FLNA_MOUSE
ID FLNA_MOUSE Reviewed; 2647 AA.
AC Q8BTM8; B7FAV0; O54934; Q7TQI1; Q8BLK1; Q8BTN7; Q8VHX5; Q8VHX8; Q99KQ2;
DT 07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 5.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Filamin-A;
DE Short=FLN-A;
DE AltName: Full=Actin-binding protein 280;
DE Short=ABP-280;
DE AltName: Full=Alpha-filamin;
DE AltName: Full=Endothelial actin-binding protein;
DE AltName: Full=Filamin-1;
DE AltName: Full=Non-muscle filamin;
GN Name=Flna; Synonyms=Fln, Fln1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 9-1253 (ISOFORM 1).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Embryo;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 14-2647 (ISOFORM 1).
RC TISSUE=Eye, and Mammary tumor;
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1490-1607 (ISOFORM 1), FUNCTION, AND
RP INTERACTION WITH FURIN.
RX PubMed=9412467; DOI=10.1083/jcb.139.7.1719;
RA Liu G., Thomas L., Warren R.A., Enns C.A., Cunningham C.C., Hartwig J.H.,
RA Thomas G.;
RT "Cytoskeletal protein ABP-280 directs the intracellular trafficking of
RT furin and modulates proprotein processing in the endocytic pathway.";
RL J. Cell Biol. 139:1719-1733(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1691-1805 AND 2076-2226 (ISOFORM 1), AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=C3H/HeJ;
RX PubMed=11807098; DOI=10.1083/jcb.200103037;
RA van Der Flier A., Kuikman I., Kramer D., Geerts D., Kreft M., Takafuta T.,
RA Shapiro S.S., Sonnenberg A.;
RT "Different splice variants of filamin-B affect myogenesis, subcellular
RT distribution, and determine binding to integrin (beta) subunits.";
RL J. Cell Biol. 156:361-376(2002).
RN [6]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=17172441; DOI=10.1073/pnas.0609628104;
RA Feng Y., Chen M.H., Moskowitz I.P., Mendonza A.M., Vidali L., Nakamura F.,
RA Kwiatkowski D.J., Walsh C.A.;
RT "Filamin A (FLNA) is required for cell-cell contact in vascular development
RT and cardiac morphogenesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:19836-19841(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1459, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2152, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1459 AND THR-1750, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; SER-20; SER-968;
RP SER-1459; THR-1750; SER-2152; SER-2180; SER-2329; THR-2336; SER-2370;
RP SER-2523; SER-2526 AND THR-2599, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [11]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=20713593; DOI=10.1084/jem.20100222;
RA Falet H., Pollitt A.Y., Begonja A.J., Weber S.E., Duerschmied D.,
RA Wagner D.D., Watson S.P., Hartwig J.H.;
RT "A novel interaction between FlnA and Syk regulates platelet ITAM-mediated
RT receptor signaling and function.";
RL J. Exp. Med. 207:1967-1979(2010).
RN [12]
RP INTERACTION WITH RFLNA AND RFLNB.
RX PubMed=21709252; DOI=10.1073/pnas.1104211108;
RA Gay O., Gilquin B., Nakamura F., Jenkins Z.A., McCartney R., Krakow D.,
RA Deshiere A., Assard N., Hartwig J.H., Robertson S.P., Baudier J.;
RT "RefilinB (FAM101B) targets filamin A to organize perinuclear actin
RT networks and regulates nuclear shape.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:11464-11469(2011).
RN [13]
RP FUNCTION IN CILIOGENESIS.
RX PubMed=22121117; DOI=10.1093/hmg/ddr557;
RA Adams M., Simms R.J., Abdelhamed Z., Dawe H.R., Szymanska K., Logan C.V.,
RA Wheway G., Pitt E., Gull K., Knowles M.A., Blair E., Cross S.H.,
RA Sayer J.A., Johnson C.A.;
RT "A meckelin-filamin A interaction mediates ciliogenesis.";
RL Hum. Mol. Genet. 21:1272-1286(2012).
RN [14]
RP INTERACTION WITH MICALL2.
RX PubMed=23890175; DOI=10.1111/gtc.12078;
RA Sakane A., Alamir Mahmoud Abdallah A., Nakano K., Honda K., Kitamura T.,
RA Imoto I., Matsushita N., Sasaki T.;
RT "Junctional Rab13-binding protein (JRAB) regulates cell spreading via
RT filamins.";
RL Genes Cells 18:810-822(2013).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-376; LYS-700; LYS-865; LYS-906;
RP LYS-1071; LYS-1372; LYS-1538; LYS-2569 AND LYS-2575, SUCCINYLATION [LARGE
RP SCALE ANALYSIS] AT LYS-1071 AND LYS-2569, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [16]
RP INTERACTION WITH RFLNA AND RFLNB.
