ID PALLD_MOUSE Reviewed; 1408 AA. AC Q9ET54; A0JNZ3; Q69ZT7; Q6DFX7; Q9CWW1; DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot. DT 11-SEP-2007, sequence version 2. DT 27-MAR-2024, entry version 175. DE RecName: Full=Palladin; GN Name=Palld; Synonyms=Kiaa0992; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S., RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., RA Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of the RT mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5), AND NUCLEOTIDE SEQUENCE RP [LARGE SCALE MRNA] OF 539-1408 (ISOFORM 6). RC STRAIN=C57BL/6J; TISSUE=Eye; 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 311-1408 (ISOFORM 6). RC TISSUE=Embryonic tail; RX PubMed=15449545; DOI=10.1093/dnares/11.2.127; RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., RA Saga Y., Kitamura H., Nakagawa T., Nagase T., Ohara O., Koga H.; RT "Prediction of the coding sequences of mouse homologues of FLJ genes: the RT complete nucleotide sequences of 110 mouse FLJ-homologous cDNAs identified RT by screening of terminal sequences of cDNA clones randomly sampled from RT size-fractionated libraries."; RL DNA Res. 11:127-135(2004). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] OF 900-1408 (ISOFORM 6), FUNCTION, SUBCELLULAR RP LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND PHOSPHORYLATION. RC STRAIN=Swiss Webster / NIH; RX PubMed=10931874; DOI=10.1083/jcb.150.3.643; RA Parast M.M., Otey C.A.; RT "Characterization of palladin, a novel protein localized to stress fibers RT and cell adhesions."; RL J. Cell Biol. 150:643-656(2000). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1015-1408 (ISOFORM 1). RC STRAIN=C57BL/6J; 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 [6] RP TISSUE SPECIFICITY. RX PubMed=11438925; DOI=10.1002/cne.1062.abs; RA Hwang S.J., Pagliardini S., Boukhelifa M., Parast M.M., Otey C.A., RA Rustioni A., Valtschanoff J.G.; RT "Palladin is expressed preferentially in excitatory terminals in the rat RT central nervous system."; RL J. Comp. Neurol. 436:211-224(2001). RN [7] RP INTERACTION WITH VASP. RX PubMed=14983521; DOI=10.1002/cm.10173; RA Boukhelifa M., Parast M.M., Bear J.E., Gertler F.B., Otey C.A.; RT "Palladin is a novel binding partner for Ena/VASP family members."; RL Cell Motil. Cytoskeleton 58:17-29(2004). RN [8] RP ALTERNATIVE SPLICING (ISOFORMS 1; 3 AND 4). RX PubMed=16164966; DOI=10.1016/s0074-7696(05)46002-7; RA Otey C.A., Rachlin A., Moza M., Arneman D., Carpen O.; RT "The palladin/myotilin/myopalladin family of actin-associated scaffolds."; RL Int. Rev. Cytol. 246:31-58(2005). RN [9] RP FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE. RX PubMed=15950489; DOI=10.1016/j.mcn.2004.12.002; RA Luo H., Liu X., Wang F., Huang Q., Shen S., Wang L., Xu G., Sun X., RA Kong H., Gu M., Chen S., Chen Z., Wang Z.; RT "Disruption of palladin results in neural tube closure defects in mice."; RL Mol. Cell. Neurosci. 