ID PALLD_HUMAN Reviewed; 1383 AA. AC Q8WX93; B3KTG2; B5MD56; B7ZMM5; Q7L3E0; Q7Z3W0; Q86WE8; Q8N1M2; Q9UGA0; AC Q9UQF5; Q9Y2J6; Q9Y3E9; DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot. DT 30-NOV-2010, sequence version 3. DT 27-MAR-2024, entry version 189. DE RecName: Full=Palladin; DE AltName: Full=SIH002; DE AltName: Full=Sarcoma antigen NY-SAR-77; GN Name=PALLD; Synonyms=KIAA0992; ORFNames=CGI-151; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 7). RA Liu T., Zhang J., Ye M., Zhang Q., Fu G., Zhou J., Wu J., Shen Y., Yu M., RA Chen S., Mao M., Chen Z.; RT "Human SIH002 gene."; RL Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RA Lockwood S.K.; RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4). RC TISSUE=Brain; RX PubMed=10231032; DOI=10.1093/dnares/6.1.63; RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., RA Tanaka A., Kotani H., Nomura N., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XIII. The RT complete sequences of 100 new cDNA clones from brain which code for large RT proteins in vitro."; RL DNA Res. 6:63-70(1999). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7). RX PubMed=10810093; DOI=10.1101/gr.10.5.703; RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.; RT "Identification of novel human genes evolutionarily conserved in RT Caenorhabditis elegans by comparative proteomics."; RL Genome Res. 10:703-713(2000). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 8), NUCLEOTIDE SEQUENCE RP [LARGE SCALE MRNA] OF 22-1383 (ISOFORM 6), AND VARIANT THR-224. RC TISSUE=Tongue; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 4."; RL Nature 434:724-731(2005). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 9), AND NUCLEOTIDE SEQUENCE RP [LARGE SCALE MRNA] OF 874-1383 (ISOFORM 1). RC TISSUE=Placenta; 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 NUCLEOTIDE SEQUENCE [MRNA] OF 874-1160 (ISOFORM 1). RX PubMed=12601173; DOI=10.1073/pnas.0437972100; RA Lee S.-Y., Obata Y., Yoshida M., Stockert E., Williamson B., RA Jungbluth A.A., Chen Y.-T., Old L.J., Scanlan M.J.; RT "Immunomic analysis of human sarcoma."; RL Proc. Natl. Acad. Sci. U.S.A. 100:2651-2656(2003). RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1188-1383 (ISOFORM 2). RC TISSUE=Heart; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [10] RP FUNCTION, INTERACTION WITH EZR, SUBCELLULAR LOCATION, AND TISSUE RP SPECIFICITY. RX PubMed=11598191; DOI=10.1091/mbc.12.10.3060; RA Mykkaenen O.-M., Groenholm M., Roenty M., Lalowski M., Salmikangas P., RA Suila H., Carpen O.; RT "Characterization of human palladin, a microfilament-associated protein."; RL Mol. Biol. Cell 12:3060-3073(2001). RN [11] RP FUNCTION, AND INTERACTION WITH ACTN. RX PubMed=15147863; DOI=10.1016/j.febslet.2004.04.006; RA Roenty M., Taivainen A., Moza M., Otey C.A., Carpen O.; RT "Molecular analysis of the interaction between palladin and alpha- RT actinin."; RL FEBS Lett. 566:30-34(2004). RN [12] RP INTERACTION WITH SORBS2, AND SUBCELLULAR LOCATION. RX PubMed=16125169; DOI=10.1016/j.yexcr.2005.06.026; RA Roenty M., Taivainen A., Moza M., Kruh G.D., Ehler E., Carpen O.; RT "Involvement of palladin and alpha-actinin in targeting of the Abl/Arg RT kinase adaptor ArgBP2 to the actin cytoskeleton."; RL Exp. Cell Res. 310:88-98(2005). