NEBL_HUMAN
ID NEBL_HUMAN Reviewed; 1014 AA.
AC O76041; B0YJ45; B9EIM9; E9PRX7; Q2TBD0; Q5VZT2; Q70I54; Q9UIC4;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Nebulette;
DE AltName: Full=Actin-binding Z-disk protein;
GN Name=NEBL {ECO:0000312|HGNC:HGNC:16932};
GN Synonyms=C10orf113 {ECO:0000312|HGNC:HGNC:16932}, LNEBL;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Heart muscle;
RX PubMed=9733644; DOI=10.1006/jmbi.1998.1999;
RA Millevoi S., Trombitas K., Kolmerer B., Kostin S., Schaper J., Pelin K.,
RA Granzier H., Labeit S.;
RT "Characterization of nebulette and nebulin and emerging concepts of their
RT roles for vertebrate Z-discs.";
RL J. Mol. Biol. 282:111-123(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Heart;
RX PubMed=10470015;
RX DOI=10.1002/(sici)1097-0169(199909)44:1<1::aid-cm1>3.0.co;2-8;
RA Moncman C.L., Wang K.;
RT "Functional dissection of nebulette demonstrates actin binding of nebulin-
RT like repeats and Z-line targeting of SH3 and linker domains.";
RL Cell Motil. Cytoskeleton 44:1-22(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, INTERACTION WITH ZYX, AND
RP SUBCELLULAR LOCATION (ISOFORM 2).
RC TISSUE=Placenta;
RX PubMed=15004028; DOI=10.1074/jbc.m310304200;
RA Li B., Zhuang L., Trueb B.;
RT "Zyxin interacts with the SH3 domains of the cytoskeletal proteins LIM-
RT nebulette and Lasp-1.";
RL J. Biol. Chem. 279:20401-20410(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NHLBI resequencing and genotyping service (RS&G);
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
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 [9]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-795, METHYLATION [LARGE SCALE
RP ANALYSIS] AT ARG-96 (ISOFORM 2), AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
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 [10]
RP FUNCTION, AND INTERACTION WITH DES.
RX PubMed=27733623; DOI=10.1091/mbc.e16-04-0237;
RA Hernandez D.A., Bennett C.M., Dunina-Barkovskaya L., Wedig T.,
RA Capetanaki Y., Herrmann H., Conover G.M.;
RT "Nebulette is a powerful cytolinker organizing desmin and actin in mouse
RT hearts.";
RL Mol. Biol. Cell 27:3869-3882(2016).
RN [11]
RP VARIANTS HIS-187; VAL-351; LYS-654 AND ALA-728.
RX PubMed=11140941; DOI=10.1007/s004390000389;
RA Arimura T., Nakamura T., Hiroi S., Satoh M., Takahashi M., Ohbuchi N.,
RA Ueda K., Nouchi T., Yamaguchi N., Akai J., Matsumori A., Sasayama S.,
RA Kimura A.;
RT "Characterization of the human nebulette gene: a polymorphism in an actin-
RT binding motif is associated with nonfamilial idiopathic dilated
RT cardiomyopathy.";
RL Hum. Genet. 107:440-451(2000).
CC -!- FUNCTION: Binds to actin and plays an important role in the assembly of
CC the Z-disk. May functionally link sarcomeric actin to the desmin
CC intermediate filaments in the heart muscle sarcomeres
CC (PubMed:27733623). Isoform 2 might play a role in the assembly of focal
CC adhesion (PubMed:15004028). {ECO:0000269|PubMed:15004028,
CC ECO:0000269|PubMed:27733623}.
CC -!- SUBUNIT: Isoform 2 interacts with ZYX (Zyxin) (PubMed:15004028).
CC Interacts (via nebulin repeats 1-5) with DESM (via rod region)
CC (PubMed:27733623). {ECO:0000269|PubMed:15004028,
CC ECO:0000269|PubMed:27733623}.