29:507-515(2005). RN [10] RP FUNCTION, ALTERNATIVE SPLICING (ISOFORMS 3 AND 4), AND INTERACTION OF RP ISOFORM 3 WITH LASP1. RX PubMed=16492705; DOI=10.1242/jcs.02825; RA Rachlin A.S., Otey C.A.; RT "Identification of palladin isoforms and characterization of an isoform- RT specific interaction between Lasp-1 and palladin."; RL J. Cell Sci. 119:995-1004(2006). RN [11] RP INTERACTION WITH EPS8. RX PubMed=16868024; DOI=10.1242/jcs.03076; RA Goicoechea S., Arneman D., Disanza A., Garcia-Mata R., Scita G., Otey C.A.; RT "Palladin binds to Eps8 and enhances the formation of dorsal ruffles and RT podosomes in vascular smooth muscle cells."; RL J. Cell Sci. 119:3316-3324(2006). RN [12] RP DISRUPTION PHENOTYPE. RX PubMed=17431131; DOI=10.1182/blood-2007-01-068528; RA Liu X.-S., Li X.-H., Wang Y., Shu R.-Z., Wang L., Lu S.-Y., Kong H., RA Jin Y.-E., Zhang L.-J., Fei J., Chen S.-J., Chen Z., Gu M.-M., Lu Z.-Y., RA Wang Z.-G.; RT "Disruption of palladin leads to defects in definitive erythropoiesis by RT interfering erythroblastic island formation in mouse fetal liver."; RL Blood 110:870-876(2007). RN [13] RP FUNCTION, AND DISRUPTION PHENOTYPE. RX PubMed=17115415; DOI=10.1002/jcb.21126; RA Liu X.-S., Luo H.-J., Yang H., Wang L., Kong H., Jin Y.-E., Wang F., RA Gu M.-M., Chen Z., Lu Z.-Y., Wang Z.-G.; RT "Palladin regulates cell and extracellular matrix interaction through RT maintaining normal actin cytoskeleton architecture and stabilizing beta1- RT integrin."; RL J. Cell. Biochem. 100:1288-1300(2007). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-901; SER-1143 AND SER-1146, RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=17242355; DOI=10.1073/pnas.0609836104; RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; RT "Large-scale phosphorylation analysis of mouse liver."; RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). RN [15] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=18630941; DOI=10.1021/pr800223m; RA Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.; RT "Specific phosphopeptide enrichment with immobilized titanium ion affinity RT chromatography adsorbent for phosphoproteome analysis."; RL J. Proteome Res. 7:3957-3967(2008). RN [16] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic fibroblast; RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200; RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.; RT "Large scale localization of protein phosphorylation by use of electron RT capture dissociation mass spectrometry."; RL Mol. Cell. Proteomics 8:904-912(2009). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-194; SER-639; THR-642; RP SER-901; SER-1004; SER-1009; SER-1141 AND SER-1146, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen, and RC Testis; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). CC -!- FUNCTION: Cytoskeletal protein required for organization of normal CC actin cytoskeleton. Roles in establishing cell morphology, motility, CC cell adhesion and cell-extracellular matrix interactions in a variety CC of cell types. May function as a scaffolding molecule with the CC potential to influence both actin polymerization and the assembly of CC existing actin filaments into higher-order arrays. Binds to proteins CC that bind to either monomeric or filamentous actin. Localizes at sites CC where active actin remodeling takes place, such as lamellipodia and CC membrane ruffles. Different isoforms may have functional differences. CC Involved in the control of morphological and cytoskeletal changes CC associated with dendritic cell maturation. Involved in targeting ACTN CC to specific subcellular locations. May be required for the initiation CC of neural tube closure. {ECO:0000269|PubMed:10931874, CC ECO:0000269|PubMed:15950489, ECO:0000269|PubMed:16492705, CC ECO:0000269|PubMed:17115415}. CC -!