ID LDB3_MOUSE Reviewed; 723 AA.
AC Q9JKS4; B2RSB0; B7ZNT6; Q6A038; Q811P2; Q811P3; Q811P4; Q811P5; Q9D130;
AC Q9JKS3; Q9R0Z1; Q9WVH1; Q9WVH2;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 24-JAN-2024, entry version 172.
DE RecName: Full=LIM domain-binding protein 3;
DE AltName: Full=Protein cypher;
DE AltName: Full=Protein oracle;
DE AltName: Full=Z-band alternatively spliced PDZ-motif protein;
GN Name=Ldb3 {ECO:0000312|MGI:MGI:1344412}; Synonyms=Kiaa0613;
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] {ECO:0000305, ECO:0000312|EMBL:AAD42950.2}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 6), INTERACTION WITH ACTN2 AND
RP PKC, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=NIH Swiss {ECO:0000312|EMBL:AAD42950.2};
RC TISSUE=Heart {ECO:0000312|EMBL:AAD42950.2}, and
RC Skeletal muscle {ECO:0000312|EMBL:AAD42951.2};
RX PubMed=10391924; DOI=10.1074/jbc.274.28.19807;
RA Zhou Q., Ruiz-Lozano P., Martone M.E., Chen J.;
RT "Cypher, a striated muscle-restricted PDZ and LIM domain-containing
RT protein, binds to alpha-actinin-2 and protein kinase C.";
RL J. Biol. Chem. 274:19807-19813(1999).
RN [2] {ECO:0000305, ECO:0000312|EMBL:CAB46747.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6), AND TISSUE SPECIFICITY.
RC TISSUE=Diaphragm {ECO:0000312|EMBL:CAB46747.1};
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 [3] {ECO:0000305, ECO:0000312|EMBL:AAF33847.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), AND TISSUE SPECIFICITY.
RC TISSUE=Heart {ECO:0000312|EMBL:AAF33847.1};
RX PubMed=10727866; DOI=10.1016/s0925-4773(99)00330-5;
RA Passier R., Richardson J.A., Olson E.N.;
RT "Oracle, a novel PDZ-LIM domain protein expressed in heart and skeletal
RT muscle.";
RL Mech. Dev. 92:277-284(2000).
RN [4] {ECO:0000305, ECO:0000312|EMBL:AAO26189.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3; 4 AND 5), TISSUE SPECIFICITY,
RP AND DEVELOPMENTAL STAGE.
RC STRAIN=NIH Swiss {ECO:0000312|EMBL:AAO26189.1};
RC TISSUE=Heart {ECO:0000312|EMBL:AAO26188.1}, and
RC Skeletal muscle {ECO:0000312|EMBL:AAO26189.1};
RX PubMed=12499364; DOI=10.1074/jbc.m211875200;
RA Huang C., Zhou Q., Liang P., Hollander M.S., Sheikh F., Li X., Greaser M.,
RA Shelton G.D., Evans S., Chen J.;
RT "Characterization and in vivo functional analysis of splice variants of
RT cypher.";
RL J. Biol. Chem. 278:7360-7365(2003).
RN [5] {ECO:0000305, ECO:0000312|EMBL:BAD32258.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Fetal brain {ECO:0000312|EMBL:BAD32258.1};
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [6] {ECO:0000305, ECO:0000312|EMBL:BAE25016.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 5), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 1-145.
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAE25016.1};
RC TISSUE=Embryo, Heart {ECO:0000312|EMBL:BAE25016.1}, and
RC Urinary bladder {ECO:0000312|EMBL:BAE23262.1};
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 [7] {ECO:0000305, ECO:0000312|EMBL:AAH99596.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 6).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH99596.1};
RC TISSUE=Lung, and Mammary gland {ECO:0000312|EMBL:AAH99596.1};
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]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44; SER-98; THR-119; SER-121;
RP SER-123; SER-214; SER-220 AND SER-251, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-112 (ISOFORMS 2; 4 AND 6), PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-327 (ISOFORM 5), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT
RP SER-288 (ISOFORM 6), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Lung, and Spleen;
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 [9]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-216; ARG-512 AND ARG-529,
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-330 (ISOFORM 3), METHYLATION
RP [LARGE SCALE ANALYSIS] AT ARG-291 (ISOFORM 4), AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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 STRUCTURE BY NMR OF 1-83.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of PDZ domain of mouse cypher protein.";
RL Submitted (MAY-2004) to the PDB data bank.