CC -!- INTERACTION:
CC O76041; Q15027: ACAP1; NbExp=3; IntAct=EBI-2880203, EBI-751746;
CC O76041; P05067: APP; NbExp=3; IntAct=EBI-2880203, EBI-77613;
CC O76041; P54253: ATXN1; NbExp=3; IntAct=EBI-2880203, EBI-930964;
CC O76041; Q86Z20: CCDC125; NbExp=3; IntAct=EBI-2880203, EBI-11977221;
CC O76041; Q8NHQ1: CEP70; NbExp=3; IntAct=EBI-2880203, EBI-739624;
CC O76041; P50570-2: DNM2; NbExp=3; IntAct=EBI-2880203, EBI-10968534;
CC O76041; Q8IZU0: FAM9B; NbExp=3; IntAct=EBI-2880203, EBI-10175124;
CC O76041; Q53SE7: FLJ13057; NbExp=3; IntAct=EBI-2880203, EBI-10172181;
CC O76041; P14136: GFAP; NbExp=3; IntAct=EBI-2880203, EBI-744302;
CC O76041; Q53GS7: GLE1; NbExp=3; IntAct=EBI-2880203, EBI-1955541;
CC O76041; Q08379: GOLGA2; NbExp=4; IntAct=EBI-2880203, EBI-618309;
CC O76041; Q9NYA3: GOLGA6A; NbExp=3; IntAct=EBI-2880203, EBI-11163335;
CC O76041; Q9NSC5: HOMER3; NbExp=3; IntAct=EBI-2880203, EBI-748420;
CC O76041; P42858: HTT; NbExp=18; IntAct=EBI-2880203, EBI-466029;
CC O76041; O60333-2: KIF1B; NbExp=3; IntAct=EBI-2880203, EBI-10975473;
CC O76041; Q9BVG8-5: KIFC3; NbExp=3; IntAct=EBI-2880203, EBI-14069005;
CC O76041; P02545: LMNA; NbExp=3; IntAct=EBI-2880203, EBI-351935;
CC O76041; Q9BRK4: LZTS2; NbExp=3; IntAct=EBI-2880203, EBI-741037;
CC O76041; Q9Y6D9: MAD1L1; NbExp=7; IntAct=EBI-2880203, EBI-742610;
CC O76041; Q8TD10: MIPOL1; NbExp=3; IntAct=EBI-2880203, EBI-2548751;
CC O76041; P07196: NEFL; NbExp=3; IntAct=EBI-2880203, EBI-475646;
CC O76041; P35240: NF2; NbExp=3; IntAct=EBI-2880203, EBI-1014472;
CC O76041; Q86Y26: NUTM1; NbExp=3; IntAct=EBI-2880203, EBI-10178410;
CC O76041; Q7Z412: PEX26; NbExp=3; IntAct=EBI-2880203, EBI-752057;
CC O76041; Q4G0R1: PIBF1; NbExp=3; IntAct=EBI-2880203, EBI-14066006;
CC O76041; Q92569: PIK3R3; NbExp=3; IntAct=EBI-2880203, EBI-79893;
CC O76041; P49810: PSEN2; NbExp=3; IntAct=EBI-2880203, EBI-2010251;
CC O76041; P47897: QARS1; NbExp=3; IntAct=EBI-2880203, EBI-347462;
CC O76041; Q96R06: SPAG5; NbExp=3; IntAct=EBI-2880203, EBI-413317;
CC O76041; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-2880203, EBI-5235340;
CC O76041; Q13077: TRAF1; NbExp=4; IntAct=EBI-2880203, EBI-359224;
CC O76041; Q12933: TRAF2; NbExp=7; IntAct=EBI-2880203, EBI-355744;
CC O76041; P14373: TRIM27; NbExp=3; IntAct=EBI-2880203, EBI-719493;
CC O76041; P18206-2: VCL; NbExp=3; IntAct=EBI-2880203, EBI-11027067;
CC O76041; Q8N5A5-2: ZGPAT; NbExp=3; IntAct=EBI-2880203, EBI-10183064;
CC O76041; B2R8Y4; NbExp=3; IntAct=EBI-2880203, EBI-10175581;
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm
CC {ECO:0000269|PubMed:15004028}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O76041-1; Sequence=Displayed;
CC Name=2; Synonyms=LIM-nebulette, LNEBL;
CC IsoId=O76041-2; Sequence=VSP_043816, VSP_043817, VSP_043818;
CC -!- TISSUE SPECIFICITY: Abundantly expressed in cardiac muscle, but not in
CC skeletal or smooth muscle. Localized to Z-lines in cardiac cells and to
CC dense bodies in nonmuscle cells. Isoform 2 is expressed in non-muscle
CC cells such as in fibroblasts.