- SUBUNIT: Interacts with EPS8 (PubMed:16868024). Interacts with LASP1 CC (PubMed:16492705). Interacts with VASP (PubMed:14983521). Interacts CC with ACTN (By similarity). Interacts with SORBS2 (By similarity). CC Interacts with PFN1 (By similarity). Interacts with LPP (By CC similarity). Interacts with SPIN90 (By similarity). Interacts with SRC CC (By similarity). Interacts with EZR (By similarity). Interacts with CC RAI14 (By similarity). {ECO:0000250|UniProtKB:P0C5E3, CC ECO:0000250|UniProtKB:Q8WX93, ECO:0000269|PubMed:14983521, CC ECO:0000269|PubMed:16492705, ECO:0000269|PubMed:16868024}. CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton CC {ECO:0000269|PubMed:10931874}. Cell junction, focal adhesion CC {ECO:0000269|PubMed:10931874}. Cytoplasm, myofibril, sarcomere, Z line CC {ECO:0000269|PubMed:10931874}. Cell projection, ruffle CC {ECO:0000250|UniProtKB:Q8WX93}. Cell projection, podosome CC {ECO:0000250|UniProtKB:P0C5E3}. Cell projection, lamellipodium CC {ECO:0000250|UniProtKB:Q8WX93}. Cell projection, axon CC {ECO:0000250|UniProtKB:P0C5E3}. Cell projection, growth cone CC {ECO:0000250|UniProtKB:P0C5E3}. Note=Localizes to stress fibers and Z CC lines (PubMed:10931874). Preferentially expressed in the excitatory CC presynaptic terminals (By similarity). {ECO:0000250|UniProtKB:P0C5E3, CC ECO:0000269|PubMed:10931874}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=6; CC Name=1; Synonyms=200 kDa isoform; CC IsoId=Q9ET54-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9ET54-2; Sequence=VSP_027934, VSP_027935, VSP_027936; CC Name=3; Synonyms=90 kDa isoform, 3Ig isoform; CC IsoId=Q9ET54-3; Sequence=VSP_027932, VSP_027935; CC Name=4; Synonyms=140 kDa isoform, 4Ig isoform; CC IsoId=Q9ET54-4; Sequence=VSP_027933, VSP_027935; CC Name=5; CC IsoId=Q9ET54-5; Sequence=VSP_027931; CC Name=6; CC IsoId=Q9ET54-6; Sequence=VSP_027935; CC -!- TISSUE SPECIFICITY: Detected in both muscle and non-muscle tissues and CC cells (at protein level). Isoform 3 is widely expressed, isoform 4 is CC particularly abundant in tissues rich in smooth muscle and in the CC cardiac muscle and isoform 1 is detected in heart. CC {ECO:0000269|PubMed:10931874, ECO:0000269|PubMed:11438925}. CC -!- DEVELOPMENTAL STAGE: Ubiquitously detected in embryonic tissues, and CC down-regulated in certain adult tissues (at protein level). Isoform 3 CC is widely expressed in embryonic tissues (at protein level). In adults CC is detected in spleen and gut, and is almost undetectable in heart, CC skeletal muscle, liver, and kidney (at protein level). Isoform 4 is CC widely expressed in neonatal tissues (brain, heart, lung, stomach, CC intestine, kidney, bone and skin) (at protein level). Late in CC development expression is restricted to cardiac muscle and to organs CC rich in smooth muscle (at protein level). Isoform 1 is detected in CC neonatal striated muscle and bone, and remains highly expressed in CC adult skeletal and cardiac muscle (at protein level). Adult brain CC express an isoform of 80-85 kDa. At 8.5 dpc is mainly expressed the CC rostral and caudal part of neural plate. No expression is detected in CC somite. At 9.5 dpc and 10.5 dpc is ubiquitously detected. CC {ECO:0000269|PubMed:10931874, ECO:0000269|PubMed:15950489}. CC -!