MPP2_HUMAN
ID MPP2_HUMAN Reviewed; 576 AA.
AC Q14168; B4DGE9; B4DRJ0; B7Z3G8; E7EV80; E7EV91; E7EX01; Q53ES9; Q5CZB9;
AC Q9BQJ2;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 02-MAR-2010, sequence version 3.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=MAGUK p55 subfamily member 2;
DE AltName: Full=Discs large homolog 2;
DE AltName: Full=Protein MPP2;
GN Name=MPP2 {ECO:0000312|HGNC:HGNC:7220}; Synonyms=DLG2;
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 1).
RC TISSUE=Brain;
RX PubMed=7590743; DOI=10.1006/geno.1995.1101;
RA Mazoyer S., Gayther S.A., Nagai M.A., Smith S.A., Dunning A.,
RA van Rensburg E.J., Albertsen H., White R., Ponder B.A.J.;
RT "A gene (DLG2) located at 17q12-q21 encodes a new homologue of the
RT Drosophila tumor suppressor dlg-A.";
RL Genomics 28:25-31(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Amygdala;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4; 5 AND 6).
RC TISSUE=Amygdala, and Hippocampus;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Salivary gland;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [9]
RP FUNCTION, INTERACTION WITH SRC, SUBCELLULAR LOCATION, MUTAGENESIS OF
RP TYR-363, AND PHOSPHORYLATION.
RX PubMed=19665017; DOI=10.1016/j.yexcr.2009.07.028;
RA Baumgartner M., Weiss A., Fritzius T., Heinrich J., Moelling K.;
RT "The PDZ protein MPP2 interacts with c-Src in epithelial cells.";
RL Exp. Cell Res. 315:2888-2898(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-141, 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 [11]
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 [12]
RP STRUCTURE BY NMR OF 163-240.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the PDZ domain from human maguk p55 subfamily member
RT 2.";
RL Submitted (JAN-2008) to the PDB data bank.
CC -!- FUNCTION: Postsynaptic MAGUK scaffold protein that links CADM1 cell
CC adhesion molecules to core components of the postsynaptic density (By
CC similarity). In CA1 pyramidal neurons, required for synaptic KCNN2-
CC containing channel function and long-term potentiation expression (By
CC similarity). Seems to negatively regulate SRC function in epithelial
CC cells (PubMed:19665017). {ECO:0000250|UniProtKB:D3ZAA9,
CC ECO:0000250|UniProtKB:Q9WV34, ECO:0000269|PubMed:19665017}.
CC -!- SUBUNIT: Can homomultimerise. Interacts with CACNG2. Interacts (via the
CC SH3-Guanylate kinase-like sub-module) with DLG4/PSD95 and DLGAP1/GKAP.
CC Interacts (via the PDZ domain) with CADM1 (via C-terminus) (By
CC similarity). Interacts with KCNN2/SK2 (via N-terminal domain) (By
CC similarity). Interacts with SRC (PubMed:19665017).
CC {ECO:0000250|UniProtKB:D3ZAA9, ECO:0000250|UniProtKB:Q9WV34,
CC ECO:0000269|PubMed:19665017}.
CC -!- INTERACTION:
CC Q14168-2; O14910: LIN7A; NbExp=4; IntAct=EBI-10181752, EBI-2513988;
CC Q14168-4; O14910: LIN7A; NbExp=7; IntAct=EBI-14385193, EBI-2513988;
CC Q14168-4; Q9HAP6: LIN7B; NbExp=3; IntAct=EBI-14385193, EBI-821335;
CC Q14168-4; Q9NUP9: LIN7C; NbExp=7; IntAct=EBI-14385193, EBI-1171517;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:19665017}. Membrane {ECO:0000269|PubMed:19665017}.
