LDB3_HUMAN
ID LDB3_HUMAN Reviewed; 727 AA.
AC O75112; A2TDB7; A6NIV4; B4E3K3; Q5K6N9; Q5K6P0; Q5K6P1; Q96FH2; Q9Y4Z3;
AC Q9Y4Z4; Q9Y4Z5;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=LIM domain-binding protein 3;
DE AltName: Full=Protein cypher;
DE AltName: Full=Z-band alternatively spliced PDZ-motif protein;
GN Name=LDB3 {ECO:0000312|HGNC:HGNC:15710};
GN Synonyms=KIAA0613 {ECO:0000312|EMBL:BAA31588.1},
GN ZASP {ECO:0000312|EMBL:CAB46728.1};
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] {ECO:0000305, ECO:0000312|EMBL:CAB46728.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3 AND 6), INTERACTION WITH ACTN2,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=10427098; DOI=10.1083/jcb.146.2.465;
RA Faulkner G., Pallavicini A., Formentin E., Comelli A., Ievolella C.,
RA Trevisan S., Bortoletto G., Scannapieco P., Salamon M., Mouly V., Valle G.,
RA Lanfranchi G.;
RT "ZASP: a new Z-band alternatively spliced PDZ-motif protein.";
RL J. Cell Biol. 146:465-475(1999).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAQ14318.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 4; 5 AND 6).
RC TISSUE=Melanoma, Skeletal muscle, and Uterus;
RA Zeng G., Rosenberg S.A., Wang R.-F.;
RT "ZASP: a new Z-band alternatively spliced PDZ-motif protein identified from
RT a melanoma tumor line.";
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000305, ECO:0000312|EMBL:BAA31588.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain {ECO:0000312|EMBL:BAA31588.1};
RX PubMed=9734811; DOI=10.1093/dnares/5.3.169;
RA Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H.,
RA Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. X. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 5:169-176(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7).
RC TISSUE=Uterus;
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] {ECO:0000305, ECO:0000312|EMBL:AAQ14318.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NHLBI resequencing and genotyping service (RS&G);
RL Submitted (DEC-2006) 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] {ECO:0000305, ECO:0000312|EMBL:AAH10929.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
RC TISSUE=Skeletal muscle {ECO:0000312|EMBL:AAH10929.1};
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 [8] {ECO:0000305}
RP INTERACTION WITH MYOZ1; MYOZ2 AND MYOZ3.
RX PubMed=11842093; DOI=10.1074/jbc.m200712200;
RA Frey N., Olson E.N.;
RT "Calsarcin-3, a novel skeletal muscle-specific member of the calsarcin
RT family, interacts with multiple Z-disc proteins.";
RL J. Biol. Chem. 277:13998-14004(2002).
RN [9] {ECO:0000305}
RP STRUCTURE BY NMR OF 3-85.
RX PubMed=15062084; DOI=10.1016/j.str.2004.02.019;
RA Au Y., Atkinson R.A., Guerrini R., Kelly G., Joseph C., Martin S.R.,
RA Muskett F.W., Pallavicini A., Faulkner G., Pastore A.;
RT "Solution structure of ZASP PDZ domain; implications for sarcomere
RT ultrastructure and enigma family redundancy.";
RL Structure 12:611-622(2004).
RN [10] {ECO:0000305}
RP VARIANTS DILATED CARDIOMYOPATHY WITH LEFT VENTRICULAR NON-COMPACTION, AND
RP VARIANTS CMD1C LEU-189; ILE-206 AND MET-345.
RX PubMed=14662268; DOI=10.1016/j.jacc.2003.10.021;
RA Vatta M., Mohapatra B., Jimenez S., Sanchez X., Faulkner G., Perles Z.,
RA Sinagra G., Lin J.-H., Vu T.M., Zhou Q., Bowles K.R., Di Lenarda A.,
RA Schimmenti L., Fox M., Chrisco M.A., Murphy R.T., McKenna W., Elliott P.,
RA Bowles N.E., Chen J., Valle G., Towbin J.A.;
RT "Mutations in Cypher/ZASP in patients with dilated cardiomyopathy and left
RT ventricular non-compaction.";
RL J. Am. Coll. Cardiol. 42:2014-2027(2003).