- PTM: Phosphorylated predominantly on serines and, to a lesser extent, CC on tyrosines. Phosphorylation at Ser-1143 by PKB/AKT1 modulates CC cytoskeletal organization and cell motility (By similarity). CC {ECO:0000250}. CC -!- DISRUPTION PHENOTYPE: Death around 15.5 dpc due to severe neural tube CC closure defects and herniation of liver and intestine. Palld-deficient CC mouse embryonic fibroblasts display disorganized actin cytoskeleton, CC decreased polymerized filament actin, and decreased cell adhesion and CC compromised cell spreading on various extracellular matrix. Mice CC embryos lacking Palld exhibit defects in erythropoiesis. CC {ECO:0000269|PubMed:15950489, ECO:0000269|PubMed:17115415, CC ECO:0000269|PubMed:17431131}. CC -!- SIMILARITY: Belongs to the myotilin/palladin family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AK031696; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=BAB26871.1; 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; AC121881; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC139846; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC147616; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC076588; AAH76588.1; -; mRNA. DR EMBL; BC127081; AAI27082.1; -; mRNA. DR EMBL; AK173081; BAD32359.1; -; mRNA. DR EMBL; AF205078; AAG00078.1; -; mRNA. DR EMBL; AK010350; BAB26871.1; ALT_INIT; mRNA. DR EMBL; AK031696; -; NOT_ANNOTATED_CDS; mRNA. DR CCDS; CCDS40350.1; -. [Q9ET54-2] DR CCDS; CCDS80880.1; -. [Q9ET54-3] DR CCDS; CCDS80881.1; -. [Q9ET54-4] DR CCDS; CCDS80882.1; -. [Q9ET54-1] DR RefSeq; NP_001074859.1; NM_001081390.1. [Q9ET54-2] DR RefSeq; NP_001280701.1; NM_001293772.1. [Q9ET54-1] DR RefSeq; NP_001280703.1; NM_001293774.1. [Q9ET54-3] DR RefSeq; XP_006509566.1; XM_006509503.2. [Q9ET54-6] DR RefSeq; XP_011240544.1; XM_011242242.2. [Q9ET54-1] DR PDB; 2LQR; NMR; -; A=1022-1126. DR PDBsum; 2LQR; -. DR AlphaFoldDB; Q9ET54; -. DR SMR; Q9ET54; -. DR BioGRID; 215316; 6. DR IntAct; Q9ET54; 2. DR STRING; 10090.ENSMUSP00000112442; -. DR GlyGen; Q9ET54; 2 sites, 1 O-linked glycan (2 sites). DR iPTMnet; Q9ET54; -. DR PhosphoSitePlus; Q9ET54; -. DR jPOST; Q9ET54; -. DR MaxQB; Q9ET54; -. DR PaxDb; 10090-ENSMUSP00000112442; -. DR PeptideAtlas; Q9ET54; -. DR ProteomicsDB; 293998; -. [Q9ET54-1] DR ProteomicsDB; 293999; -. [Q9ET54-2] DR ProteomicsDB; 294000; -. [Q9ET54-3] DR ProteomicsDB; 294001; -. [Q9ET54-4] DR ProteomicsDB; 294002; -. [Q9ET54-5] DR ProteomicsDB; 294003; -. [Q9ET54-6] DR Pumba; Q9ET54; -. DR Antibodypedia; 28415; 374 antibodies from 37 providers. DR DNASU; 72333; -. DR Ensembl; ENSMUST00000034057.14; ENSMUSP00000034057.8; ENSMUSG00000058056.17. [Q9ET54-2] DR Ensembl; ENSMUST00000121200.9; ENSMUSP00000112374.2; ENSMUSG00000058056.17. [Q9ET54-3] DR Ensembl; ENSMUST00000121493.9; ENSMUSP00000113874.2; ENSMUSG00000058056.17. [Q9ET54-4] DR