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-893 AND SER-1121, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [14] RP INTERACTION WITH PFN1. RX PubMed=16367745; DOI=10.1111/j.1742-4658.2005.05036.x; RA Boukhelifa M., Moza M., Johansson T., Rachlin A., Parast M., RA Huttelmaier S., Roy P., Jockusch B.M., Carpen O., Karlsson R., Otey C.A.; RT "The proline-rich protein palladin is a binding partner for profilin."; RL FEBS J. 273:26-33(2006). RN [15] RP CHARACTERIZATION (ISOFORMS 3 AND 4), AND INDUCTION. RX PubMed=16794588; DOI=10.1038/sj.jid.5700427; RA Roenty M.J., Leivonen S.-K., Hinz B., Rachlin A., Otey C.A., RA Kaehaeri V.-M., Carpen O.M.; RT "Isoform-specific regulation of the actin-organizing protein Palladin RT during TGF-beta1-induced myofibroblast differentiation."; RL J. Invest. Dermatol. 126:2387-2396(2006). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-401 AND SER-893, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=16964243; DOI=10.1038/nbt1240; RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; RT "A probability-based approach for high-throughput protein phosphorylation RT analysis and site localization."; RL Nat. Biotechnol. 24:1285-1292(2006). RN [17] RP INTERACTION WITH LPP, AND SUBCELLULAR LOCATION. RX PubMed=17322171; DOI=10.1161/01.res.0000261351.54147.de; RA Jin L., Kern M.J., Otey C.A., Wamhoff B.R., Somlyo A.V.; RT "Angiotensin II, focal adhesion kinase, and PRX1 enhance smooth muscle RT expression of lipoma preferred partner and its newly identified binding RT partner palladin to promote cell migration."; RL Circ. Res. 100:817-825(2007). RN [18] RP FUNCTION, INTERACTION WITH SPIN90 AND SRC, SUBCELLULAR LOCATION, AND RP PHOSPHORYLATION. RX PubMed=17537434; DOI=10.1016/j.yexcr.2007.04.030; RA Ronty M., Taivainen A., Heiska L., Otey C., Ehler E., Song W.K., Carpen O.; RT "Palladin interacts with SH3 domains of SPIN90 and Src and is required for RT Src-induced cytoskeletal remodeling."; RL Exp. Cell Res. 313:2575-2585(2007). RN [19] RP INVOLVEMENT IN PNCA1. RX PubMed=17194196; DOI=10.1371/journal.pmed.0030516; RA Pogue-Geile K.L., Chen R., Bronner M.P., Crnogorac-Jurcevic T., Moyes K.W., RA Dowen S., Otey C.A., Crispin D.A., George R.D., Whitcomb D.C., RA Brentnall T.A.; RT "Palladin mutation causes familial pancreatic cancer and suggests a new RT cancer mechanism."; RL PLoS Med. 3:2216-2228(2006). RN [20] RP POSSIBLE INVOLVEMENT IN MYOCARDIAL INFARCTION. RX PubMed=16175505; DOI=10.1086/491674; RA Shiffman D., Ellis S.G., Rowland C.M., Malloy M.J., Luke M.M., RA Iakoubova O.A., Pullinger C.R., Cassano J., Aouizerat B.E., Fenwick R.G., RA Reitz R.E., Catanese J.J., Leong D.U., Zellner C., Sninsky J.J., RA Topol E.J., Devlin J.J., Kane J.P.; RT "Identification of four gene variants associated with myocardial RT infarction."; RL Am. J. Hum. Genet. 77:596-605(2005). RN [21] RP INVOLVEMENT IN PNCA1. RX PubMed=17415588; DOI=10.1007/s00439-007-0361-z; RA Zogopoulous G., Rothenmund H., Eppel A., Ash C., Akbari M.R., Hedley D., RA Narod S.A., Gallinger S.; RT "The P239S palladin variant does not account for a significant fraction of RT hereditary or early onset pancreas cancer."; RL Hum. Genet. 