RX PubMed=24436304; DOI=10.1093/hmg/ddu007;
RA Mizuhashi K., Kanamoto T., Moriishi T., Muranishi Y., Miyazaki T.,
RA Terada K., Omori Y., Ito M., Komori T., Furukawa T.;
RT "Filamin-interacting proteins, Cfm1 and Cfm2, are essential for the
RT formation of cartilaginous skeletal elements.";
RL Hum. Mol. Genet. 23:2953-2967(2014).
RN [17]
RP FUNCTION, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=25358863; DOI=10.1038/ncomms6325;
RA Nakamura F., Kumeta K., Hida T., Isono T., Nakayama Y.,
RA Kuramata-Matsuoka E., Yamashita N., Uchida Y., Ogura K., Gengyo-Ando K.,
RA Mitani S., Ogino T., Goshima Y.;
RT "Amino- and carboxyl-terminal domains of Filamin-A interact with CRMP1 to
RT mediate Sema3A signalling.";
RL Nat. Commun. 5:5325-5325(2014).
CC -!- FUNCTION: Actin binding protein that promotes orthogonal branching of
CC actin filaments and links actin filaments to membrane glycoproteins.
CC Anchors various transmembrane proteins to the actin cytoskeleton and
CC serves as a scaffold for a wide range of cytoplasmic signaling proteins
CC (By similarity). Interaction with FLNB may allow neuroblast migration
CC from the ventricular zone into the cortical plate. Tethers cell
CC surface-localized furin, modulates its rate of internalization and
CC directs its intracellular trafficking. Involved in ciliogenesis. Plays
CC a role in cell-cell contacts and adherens junctions during the
CC development of blood vessels, heart and brain organs (PubMed:17172441).
CC Plays a role in platelets morphology through interaction with SYK that
CC regulates ITAM- and ITAM-like-containing receptor signaling, resulting
CC in by platelet cytoskeleton organization maintenance (PubMed:20713593).
CC During the axon guidance process, required for growth cone collapse
CC induced by SEMA3A-mediated stimulation of neurons (PubMed:25358863).
CC {ECO:0000250, ECO:0000269|PubMed:17172441, ECO:0000269|PubMed:20713593,
CC ECO:0000269|PubMed:22121117, ECO:0000269|PubMed:25358863,
CC ECO:0000269|PubMed:9412467}.
CC -!- SUBUNIT: Homodimer. Interacts with FCGR1A, FLNB, FURIN, HSPB7, KCND2,
CC INPPL1, MYOT, MYOZ1, PDLIM2, ARHGAP24, PSEN1, PSEN2 and ECSCR.
CC Interacts also with various other binding partners in addition to
CC filamentous actin. Interacts (via N-terminus) with TAF1B. Interacts
CC (via N-terminus) with MIS18BP1 (via N-terminus) (By similarity).
CC Interacts with TMEM67 (via C-terminus) and MKS1 (By similarity).
CC Interacts (via actin-binding domain) with MICALL2 (via calponin-
CC homology (CH) domain). Interacts with RFLNA and RFLNB (PubMed:24436304,
CC PubMed:21709252). Interacts (via filamin repeat 5) with SYK; docks SYK
CC to the plasma membrane. Interacts (via filamin repeats 19 and 21) with
CC DRD3; increased PKA-mediated phosphorylation at Ser-2152. Interacts
CC (via filamin repeat 21) with MAS1, AGTR1 and ADRA1D; increases PKA-
CC mediated phosphorylation of FLNA at Ser-2152. Interacts (via filamin
CC repeats 4, 9, 12, 17, 19, 21, and 23) with GP1BA (high affinity),
CC ITGB7, ITGB2 and FBLIM1 (By similarity). Interacts with CEACAM1 (via
CC cytoplasmic domain); inhibits cell migration and cell scattering by
CC interfering with the interaction between FLNA and RALA (By similarity).
CC Interacts with FOXC1 (By similarity). Interacts (via calponin-homology
CC (CH) domain 1 and filamin repeat 24) with CRMP1; the interaction alters
CC FLNA ternary structure and thus promotes FLNA dissociation from F-actin
CC (By similarity). Interacts with DPYSL3/CRMP3 and DPYSL4/CRMP4 (By
CC similarity). {ECO:0000250, ECO:0000250|UniProtKB:P21333,
CC ECO:0000269|PubMed:21709252, ECO:0000269|PubMed:23890175,
CC ECO:0000269|PubMed:24436304, ECO:0000269|PubMed:9412467}.