RN [11] {ECO:0000305}
RP VARIANT CMD1C ASN-673, AND VARIANTS ILE-55 AND ILE-635.
RX PubMed=14660611; DOI=10.1074/jbc.m311849200;
RA Arimura T., Hayashi T., Terada H., Lee S.-Y., Zhou Q., Takahashi M.,
RA Ueda K., Nouchi T., Hohda S., Shibutani M., Hirose M., Chen J., Park J.-E.,
RA Yasunami M., Hayashi H., Kimura A.;
RT "A Cypher/ZASP mutation associated with dilated cardiomyopathy alters the
RT binding affinity to protein kinase C.";
RL J. Biol. Chem. 279:6746-6752(2004).
RN [12] {ECO:0000305}
RP VARIANTS MYOPATHY.
RX PubMed=15668942; DOI=10.1002/ana.20376;
RA Selcen D., Engel A.G.;
RT "Mutations in ZASP define a novel form of muscular dystrophy in humans.";
RL Ann. Neurol. 57:269-276(2005).
CC -!- FUNCTION: May function as an adapter in striated muscle to couple
CC protein kinase C-mediated signaling via its LIM domains to the
CC cytoskeleton. {ECO:0000305}.
CC -!- SUBUNIT: Interacts via its LIM domains with various PKC isoforms (By
CC similarity). Interacts via its PDZ domain with the ACTN2 C-terminal
CC region. Interacts with MYOZ1, MYOZ2 and MYOZ3.
CC {ECO:0000250|UniProtKB:Q9JKS4, ECO:0000269|PubMed:10427098,
CC ECO:0000269|PubMed:11842093}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:10427098}. Cell projection, pseudopodium
CC {ECO:0000269|PubMed:10427098}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:10427098}. Cytoplasm, myofibril, sarcomere, Z line
CC {ECO:0000269|PubMed:10427098}. Note=Localized to the cytoplasm around
CC nuclei and pseudopodia of undifferentiated cells and detected
CC throughout the myotubes of differentiated cells. Colocalizes with ACTN2
CC at the Z-lines.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=1 {ECO:0000305};
CC IsoId=O75112-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:10427098};
CC IsoId=O75112-2; Sequence=VSP_051898, VSP_051900;
CC Name=3 {ECO:0000269|PubMed:10427098};
CC IsoId=O75112-3; Sequence=VSP_051897;
CC Name=4 {ECO:0000269|PubMed:10427098};
CC IsoId=O75112-4; Sequence=VSP_051899, VSP_051901, VSP_051902;
CC Name=5 {ECO:0000269|PubMed:10427098};
CC IsoId=O75112-5; Sequence=VSP_051901, VSP_051902;
CC Name=6 {ECO:0000269|PubMed:10427098};
CC IsoId=O75112-6; Sequence=VSP_051898, VSP_051901, VSP_051902;
CC Name=7;
CC IsoId=O75112-7; Sequence=VSP_051899, VSP_051900;
CC -!- TISSUE SPECIFICITY: Expressed primarily in skeletal muscle and to a
CC lesser extent in heart. Also detected in brain and placenta.
CC {ECO:0000269|PubMed:10427098}.