CC -!- MISCELLANEOUS: [Isoform 2]: Expressed in non-muscle cells. May be
CC transcribed from an upstream promoter active in non-muscle cells.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI40745.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; Y16241; CAA76130.1; -; mRNA.
DR EMBL; Y17673; CAA76810.1; -; mRNA.
DR EMBL; AF047368; AAF24858.1; -; mRNA.
DR EMBL; AJ580772; CAE45323.1; -; mRNA.
DR EMBL; AK295186; BAG58190.1; -; mRNA.
DR EMBL; EF445000; ACA06022.1; -; Genomic_DNA.
DR EMBL; EF445000; ACA06023.1; -; Genomic_DNA.
DR EMBL; EF445000; ACA06024.1; -; Genomic_DNA.
DR EMBL; EF445000; ACA06026.1; -; Genomic_DNA.
DR EMBL; AL359175; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL731547; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL157398; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL158160; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471072; EAW86175.1; -; Genomic_DNA.
DR EMBL; BC110453; AAI10454.1; -; mRNA.
DR EMBL; BC126132; AAI26133.1; -; mRNA.
DR EMBL; BC126134; AAI26135.1; -; mRNA.
DR EMBL; BC140744; AAI40745.1; ALT_SEQ; mRNA.
DR EMBL; BC144447; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS7133.1; -. [O76041-2]
DR CCDS; CCDS7134.1; -. [O76041-1]
DR RefSeq; NP_001010896.2; NM_001010896.2.
DR RefSeq; NP_001166955.1; NM_001173484.1.
DR RefSeq; NP_006384.1; NM_006393.2. [O76041-1]
DR RefSeq; NP_998734.1; NM_213569.2. [O76041-2]
DR PDB; 4F14; X-ray; 1.20 A; A=955-1014.
DR PDBsum; 4F14; -.
DR AlphaFoldDB; O76041; -.
DR SMR; O76041; -.
DR BioGRID; 115784; 73.
DR IntAct; O76041; 57.
DR MINT; O76041; -.
DR STRING; 9606.ENSP00000366326; -.
DR GlyGen; O76041; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O76041; -.
DR PhosphoSitePlus; O76041; -.
DR SwissPalm; O76041; -.
DR BioMuta; C10orf113; -.
DR BioMuta; NEBL; -.
DR EPD; O76041; -.
DR jPOST; O76041; -.
DR MassIVE; O76041; -.
DR PaxDb; O76041; -.
DR PeptideAtlas; O76041; -.
DR PRIDE; O76041; -.
DR ProteomicsDB; 50360; -. [O76041-1]
DR ProteomicsDB; 50361; -. [O76041-2]
DR ABCD; O76041; 6 sequenced antibodies.
DR Antibodypedia; 2823; 82 antibodies from 18 providers.
DR DNASU; 10529; -.
DR Ensembl; ENST00000377122.9; ENSP00000366326.4; ENSG00000078114.19. [O76041-1]
DR Ensembl; ENST00000417816.2; ENSP00000393896.2; ENSG00000078114.19. [O76041-2]
DR GeneID; 10529; -.