CC Cell projection, dendrite {ECO:0000250|UniProtKB:Q9WV34}. Postsynaptic
CC density {ECO:0000250|UniProtKB:Q9WV34}. Note=Prominently expressed in
CC the postsynaptic densities of dendritic spines, is also detected in
CC dendritic shafts. {ECO:0000250|UniProtKB:Q9WV34}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1;
CC IsoId=Q14168-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q14168-2; Sequence=VSP_003156;
CC Name=3;
CC IsoId=Q14168-3; Sequence=VSP_022951, VSP_003156;
CC Name=4;
CC IsoId=Q14168-4; Sequence=VSP_055138, VSP_003156;
CC Name=5;
CC IsoId=Q14168-5; Sequence=VSP_055136;
CC Name=6;
CC IsoId=Q14168-6; Sequence=VSP_055137, VSP_003156;
CC -!- PTM: Phosphorylated by SRC. {ECO:0000269|PubMed:19665017}.
CC -!- SIMILARITY: Belongs to the MAGUK family. {ECO:0000305}.
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DR EMBL; X82895; CAA58067.1; -; mRNA.
DR EMBL; AL136554; CAB66489.1; -; mRNA.
DR EMBL; AK294564; BAG57760.1; -; mRNA.
DR EMBL; AK295858; BAH12204.1; -; mRNA.
DR EMBL; AK299286; BAG61302.1; -; mRNA.
DR EMBL; CR936598; CAI56746.1; -; mRNA.
DR EMBL; AK223560; BAD97280.1; -; mRNA.
DR EMBL; AC007993; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC030287; AAH30287.1; -; mRNA.
DR CCDS; CCDS11471.1; -. [Q14168-2]
DR CCDS; CCDS62206.1; -. [Q14168-5]
DR CCDS; CCDS62207.1; -. [Q14168-6]
DR CCDS; CCDS62208.1; -. [Q14168-3]
DR CCDS; CCDS62209.1; -. [Q14168-1]
DR CCDS; CCDS62210.1; -. [Q14168-4]
DR PIR; A57653; A57653.
DR RefSeq; NP_001265299.1; NM_001278370.1.
DR RefSeq; NP_001265300.1; NM_001278371.1.
DR RefSeq; NP_001265301.1; NM_001278372.1.
DR RefSeq; NP_001265302.1; NM_001278373.1.
DR RefSeq; NP_001265303.1; NM_001278374.1. [Q14168-5]
DR RefSeq; NP_001265304.1; NM_001278375.1.
DR RefSeq; NP_001265305.2; NM_001278376.2.
DR RefSeq; NP_001265310.1; NM_001278381.1.
DR RefSeq; NP_005365.4; NM_005374.4.
DR PDB; 2E7K; NMR; -; A=163-240.
DR PDBsum; 2E7K; -.
DR AlphaFoldDB; Q14168; -.
DR BMRB; Q14168; -.
DR SMR; Q14168; -.
DR BioGRID; 110495; 36.
DR IntAct; Q14168; 17.
DR MINT; Q14168; -.
DR STRING; 9606.ENSP00000428182; -.
DR iPTMnet; Q14168; -.
DR PhosphoSitePlus; Q14168; -.
DR SwissPalm; Q14168; -.
DR BioMuta; MPP2; -.
DR DMDM; 290457681; -.
DR EPD; Q14168; -.
DR jPOST; Q14168; -.
DR MassIVE; Q14168; -.
DR MaxQB; Q14168; -.
DR PaxDb; Q14168; -.
DR PeptideAtlas; Q14168; -.
DR PRIDE; Q14168; -.
DR ProteomicsDB; 18580; -.
DR ProteomicsDB; 18587; -.
DR ProteomicsDB; 18952; -.
DR ProteomicsDB; 59895; -. [Q14168-1]
DR ProteomicsDB; 59896; -. [Q14168-2]
DR ProteomicsDB; 59897; -. [Q14168-3]
DR TopDownProteomics; Q14168-2; -. [Q14168-2]
DR Antibodypedia; 17305; 222 antibodies from 26 providers.
DR DNASU; 4355; -.