CC -!- DISEASE: Cardiomyopathy, dilated 1C, with or without left ventricular
CC non-compaction (CMD1C) [MIM:601493]: A disorder characterized by
CC ventricular dilation and impaired systolic function, resulting in
CC congestive heart failure and arrhythmia. Patients are at risk of
CC premature death. Cardiomyopathy dilated type 1C is associated with left
CC ventricular non-compaction in some patients. Left ventricular non-
CC compaction is characterized by numerous prominent trabeculations and
CC deep intertrabecular recesses in hypertrophied and hypokinetic segments
CC of the left ventricle. {ECO:0000269|PubMed:14660611,
CC ECO:0000269|PubMed:14662268}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Left ventricular non-compaction 3 (LVNC3) [MIM:601493]: A form
CC of left ventricular non-compaction, a cardiomyopathy due to myocardial
CC morphogenesis arrest and characterized by a hypertrophic left
CC ventricle, a severely thickened 2-layered myocardium, numerous
CC prominent trabeculations, deep intertrabecular recesses, and poor
CC systolic function. Clinical manifestations are variable. Some affected
CC individuals experience no symptoms at all, others develop heart
CC failure. In some cases, left ventricular non-compaction is associated
CC with other congenital heart anomalies. LVNC3 is an autosomal dominant
CC condition. Note=The disease is caused by variants affecting the gene
CC represented in this entry.
CC -!- DISEASE: Myopathy, myofibrillar, 4 (MFM4) [MIM:609452]: A form of
CC myofibrillar myopathy, a group of chronic neuromuscular disorders
CC characterized at ultrastructural level by disintegration of the
CC sarcomeric Z disk and myofibrils, and replacement of the normal
CC myofibrillar markings by small dense granules, or larger hyaline
CC masses, or amorphous material. MFM4 is characterized by distal and
CC proximal muscle weakness with signs of cardiomyopathy and neuropathy.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA31588.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC -!- SEQUENCE CAUTION: [Isoform 6]:
CC Sequence=AAQ14317.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAB46727.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AJ133766; CAB46727.1; ALT_FRAME; mRNA.
DR EMBL; AJ133767; CAB46728.1; -; mRNA.
DR EMBL; AJ133768; CAB46729.1; -; mRNA.
DR EMBL; AF276807; AAQ14316.1; -; mRNA.
DR EMBL; AF276808; AAQ14317.1; ALT_FRAME; mRNA.
DR EMBL; AF276809; AAQ14318.1; -; mRNA.
DR EMBL; AB014513; BAA31588.1; ALT_INIT; mRNA.
DR EMBL; AK304760; BAG65515.1; -; mRNA.
DR EMBL; EF179181; ABN05284.1; -; Genomic_DNA.
DR EMBL; AC067750; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC010929; AAH10929.1; -; mRNA.
DR CCDS; CCDS41544.1; -. [O75112-2]
DR CCDS; CCDS41545.1; -. [O75112-6]
DR CCDS; CCDS44450.1; -. [O75112-5]
DR CCDS; CCDS53549.1; -. [O75112-4]
DR CCDS; CCDS53550.1; -. [O75112-7]
DR CCDS; CCDS7377.1; -. [O75112-1]
DR RefSeq; NP_001073583.1; NM_001080114.1. [O75112-2]
DR RefSeq; NP_001073584.1; NM_001080115.1. [O75112-5]
DR RefSeq; NP_001073585.1; NM_001080116.1. [O75112-6]
DR RefSeq; NP_001165081.1; NM_001171610.1. [O75112-7]
DR RefSeq; NP_001165082.1; NM_001171611.1. [O75112-4]
DR RefSeq; NP_009009.1; NM_007078.2. [O75112-1]
DR RefSeq; XP_005269521.1; XM_005269464.4.
DR RefSeq; XP_005269525.1; XM_005269468.4.
DR RefSeq; XP_011537497.1; XM_011539195.2.
DR RefSeq; XP_016871097.1; XM_017015608.1.
DR RefSeq; XP_016871098.1; XM_017015609.1.
DR PDB; 1RGW; NMR; -; A=1-85.
DR PDB; 4YDP; X-ray; 1.40 A; A/B=1-84.
DR PDBsum; 1RGW; -.
DR PDBsum; 4YDP; -.
DR AlphaFoldDB; O75112; -.
DR BMRB; O75112; -.
DR SMR; O75112; -.
