PALLD_HUMAN
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 03-AUG-2022, entry version 180.
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};
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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; 99.
DR IntAct; Q8WX93; 42.
DR MINT; Q8WX93; -.
DR GlyGen; Q8WX93; 1 site, 1 O-linked glycan (1 site).
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 PaxDb; Q8WX93; -.
DR PeptideAtlas; Q8WX93; -.
DR PRIDE; 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 Antibodypedia; 28415; 341 antibodies from 37 providers.
DR DNASU; 23022; -.
DR Ensembl; ENST00000261509.10; ENSP00000261509.6; ENSG00000129116.19. [Q8WX93-2]
DR Ensembl; ENST00000505667.6; ENSP00000425556.1; ENSG00000129116.19. [Q8WX93-9]
DR Ensembl; ENST00000507735.6; ENSP00000424016.1; ENSG00000129116.19. [Q8WX93-4]
DR Ensembl; ENST00000512127.5; ENSP00000426947.1; ENSG00000129116.19. [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 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; RIYLECR; -.
DR OrthoDB; 100208at2759; -.
DR PhylomeDB; Q8WX93; -.
DR TreeFam; TF343193; -.
DR PathwayCommons; Q8WX93; -.
DR SignaLink; Q8WX93; -.
DR SIGNOR; Q8WX93; -.
DR BioGRID-ORCS; 23022; 9 hits in 1072 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 211 other tissues.
DR ExpressionAtlas; Q8WX93; baseline and differential.
DR Genevisible; Q8WX93; HS.
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; 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..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