CC -!- INTERACTION:
CC Q8BTM8; Q8CIH5: Plcg2; NbExp=3; IntAct=EBI-641991, EBI-617954;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex {ECO:0000250}. Cytoplasm,
CC cytoskeleton {ECO:0000269|PubMed:25358863}. Perikaryon
CC {ECO:0000269|PubMed:25358863}. Cell projection, growth cone
CC {ECO:0000269|PubMed:25358863}. Note=Colocalizes with CPMR1 in the
CC central region of DRG neuron growth cone (PubMed:25358863). Following
CC SEMA3A stimulation of DRG neurons, colocalizes with F-actin
CC (PubMed:25358863). {ECO:0000269|PubMed:25358863}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8BTM8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BTM8-2; Sequence=VSP_008779, VSP_008780;
CC -!- TISSUE SPECIFICITY: Widely expressed. Highly expressed in Purkinje
CC cells.
CC -!- DEVELOPMENTAL STAGE: Widely distributed (PubMed:11807098). Expressed at
CC 12.5 dpc in the ventricular and subventricular zones. Highly expressed
CC at 16 dpc in blood vessels, renal cortices, respiratory and alimentary
CC tracts, olfactory epithelium, presumed isles of hematopoiesis within
CC the liver; lower expression in the cerebral cortex and choroid plexus
CC (PubMed:11807098). In 12 dpc embryos, expressed in DRG neurons,
CC motoneurons and the neuroepithelial cell layer around the central canal
CC in spinal cord (PubMed:25358863). {ECO:0000269|PubMed:11807098,
CC ECO:0000269|PubMed:25358863}.
CC -!- DOMAIN: Comprised of a NH2-terminal actin-binding domain, 24
CC immunoglobulin-like internally homologous repeats and two hinge
CC regions. Repeat 24 and the second hinge domain are important for dimer
CC formation. Filamin repeat 20 interacts with filamin repeat 21 masking
CC the ligand binding site on filamin repeat 21, resulting in an
CC autoinhibited conformation. The autoinhibition can be relieved by
CC ligands like ITGB7 or FBLIM1. Filamin repeats 19 and 21 can
CC simultaneously engage ligands. {ECO:0000250|UniProtKB:P21333}.
CC -!- PTM: Phosphorylation at Ser-2152 is negatively regulated by the
CC autoinhibited conformation of filamin repeats 19-21. Ligand binding
CC induces a conformational switch triggering phosphorylation at Ser-2152
CC by PKA. {ECO:0000250|UniProtKB:P21333}.
CC -!- PTM: Polyubiquitination in the CH1 domain by a SCF-like complex
CC containing ASB2 leads to proteasomal degradation. Prior dissociation
CC from actin may be required to expose the target lysines. Ubiquitinated
CC in endothelial cells by RNF213 downstream of the non-canonical Wnt
CC signaling pathway, leading to its degradation by the proteasome.
CC {ECO:0000250|UniProtKB:P21333}.
CC -!- DISRUPTION PHENOTYPE: Female heterozygous knockout mice show normal
CC development, but 20% die in the first 3-4 months with many anomalies,
CC including lung edema and emphysema, liver thrombi and necrosis,
CC leukocytosis, and heart dilation. Some females die after birth; only
CC about 50% of expected female heterozygous mice are observed at weaning.
CC Male hemizygous knockout mice die by embryonic day 14.5 dpc with
CC vascular defects; their blood vessels are coarse and dilated and extend
CC aberrant branches and sprouts into somitic tissues. Male hemizygous
CC knockout mice display severe cardiac structural defects involving
CC ventricles, atria, and outflow tracts. Conditional Flna knockout males,
CC in the neural crest, survive until birth but die on the first postnatal
CC day with cyanosis; all males show abnormal cardiac outflow tracts
CC (PubMed:17172441). Female heterozygous knockout mice present a mild
CC thrombocytopenia and conditional Flna knockout males, in platelets
CC display a macrothrombocytopenia (PubMed:20713593).
CC {ECO:0000269|PubMed:17172441, ECO:0000269|PubMed:20713593}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to an intron retention.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the filamin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC40787.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC40837.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BC038478; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK044856; BAC32121.1; -; mRNA.
