR Ensembl; ENSMUST00000105653; ENSMUSP00000101278; ENSMUSG00000028943. [Q9ET47-7]
DR Ensembl; ENSMUST00000105657; ENSMUSP00000101282; ENSMUSG00000028943. [Q9ET47-5]
DR GeneID; 56226; -.
DR KEGG; mmu:56226; -.
DR UCSC; uc008vzn.1; mouse. [Q9ET47-6]
DR UCSC; uc008vzo.1; mouse. [Q9ET47-7]
DR UCSC; uc008vzp.1; mouse. [Q9ET47-4]
DR UCSC; uc008vzq.1; mouse. [Q9ET47-3]
DR UCSC; uc008vzr.1; mouse. [Q9ET47-5]
DR UCSC; uc008vzs.1; mouse. [Q9ET47-2]
DR UCSC; uc008vzt.1; mouse. [Q9ET47-1]
DR CTD; 83715; -.
DR MGI; MGI:1861630; Espn.
DR VEuPathDB; HostDB:ENSMUSG00000028943; -.
DR eggNOG; KOG0504; Eukaryota.
DR GeneTree; ENSGT00940000160408; -.
DR HOGENOM; CLU_543542_0_0_1; -.
DR InParanoid; Q9ET47; -.
DR OrthoDB; 347029at2759; -.
DR PhylomeDB; Q9ET47; -.
DR TreeFam; TF326392; -.
DR BioGRID-ORCS; 56226; 4 hits in 74 CRISPR screens.
DR ChiTaRS; Espn; mouse.
DR PRO; PR:Q9ET47; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q9ET47; protein.
DR Bgee; ENSMUSG00000028943; Expressed in interventricular septum and 76 other tissues.
DR ExpressionAtlas; Q9ET47; baseline and differential.
DR Genevisible; Q9ET47; MM.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:MGI.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005903; C:brush border; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell.
DR GO; GO:0031941; C:filamentous actin; ISS:UniProtKB.
DR GO; GO:0005902; C:microvillus; ISO:MGI.
DR GO; GO:0032420; C:stereocilium; IDA:MGI.
DR GO; GO:0032421; C:stereocilium bundle; IDA:MGI.
DR GO; GO:0032426; C:stereocilium tip; IDA:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; ISS:UniProtKB.
DR GO; GO:0017124; F:SH3 domain binding; ISS:UniProtKB.
DR GO; GO:0051017; P:actin filament bundle assembly; IDA:MGI.
DR GO; GO:0051639; P:actin filament network formation; NAS:UniProtKB.
DR GO; GO:0007626; P:locomotory behavior; IMP:MGI.
DR GO; GO:0030034; P:microvillar actin bundle assembly; ISO:MGI.
DR GO; GO:0051494; P:negative regulation of cytoskeleton organization; IDA:UniProtKB.
DR GO; GO:0030046; P:parallel actin filament bundle assembly; IDA:MGI.
DR GO; GO:0051491; P:positive regulation of filopodium assembly; IGI:MGI.
DR GO; GO:0007605; P:sensory perception of sound; IEA:UniProtKB-KW.
DR Gene3D; 1.25.40.20; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR030233; Espn.
DR InterPro; IPR003124; WH2_dom.
DR PANTHER; PTHR24153:SF14; PTHR24153:SF14; 1.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF13637; Ank_4; 1.
DR Pfam; PF13857; Ank_5; 1.
DR Pfam; PF02205; WH2; 1.
DR SMART; SM00248; ANK; 9.
DR SMART; SM00246; WH2; 1.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 6.
DR PROSITE; PS51082; WH2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Actin-binding; Alternative splicing; ANK repeat;
KW Cell junction; Cell projection; Coiled coil; Cytoplasm; Cytoskeleton;
KW Hearing; Phosphoprotein; Reference proteome; Repeat; Synapse.