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:0000303|PubMed:10391924}.
CC -!- SUBUNIT: Interacts via its LIM domains with various PKC isoforms.
CC Interacts via its PDZ domain with the ACTN2 C-terminal region.
CC Interacts with MYOZ1, MYOZ2 and MYOZ3. {ECO:0000250|UniProtKB:O75112,
CC ECO:0000269|PubMed:10391924}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:10391924}. Cell projection, pseudopodium
CC {ECO:0000269|PubMed:10391924}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:10391924}. Cytoplasm, myofibril, sarcomere, Z line
CC {ECO:0000269|PubMed:10391924}. 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=6;
CC Name=1 {ECO:0000269|PubMed:10391924}; Synonyms=Cypher1c
CC {ECO:0000303|PubMed:12499364}, Oracle 1 {ECO:0000303|PubMed:10727866};
CC IsoId=Q9JKS4-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:12499364}; Synonyms=Cypher1s
CC {ECO:0000303|PubMed:12499364};
CC IsoId=Q9JKS4-2; Sequence=VSP_051903;
CC Name=3 {ECO:0000269|PubMed:10427098, ECO:0000269|PubMed:12499364};
CC Synonyms=Cypher3c {ECO:0000303|PubMed:12499364}, Oracle 2
CC {ECO:0000303|PubMed:10727866};
CC IsoId=Q9JKS4-3; Sequence=VSP_051904;
CC Name=4 {ECO:0000269|PubMed:12499364}; Synonyms=Cypher3s
CC {ECO:0000303|PubMed:12499364};
CC IsoId=Q9JKS4-4; Sequence=VSP_051903, VSP_051904;
CC Name=5 {ECO:0000269|PubMed:12499364}; Synonyms=Cypher2c
CC {ECO:0000303|PubMed:12499364};
CC IsoId=Q9JKS4-5; Sequence=VSP_051905, VSP_051906;
CC Name=6 {ECO:0000269|PubMed:10391924, ECO:0000269|PubMed:10427098};
CC Synonyms=Cypher2s {ECO:0000303|PubMed:12499364};
CC IsoId=Q9JKS4-6; Sequence=VSP_051903, VSP_051905, VSP_051906;
CC -!- TISSUE SPECIFICITY: Expressed primarily in adult heart and skeletal
CC muscle, and detected at lower levels in lung. Isoforms are expressed in
CC a tissue-specific manner. Isoform 1, isoform 3 and isoform 5 are
CC expressed in heart, whereas isoform 2, isoform 4 and isoform 6 are
CC expressed in skeletal muscle. {ECO:0000269|PubMed:10391924,
CC ECO:0000269|PubMed:10427098, ECO:0000269|PubMed:10727866,
CC ECO:0000269|PubMed:12499364}.
CC -!- DEVELOPMENTAL STAGE: Initially expressed in a myocardium-specific
CC manner at 8.5-9 dpc and remains cardiac-restricted until day 12.
CC Strongly expressed throughout heart in all stages examined. At 12.5 dpc
CC expressed at low levels in non-cardiac striated muscles. By 14.5 dpc
CC expressed at high levels in both cardiac and skeletal muscle, and also
CC strongly expressed in striated muscles of tongue, thoracic and
CC abdominal muscles, leg and diaphragm. The various isoforms are
CC developmentally regulated in both skeletal and cardiac muscle. Isoform
CC 5 and isoform 6, which are barely detectable during embryogenesis are
CC up-regulated postnatally. In heart, isoform 3 is up-regulated
CC developmentally, whereas the predominant isoform 1 is expressed
CC throughout development and into adulthood. In skeletal muscle, the
CC predominant isoform 2 is gradually replaced by isoform 4 postnatally.
CC {ECO:0000269|PubMed:10391924, ECO:0000269|PubMed:12499364}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB23128.1; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
CC Sequence=BAD32258.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF114378; AAD42950.2; -; mRNA.
DR EMBL; AF114379; AAD42951.2; -; mRNA.
DR EMBL; AJ005621; CAB46747.1; -; mRNA.
DR EMBL; AF228057; AAF33847.1; -; mRNA.
DR EMBL; AF228058; AAF33848.1; -; mRNA.
DR EMBL; AY206011; AAO26187.1; -; mRNA.
DR EMBL; AY206012; AAO26188.1; -; mRNA.