DR Ensembl; ENST00000520305.5; ENSP00000428136.1; ENSG00000108852.16. [Q14168-5]
DR GeneID; 4355; -.
DR KEGG; hsa:4355; -.
DR UCSC; uc010win.3; human. [Q14168-1]
DR CTD; 4355; -.
DR DisGeNET; 4355; -.
DR GeneCards; MPP2; -.
DR HGNC; HGNC:7220; MPP2.
DR HPA; ENSG00000108852; Tissue enhanced (brain).
DR MIM; 600723; gene.
DR neXtProt; NX_Q14168; -.
DR OpenTargets; ENSG00000108852; -.
DR PharmGKB; PA30925; -.
DR VEuPathDB; HostDB:ENSG00000108852; -.
DR eggNOG; KOG0609; Eukaryota.
DR GeneTree; ENSGT00940000155348; -.
DR HOGENOM; CLU_001715_5_1_1; -.
DR InParanoid; Q14168; -.
DR OrthoDB; 847888at2759; -.
DR PhylomeDB; Q14168; -.
DR TreeFam; TF314263; -.
DR PathwayCommons; Q14168; -.
DR SignaLink; Q14168; -.
DR BioGRID-ORCS; 4355; 22 hits in 1073 CRISPR screens.
DR ChiTaRS; MPP2; human.
DR EvolutionaryTrace; Q14168; -.
DR GeneWiki; MPP2; -.
DR GenomeRNAi; 4355; -.
DR Pharos; Q14168; Tbio.
DR PRO; PR:Q14168; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q14168; protein.
DR Bgee; ENSG00000108852; Expressed in C1 segment of cervical spinal cord and 147 other tissues.
DR ExpressionAtlas; Q14168; baseline and differential.
DR GO; GO:0005911; C:cell-cell junction; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IDA:UniProtKB.
DR GO; GO:0032590; C:dendrite membrane; ISS:UniProtKB.
DR GO; GO:0043198; C:dendritic shaft; ISS:UniProtKB.
DR GO; GO:0043197; C:dendritic spine; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0014069; C:postsynaptic density; ISS:UniProtKB.
DR GO; GO:0060079; P:excitatory postsynaptic potential; ISS:UniProtKB.
DR GO; GO:0060291; P:long-term synaptic potentiation; ISS:UniProtKB.
DR GO; GO:0051260; P:protein homooligomerization; ISS:UniProtKB.
DR CDD; cd12037; SH3_MPP2; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR008145; GK/Ca_channel_bsu.
DR InterPro; IPR008144; Guanylate_kin-like_dom.
DR InterPro; IPR020590; Guanylate_kinase_CS.
DR InterPro; IPR014775; L27_C.
DR InterPro; IPR004172; L27_dom.
DR InterPro; IPR036892; L27_dom_sf.
DR InterPro; IPR035602; MPP2_SH3.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR Pfam; PF00625; Guanylate_kin; 1.
DR Pfam; PF02828; L27; 2.
DR Pfam; PF00595; PDZ; 1.
DR Pfam; PF07653; SH3_2; 1.
DR SMART; SM00072; GuKc; 1.
DR SMART; SM00569; L27; 2.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF101288; SSF101288; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00856; GUANYLATE_KINASE_1; 1.
DR PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
DR PROSITE; PS51022; L27; 2.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell projection; Cytoplasm;
KW Cytoskeleton; Membrane; Phosphoprotein; Reference proteome; Repeat;
KW SH3 domain; Synapse.