DR EMBL; AK089195; BAC40787.1; ALT_INIT; mRNA.
DR EMBL; AK089311; BAC40837.2; ALT_INIT; mRNA.
DR EMBL; AL807376; CAT00728.1; -; Genomic_DNA.
DR EMBL; BC004061; AAH04061.1; -; mRNA.
DR EMBL; BC038478; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC054432; AAH54432.1; -; mRNA.
DR EMBL; AF034129; AAC02062.1; -; mRNA.
DR EMBL; AF353668; AAL68444.1; -; mRNA.
DR EMBL; AF353671; AAL68447.1; -; mRNA.
DR RefSeq; XP_006527974.1; XM_006527911.3. [Q8BTM8-1]
DR AlphaFoldDB; Q8BTM8; -.
DR SMR; Q8BTM8; -.
DR BioGRID; 228662; 36.
DR ComplexPortal; CPX-118; Glycoprotein Ib-IX-V-Filamin-A complex.
DR ComplexPortal; CPX-123; Filamin A homodimer.
DR IntAct; Q8BTM8; 14.
DR MINT; Q8BTM8; -.
DR STRING; 10090.ENSMUSP00000033699; -.
DR GlyConnect; 2316; 1 N-Linked glycan (1 site).
DR GlyGen; Q8BTM8; 1 site, 1 N-linked glycan (1 site).
DR iPTMnet; Q8BTM8; -.
DR PhosphoSitePlus; Q8BTM8; -.
DR SwissPalm; Q8BTM8; -.
DR EPD; Q8BTM8; -.
DR jPOST; Q8BTM8; -.
DR MaxQB; Q8BTM8; -.
DR PaxDb; Q8BTM8; -.
DR PeptideAtlas; Q8BTM8; -.
DR PRIDE; Q8BTM8; -.
DR ProteomicsDB; 267595; -. [Q8BTM8-1]
DR ProteomicsDB; 267596; -. [Q8BTM8-2]
DR Antibodypedia; 341; 691 antibodies from 39 providers.
DR Ensembl; ENSMUST00000033699; ENSMUSP00000033699; ENSMUSG00000031328. [Q8BTM8-1]
DR GeneID; 192176; -.
DR UCSC; uc009tnz.1; mouse. [Q8BTM8-1]
DR CTD; 2316; -.
DR MGI; MGI:95556; Flna.
DR VEuPathDB; HostDB:ENSMUSG00000031328; -.
DR eggNOG; KOG0518; Eukaryota.
DR GeneTree; ENSGT00940000153588; -.
DR InParanoid; Q8BTM8; -.
DR OrthoDB; 35998at2759; -.
DR PhylomeDB; Q8BTM8; -.
DR TreeFam; TF313685; -.
DR Reactome; R-MMU-114608; Platelet degranulation.
DR Reactome; R-MMU-430116; GP1b-IX-V activation signalling.
DR Reactome; R-MMU-446353; Cell-extracellular matrix interactions.
DR Reactome; R-MMU-5627123; RHO GTPases activate PAKs.
DR BioGRID-ORCS; 192176; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Flna; mouse.
DR PRO; PR:Q8BTM8; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q8BTM8; protein.
DR Bgee; ENSMUSG00000031328; Expressed in aorta tunica media and 242 other tissues.
DR ExpressionAtlas; Q8BTM8; baseline and differential.
DR Genevisible; Q8BTM8; MM.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:WormBase.
DR GO; GO:0005884; C:actin filament; ISO:MGI.
DR GO; GO:0032432; C:actin filament bundle; IDA:MGI.
DR GO; GO:0097440; C:apical dendrite; ISO:MGI.
DR GO; GO:0044295; C:axonal growth cone; IDA:CACAO.
DR GO; GO:0005903; C:brush border; IDA:UniProtKB.
DR GO; GO:0005938; C:cell cortex; ISO:MGI.
DR GO; GO:0005911; C:cell-cell junction; ISS:UniProtKB.
DR GO; GO:0030863; C:cortical cytoskeleton; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0043198; C:dendritic shaft; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:1990779; C:glycoprotein Ib-IX-V complex; IC:ComplexPortal.
DR GO; GO:0030426; C:growth cone; IDA:WormBase.
DR GO; GO:0031523; C:Myb complex; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0098794; C:postsynapse; ISO:MGI.
DR GO; GO:0005802; C:trans-Golgi network; IDA:MGI.
DR GO; GO:0030018; C:Z disc; IDA:BHF-UCL.
DR GO; GO:0003779; F:actin binding; TAS:MGI.