DR EMBL; AY206013; AAO26189.1; -; mRNA.
DR EMBL; AY206015; AAO26190.1; -; mRNA.
DR EMBL; AK172980; BAD32258.1; ALT_INIT; mRNA.
DR EMBL; AK004020; BAB23128.1; ALT_SEQ; mRNA.
DR EMBL; AK137181; BAE23262.1; -; mRNA.
DR EMBL; AK142292; BAE25016.1; -; mRNA.
DR EMBL; BC099596; AAH99596.1; -; mRNA.
DR EMBL; BC138793; AAI38794.1; -; mRNA.
DR EMBL; BC145420; AAI45421.1; -; mRNA.
DR CCDS; CCDS26940.1; -. [Q9JKS4-3]
DR CCDS; CCDS26941.1; -. [Q9JKS4-1]
DR CCDS; CCDS26942.1; -. [Q9JKS4-5]
DR CCDS; CCDS36879.1; -. [Q9JKS4-2]
DR CCDS; CCDS88626.1; -. [Q9JKS4-4]
DR CCDS; CCDS88627.1; -. [Q9JKS4-6]
DR RefSeq; NP_001034160.1; NM_001039071.2. [Q9JKS4-3]
DR RefSeq; NP_001034161.1; NM_001039072.2.
DR RefSeq; NP_001034162.1; NM_001039073.2. [Q9JKS4-4]
DR RefSeq; NP_001034163.1; NM_001039074.2. [Q9JKS4-2]
DR RefSeq; NP_001034164.1; NM_001039075.2. [Q9JKS4-6]
DR RefSeq; NP_001034165.1; NM_001039076.2. [Q9JKS4-5]
DR RefSeq; NP_036048.3; NM_011918.4. [Q9JKS4-1]
DR RefSeq; XP_006519080.1; XM_006519017.3. [Q9JKS4-2]
DR RefSeq; XP_017171508.1; XM_017316019.1. [Q9JKS4-1]
DR PDB; 1WJL; NMR; -; A=1-83.
DR PDBsum; 1WJL; -.
DR AlphaFoldDB; Q9JKS4; -.
DR BMRB; Q9JKS4; -.
DR SMR; Q9JKS4; -.
DR BioGRID; 204912; 17.
DR IntAct; Q9JKS4; 3.
DR MINT; Q9JKS4; -.
DR STRING; 10090.ENSMUSP00000022327; -.
DR GlyGen; Q9JKS4; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; Q9JKS4; -.
DR PhosphoSitePlus; Q9JKS4; -.
DR SwissPalm; Q9JKS4; -.
DR MaxQB; Q9JKS4; -.
DR PaxDb; 10090-ENSMUSP00000022327; -.
DR PeptideAtlas; Q9JKS4; -.
DR ProteomicsDB; 264925; -. [Q9JKS4-1]
DR ProteomicsDB; 264926; -. [Q9JKS4-2]
DR ProteomicsDB; 264927; -. [Q9JKS4-3]
DR ProteomicsDB; 264928; -. [Q9JKS4-4]
DR ProteomicsDB; 264929; -. [Q9JKS4-5]
DR ProteomicsDB; 264930; -. [Q9JKS4-6]
DR Antibodypedia; 15974; 285 antibodies from 36 providers.
DR DNASU; 24131; -.
DR Ensembl; ENSMUST00000022327.13; ENSMUSP00000022327.6; ENSMUSG00000021798.15. [Q9JKS4-1]
DR Ensembl; ENSMUST00000022328.14; ENSMUSP00000022328.7; ENSMUSG00000021798.15. [Q9JKS4-3]
DR Ensembl; ENSMUST00000022330.9; ENSMUSP00000022330.8; ENSMUSG00000021798.15. [Q9JKS4-5]
DR Ensembl; ENSMUST00000090040.12; ENSMUSP00000087494.5; ENSMUSG00000021798.15. [Q9JKS4-2]
DR Ensembl; ENSMUST00000227819.2; ENSMUSP00000154119.2; ENSMUSG00000021798.15. [Q9JKS4-6]
DR Ensembl; ENSMUST00000228044.2; ENSMUSP00000154758.2; ENSMUSG00000021798.15. [Q9JKS4-4]
DR GeneID; 24131; -.
DR KEGG; mmu:24131; -.