FT CHAIN 1..871
FT /note="Espin"
FT /id="PRO_0000334667"
FT REPEAT 1..31
FT /note="ANK 1"
FT REPEAT 35..66
FT /note="ANK 2"
FT REPEAT 69..99
FT /note="ANK 3"
FT REPEAT 103..132
FT /note="ANK 4"
FT REPEAT 137..167
FT /note="ANK 5"
FT REPEAT 171..201
FT /note="ANK 6"
FT REPEAT 205..235
FT /note="ANK 7"
FT REPEAT 239..268
FT /note="ANK 8"
FT REPEAT 271..300
FT /note="ANK 9"
FT DOMAIN 669..686
FT /note="WH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00406"
FT REGION 349..400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 416..469
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 493..750
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 819..850
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 772..848
FT /evidence="ECO:0000255"
FT COMPBIAS 349..396
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 425..464
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 514..552
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 604..630
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 686..707
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 708..722
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 338
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63618"
FT MOD_RES 342
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 517
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63618"
FT MOD_RES 524
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63618"
FT MOD_RES 556
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63618"
FT MOD_RES 665
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 704
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 708
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 714
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63618"
FT VAR_SEQ 1..643
FT /note="Missing (in isoform 8)"
FT /evidence="ECO:0000305"
FT /id="VSP_033730"
FT VAR_SEQ 1..577
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:15190118"
FT /id="VSP_033731"
FT VAR_SEQ 1..547
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:15190118"
FT /id="VSP_033732"
FT VAR_SEQ 1..327
FT /note="Missing (in isoform 2, isoform 4, isoform 3 and
FT isoform 5)"
FT /evidence="ECO:0000303|PubMed:12598619"
FT /id="VSP_033733"
FT VAR_SEQ 328..330
FT /note="QTL -> MGN (in isoform 2, isoform 4, isoform 3 and
FT isoform 5)"
FT /evidence="ECO:0000303|PubMed:12598619"
FT /id="VSP_033734"
FT VAR_SEQ 492..583
FT /note="Missing (in isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:12598619"
FT /id="VSP_033735"
FT VAR_SEQ 492..502
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:12598619"
FT /id="VSP_033736"
FT VAR_SEQ 548..583
FT /note="QRSFSKQPSTGDYYRQLGRSPGEPLAARPGMAHSEE -> MAHSEEVRVHQP
FT ALAGCSGPSPVPRPSLSGPSAPPQ (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:15190118"
FT /id="VSP_033737"
FT VAR_SEQ 644..656