121:635-637(2007). RN [22] RP QUESTIONING OF INVOLVEMENT IN PNCA1. RX PubMed=17455999; DOI=10.1371/journal.pmed.0040164; RA Slater E., Amrillaeva V., Fendrich V., Bartsch D., Earl J., Vitone L.J., RA Neoptolemos J.P., Greenhalf W.; RT "Palladin mutation causes familial pancreatic cancer: absence in European RT families."; RL PLoS Med. 4:774-775(2007). RN [23] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-401; SER-893; SER-979 AND RP SER-984, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [24] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-893, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [25] RP PHOSPHORYLATION AT SER-1118. RX PubMed=20471940; DOI=10.1016/j.molcel.2010.02.031; RA Chin Y.R., Toker A.; RT "The actin-bundling protein palladin is an Akt1-specific substrate that RT regulates breast cancer cell migration."; RL Mol. Cell 38:333-344(2010). RN [26] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-401; SER-684; SER-688; RP SER-893; SER-979; SER-984; SER-1101; SER-1104; SER-1106; SER-1116; SER-1118 RP AND SER-1121, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [27] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [28] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-893; SER-1104; SER-1116; RP SER-1118 AND SER-1121, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [29] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641; SER-728; SER-893; RP SER-1116; SER-1118; SER-1121 AND SER-1352, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [30] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-893 AND SER-1104, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [31] RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1233-1324. RX PubMed=16754980; DOI=10.1107/s1744309106016411; RA Liang W., Yang H., Xue X., Huang Q., Bartlam M., Chen S.; RT "Expression, crystallization and preliminary X-ray studies of the RT immunoglobulin-like domain 3 of human palladin."; RL Acta Crystallogr. F 62:556-558(2006). RN [32] RP STRUCTURE BY NMR OF 1000-1230. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of the first and second Ig domains of human palladin."; RL Submitted (APR-2007) to the PDB data bank. 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 foci. {ECO:0000269|PubMed:11598191, CC ECO:0000269|PubMed:15147863, ECO:0000269|PubMed:17537434}. CC -!- SUBUNIT: Interacts with EPS8 (By similarity). Interacts with LASP1 (By CC similarity). Interacts with VASP (By similarity). Interacts with ACTN CC (PubMed:15147863). Interacts with SORBS2 (PubMed:16125169). Interacts CC with PFN1 (PubMed:16367745). Interacts with LPP (PubMed:17322171). CC Interacts with SPIN90 (PubMed:17537434). Interacts with SRC CC (PubMed:17537434). Interacts with EZR (PubMed:11598191). Interacts with CC RAI14 (By similarity). {ECO:0000250|UniProtKB:P0C5E3, CC ECO:0000250|UniProtKB:Q9ET54, ECO:0000269|PubMed:11598191, CC ECO:0000269|PubMed:15147863, ECO:0000269|PubMed:16125169, CC ECO:0000269|PubMed:16367745, ECO:0000269|PubMed:17322171, CC ECO:0000269|PubMed:17537434}. CC -!- INTERACTION: CC Q8WX93; O94875: SORBS2; NbExp=2; IntAct=EBI-2803991, EBI-311323; CC Q8WX93-2; Q9NSB8-2: HOMER2; NbExp=3; IntAct=EBI-12218525, EBI-12017090; CC Q8WX93-2; Q9NSC5: HOMER3; NbExp=3; IntAct=EBI-12218525, EBI-748420; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton CC {ECO:0000269|PubMed:11598191, ECO:0000269|PubMed:17322171, CC ECO:0000269|PubMed:17537434}. Cell junction, focal adhesion CC {ECO:0000269|PubMed:17322171}. Cytoplasm, myofibril, sarcomere, Z line CC {ECO:0000269|PubMed:16125169}. Cell projection, ruffle CC {ECO:0000269|PubMed:17537434}. Cell projection, podosome CC {ECO:0000250|UniProtKB:P0C5E3}. Cell projection, lamellipodium CC {ECO:0000269|PubMed:17537434}. 