DR UCSC; uc007taz.1; mouse. [Q9JKS4-2]
DR UCSC; uc007tba.1; mouse. [Q9JKS4-4]
DR UCSC; uc007tbc.1; mouse. [Q9JKS4-1]
DR UCSC; uc007tbd.1; mouse. [Q9JKS4-3]
DR UCSC; uc007tbe.1; mouse. [Q9JKS4-6]
DR UCSC; uc007tbf.1; mouse. [Q9JKS4-5]
DR AGR; MGI:1344412; -.
DR CTD; 11155; -.
DR MGI; MGI:1344412; Ldb3.
DR VEuPathDB; HostDB:ENSMUSG00000021798; -.
DR eggNOG; KOG1703; Eukaryota.
DR GeneTree; ENSGT00940000154877; -.
DR HOGENOM; CLU_038114_0_0_1; -.
DR InParanoid; Q9JKS4; -.
DR OMA; GAPYCKL; -.
DR OrthoDB; 370973at2759; -.
DR PhylomeDB; Q9JKS4; -.
DR TreeFam; TF106408; -.
DR BioGRID-ORCS; 24131; 0 hits in 75 CRISPR screens.
DR ChiTaRS; Ldb3; mouse.
DR EvolutionaryTrace; Q9JKS4; -.
DR PRO; PR:Q9JKS4; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q9JKS4; Protein.
DR Bgee; ENSMUSG00000021798; Expressed in triceps brachii and 222 other cell types or tissues.
DR ExpressionAtlas; Q9JKS4; baseline and differential.
DR Genevisible; Q9JKS4; MM.
DR GO; GO:0005912; C:adherens junction; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; ISS: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; ISO:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051371; F:muscle alpha-actinin binding; IDA:MGI.
DR GO; GO:0005080; F:protein kinase C binding; IDA:UniProtKB.
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; IMP:MGI.
DR CDD; cd09454; LIM1_ZASP_Cypher; 1.
DR CDD; cd09362; LIM2_Enigma_like; 1.
DR CDD; cd09460; LIM3_ZASP_Cypher; 1.
DR CDD; cd00992; PDZ_signaling; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 2.10.110.10; Cysteine Rich Protein; 3.
DR InterPro; IPR031847; PDLI1-4/Zasp-like_mid.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR006643; Zasp-like_motif.
DR InterPro; IPR001781; Znf_LIM.
DR PANTHER; PTHR24214:SF9; LIM DOMAIN-BINDING PROTEIN 3; 1.
DR PANTHER; PTHR24214; PDZ AND LIM DOMAIN PROTEIN ZASP; 1.
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; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 4.
DR SUPFAM; SSF50156; PDZ domain-like; 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; Cell projection; Cytoplasm;
KW Cytoskeleton; LIM domain; Metal-binding; Methylation; Phosphoprotein;
KW Reference proteome; Repeat; Zinc.
FT CHAIN 1..723
FT /note="LIM domain-binding protein 3"
FT /id="PRO_0000075768"
FT DOMAIN 1..84
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 545..603
FT /note="LIM zinc-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 604..663
FT /note="LIM zinc-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 664..723
FT /note="LIM zinc-binding 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT REGION 89..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 164..193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 280..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 436..525
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..193
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..326
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..419
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 436..466
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 484..513
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 44
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 98
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 119
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 121
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 123
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 214
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 216
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 220
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 251
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 512