DR KEGG; hsa:10529; -.
DR MANE-Select; ENST00000377122.9; ENSP00000366326.4; NM_006393.3; NP_006384.1.
DR UCSC; uc001iqi.4; human. [O76041-1]
DR CTD; 10529; -.
DR DisGeNET; 10529; -.
DR GeneCards; C10orf113; -.
DR GeneCards; NEBL; -.
DR HGNC; HGNC:16932; NEBL.
DR HPA; ENSG00000078114; Tissue enriched (heart).
DR MalaCards; NEBL; -.
DR MIM; 605491; gene.
DR neXtProt; NX_O76041; -.
DR OpenTargets; ENSG00000078114; -.
DR Orphanet; 155; NON RARE IN EUROPE: Familial isolated hypertrophic cardiomyopathy.
DR PharmGKB; PA134981177; -.
DR VEuPathDB; HostDB:ENSG00000078114; -.
DR eggNOG; ENOG502TDXB; Eukaryota.
DR eggNOG; KOG1702; Eukaryota.
DR GeneTree; ENSGT00940000156390; -.
DR HOGENOM; CLU_014106_0_0_1; -.
DR InParanoid; O76041; -.
DR OMA; DHSMERY; -.
DR OrthoDB; 1305510at2759; -.
DR PhylomeDB; O76041; -.
DR TreeFam; TF319104; -.
DR TreeFam; TF353304; -.
DR PathwayCommons; O76041; -.
DR SignaLink; O76041; -.
DR BioGRID-ORCS; 10529; 4 hits in 1076 CRISPR screens.
DR BioGRID-ORCS; 387638; 6 hits in 1040 CRISPR screens.
DR ChiTaRS; NEBL; human.
DR GenomeRNAi; 10529; -.
DR Pharos; O76041; Tbio.
DR PRO; PR:Q5VZT2; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; O76041; protein.
DR Bgee; ENSG00000078114; Expressed in heart right ventricle and 196 other tissues.
DR ExpressionAtlas; O76041; baseline and differential.
DR Genevisible; O76041; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0031674; C:I band; NAS:UniProtKB.
DR GO; GO:0001725; C:stress fiber; IDA:UniProtKB.
DR GO; GO:0030018; C:Z disc; IDA:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; IDA:UniProtKB.
DR GO; GO:0008092; F:cytoskeletal protein binding; IDA:UniProtKB.
DR GO; GO:0031005; F:filamin binding; IPI:UniProtKB.
DR GO; GO:0008307; F:structural constituent of muscle; NAS:UniProtKB.
DR GO; GO:0005523; F:tropomyosin binding; IPI:UniProtKB.
DR GO; GO:0071691; P:cardiac muscle thin filament assembly; IMP:UniProtKB.
DR CDD; cd11935; SH3_Nebulette_C; 1.
DR InterPro; IPR035631; Nebulette_SH3.
DR InterPro; IPR000900; Nebulin_repeat.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR Pfam; PF00880; Nebulin; 9.
DR Pfam; PF14604; SH3_9; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00227; NEBU; 23.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS51216; NEBULIN; 23.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Actin-binding; Alternative splicing; Cytoplasm; Methylation;
KW Reference proteome; Repeat; SH3 domain.