FT /note="SSTGKVRVLRHRK -> MNSQGPLGGGRIP (in isoform 8)"
FT /evidence="ECO:0000305"
FT /id="VSP_033738"
FT VAR_SEQ 648..656
FT /note="Missing (in isoform 2, isoform 5, isoform 6 and
FT isoform 7)"
FT /evidence="ECO:0000303|PubMed:12598619,
FT ECO:0000303|PubMed:15190118"
FT /id="VSP_033739"
FT VAR_SEQ 705
FT /note="Q -> QVGTGRVPRPGSQCLPSAQPYCFSRQ (in isoform 8)"
FT /evidence="ECO:0000305"
FT /id="VSP_033740"
FT CONFLICT 564
FT /note="L -> M (in Ref. 2; AAO50326/AAO50327 and 1;
FT AAF98134)"
FT /evidence="ECO:0000305"
FT CONFLICT 720
FT /note="T -> A (in Ref. 4; AAF18322)"
FT /evidence="ECO:0000305"
FT HELIX 1..12
FT /evidence="ECO:0007829|PDB:5ET1"
FT HELIX 15..23
FT /evidence="ECO:0007829|PDB:5ET1"
FT HELIX 39..44
FT /evidence="ECO:0007829|PDB:5ET1"
FT TURN 45..47
FT /evidence="ECO:0007829|PDB:5ET1"
FT HELIX 49..57
FT /evidence="ECO:0007829|PDB:5ET1"
FT HELIX 73..80
FT /evidence="ECO:0007829|PDB:5ET1"
FT HELIX 83..90
FT /evidence="ECO:0007829|PDB:5ET1"
FT TURN 91..93
FT /evidence="ECO:0007829|PDB:5ET0"
FT HELIX 107..113
FT /evidence="ECO:0007829|PDB:5ET1"
FT HELIX 117..125
FT /evidence="ECO:0007829|PDB:5ET1"
FT HELIX 141..148
FT /evidence="ECO:0007829|PDB:5ET1"
FT HELIX 151..160
FT /evidence="ECO:0007829|PDB:5ET1"
FT HELIX 162..164
FT /evidence="ECO:0007829|PDB:5ET1"
FT HELIX 175..181
FT /evidence="ECO:0007829|PDB:5ET1"
FT HELIX 185..195
FT /evidence="ECO:0007829|PDB:5ET1"
FT HELIX 209..215
FT /evidence="ECO:0007829|PDB:5ET1"
FT HELIX 219..228
FT /evidence="ECO:0007829|PDB:5ET1"
FT HELIX 243..249
FT /evidence="ECO:0007829|PDB:5ET1"
FT HELIX 253..261
FT /evidence="ECO:0007829|PDB:5ET1"
FT HELIX 275..281
FT /evidence="ECO:0007829|PDB:5ET1"
FT HELIX 285..293
FT /evidence="ECO:0007829|PDB:5ET1"
FT HELIX 308..314
FT /evidence="ECO:0007829|PDB:5ET1"
FT HELIX 318..329
FT /evidence="ECO:0007829|PDB:5ET1"
SQ SEQUENCE 871 AA; 94497 MW; C7707D5C73678DA1 CRC64;
MALEQALQAA RRGDLDVLRS LHAAGLLGPS LRDSLDALPV HHAARSGKLH CLRYLVEEVA
LPAVSRARNG ATPAHDAAAT GYLSCLQWLL TQGGCRVQEK DNSGATVLHL AARFGHPDVV
KWLLYQGGAN SAITTDTGAL PIHYAAAKGD LPSLKLLVGH YPEGVNAQTN NGATPLYLAC
QEGHLEVTKY LVQECSADPH LRAQDGMTPL HAAAQMGHNP VLVWLVSFAD VSFSEQDHDG
ATAMHFAASR GHTKVLSWLL LHGAEISQDL WGGTPLHDAA ENGELECCQI LAVNGAGLDV
RDHDGYTAAD LAEFNGHTHC SRYLRTVQTL SLEHRVLSRD QSMDLEAKQL DSGMSSPNTT
MSVQPMTFDL GSPTSTFSNY DSCSSSHSSS KGQRSNRGIP GARAADLQSY MDMLNPEKSL
PRGKLGKPSP PPPPPPPPPS FPPPPPPTGT QPPPPPPGYP APNPPVGLHL NNIYMQTKNK
LRHVEVDSLK EPKVELNDQF AQPSSGDGHS GLHRQDSGLL RQDSELLHRQ ELLRHSTGLR
RQDSDRKQRS FSKQPSTGDY YRQLGRSPGE PLAARPGMAH SEEAALLPGN HVHNGCSADS
KASRELPPPP PPPPLPEALS SPPPAPPLPI EGAGAACGQR RSSSSTGKVR VLRHRKSTKS
FNMMSPTGDN SELLAEIKAG KSLKPTPQSK GLTTVFSGSG QPASQPESPQ PLVSPAPSRT
RSPTPPASGS QPLLNGSVVP APPATPAPGV HLDVEALIPT LDEQGRPIPE WKRQVMVRKL
QQKMQEEEEQ RRKEEEEEAR LASLPAWRRD ILRKKLEEER EQKRKEEERQ KLEEIQRAKE
QSEKLRTLGY DEAKLAPWQR QVILKKGEIP K