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 529
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT VAR_SEQ 108..227
FT /note="DPALDTNGSLATPSPSPEARASPGALEFGDTFSSSFSQTSVCSPLMEASGPV
FT LPLGSPVAKASSEGAQGSVSPKVLPGPSQPRQYNNPIGLYSAETLREMAQMYQMSLRGK
FT ASGAGLLGG -> VVANSPANADYQERFNPSVLKDSALSTHKPIEVKGLGGKATIIHAQ
FT YNTPISMYSQDAIMDAIAGQAQAQGSDFSGASPLA (in isoform 2, isoform
FT 4 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:10391924,
FT ECO:0000303|PubMed:10427098, ECO:0000303|PubMed:12499364,
FT ECO:0000303|PubMed:15368895, ECO:0000303|PubMed:15489334"
FT /id="VSP_051903"
FT VAR_SEQ 296..357
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:10727866,
FT ECO:0000303|PubMed:12499364, ECO:0000303|PubMed:15489334"
FT /id="VSP_051904"
FT VAR_SEQ 296..327
FT /note="STPIEHAPVCTSQATSPLLPASAQSPAAASPI -> RERFETERNSPRFAKL
FT RNWHHGLSAQILNVKS (in isoform 5 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:10391924,
FT ECO:0000303|PubMed:10427098, ECO:0000303|PubMed:12499364,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16141072"
FT /id="VSP_051905"
FT VAR_SEQ 328..723
FT /note="Missing (in isoform 5 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:10391924,
FT ECO:0000303|PubMed:10427098, ECO:0000303|PubMed:12499364,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16141072"
FT /id="VSP_051906"
FT CONFLICT 108..145
FT /note="DPALDTNGSLATPSPSPEARASPGALEFGDTFSSSFSQ -> VVANSPANAD
FT YQERFNPSVLKGLSSVLKGLSSVHPQAH (in Ref. 6; BAB23128)"
FT /evidence="ECO:0000305"
FT CONFLICT 450
FT /note="S -> T (in Ref. 1; AAD42950 and 4; AAO26188/
FT AAO26189)"
FT /evidence="ECO:0000305"
FT CONFLICT 512
FT /note="R -> W (in Ref. 5; BAD32258)"
FT /evidence="ECO:0000305"
FT STRAND 2..10
FT /evidence="ECO:0007829|PDB:1WJL"
FT STRAND 15..17
FT /evidence="ECO:0007829|PDB:1WJL"
FT TURN 21..24
FT /evidence="ECO:0007829|PDB:1WJL"
FT STRAND 28..32
FT /evidence="ECO:0007829|PDB:1WJL"
FT HELIX 37..40
FT /evidence="ECO:0007829|PDB:1WJL"
FT STRAND 48..54
FT /evidence="ECO:0007829|PDB:1WJL"
FT STRAND 56..60
FT /evidence="ECO:0007829|PDB:1WJL"
FT HELIX 62..71
FT /evidence="ECO:0007829|PDB:1WJL"
FT STRAND 74..81
FT /evidence="ECO:0007829|PDB:1WJL"
FT MOD_RES Q9JKS4-2:112
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT Q9JKS4-2:176..188
FT /note="AQGSDFSGASPLA -> AQGSDFSG (in Ref. 4; AAO26189)"
FT /evidence="ECO:0000305"
FT MOD_RES Q9JKS4-3:330
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES Q9JKS4-4:112
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES Q9JKS4-4:291
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES Q9JKS4-5:327
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES Q9JKS4-6:112
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES Q9JKS4-6:288
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 723 AA; 76432 MW; CC67D38AC2FFA6B6 CRC64;
MSYSVTLTGP GPWGFRLQGG KDFNMPLTIS RITPGSKAAQ SQLSQGDLVV AIDGVNTDTM
THLEAQNKIK SASYNLSLTL QKSKRPIPIS TTAPPIQSPL PVIPHQKDPA LDTNGSLATP
SPSPEARASP GALEFGDTFS SSFSQTSVCS PLMEASGPVL PLGSPVAKAS SEGAQGSVSP
KVLPGPSQPR QYNNPIGLYS AETLREMAQM YQMSLRGKAS GAGLLGGSLP VKDLAVDSAS
PVYQAVIKTQ SKPEDEADEW ARRSSNLQSR SFRILAQMTG TEYMQDPDEE ALRRSSTPIE
HAPVCTSQAT SPLLPASAQS PAAASPIAAS PTLATAAATH AAAASAAGPA ASPVENPRPQ
ASAYSPAAAA SPAPSAHTSY SEGPAAPAPK PRVVTTASIR PSVYQPVPAS SYSPSPGANY
SPTPYTPSPA PAYTPSPAPT YTPSPAPTYS PSPAPAYTPS PAPNYTPTPS AAYSGGPSES
ASRPPWVTDD SFSQKFAPGK STTTVSKQTL PRGAPAYNPT GPQVTPLARG TFQRAERFPA
SSRTPLCGHC NNVIRGPFLV AMGRSWHPEE FNCAYCKTSL ADVCFVEEQN NVYCERCYEQ
FFAPICAKCN TKIMGEVMHA LRQTWHTTCF VCAACKKPFG NSLFHMEDGE PYCEKDYINL
FSTKCHGCDF PVEAGDKFIE ALGHTWHDTC FICAVCHVNL EGQPFYSKKD KPLCKKHAHA
INV
//