Ensembl; ENSMUST00000121785.9; ENSMUSP00000112442.2; ENSMUSG00000058056.17. [Q9ET54-1] DR GeneID; 72333; -. DR KEGG; mmu:72333; -. DR UCSC; uc009lud.3; mouse. [Q9ET54-3] DR UCSC; uc009lue.3; mouse. [Q9ET54-4] DR UCSC; uc009luf.3; mouse. [Q9ET54-1] DR UCSC; uc009lug.3; mouse. [Q9ET54-2] DR AGR; MGI:1919583; -. DR CTD; 23022; -. DR MGI; MGI:1919583; Palld. DR VEuPathDB; HostDB:ENSMUSG00000058056; -. DR eggNOG; ENOG502QSRV; Eukaryota. DR GeneTree; ENSGT00940000153441; -. DR HOGENOM; CLU_006487_2_0_1; -. DR InParanoid; Q9ET54; -. DR OMA; XPRSRSR; -. DR OrthoDB; 5356884at2759; -. DR PhylomeDB; Q9ET54; -. DR TreeFam; TF343193; -. DR BioGRID-ORCS; 72333; 5 hits in 76 CRISPR screens. DR ChiTaRS; Palld; mouse. DR PRO; PR:Q9ET54; -. DR Proteomes; UP000000589; Chromosome 8. DR RNAct; Q9ET54; Protein. DR Bgee; ENSMUSG00000058056; Expressed in umbilical cord and 249 other cell types or tissues. DR ExpressionAtlas; Q9ET54; baseline and differential. DR GO; GO:0015629; C:actin cytoskeleton; ISO:MGI. DR GO; GO:0005884; C:actin filament; ISS:HGNC-UCL. DR GO; GO:0030424; C:axon; ISO:MGI. DR GO; GO:0044295; C:axonal growth cone; ISO:MGI. DR GO; GO:0005856; C:cytoskeleton; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; ISO:MGI. DR GO; GO:0060076; C:excitatory synapse; ISS:UniProtKB. DR GO; GO:0030175; C:filopodium; ISO:MGI. DR GO; GO:0005925; C:focal adhesion; IDA:UniProtKB. DR GO; GO:0030426; C:growth cone; ISO:MGI. DR GO; GO:0030027; C:lamellipodium; ISO:MGI. DR GO; GO:0005739; C:mitochondrion; ISO:MGI. DR GO; GO:0043025; C:neuronal cell body; ISO:MGI. DR GO; GO:0005634; C:nucleus; ISS:HGNC-UCL. DR GO; GO:0005886; C:plasma membrane; ISO:MGI. DR GO; GO:0002102; C:podosome; ISO:MGI. DR GO; GO:0001726; C:ruffle; ISO:MGI. DR GO; GO:0001725; C:stress fiber; IDA:UniProtKB. DR GO; GO:0030018; C:Z disc; IDA:UniProtKB. DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW. DR GO; GO:0008046; F:axon guidance receptor activity; IBA:GO_Central. DR GO; GO:0008092; F:cytoskeletal protein binding; ISO:MGI. DR GO; GO:0030036; P:actin cytoskeleton organization; IMP:MGI. DR GO; GO:0016477; P:cell migration; IEA:InterPro. DR GO; GO:0003382; P:epithelial cell morphogenesis; IMP:MGI. DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IBA:GO_Central. DR GO; GO:0003334; P:keratinocyte development; IMP:MGI. DR GO; GO:0050808; P:synapse organization; IBA:GO_Central. DR CDD; cd05893; IgI_1_Palladin_C; 1. DR CDD; cd20972; IgI_2_Titin_Z1z2-like; 1. DR CDD; cd05892; IgI_Myotilin_C; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 5. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR013098; Ig_I-set. DR InterPro; IPR003599; Ig_sub. DR InterPro; IPR003598; Ig_sub2. DR InterPro; IPR033017; Palladin_C. DR PANTHER; PTHR45080; CONTACTIN 5; 1. DR PANTHER; PTHR45080:SF8; WRAPPER_REGA-1_KLINGON HOMOLOG; 1. DR Pfam; PF07679; I-set; 5. DR SMART; SM00409; IG; 5. DR SMART; SM00408; IGc2; 5. DR SUPFAM; SSF48726; Immunoglobulin; 5. DR PROSITE; PS50835; IG_LIKE; 5. DR Genevisible; Q9ET54; MM. PE 1: Evidence at protein level; KW 3D-structure; Actin-binding; Alternative splicing; Cell junction; KW Cell projection; Cytoplasm; Cytoskeleton; Disulfide bond; KW Immunoglobulin