FT CHAIN 1..1014
FT /note="Nebulette"
FT /id="PRO_0000096774"
FT REPEAT 29..63
FT /note="Nebulin 1"
FT REPEAT 64..99
FT /note="Nebulin 2"
FT REPEAT 100..136
FT /note="Nebulin 3"
FT REPEAT 137..172
FT /note="Nebulin 4"
FT REPEAT 173..205
FT /note="Nebulin 5"
FT REPEAT 206..241
FT /note="Nebulin 6"
FT REPEAT 242..278
FT /note="Nebulin 7"
FT REPEAT 279..313
FT /note="Nebulin 8"
FT REPEAT 314..348
FT /note="Nebulin 9"
FT REPEAT 349..385
FT /note="Nebulin 10"
FT REPEAT 386..422
FT /note="Nebulin 11"
FT REPEAT 423..459
FT /note="Nebulin 12"
FT REPEAT 460..496
FT /note="Nebulin 13"
FT REPEAT 497..533
FT /note="Nebulin 14"
FT REPEAT 534..569
FT /note="Nebulin 15"
FT REPEAT 570..599
FT /note="Nebulin 16"
FT REPEAT 600..635
FT /note="Nebulin 17"
FT REPEAT 636..666
FT /note="Nebulin 18"
FT REPEAT 667..693
FT /note="Nebulin 19"
FT REPEAT 694..728
FT /note="Nebulin 20"
FT REPEAT 729..759
FT /note="Nebulin 21"
FT REPEAT 760..794
FT /note="Nebulin 22"
FT REPEAT 795..830
FT /note="Nebulin 23"
FT DOMAIN 954..1014
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 836..953
FT /note="Linker"
FT MOD_RES 795
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT VAR_SEQ 1..664
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15004028, ECO:0000303|PubMed:15489334"
FT /id="VSP_043816"
FT VAR_SEQ 665..782
FT /note="TPVSMTPEIERVRRNQEQLSAVKYKGELQRGTAISDPPELKRAKENQKNISN
FT VYYRGQLGRATTLSVTPEMERVKKNQENISSVKYTQDHKQMKGRPSLILDTPAMRHVKE
FT AQNHISM -> MNPQCARCGKVVYPTEKVNCLDKYWHKGCFHCEVCKMALNMNNYKGYE
FT KKPYCNAHYPKQSFTTVADTPENLRLKQQSELQSQVKYKRDFEESKGRGFSIVTDTPEL
FT QRLKRTQEQISN (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15004028, ECO:0000303|PubMed:15489334"
FT /id="VSP_043817"
FT VAR_SEQ 840..920
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15004028, ECO:0000303|PubMed:15489334"
FT /id="VSP_043818"
FT VARIANT 187
FT /note="Q -> H (in dbSNP:rs75301590)"
FT /evidence="ECO:0000269|PubMed:11140941"
FT /id="VAR_010289"
FT VARIANT 219
FT /note="A -> D (in dbSNP:rs2296610)"
FT /id="VAR_021887"
FT VARIANT 351
FT /note="M -> V (in dbSNP:rs4025981)"
FT /evidence="ECO:0000269|PubMed:11140941"
FT /id="VAR_010290"
FT VARIANT 378
FT /note="D -> H (in dbSNP:rs41277370)"
FT /id="VAR_051229"
FT VARIANT 654
FT /note="N -> K (higher frequency of homozygotes in a cohort
FT of non-familial cardiomyopathy Japanese patients as
FT compared to healthy controls; dbSNP:rs4748728)"
FT /evidence="ECO:0000269|PubMed:11140941"
FT /id="VAR_010291"
FT VARIANT 728
FT /note="T -> A (in dbSNP:rs71535732)"
FT /evidence="ECO:0000269|PubMed:11140941"