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:11598191, PubMed:16125169, PubMed:17322171, CC PubMed:17537434). Preferentially expressed in the excitatory CC presynaptic terminals (By similarity). {ECO:0000250|UniProtKB:P0C5E3, CC ECO:0000269|PubMed:11598191, ECO:0000269|PubMed:16125169, CC ECO:0000269|PubMed:17322171, ECO:0000269|PubMed:17537434}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=9; CC Name=1; Synonyms=200-kDa; CC IsoId=Q8WX93-1; Sequence=Displayed; CC Name=2; CC IsoId=Q8WX93-2; Sequence=VSP_027929, VSP_027930; CC Name=3; Synonyms=140-kDa; CC IsoId=Q8WX93-3; Sequence=VSP_027927; CC Name=4; Synonyms=90-kDa; CC IsoId=Q8WX93-4; Sequence=VSP_027926; CC Name=5; CC IsoId=Q8WX93-5; Sequence=VSP_027929; CC Name=6; CC IsoId=Q8WX93-6; Sequence=VSP_027928; CC Name=7; CC IsoId=Q8WX93-7; Sequence=VSP_027925; CC Name=8; CC IsoId=Q8WX93-8; Sequence=VSP_027927, VSP_027929; CC Name=9; CC IsoId=Q8WX93-9; Sequence=VSP_027929, VSP_043794, VSP_043795; CC -!- TISSUE SPECIFICITY: Detected in both muscle and non-muscle tissues. CC High expression in prostate, ovary, colon, and kidney. Not detected in CC spleen, skeletal muscle, lung and peripheral blood lymphocytes (at CC protein level). Protein is overexpressed in FA6, HPAF, IMIM-PC2, SUIT-2 CC and PancTu-II sporadic pancreatic cancer cell lines. CC {ECO:0000269|PubMed:11598191}. CC -!- INDUCTION: Isoform 3 is expressed de novo. Isoform 4 is up-regulated by CC TGFB1 during myofibroblast differentiation. CC {ECO:0000269|PubMed:16794588}. CC -!- PTM: Phosphorylated predominantly on serines and, to a lesser extent, CC on tyrosines (By similarity). Phosphorylation at Ser-1118 by PKB/AKT1 CC modulates cytoskeletal organization and cell motility. {ECO:0000250, CC ECO:0000269|PubMed:17537434, ECO:0000269|PubMed:20471940}. CC -!- DISEASE: Pancreatic cancer 1 (PNCA1) [MIM:606856]: A malignant neoplasm CC of the pancreas. Tumors can arise from both the exocrine and endocrine CC portions of the pancreas, but 95% of them develop from the exocrine CC portion, including the ductal epithelium, acinar cells, connective CC tissue, and lymphatic tissue. {ECO:0000269|PubMed:17194196, CC ECO:0000269|PubMed:17415588, ECO:0000269|PubMed:17455999}. Note=Disease CC susceptibility is associated with variants affecting the gene CC represented in this entry. CC -!- DISEASE: Note=Genetic variations in PALLD may be associated with CC susceptibility to myocardial infarction. {ECO:0000269|PubMed:16175505}. CC -!- SIMILARITY: Belongs to the myotilin/palladin family. {ECO:0000305}. CC -!- CAUTION: Was wrongly assigned as myoneurin (Ref.2). {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAD34146.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAO65174.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=BAA76836.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAC04796.1; Type=Erroneous initiation; Note=Truncated N-terminus.; 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; AF077041; AAD27774.1; -; mRNA. DR EMBL; AF464873; AAL69964.1; -; mRNA. DR EMBL; AB023209; BAA76836.1; ALT_INIT; mRNA. DR EMBL; AF151909; AAD34146.1; ALT_INIT; mRNA. DR EMBL; AK095512; BAG53074.1; -; mRNA. DR EMBL; AK096458; BAC04796.1; ALT_INIT; mRNA. DR EMBL; AC079858; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC079926; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC080188; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC084353; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC115538; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC013867; AAH13867.2; -; mRNA. DR EMBL; BC144666; AAI44667.1; -; mRNA. DR