DR BioGRID; 116326; 13.
DR IntAct; O75112; 4.
DR GlyGen; O75112; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O75112; -.
DR PhosphoSitePlus; O75112; -.
DR BioMuta; LDB3; -.
DR UCD-2DPAGE; O75112; -.
DR jPOST; O75112; -.
DR MassIVE; O75112; -.
DR MaxQB; O75112; -.
DR PeptideAtlas; O75112; -.
DR PRIDE; O75112; -.
DR ProteomicsDB; 49765; -. [O75112-1]
DR ProteomicsDB; 49766; -. [O75112-2]
DR ProteomicsDB; 49767; -. [O75112-3]
DR ProteomicsDB; 49768; -. [O75112-4]
DR ProteomicsDB; 49769; -. [O75112-5]
DR ProteomicsDB; 49770; -. [O75112-6]
DR ProteomicsDB; 49771; -. [O75112-7]
DR Antibodypedia; 15974; 261 antibodies from 36 providers.
DR DNASU; 11155; -.
DR Ensembl; ENST00000263066.11; ENSP00000263066.7; ENSG00000122367.21. [O75112-6]
DR Ensembl; ENST00000361373.9; ENSP00000355296.3; ENSG00000122367.21. [O75112-1]
DR Ensembl; ENST00000372056.8; ENSP00000361126.4; ENSG00000122367.21. [O75112-4]
DR Ensembl; ENST00000372066.8; ENSP00000361136.3; ENSG00000122367.21. [O75112-6]
DR Ensembl; ENST00000429277.7; ENSP00000401437.3; ENSG00000122367.21. [O75112-2]
DR Ensembl; ENST00000623007.3; ENSP00000485389.1; ENSG00000122367.21. [O75112-5]
DR Ensembl; ENST00000623056.4; ENSP00000485500.1; ENSG00000122367.21. [O75112-7]
DR GeneID; 11155; -.
DR KEGG; hsa:11155; -.
DR MANE-Select; ENST00000361373.9; ENSP00000355296.3; NM_007078.3; NP_009009.1.
DR UCSC; uc001kdr.4; human. [O75112-1]
DR CTD; 11155; -.
DR DisGeNET; 11155; -.
DR GeneCards; LDB3; -.
DR GeneReviews; LDB3; -.
DR HGNC; HGNC:15710; LDB3.
DR HPA; ENSG00000122367; Group enriched (heart muscle, skeletal muscle, tongue).
DR MalaCards; LDB3; -.
DR MIM; 601493; phenotype.
DR MIM; 605906; gene+phenotype.
DR MIM; 609452; phenotype.
DR neXtProt; NX_O75112; -.
DR OpenTargets; ENSG00000122367; -.
DR Orphanet; 293899; Familial isolated arrhythmogenic ventricular dysplasia, biventricular form.
DR Orphanet; 293888; Familial isolated arrhythmogenic ventricular dysplasia, left dominant form.
DR Orphanet; 293910; Familial isolated arrhythmogenic ventricular dysplasia, right dominant form.
DR Orphanet; 154; Familial isolated dilated cardiomyopathy.
DR Orphanet; 98912; Late-onset distal myopathy, Markesbery-Griggs type.
DR Orphanet; 54260; Left ventricular noncompaction.
DR Orphanet; 155; NON RARE IN EUROPE: Familial isolated hypertrophic cardiomyopathy.
DR PharmGKB; PA30318; -.
DR VEuPathDB; HostDB:ENSG00000122367; -.
DR GeneTree; ENSGT00940000154877; -.
DR HOGENOM; CLU_038114_0_1_1; -.
DR InParanoid; O75112; -.
DR OMA; SNVYCER; -.
DR OrthoDB; 1013114at2759; -.
DR PhylomeDB; O75112; -.
DR TreeFam; TF106408; -.
DR PathwayCommons; O75112; -.
DR SignaLink; O75112; -.