domain; Phosphoprotein; Reference proteome; Repeat. FT CHAIN 1..1408 FT /note="Palladin" FT /id="PRO_0000302721" FT DOMAIN 278..367 FT /note="Ig-like C2-type 1" FT DOMAIN 448..546 FT /note="Ig-like C2-type 2" FT DOMAIN 1026..1110 FT /note="Ig-like C2-type 3" FT DOMAIN 1160..1251 FT /note="Ig-like C2-type 4" FT DOMAIN 1259..1349 FT /note="Ig-like C2-type 5" FT REGION 69..229 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 569..573 FT /note="Interaction with VASP" FT /evidence="ECO:0000269|PubMed:14983521" FT REGION 631..660 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 653..683 FT /note="Interaction with LASP1" FT REGION 683..713 FT /note="Interaction with SORBS2, SPIN90 and SRC" FT /evidence="ECO:0000250" FT REGION 687..727 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 758..854 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 782..842 FT /note="Interaction with EPS8" FT /evidence="ECO:0000269|PubMed:16868024" FT REGION 807..842 FT /note="Interaction with SORBS2, SPIN90, SRC and PFN1" FT /evidence="ECO:0000250" FT REGION 830..834 FT /note="Interaction with VASP" FT /evidence="ECO:0000269|PubMed:14983521" FT REGION 882..904 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 960..981 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1121..1150 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1162..1251 FT /note="Interaction with EZR" FT /evidence="ECO:0000250" FT REGION 1261..1351 FT /note="Interaction with EZR" FT /evidence="ECO:0000250" FT COMPBIAS 81..95 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 150..168 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 193..229 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 646..660 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 701..718 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 762..777 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 778..843 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 194 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 639 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 642 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 648 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8WX93" FT MOD_RES 700 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8WX93" FT MOD_RES 704 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8WX93" FT MOD_RES 744 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8WX93" FT MOD_RES 901 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17242355, FT ECO:0007744|PubMed:21183079" FT MOD_RES 1004 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 1009 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 1126 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8WX93" FT MOD_RES 1129 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8WX93" FT MOD_RES 1131 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8WX93" FT MOD_RES 1141 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 1143 FT /note="Phosphoserine; by PKB/AKT1" FT /evidence="ECO:0007744|PubMed:17242355" FT MOD_RES 1146 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17242355, FT ECO:0007744|PubMed:21183079" FT MOD_RES 1377 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8WX93" FT