DR GO; GO:0051015; F:actin filament binding; ISS:UniProtKB.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISS:UniProtKB.
DR GO; GO:0034988; F:Fc-gamma receptor I complex binding; ISS:UniProtKB.
DR GO; GO:0001664; F:G protein-coupled receptor binding; ISO:MGI.
DR GO; GO:0051020; F:GTPase binding; ISO:MGI.
DR GO; GO:0019900; F:kinase binding; ISO:MGI.
DR GO; GO:0031852; F:mu-type opioid receptor binding; ISO:MGI.
DR GO; GO:0015459; F:potassium channel regulator activity; IMP:BHF-UCL.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0005080; F:protein kinase C binding; IDA:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0046332; F:SMAD binding; ISO:MGI.
DR GO; GO:0031267; F:small GTPase binding; ISS:UniProtKB.
DR GO; GO:0044325; F:transmembrane transporter binding; ISO:MGI.
DR GO; GO:0051764; P:actin crosslink formation; ISS:UniProtKB.
DR GO; GO:0030036; P:actin cytoskeleton organization; IGI:MGI.
DR GO; GO:0031532; P:actin cytoskeleton reorganization; ISS:UniProtKB.
DR GO; GO:0007195; P:adenylate cyclase-inhibiting dopamine receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0001525; P:angiogenesis; IMP:UniProtKB.
DR GO; GO:0007597; P:blood coagulation, intrinsic pathway; IC:ComplexPortal.
DR GO; GO:0001974; P:blood vessel remodeling; IMP:UniProtKB.
DR GO; GO:0045216; P:cell-cell junction organization; IMP:UniProtKB.
DR GO; GO:0060271; P:cilium assembly; ISO:MGI.
DR GO; GO:0051220; P:cytoplasmic sequestering of protein; ISS:UniProtKB.
DR GO; GO:0045022; P:early endosome to late endosome transport; IDA:MGI.
DR GO; GO:0001837; P:epithelial to mesenchymal transition; IGI:MGI.
DR GO; GO:0045184; P:establishment of protein localization; ISS:UniProtKB.
DR GO; GO:0097368; P:establishment of Sertoli cell barrier; ISO:MGI.
DR GO; GO:0021943; P:formation of radial glial scaffolds; ISO:MGI.
DR GO; GO:0003007; P:heart morphogenesis; IMP:UniProtKB.
DR GO; GO:0035855; P:megakaryocyte development; IC:ComplexPortal.
DR GO; GO:0090307; P:mitotic spindle assembly; ISO:MGI.
DR GO; GO:0042789; P:mRNA transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; ISS:UniProtKB.
DR GO; GO:0010977; P:negative regulation of neuron projection development; IGI:WormBase.
DR GO; GO:0042177; P:negative regulation of protein catabolic process; ISS:UniProtKB.
DR GO; GO:0016479; P:negative regulation of transcription by RNA polymerase I; ISO:MGI.
DR GO; GO:0032233; P:positive regulation of actin filament bundle assembly; ISO:MGI.
DR GO; GO:0048680; P:positive regulation of axon regeneration; IMP:CACAO.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; ISS:UniProtKB.
DR GO; GO:2001046; P:positive regulation of integrin-mediated signaling pathway; ISO:MGI.
DR GO; GO:2000179; P:positive regulation of neural precursor cell proliferation; ISO:MGI.
DR GO; GO:2001224; P:positive regulation of neuron migration; ISO:MGI.
DR GO; GO:0010572; P:positive regulation of platelet activation; IC:ComplexPortal.
DR GO; GO:1901381; P:positive regulation of potassium ion transmembrane transport; IMP:BHF-UCL.
DR GO; GO:0042307; P:positive regulation of protein import into nucleus; ISS:UniProtKB.
DR GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; ISO:MGI.
DR GO; GO:1902396; P:protein localization to bicellular tight junction; ISO:MGI.
DR GO; GO:0034394; P:protein localization to cell surface; ISS:UniProtKB.
DR GO; GO:0072659; P:protein localization to plasma membrane; IMP:BHF-UCL.
DR GO; GO:0050821; P:protein stabilization; ISS:UniProtKB.
DR GO; GO:0043113; P:receptor clustering; ISS:UniProtKB.
DR GO; GO:0032231; P:regulation of actin filament bundle assembly; IMP:UniProtKB.
DR GO; GO:0030334; P:regulation of cell migration; ISS:UniProtKB.
DR GO; GO:1905000; P:regulation of membrane repolarization during atrial cardiac muscle cell action potential; IC:BHF-UCL.