FT /id="VAR_010292"
FT CONFLICT 53..60
FT /note="RYKEEFKK -> VIKKSLKS (in Ref. 2; AAF24858)"
FT /evidence="ECO:0000305"
FT CONFLICT 75
FT /note="N -> T (in Ref. 2; AAF24858)"
FT /evidence="ECO:0000305"
FT CONFLICT 129..138
FT /note="KHDAAKGFSD -> NMMLPRILS (in Ref. 2; AAF24858)"
FT /evidence="ECO:0000305"
FT CONFLICT 439..445
FT /note="RASEMAS -> QPLKWQG (in Ref. 2; AAF24858)"
FT /evidence="ECO:0000305"
FT CONFLICT 706..726
FT /note="RAKENQKNISNVYYRGQLGRA -> PKETRKTSACLLQSSAGES (in
FT Ref. 2; AAF24858)"
FT /evidence="ECO:0000305"
FT CONFLICT 732
FT /note="T -> I (in Ref. 2; AAF24858)"
FT /evidence="ECO:0000305"
FT CONFLICT 740
FT /note="K -> E (in Ref. 2; AAF24858)"
FT /evidence="ECO:0000305"
FT CONFLICT 743
FT /note="E -> G (in Ref. 2; AAF24858)"
FT /evidence="ECO:0000305"
FT CONFLICT 902..904
FT /note="EIY -> RDL (in Ref. 2; AAF24858)"
FT /evidence="ECO:0000305"
FT STRAND 959..963
FT /evidence="ECO:0007829|PDB:4F14"
FT STRAND 980..986
FT /evidence="ECO:0007829|PDB:4F14"
FT STRAND 988..996
FT /evidence="ECO:0007829|PDB:4F14"
FT TURN 997..1000
FT /evidence="ECO:0007829|PDB:4F14"
FT STRAND 1001..1006
FT /evidence="ECO:0007829|PDB:4F14"
FT HELIX 1007..1009
FT /evidence="ECO:0007829|PDB:4F14"
FT STRAND 1010..1012
FT /evidence="ECO:0007829|PDB:4F14"
FT MOD_RES O76041-2:96
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
SQ SEQUENCE 1014 AA; 116453 MW; 81712E38BC6AC9E1 CRC64;
MRVPVFEDIK DETEEEKIGE EENEEDQVFY KPVIEDLSME LARKCTELIS DIRYKEEFKK
SKDKCTFVTD SPMLNHVKNI GAFISEAKYK GTIKADLSNS LYKRMPATID SVFAGEVTQL
QSEVAYKQKH DAAKGFSDYA HMKEPPEVKH AMEVNKHQSN ISYRKDVQDT HTYSAELDRP
DIKMATQISK IISNAEYKKG QGIMNKEPAV IGRPDFEHAV EASKLSSQIK YKEKFDNEMK
DKKHHYNPLE SASFRQNQLA ATLASNVKYK KDIQNMHDPV SDLPNLLFLD HVLKASKMLS
GREYKKLFEE NKGMYHFDAD AVEHLHHKGN AVLQSQVKYK EEYEKNKGKP MLEFVETPSY
QASKEAQKMQ SEKVYKEDFE KEIKGRSSLD LDKTPEFLHV KYITNLLREK EYKKDLENEI
KGKGMELNSE VLDIQRAKRA SEMASEKEYK KDLESIIKGK GMQAGTDTLE MQHAKKAAEI
ASEKDYKRDL ETEIKGKGMQ VSTDTLDVQR AKKASEMASQ KQYKKDLENE IKGKGMQVSM
DIPDILRAKR TSEIYSQRKY KDEAEKMLSN YSTIADTPEI QRIKTTQQNI SAVFYKKEVG
AGTAVKDSPE IERVKKNQQN ISSVKYKEEI KHATAISDPP ELKRVKENQK NISNLQYKEQ
NYKATPVSMT PEIERVRRNQ EQLSAVKYKG ELQRGTAISD PPELKRAKEN QKNISNVYYR
GQLGRATTLS VTPEMERVKK NQENISSVKY TQDHKQMKGR PSLILDTPAM RHVKEAQNHI
SMVKYHEDFE KTKGRGFTPV VDDPVTERVR KNTQVVSDAA YKGVHPHIVE MDRRPGIIVD
LKVWRTDPGS IFDLDPLEDN IQSRSLHMLS EKASHYRRHW SRSHSSSTFG TGLGDDRSEI
SEIYPSFSCC SEVTRPSDEG APVLPGAYQQ SHSQGYGYMH QTSVSSMRSM QHSPNLRTYR
AMYDYSAQDE DEVSFRDGDY IVNVQPIDDG WMYGTVQRTG RTGMLPANYI EFVN