FT CHAIN 1..576
FT /note="MAGUK p55 subfamily member 2"
FT /id="PRO_0000094573"
FT DOMAIN 8..60
FT /note="L27 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00365"
FT DOMAIN 84..142
FT /note="L27 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00365"
FT DOMAIN 185..240
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 249..317
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 374..561
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00100"
FT MOD_RES 42
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:D3ZAA9"
FT MOD_RES 141
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 145
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9WV34"
FT VAR_SEQ 1..163
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055136"
FT VAR_SEQ 1..11
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055137"
FT VAR_SEQ 1..10
FT /note="MPVAATNSET -> MAGSPGSGVSLEGISLESSEEAELQRE (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_022951"
FT VAR_SEQ 1
FT /note="M -> MSWAPPPQVGQNLRSQTVLRILNGMEDLMWVAMEERRFRALASFTM
FT (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055138"
FT VAR_SEQ 51..74
FT /note="Missing (in isoform 2, isoform 3, isoform 4 and
FT isoform 6)"
FT /evidence="ECO:0000303|PubMed:11230166,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:17974005, ECO:0000303|Ref.5"
FT /id="VSP_003156"
FT MUTAGEN 363
FT /note="Y->A: Enhances association with the cytoskeleton.
FT Diminishes the inhibitory effect on SRC."
FT /evidence="ECO:0000269|PubMed:19665017"
FT MUTAGEN 363
FT /note="Y->D: Enhances association with the cytoskeleton."
FT /evidence="ECO:0000269|PubMed:19665017"
FT CONFLICT 80
FT /note="E -> G (in Ref. 4; CAI56746)"
FT /evidence="ECO:0000305"
FT CONFLICT 104..105
FT /note="HV -> QL (in Ref. 1; CAA58067, 2; BAD97280, 5;
FT CAB66489, 4; CAI56746, 7; AAH30287 and 3; BAG61302/
FT BAH12204)"
FT /evidence="ECO:0000305"
FT CONFLICT 242
FT /note="S -> N (in Ref. 1; CAA58067)"
FT /evidence="ECO:0000305"
FT CONFLICT 531
FT /note="R -> C (in Ref. 3; BAG57760)"
FT /evidence="ECO:0000305"
FT CONFLICT 554
FT /note="R -> C (in Ref. 3; BAG61302)"
FT /evidence="ECO:0000305"
FT STRAND 177..191
FT /evidence="ECO:0007829|PDB:2E7K"
FT STRAND 193..195
FT /evidence="ECO:0007829|PDB:2E7K"
FT HELIX 196..200
FT /evidence="ECO:0007829|PDB:2E7K"
FT STRAND 208..212
FT /evidence="ECO:0007829|PDB:2E7K"
FT HELIX 221..229
FT /evidence="ECO:0007829|PDB:2E7K"
FT STRAND 233..235
FT /evidence="ECO:0007829|PDB:2E7K"
FT STRAND 237..240
FT /evidence="ECO:0007829|PDB:2E7K"
SQ SEQUENCE 576 AA; 64581 MW; A08E858EA646A305 CRC64;
MPVAATNSET AMQQVLDNLG SLPSATGAAE LDLIFLRGIM ESPIVRSLAK VIMVLWFMQQ
NVFVPMKYML KYFGAHERLE ETKLEAVRDN NLELVQEILR DLAHVAEQSS TAAELAHILQ
EPHFQSLLET HDSVASKTYE TPPPSPGLDP TFSNQPVPPD AVRMVGIRKT AGEHLGVTFR
VEGGELVIAR ILHGGMVAQQ GLLHVGDIIK EVNGQPVGSD PRALQELLRN ASGSVILKIL
PSYQEPHLPR QVFVKCHFDY DPARDSLIPC KEAGLRFNAG DLLQIVNQDD ANWWQACHVE
GGSAGLIPSQ LLEEKRKAFV KRDLELTPNS GTLCGSLSGK KKKRMMYLTT KNAEFDRHEL
LIYEEVARMP PFRRKTLVLI GAQGVGRRSL KNKLIMWDPD RYGTTVPYTS RRPKDSEREG
QGYSFVSRGE MEADVRAGRY LEHGEYEGNL YGTRIDSIRG VVAAGKVCVL DVNPQAVKVL
RTAEFVPYVV FIEAPDFETL RAMNRAALES GISTKQLTEA DLRRTVEESS RIQRGYGHYF
DLCLVNSNLE RTFRELQTAM EKLRTEPQWV PVSWVY