DR BioGRID-ORCS; 11155; 13 hits in 1065 CRISPR screens.
DR ChiTaRS; LDB3; human.
DR EvolutionaryTrace; O75112; -.
DR GeneWiki; LDB3; -.
DR GenomeRNAi; 11155; -.
DR Pharos; O75112; Tbio.
DR PRO; PR:O75112; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; O75112; protein.
DR Bgee; ENSG00000122367; Expressed in skeletal muscle tissue of biceps brachii and 180 other tissues.
DR ExpressionAtlas; O75112; baseline and differential.
DR Genevisible; O75112; HS.
DR GO; GO:0005912; C:adherens junction; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IDA:UniProtKB.
DR GO; GO:0031941; C:filamentous actin; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0031143; C:pseudopodium; IEA:UniProtKB-SubCell.
DR GO; GO:0001725; C:stress fiber; IBA:GO_Central.
DR GO; GO:0030018; C:Z disc; IDA:MGI.
DR GO; GO:0003779; F:actin binding; IBA:GO_Central.
DR GO; GO:0008092; F:cytoskeletal protein binding; IPI:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051371; F:muscle alpha-actinin binding; IBA:GO_Central.
DR GO; GO:0005080; F:protein kinase C binding; IEA:Ensembl.
DR GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0007507; P:heart development; IBA:GO_Central.
DR GO; GO:0061061; P:muscle structure development; IBA:GO_Central.
DR GO; GO:0045214; P:sarcomere organization; IEA:Ensembl.
DR DisProt; DP01781; -. [O75112-6]
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR031847; DUF4749.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR006643; Zasp-like_motif.
DR InterPro; IPR001781; Znf_LIM.
DR Pfam; PF15936; DUF4749; 1.
DR Pfam; PF00412; LIM; 3.
DR Pfam; PF00595; PDZ; 1.
DR SMART; SM00132; LIM; 3.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00735; ZM; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR PROSITE; PS00478; LIM_DOMAIN_1; 2.
DR PROSITE; PS50023; LIM_DOMAIN_2; 3.
DR PROSITE; PS50106; PDZ; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cardiomyopathy; Cell projection;
KW Cytoplasm; Cytoskeleton; Disease variant; LIM domain; Metal-binding;
KW Methylation; Myofibrillar myopathy; Phosphoprotein; Reference proteome;
KW Repeat; Zinc.
FT CHAIN 1..727
FT /note="LIM domain-binding protein 3"
FT /id="PRO_0000075767"
FT DOMAIN 1..84
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 549..607
FT /note="LIM zinc-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 608..667
FT /note="LIM zinc-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 668..727
FT /note="LIM zinc-binding 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT REGION 86..197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 284..440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 472..529
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..318
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 343..383
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 402..423
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..440
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 498..515
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 44
