PALLD_MOUSE
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 03-AUG-2022, entry version 166.
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; 5.
DR IntAct; Q9ET54; 2.
DR STRING; 10090.ENSMUSP00000112442; -.
DR iPTMnet; Q9ET54; -.
DR PhosphoSitePlus; Q9ET54; -.
DR jPOST; Q9ET54; -.
DR MaxQB; Q9ET54; -.
DR PaxDb; Q9ET54; -.
DR PeptideAtlas; Q9ET54; -.
DR PRIDE; 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 Antibodypedia; 28415; 341 antibodies from 37 providers.
DR DNASU; 72333; -.
DR Ensembl; ENSMUST00000034057; ENSMUSP00000034057; ENSMUSG00000058056. [Q9ET54-2]
DR Ensembl; ENSMUST00000121200; ENSMUSP00000112374; ENSMUSG00000058056. [Q9ET54-3]
DR Ensembl; ENSMUST00000121493; ENSMUSP00000113874; ENSMUSG00000058056. [Q9ET54-4]
DR Ensembl; ENSMUST00000121785; ENSMUSP00000112442; ENSMUSG00000058056. [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 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; HNTDRIM; -.
DR OrthoDB; 100208at2759; -.
DR PhylomeDB; Q9ET54; -.
DR TreeFam; TF343193; -.
DR BioGRID-ORCS; 72333; 5 hits in 71 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 246 other tissues.
DR ExpressionAtlas; Q9ET54; baseline and differential.
DR Genevisible; Q9ET54; MM.
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; IBA:GO_Central.
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:0005925; C:focal adhesion; IDA:UniProtKB.
DR GO; GO:0030426; C:growth cone; IEA:UniProtKB-SubCell.
DR GO; GO:0030027; C:lamellipodium; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISS:HGNC-UCL.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0002102; C:podosome; IEA:UniProtKB-SubCell.
DR GO; GO:0001726; C:ruffle; IEA:UniProtKB-SubCell.
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: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; Ig_Palladin_C; 1.
DR Gene3D; 2.60.40.10; -; 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 Pfam; PF07679; I-set; 5.
DR SMART; SM00409; IG; 5.
DR SMART; SM00408; IGc2; 5.
DR SUPFAM; SSF48726; SSF48726; 5.
DR PROSITE; PS50835; IG_LIKE; 5.
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