DR GO; GO:1905031; P:regulation of membrane repolarization during cardiac muscle cell action potential; IMP:BHF-UCL.
DR GO; GO:0051209; P:release of sequestered calcium ion into cytosol; IC:ComplexPortal.
DR GO; GO:0071526; P:semaphorin-plexin signaling pathway; IGI:WormBase.
DR GO; GO:0050808; P:synapse organization; IDA:SynGO.
DR GO; GO:0090042; P:tubulin deacetylation; ISO:MGI.
DR GO; GO:0044319; P:wound healing, spreading of cells; ISS:UniProtKB.
DR CDD; cd00014; CH; 2.
DR Gene3D; 1.10.418.10; -; 2.
DR Gene3D; 2.60.40.10; -; 24.
DR InterPro; IPR001589; Actinin_actin-bd_CS.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR044801; Filamin.
DR InterPro; IPR017868; Filamin/ABP280_repeat-like.
DR InterPro; IPR001298; Filamin/ABP280_rpt.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR PANTHER; PTHR38537; PTHR38537; 1.
DR Pfam; PF00307; CH; 2.
DR Pfam; PF00630; Filamin; 23.
DR SMART; SM00033; CH; 2.
DR SMART; SM00557; IG_FLMN; 24.
DR SUPFAM; SSF47576; SSF47576; 1.
DR SUPFAM; SSF81296; SSF81296; 24.
DR PROSITE; PS00019; ACTININ_1; 1.
DR PROSITE; PS00020; ACTININ_2; 1.
DR PROSITE; PS50021; CH; 2.
DR PROSITE; PS50194; FILAMIN_REPEAT; 24.
PE 1: Evidence at protein level;
KW Acetylation; Actin-binding; Alternative splicing; Cell projection;
KW Cilium biogenesis/degradation; Cytoplasm; Cytoskeleton; Isopeptide bond;
KW Phosphoprotein; Reference proteome; Repeat; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P21333"
FT CHAIN 2..2647
FT /note="Filamin-A"
FT /id="PRO_0000087297"
FT DOMAIN 43..149
FT /note="Calponin-homology (CH) 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 166..269
FT /note="Calponin-homology (CH) 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT REPEAT 276..374
FT /note="Filamin 1"
FT REPEAT 376..474
FT /note="Filamin 2"
FT REPEAT 475..570
FT /note="Filamin 3"
FT REPEAT 571..663
FT /note="Filamin 4"
FT REPEAT 667..763
FT /note="Filamin 5"
FT REPEAT 764..866
FT /note="Filamin 6"
FT REPEAT 867..965
FT /note="Filamin 7"
FT REPEAT 966..1061
FT /note="Filamin 8"
FT REPEAT 1062..1154
FT /note="Filamin 9"
FT REPEAT 1155..1249
FT /note="Filamin 10"
FT REPEAT 1250..1349
FT /note="Filamin 11"
FT REPEAT 1350..1442
FT /note="Filamin 12"
FT REPEAT 1443..1539
FT /note="Filamin 13"
FT REPEAT 1540..1636
FT /note="Filamin 14"
FT REPEAT 1641..1740
FT /note="Filamin 15"
FT REPEAT 1765..1860
FT /note="Filamin 16"
FT REPEAT 1861..1952
FT /note="Filamin 17"
FT REPEAT 1953..2039
FT /note="Filamin 18"
FT REPEAT 2042..2134
FT /note="Filamin 19"
FT REPEAT 2135..2230
FT /note="Filamin 20"
FT REPEAT 2233..2325
FT /note="Filamin 21"
FT REPEAT 2327..2420
FT /note="Filamin 22"
FT REPEAT 2424..2516
FT /note="Filamin 23"
FT REPEAT 2552..2646
FT /note="Filamin 24"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2..274
FT /note="Actin-binding"
FT REGION 271..294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1490..1607
FT /note="Interaction with furin"
FT REGION 1741..1778
FT /note="Hinge 1"
FT /evidence="ECO:0000250"
FT REGION 2517..2647
FT /note="Self-association site, tail"
FT /evidence="ECO:0000250"
FT REGION 2517..2553
FT /note="Hinge 2"
FT /evidence="ECO:0000250"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P21333"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P21333"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 20
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 376
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 508
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P21333"
FT MOD_RES 700