EMBL; AY211921; AAO65174.1; ALT_FRAME; mRNA. DR EMBL; BX537391; CAD97633.1; -; mRNA. DR CCDS; CCDS34098.1; -. [Q8WX93-2] DR CCDS; CCDS54818.1; -. [Q8WX93-9] DR CCDS; CCDS54819.1; -. [Q8WX93-8] DR CCDS; CCDS54820.1; -. [Q8WX93-4] DR PIR; T13078; T13078. DR RefSeq; NP_001159580.1; NM_001166108.1. [Q8WX93-9] DR RefSeq; NP_001159581.1; NM_001166109.1. [Q8WX93-8] DR RefSeq; NP_001159582.1; NM_001166110.1. [Q8WX93-4] DR RefSeq; NP_057165.3; NM_016081.3. [Q8WX93-2] DR PDB; 2DM2; NMR; -; A=1000-1096. DR PDB; 2DM3; NMR; -; A=1133-1229. DR PDBsum; 2DM2; -. DR PDBsum; 2DM3; -. DR AlphaFoldDB; Q8WX93; -. DR SMR; Q8WX93; -. DR BioGRID; 116662; 118. DR IntAct; Q8WX93; 45. DR MINT; Q8WX93; -. DR STRING; 9606.ENSP00000425556; -. DR GlyCosmos; Q8WX93; 1 site, 1 glycan. DR GlyGen; Q8WX93; 9 sites, 1 O-linked glycan (9 sites). DR iPTMnet; Q8WX93; -. DR MetOSite; Q8WX93; -. DR PhosphoSitePlus; Q8WX93; -. DR SwissPalm; Q8WX93; -. DR BioMuta; PALLD; -. DR DMDM; 313104206; -. DR CPTAC; CPTAC-987; -. DR EPD; Q8WX93; -. DR jPOST; Q8WX93; -. DR MassIVE; Q8WX93; -. DR MaxQB; Q8WX93; -. DR PeptideAtlas; Q8WX93; -. DR ProteomicsDB; 74979; -. [Q8WX93-1] DR ProteomicsDB; 74980; -. [Q8WX93-2] DR ProteomicsDB; 74981; -. [Q8WX93-3] DR ProteomicsDB; 74982; -. [Q8WX93-4] DR ProteomicsDB; 74983; -. [Q8WX93-5] DR ProteomicsDB; 74984; -. [Q8WX93-6] DR ProteomicsDB; 74985; -. [Q8WX93-7] DR ProteomicsDB; 74986; -. [Q8WX93-8] DR ProteomicsDB; 74987; -. [Q8WX93-9] DR Pumba; Q8WX93; -. DR Antibodypedia; 28415; 374 antibodies from 37 providers. DR DNASU; 23022; -. DR Ensembl; ENST00000261509.10; ENSP00000261509.6; ENSG00000129116.20. [Q8WX93-2] DR Ensembl; ENST00000505667.6; ENSP00000425556.1; ENSG00000129116.20. [Q8WX93-9] DR Ensembl; ENST00000507735.6; ENSP00000424016.1; ENSG00000129116.20. [Q8WX93-4] DR Ensembl; ENST00000512127.5; ENSP00000426947.1; ENSG00000129116.20. [Q8WX93-8] DR GeneID; 23022; -. DR KEGG; hsa:23022; -. DR MANE-Select; ENST00000505667.6; ENSP00000425556.1; NM_001166108.2; NP_001159580.1. [Q8WX93-9] DR UCSC; uc003iru.3; human. [Q8WX93-1] DR AGR; HGNC:17068; -. DR CTD; 23022; -. DR DisGeNET; 23022; -. DR GeneCards; PALLD; -. DR HGNC; HGNC:17068; PALLD. DR HPA; ENSG00000129116; Low tissue specificity. DR MalaCards; PALLD; -. DR MIM; 606856; phenotype. DR MIM; 608092; gene. DR neXtProt; NX_Q8WX93; -. DR OpenTargets; ENSG00000129116; -. DR Orphanet; 1333; Familial pancreatic carcinoma. DR PharmGKB; PA142671205; -. DR VEuPathDB; HostDB:ENSG00000129116; -. DR eggNOG; ENOG502QSRV; Eukaryota. DR GeneTree; ENSGT00940000153441; -. DR HOGENOM; CLU_006487_1_0_1; -. DR InParanoid; Q8WX93; -. DR OMA; IYLECRV; -. DR OrthoDB; 5356884at2759; -. DR PhylomeDB; Q8WX93; -. DR TreeFam; TF343193; -. DR PathwayCommons; Q8WX93; -. DR SignaLink; Q8WX93; -. DR SIGNOR; Q8WX93; -. DR BioGRID-ORCS; 23022; 9 hits in 1150 CRISPR screens. DR ChiTaRS; PALLD; human. DR EvolutionaryTrace; Q8WX93; -. DR GeneWiki; Palladin; -. DR GenomeRNAi; 23022; -. DR Pharos; Q8WX93; Tbio. DR PRO; PR:Q8WX93; -. DR Proteomes; UP000005640; Chromosome 4. DR RNAct; Q8WX93; Protein. DR Bgee; ENSG00000129116; Expressed in saphenous vein and 213 other cell types or tissues. DR ExpressionAtlas; Q8WX93; baseline and differential. DR GO; GO:0015629; C:actin cytoskeleton; IDA:HPA. DR GO; GO:0005884; C:actin filament; IDA:HGNC-UCL. DR GO; GO:0030424; C:axon; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; IDA:HPA. 