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 Skeletal muscle RC {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 Skeletal muscle RC {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 Urinary RC 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 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. DR Genevisible; Q9JKS4; MM. 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; FT AAO26188/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 //