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 781
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P21333"
FT MOD_RES 837
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P21333"
FT MOD_RES 865
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 906
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 968
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1055
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P21333"
FT MOD_RES 1071
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 1071
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 1084
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P21333"
FT MOD_RES 1089
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P21333"
FT MOD_RES 1301
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P21333"
FT MOD_RES 1338
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P21333"
FT MOD_RES 1372
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 1459
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:21183079"
FT MOD_RES 1533
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P21333"
FT MOD_RES 1538
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 1630
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P21333"
FT MOD_RES 1734
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P21333"
FT MOD_RES 1750
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1835
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P21333"
FT MOD_RES 1967
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P21333"
FT MOD_RES 2053
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P21333"
FT MOD_RES 2128
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P21333"
FT MOD_RES 2152
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 2158
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P21333"
FT MOD_RES 2163
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P21333"
FT MOD_RES 2180
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2284
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P21333"
FT MOD_RES 2327
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P21333"
FT MOD_RES 2329
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2336
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2338
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P21333"
FT MOD_RES 2370
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2414
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P21333"
FT MOD_RES 2510
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P21333"
FT MOD_RES 2523
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2526
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2569
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 2569
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 2575
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 2599
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2607
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P21333"
FT MOD_RES 2621
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P21333"
FT CROSSLNK 42
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P21333"
FT CROSSLNK 43
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P21333"
FT CROSSLNK 135
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P21333"
FT CROSSLNK 299
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P21333"
FT CROSSLNK 299
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P21333"
FT VAR_SEQ 125..249
FT /note="DSKAIVDGNLKLILGLIWTLILHYSISMPMWDEEEDEEAKKQTPKQRLLGWI
FT QNKLPQLPITNFSRDWQSGRALGALVDSCAPGLCPDWDSWDASKPVNNAREAMQQADDW