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; IDA:UniProtKB. DR GO; GO:0005739; C:mitochondrion; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:HGNC-UCL. DR GO; GO:0005886; C:plasma membrane; IDA:HPA. 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:0098632; F:cell-cell adhesion mediator activity; IBA:GO_Central. DR GO; GO:0051371; F:muscle alpha-actinin binding; TAS:HGNC-UCL. DR GO; GO:0030036; P:actin cytoskeleton organization; IEA:Ensembl. DR GO; GO:0007411; P:axon guidance; IBA:GO_Central. DR GO; GO:0016477; P:cell migration; IEA:InterPro. DR GO; GO:0007010; P:cytoskeleton organization; NAS:HGNC-UCL. DR GO; GO:0070593; P:dendrite self-avoidance; IBA:GO_Central. DR GO; GO:0003382; P:epithelial cell morphogenesis; IEA:Ensembl. DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IBA:GO_Central. DR GO; GO:0003334; P:keratinocyte development; IEA:Ensembl. 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; Q8WX93; HS. 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..1383 FT /note="Palladin" FT /id="PRO_0000302720" FT DOMAIN 271..360 FT /note="Ig-like C2-type 1" FT DOMAIN 440..539 FT /note="Ig-like C2-type 2" FT DOMAIN 1001..1085 FT /note="Ig-like C2-type 3" FT DOMAIN 1135..1226 FT /note="Ig-like C2-type 4" FT DOMAIN 1233..1324 FT /note="Ig-like C2-type 5" FT REGION 1..22 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 52..169 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 183..238 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 562..566 FT /note="Interaction with VASP" FT /evidence="ECO:0000250" FT REGION 609..653 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 646..676 FT /note="Interaction with LASP1" FT /evidence="ECO:0000250" FT REGION 673..728 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 676..696 FT /note="Interaction with SORBS2, SPIN90 and SRC" FT /evidence="ECO:0000269|PubMed:16125169" FT REGION 740..846 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 766..831 FT /note="Interaction with EPS8" FT /evidence="ECO:0000250" FT REGION 796..831 FT /note="Interaction with SORBS2, SPIN90, SRC and PFN1" FT /evidence="ECO:0000269|PubMed:16125169, FT ECO:0000269|PubMed:16367745" FT REGION 819..823 FT /note="Interaction with VASP" FT /evidence="ECO:0000250" FT REGION 833..890 FT /note="Interaction with ACTN" FT /evidence="ECO:0000269|PubMed:15147863" FT REGION 1096..1125 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1137..1226 FT /note="Interaction with EZR" FT /evidence="ECO:0000269|PubMed:11598191" FT REGION 1236..1326 FT /note="Interaction with EZR" FT /evidence="ECO:0000269|PubMed:11598191" FT COMPBIAS 78..95 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 96..119 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 149..163 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 191..225 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 622..637 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 679..705 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 747..767 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 769..785 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 793..833 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 192 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9ET54" FT MOD_RES 401 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:16964243, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231" FT MOD_RES 632 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9ET54" FT MOD_RES 635 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q9ET54" FT