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JKS4"
FT MOD_RES 121
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JKS4"
FT MOD_RES 123
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JKS4"
FT MOD_RES 217
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JKS4"
FT MOD_RES 219
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9JKS4"
FT MOD_RES 223
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JKS4"
FT MOD_RES 516
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9JKS4"
FT MOD_RES 533
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9JKS4"
FT VAR_SEQ 108..364
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10427098"
FT /id="VSP_051897"
FT VAR_SEQ 108..229
FT /note="DPALDTNGSLVAPSPSPEARASPGTPGTPELRPTFSPAFSRPSAFSSLAEAS
FT DPGPPRASLRAKTSPEGARDLLGPKALPGSSQPRQYNNPIGLYSAETLREMAQMYQMSL
FT RGKASGVGLPG -> VVVNSPANADYQERFNPSALKDSALSTHKPIEVKGLGGKATIIH
FT AQYNTPISMYSQDAIMDAIAGQAQAQGSDFS (in isoform 2 and isoform
FT 6)"
FT /evidence="ECO:0000303|PubMed:10427098,
FT ECO:0000303|PubMed:15489334, ECO:0000303|Ref.2"
FT /id="VSP_051898"
FT VAR_SEQ 230
FT /note="G -> GADYQERFNPSALKDSALSTHKPIEVKGLGGKATIIHAQYNTPISMY
FT SQDAIMDAIAGQAQAQGSDFSG (in isoform 4 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.2"
FT /id="VSP_051899"
FT VAR_SEQ 299..361
FT /note="Missing (in isoform 2 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:10427098,
FT ECO:0000303|PubMed:14702039"
FT /id="VSP_051900"
FT VAR_SEQ 299..329
FT /note="STPIEHAPVCTSQATTPLLPASAQPPAAASP -> RERFETERNSPRFAKLR
FT NWHHGLSAQILNVK (in isoform 4, isoform 5 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:10427098,
FT ECO:0000303|PubMed:15489334, ECO:0000303|Ref.2"
FT /id="VSP_051901"
FT VAR_SEQ 331..727
FT /note="Missing (in isoform 4, isoform 5 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:10427098,
FT ECO:0000303|PubMed:15489334, ECO:0000303|Ref.2"
FT /id="VSP_051902"
FT VARIANT 55
FT /note="V -> I (in dbSNP:rs3740343)"
FT /evidence="ECO:0000269|PubMed:14660611"
FT /id="VAR_024008"
FT VARIANT 101
FT /note="P -> L (in dbSNP:rs45592139)"
FT /id="VAR_050146"
FT VARIANT 189
FT /note="S -> L (in CMD1C; dbSNP:rs45487699)"
FT /evidence="ECO:0000269|PubMed:14662268"
FT /id="VAR_024009"
FT VARIANT 206
FT /note="T -> I (in CMD1C; dbSNP:rs121908337)"
FT /evidence="ECO:0000269|PubMed:14662268"
FT /id="VAR_024010"
FT VARIANT 345
FT /note="I -> M (in CMD1C; dbSNP:rs121908336)"
FT /evidence="ECO:0000269|PubMed:14662268"
FT /id="VAR_024011"
FT VARIANT 635
FT /note="V -> I (in dbSNP:rs45618633)"
FT /evidence="ECO:0000269|PubMed:14660611"
FT /id="VAR_024012"
FT VARIANT 673
FT /note="D -> N (in CMD1C; dbSNP:rs45514002)"
FT /evidence="ECO:0000269|PubMed:14660611"
FT /id="VAR_024013"
FT CONFLICT 365..368
FT /note="ASSY -> VVVN (in Ref. 1; CAB46729)"
FT /evidence="ECO:0000305"
FT CONFLICT 372
FT /note="V -> N (in Ref. 1; CAB46729)"
FT /evidence="ECO:0000305"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:4YDP"
FT STRAND 9..11