FT LGIPQVITPEEIVD -> GEGTGYTGALSGCGRGRNKFFLSSPLESLLVVFPSCCTQPR
FT LPLGPLAALFFEVLENKRLAWRACEPLRAPARSALLACSQAELTSSVGRAPNAAPEVGQ
FT AQTRLLPLRAAPHPWDTHAFHLQQF (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_008779"
FT VAR_SEQ 250..2647
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_008780"
FT CONFLICT 661
FT /note="A -> T (in Ref. 1; BAC40837)"
FT /evidence="ECO:0000305"
FT CONFLICT 2127
FT /note="G -> D (in Ref. 5; AAL68447)"
FT /evidence="ECO:0000305"
FT CONFLICT 2253
FT /note="V -> A (in Ref. 3; AAH04061/BC038478)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2647 AA; 281222 MW; 217E3275F8468FEB CRC64;
MSSSHSRCGQ SAAVASPGGS IDSRDAEMPA TEKDLAEDAP WKKIQQNTFT RWCNEHLKCV
SKRIANLQTD LSDGLRLIAL LEVLSQKKMH RKHNQRPTFR QMQLENVSVA LEFLDRESIK
LVSIDSKAIV DGNLKLILGL IWTLILHYSI SMPMWDEEED EEAKKQTPKQ RLLGWIQNKL
PQLPITNFSR DWQSGRALGA LVDSCAPGLC PDWDSWDASK PVNNAREAMQ QADDWLGIPQ
VITPEEIVDP NVDEHSVMTY LSQFPKAKLK PGAPLRPKLN PKKARAYGPG IEPTGNMVKK
RAEFTVETRS AGQGEVLVYV EDPAGHQEEA KVTANNDKNR TFSVWYVPEV TGTHKVTVLF
AGQHIAKSPF EVYVDKSQGD ASKVTAQGPG LEPSGNIANK TTYFEIFTAG AGMGEVEVVI
QDPTGQKGTV EPQLEARGDS TYRCSYQPTM EGVHTVHVTF AGVPIPRSPY TVTVGQACNP
AACRAIGRGL QPKGVRVKET ADFKVYTKGA GSGELKVTVK GPKGEERVKQ KDLGDGVYGF
EYYPTIPGTY TVTITWGGQN IGRSPFEVKV GTECGNQKVR AWGPGLEGGI VGKSADFVVE
AIGDDVGTLG FSVEGPSQAK IECDDKGDGS CDVRYWPQEA GEYAVHVLCN SEDIRLSPFM
ADIREAPQDF HPDRVKARGP GLEKTGVAVN KPAEFTVDAK HAGKAPLRVQ VQDNEGCSVE
ATVKDNGNGT YSCSYVPRKP VKHTAMVSWG GVSIPNSPFR VNVGAGSHPN KVKVYGPGVA
KTGLKAHEPT YFTVDCTEAG QGDVSIGIKC APGVVGPTEA DIDFDIIRND NDTFTVKYTP
CGAGSYTIMV LFADQATPTS PIRVKVEPSH DASKVKAEGP GLNRTGVELG KPTHFTVNAK
TAGKGKLDVQ FSGLAKGDAV RDVDIIDHHD NTYTVKYIPV QQGPVGVNVT YGGDHIPKSP
FSVGVSPSLD LSKIKVSGLG DKVDVGKDQE FTVKSKGAGG QGKVASKIVS PSGAAVPCKV
EPGLGADNSV VRFVPREEGP YEVEVTYDGV PVPGSPFPLE AVAPTKPSKV KAFGPGLQGG
NAGSPARFTI DTKGAGTGGL GLTVEGPCEA QLECLDNGDG TCSVSYVPTE PGDYNINILF
ADTHIPGSPF KAHVAPCFDA SKVKCSGPGL ERATAGEVGQ FQVDCSSAGS AELTIEICSE
AGLPAEVYIQ DHGDGTHTIT YIPLCPGAYT VTIKYGGQPV PNFPSKLQVE PAVDTSGVQC
YGPGIEGQGV FREATTEFSV DARALTQTGG PHVKARVANP SGNLTDTYVQ DCGDGTYKVE
YTPYEEGVHS VDVTYDGSPV PSSPFQVPVT EGCDPSRVRV HGPGIQSGTT NKPNKFTVET
RGAGTGGLGL AVEGPSEAKM SCMDNKDGSC SVEYIPYEAG TYSLNVTYGG HQVPGSPFKV
PVHDVTDASK VKCSGPGLSP GMVRANLPQS FQVDTSKAGV APLQVKVQGP KGLVEPVDVV
DNADGTQTVN YVPSREGSYS ISVLYGEEEV PRSPFKVKVL PTHDASKVKA SGPGLNTTGV
PASLPVEFTI DAKDAGEGLL AVQITDPEGK PKKTHIQDNH DGTYTVAYVP DVPGRYTILI
KYGGDEIPFS PYRVRAVPTG DASKCTVTVS IGGHGLGAGI GPTIQIGEET VITVDTKAAG
KGKVTCTVCT PDGSEVDVDV VENEDGTFDI FYTAPQPGKY VICVRFGGEH VPNSPFQVTA
LAGDQPTVQT PLRSQQLAPQ YNYPQGSQQT WIPERPMVGV NGLDVTSLRP FDLVIPFTIK
KGEITGEVRM PSGKVAQPSI TDNKDGTVTV RYSPSEAGLH EMDIRYDNMH IPGSPLQFYV
DYVNCGHITA YGPGLTHGVV NKPATFTVNT KDAGEGGLSL AIEGPSKAEI SCTDNQDGTC
SVSYLPVLPG DYSILVKYND QHIPGSPFTA RVTGDDSMRM SHLKVGSAAD IPINISETDL
SLLTATVVPP SGREEPCLLK RLRNGHVGIS FVPKETGEHL VHVKKNGQHV ASSPIPVVIS
QSEIGDASRV RVSGQGLHEG HTFEPAEFII DTRDAGYGGL SLSIEGPSKV DINTEDLEDG
TCRVTYCPTE PGNYIINIKF ADQHVPGSPF SVKVTGEGRV KESITRRRRA PSVANIGSHC
DLSLKIPEIS IQDMTAQVTS PSGKTHEAEI VEGENHTYCI RFVPAEMGMH TVSVKYKGQH
VPGSPFQFTV GPLGEGGAHK VRAGGPGLER AEVGVPAEFG IWTREAGAGG LAIAVEGPSK
AEISFEDRKD GSCGVAYVVQ EPGDYEVSVK FNEEHIPDSP FVVPVASPSG DARRLTVSSL
QESGLKVNQP ASFAVSLNGA KGAIDAKVHS PSGALEECYV TEIDQDKYAV RFIPRENGIY
LIDVKFNGTH IPGSPFKIRV GEPGHGGDPG LVSAYGAGLE GGVTGSPAEF IVNTSNAGAG
ALSVTIDGPS KVKMDCQECP EGYRVTYTPM APGSYLISIK YGGPYHIGGS PFKAKVTGPR
LVSNHSLHET SSVFVDSLTK VATVPQHATS GPGPADVSKV VAKGLGLSKA YVGQKSNFTV
DCSKAGNNML LVGVHGPRTP CEEILVKHMG SRLYSVSYLL KDKGEYTLVV KWGDEHIPGS
PYRIMVP