MOD_RES 641 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 684 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 688 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 728 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 893 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:16964243, FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 979 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231" FT MOD_RES 984 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231" FT MOD_RES 1101 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 1104 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569" FT MOD_RES 1106 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 1116 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 1118 FT /note="Phosphoserine; by PKB/AKT1" FT /evidence="ECO:0000269|PubMed:20471940, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 1121 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 1352 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT DISULFID 292..344 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT DISULFID 462..521 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT DISULFID 1156..1208 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT VAR_SEQ 1..998 FT /note="Missing (in isoform 7)" FT /evidence="ECO:0000303|PubMed:10810093, ECO:0000303|Ref.1" FT /id="VSP_027925" FT VAR_SEQ 1..711 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:10231032" FT /id="VSP_027926" FT VAR_SEQ 1..382 FT /note="Missing (in isoform 3 and isoform 8)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_027927" FT VAR_SEQ 500..1383 FT /note="PEEICTLVIAETFPEDAGIFTCSARNDYGSATSTAQLVVTSANTENCSYESM FT GESNNDHFQHFPPPPPILETSSLELASKKPSEIQQVNNPELGLSRAALQMQFNAAERET FT NGVHPSRGVNGLINGKANSNKSLPTPAVLLSPTKEPPPLLAKPKLDPLKLQQLQNQIRL FT EQEAGARQPPPAPRSAPPSPPFPPPPAFPELAACTPPASPEPMSALASRSAPAMQSSGS FT FNYARPKQFIAAQNLGPASGHGTPASSPSSSSLPSPMSPTPRQFGRAPVPPFAQPFGAE FT PEAPWGSSSPSPPPPPPPVFSPTAAFPVPDVFPLPPPPPPLPSPGQASHCSSPATRFGH FT SQTPAAFLSALLPSQPPPAAVNALGLPKGVTPAGFPKKASRTARIASDEEIQGTKDAVI FT QDLERKLRFKEDLLNNGQPRLTYEERMARRLLGADSATVFNIQEPEEETANQEYKVSSC FT EQRLISEIEYRLERSPVDESGDEVQYGDVPVENGMAPFFEMKLKHYKIFEGMPVTFTCR FT VAGNPKPKIYWFKDGKQISPKSDHYTIQRDLDGTCSLHTTASTLDDDGNYTIMAANPQG FT RISCTGRLMVQAVNQRGRSPRSPSGHPHVRRPRSRSRDSGDENEPIQERFFRPHFLQAP FT GDLTVQEGKLCRMDCKVSGLPTPDLSWQLDGKPVRPDSAHKMLVRENGVHSLIIEPVTS FT RDAGIYTCIATNRAGQNSFSLELVVAAKEAHKPPVFIEKLQNTGVADGYPVRLECRVLG FT VPPPQIFWKKENESLTHSTDRVSMHQDNHGYICLLIQGATKEDAGWYTVSAKNEAGIVS FT CTARLDVYTQWHQQSQSTKPKKVRPSASRYAALSDQGLDIKAAFQPEANPSHLTLNTAL FT VESEDL -> PDVLYVFVRVRCHQMKIQYYNLAHLISSWLSSFL (in isoform FT 6)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_027928" FT VAR_SEQ 656..879 FT /note="Missing (in isoform 2, isoform 5, isoform 8 and FT isoform 9)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:17974005, FT ECO:0000303|Ref.2" FT /id="VSP_027929" FT VAR_SEQ 957 FT /note="Q -> QDIGSPHASVGSPLDGQK (in isoform 9)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_043794" FT VAR_SEQ 1326..1383 FT /note="YTQWHQQSQSTKPKKVRPSASRYAALSDQGLDIKAAFQPEANPSHLTLNTAL FT VESEDL -> YISRH (in isoform 2)" FT /evidence="ECO:0000303|PubMed:17974005, ECO:0000303|Ref.2" FT /id="VSP_027930" FT VAR_SEQ 1327..1383 FT /note="TQWHQQSQSTKPKKVRPSASRYAALSDQGLDIKAAFQPEANPSHLTLNTALV FT ESEDL -> ISRH (in isoform 9)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_043795" FT VARIANT 224 FT /note="M -> I (in dbSNP:rs7671781)" FT /id="VAR_034940" FT VARIANT 224 FT /note="M -> T (in dbSNP:rs7655494)" FT /evidence="ECO:0000269|PubMed:14702039" FT /id="VAR_059401" FT CONFLICT 277 FT /note="L -> P (in Ref. 5; BAC04796)" FT /evidence="ECO:0000305" FT CONFLICT 472 FT /note="V -> D (in Ref. 5; BAC04796)" FT /evidence="ECO:0000305" FT CONFLICT 611 FT /note="N -> S (in Ref. 2; AAL69964)" FT /evidence="ECO:0000305" FT CONFLICT 847 FT /note="S -> G (in Ref. 3; BAA76836)" FT /evidence="ECO:0000305" FT CONFLICT 1126 FT /note="E -> D (in Ref. 8; AAO65174)" FT /evidence="ECO:0000305" FT CONFLICT 1146 FT /note="V -> G (in Ref. 8; AAO65174)" FT /evidence="ECO:0000305" FT STRAND 1003..1005 FT /evidence="ECO:0007829|PDB:2DM2" FT STRAND 1010..1013 FT /evidence="ECO:0007829|PDB:2DM2" FT STRAND 1018..1024 FT /evidence="ECO:0007829|PDB:2DM2" FT STRAND 1031..1035 FT /evidence="ECO:0007829|PDB:2DM2" FT STRAND 1046..1052 FT /evidence="ECO:0007829|PDB:2DM2" FT STRAND 1057..1064 FT /evidence="ECO:0007829|PDB:2DM2" FT TURN 1067..1069 FT /evidence="ECO:0007829|PDB:2DM2" FT STRAND 1074..1078 FT /evidence="ECO:0007829|PDB:2DM2" FT STRAND 1084..1086 FT /evidence="ECO:0007829|PDB:2DM2" FT STRAND 1090..1093 FT /evidence="ECO:0007829|PDB:2DM2" FT STRAND 1136..1139 FT /evidence="ECO:0007829|PDB:2DM3" FT STRAND 1143..1150 FT /evidence="ECO:0007829|PDB:2DM3" FT STRAND 1155..1159 FT /evidence="ECO:0007829|PDB:2DM3" FT STRAND 1165..1167 FT /evidence="ECO:0007829|PDB:2DM3" FT STRAND 1169..1174 FT /evidence="ECO:0007829|PDB:2DM3" FT STRAND 1179..1185 FT /evidence="ECO:0007829|PDB:2DM3" FT STRAND 1191..1197 FT /evidence="ECO:0007829|PDB:2DM3" FT HELIX 1200..1202 FT /evidence="ECO:0007829|PDB:2DM3" FT STRAND 1204..1206 FT /evidence="ECO:0007829|PDB:2DM3" FT STRAND 1208..1211 FT /evidence="ECO:0007829|PDB:2DM3" FT STRAND 1216..1219 FT /evidence="ECO:0007829|PDB:2DM3" FT STRAND 1222..1226 FT /evidence="ECO:0007829|PDB:2DM3" SQ SEQUENCE 1383 AA; 150564 MW; 2CABAE1A6FEE855F CRC64; MSGTSSHESF YDSLSDMQEE SKNTDFFPGL SAFLSQEEIN KSLDLARRAI ADSETEDFDS EKEISQIFST SPASLCEHPS HKETKLGEHA SRRPQDNRST PVQPLAEKQT KSISSPVSKR KPAMSPLLTR PSYIRSLRKA EKRGAKTPST NVKPKTPHQR KGGPQSQLCD KAANLIEELT SIFKAAKPRN RSPNGESSSP DSGYLSPKNQ PSALLSASAS QSPMEDQGEM EREVKSPGAR HCYQDNQDLA VPHNRKSHPQ PHSALHFPAA PRFIQKLRSQ EVAEGSRVYL ECRVTGNPTP RVRWFCEGKE LHNTPDIQIH CEGGDLHTLI IAEAFEDDTG RYTCLATNPS GSDTTSAEVF IEGASSTDSD SESLAFKSRA GAMPQAQKKT TSVSLTIGSS SPKTGVTTAV IQPLSVPVQQ VHSPTSYLCR PDGTTTAYFP PVFTKELQNT AVAEGQVVVL ECRVRGAPPL QVQWFRQGSE IQDSPDFRIL QKKPRSTAEP EEICTLVIAE TFPEDAGIFT CSARNDYGSA TSTAQLVVTS ANTENCSYES MGESNNDHFQ HFPPPPPILE TSSLELASKK PSEIQQVNNP ELGLSRAALQ MQFNAAERET NGVHPSRGVN GLINGKANSN KSLPTPAVLL SPTKEPPPLL AKPKLDPLKL QQLQNQIRLE QEAGARQPPP APRSAPPSPP FPPPPAFPEL AACTPPASPE PMSALASRSA PAMQSSGSFN YARPKQFIAA QNLGPASGHG TPASSPSSSS LPSPMSPTPR QFGRAPVPPF AQPFGAEPEA PWGSSSPSPP PPPPPVFSPT AAFPVPDVFP LPPPPPPLPS PGQASHCSSP ATRFGHSQTP AAFLSALLPS QPPPAAVNAL GLPKGVTPAG FPKKASRTAR IASDEEIQGT KDAVIQDLER KLRFKEDLLN NGQPRLTYEE RMARRLLGAD SATVFNIQEP EEETANQEYK VSSCEQRLIS EIEYRLERSP VDESGDEVQY GDVPVENGMA PFFEMKLKHY KIFEGMPVTF TCRVAGNPKP KIYWFKDGKQ ISPKSDHYTI QRDLDGTCSL HTTASTLDDD GNYTIMAANP QGRISCTGRL MVQAVNQRGR SPRSPSGHPH VRRPRSRSRD SGDENEPIQE RFFRPHFLQA PGDLTVQEGK LCRMDCKVSG LPTPDLSWQL DGKPVRPDSA HKMLVRENGV HSLIIEPVTS RDAGIYTCIA TNRAGQNSFS LELVVAAKEA HKPPVFIEKL QNTGVADGYP VRLECRVLGV PPPQIFWKKE NESLTHSTDR VSMHQDNHGY ICLLIQGATK EDAGWYTVSA KNEAGIVSCT ARLDVYTQWH QQSQSTKPKK VRPSASRYAA LSDQGLDIKA AFQPEANPSH LTLNTALVES EDL //