DISULFID 299..351 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT DISULFID 469..528 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT DISULFID 1181..1233 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT VAR_SEQ 1..738 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_027931" FT VAR_SEQ 1..728 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000305" FT /id="VSP_027932" FT VAR_SEQ 1..389 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000305" FT /id="VSP_027933" FT VAR_SEQ 663..887 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000305" FT /id="VSP_027934" FT VAR_SEQ 966..982 FT /note="Missing (in isoform 2, isoform 3, isoform 4 and FT isoform 6)" FT /evidence="ECO:0000303|PubMed:10931874, FT ECO:0000303|PubMed:15449545, ECO:0000303|PubMed:15489334" FT /id="VSP_027935" FT VAR_SEQ 1352..1408 FT /note="TQWHQQPQTTKPKKVRPSASRYAALSDQGLDIKAAFQPEASPSHLTLNSGLV FT ESEDL -> ISRH (in isoform 2)" FT /evidence="ECO:0000305" FT /id="VSP_027936" FT CONFLICT 1022 FT /note="N -> K (in Ref. 5; AK031696)" FT /evidence="ECO:0000305" FT CONFLICT 1053 FT /note="P -> T (in Ref. 5; AK031696)" FT /evidence="ECO:0000305" FT STRAND 1035..1038 FT /evidence="ECO:0007829|PDB:2LQR" FT STRAND 1043..1048 FT /evidence="ECO:0007829|PDB:2LQR" FT STRAND 1058..1061 FT /evidence="ECO:0007829|PDB:2LQR" FT STRAND 1071..1077 FT /evidence="ECO:0007829|PDB:2LQR" FT STRAND 1081..1089 FT /evidence="ECO:0007829|PDB:2LQR" FT TURN 1092..1094 FT /evidence="ECO:0007829|PDB:2LQR" FT STRAND 1096..1101 FT /evidence="ECO:0007829|PDB:2LQR" FT STRAND 1114..1118 FT /evidence="ECO:0007829|PDB:2LQR" SQ SEQUENCE 1408 AA; 152131 MW; 5BCF647C110619C9 CRC64; MSETSSHDSF YDSLSDVQEE GKSADFFPGL SAFLSQEEIN KSLDLARRAI DSSETEDFDS EKEISQIFSK SPISLCETPS HEEPKSGKQT SSERPQDSRR APVQPLTGDQ AERITSPGSK RKPGVSPLLA SPSYIRSLRK AEKRGAKNPN PSSKPKTAQQ SKAGPQSQLC DKAASFIEEL TSIFREAAKP RNRSPNGESS SPDSGYLSPK NQPSALMSAS ASQSPTADQL DQLEMDAEVK QAQGSLCYQA HQASEETLPL AHIPHPQPQK ARHLPTAPRF IQKLRSQEVA EGSRVYLECR VTGNPTPRVR WFCEGKELYN SPDVQIHCES GELHTLVIAE AFEDDTGRYT CLATNPSGSD STSAEVFIEG ASSTDSDSES LSFISKAGAM PQAQKKTTSV SLTIGSSAPK TGVTTAVIQP LSVPVQQAHS ATSYLCRPDG TTMGCLLPVF TKELQNTAAS EGQVVVLECR VRGAPPLQVQ WFRQGSEIQD SPDFRILQKK PRSTAEPEEI CTLVIAESFP EDAGIFTCSA TNDYGSVTST AQLVITSANN ENCSYDSTGE PNSDHFQHFP PPPPILETGS YELASQKPSE IQQVNSPNLG FSMAALQMQF NTAERETNGV HPSHGVNGLI NGKAYGNKSP PTPTALLSPT KEPPPLLAKP KLDPLKLQQL QNQVRLEQEA CAWPPAPPGV PCNSSSSGSS APPSPPFPPP PPAFPELAAC ASPVPSEPMS ALASRATAMQ SSGSFNYARP KQFIAAQNLG PASGLPTPTS SPSSSSLPSP LSPTPRPFGR APGPPFVEPE AMWGPSSPSP PPPPPPVFSP SAAYPVPDVF PLPPPPPPLP SSTSHCASPA RFGPSQTPAA FLSALLPSQP PPVAVNALGL PKGVTPAGFP KKSSRTARIA SDEEIQGTKD AVIQDLERKL RFKEDLLNNG QPRLTYEERM ARRLLGADSA NVFNIQEPEE TAANQDAGAP RASVGGPLDG QKEYKVSSCE QRLISEIEYR LERSPVDESG DEVQDPDVPV ENATAPFFEM KLKHYKIFEG MPVTFTCRVA GNPKPKIYWF KDGKQISPKS DHYTIQRDLD GTCSLHTTAS TLDDDGNYTI MAANPQGRVS CTGRLMVQAV NQRGRSPRSP SGHPHARRPR SRSRDSGDEN EPIQERFFRP HFLQAPGDLT VQEGKLCRMD CKVSGLPTPD LSWQLDGKPI RPDSAHKMLV RENGVHSLII EPVTSRDAGI YTCIATNRAG QNSFNLELVV AAKEAHKAPV FMEKLQNTGV ADGYPVRLEC RVSGVPPPQI FWKKENESLT HSTERVSMHQ DNHGYICLLI QGATKEDAGW YTVSAKNEAG IVSCTARLDV YTQWHQQPQT TKPKKVRPSA SRYAALSDQG LDIKAAFQPE ASPSHLTLNS GLVESEDL //