FT /evidence="ECO:0007829|PDB:4YDP"
FT STRAND 14..20
FT /evidence="ECO:0007829|PDB:4YDP"
FT HELIX 21..23
FT /evidence="ECO:0007829|PDB:4YDP"
FT STRAND 25..32
FT /evidence="ECO:0007829|PDB:4YDP"
FT HELIX 37..40
FT /evidence="ECO:0007829|PDB:4YDP"
FT STRAND 48..52
FT /evidence="ECO:0007829|PDB:4YDP"
FT HELIX 62..70
FT /evidence="ECO:0007829|PDB:4YDP"
FT STRAND 73..81
FT /evidence="ECO:0007829|PDB:4YDP"
FT VARIANT O75112-2:117
FT /note="D -> N (in dilated cardiomyopathy with left
FT ventricular non-compaction; dbSNP:rs121908338)"
FT /evidence="ECO:0000305"
FT /id="VAR_082846"
FT VARIANT O75112-2:136
FT /note="K -> M (in dilated cardiomyopathy with left
FT ventricular non-compaction)"
FT /evidence="ECO:0000305"
FT /id="VAR_082847"
FT VARIANT O75112-2:147
FT /note="A -> T (in MFM4; dbSNP:rs121908333)"
FT /evidence="ECO:0000305"
FT /id="VAR_082848"
FT VARIANT O75112-2:165
FT /note="A -> V (in MFM4; dbSNP:rs121908334)"
FT /evidence="ECO:0000305"
FT /id="VAR_082849"
FT VARIANT O75112-4:232
FT /note="D -> N (in dilated cardiomyopathy with left
FT ventricular non-compaction; dbSNP:rs121908338)"
FT /evidence="ECO:0000305"
FT /id="VAR_082850"
FT VARIANT O75112-4:251
FT /note="K -> M (in dilated cardiomyopathy with left
FT ventricular non-compaction)"
FT /evidence="ECO:0000305"
FT /id="VAR_082851"
FT VARIANT O75112-4:262
FT /note="A -> T (in MFM4; dbSNP:rs121908333)"
FT /evidence="ECO:0000305"
FT /id="VAR_082852"
FT VARIANT O75112-4:280
FT /note="A -> V (in MFM4; dbSNP:rs121908334)"
FT /evidence="ECO:0000305"
FT /id="VAR_082853"
FT VARIANT O75112-4:383
FT /note="R -> C (in MFM4; dbSNP:rs121908335)"
FT /evidence="ECO:0000305"
FT /id="VAR_082854"
FT VARIANT O75112-5:315
FT /note="R -> C (in MFM-ZASP; dbSNP:rs121908335)"
FT /evidence="ECO:0000305"
FT /id="VAR_082855"
FT VARIANT O75112-6:147
FT /note="A -> T (in MFM4; dbSNP:rs121908333)"
FT /evidence="ECO:0000305"
FT /id="VAR_082856"
FT VARIANT O75112-6:165
FT /note="A -> V (in MFM4; dbSNP:rs121908334)"
FT /evidence="ECO:0000305"
FT /id="VAR_082857"
FT VARIANT O75112-6:268
FT /note="R -> C (in MFM4; dbSNP:rs121908335)"
FT /evidence="ECO:0000305"
FT /id="VAR_082858"
SQ SEQUENCE 727 AA; 77135 MW; 67B5B699D2B2AB68 CRC64;
MSYSVTLTGP GPWGFRLQGG KDFNMPLTIS RITPGSKAAQ SQLSQGDLVV AIDGVNTDTM
THLEAQNKIK SASYNLSLTL QKSKRPIPIS TTAPPVQTPL PVIPHQKDPA LDTNGSLVAP
SPSPEARASP GTPGTPELRP TFSPAFSRPS AFSSLAEASD PGPPRASLRA KTSPEGARDL
LGPKALPGSS QPRQYNNPIG LYSAETLREM AQMYQMSLRG KASGVGLPGG SLPIKDLAVD
SASPVYQAVI KSQNKPEDEA DEWARRSSNL QSRSFRILAQ MTGTEFMQDP DEEALRRSST
PIEHAPVCTS QATTPLLPAS AQPPAAASPS AASPPLATAA AHTAIASAST TAPASSPADS
PRPQASSYSP AVAASSAPAT HTSYSEGPAA PAPKPRVVTT ASIRPSVYQP VPASTYSPSP
GANYSPTPYT PSPAPAYTPS PAPAYTPSPV PTYTPSPAPA YTPSPAPNYN PAPSVAYSGG
PAEPASRPPW VTDDSFSQKF APGKSTTSIS KQTLPRGGPA YTPAGPQVPP LARGTVQRAE
RFPASSRTPL CGHCNNVIRG PFLVAMGRSW HPEEFTCAYC KTSLADVCFV EEQNNVYCER
CYEQFFAPLC AKCNTKIMGE VMHALRQTWH TTCFVCAACK KPFGNSLFHM EDGEPYCEKD
YINLFSTKCH GCDFPVEAGD KFIEALGHTW HDTCFICAVC HVNLEGQPFY SKKDRPLCKK
HAHTINL
