FBLI1_HUMAN
ID FBLI1_HUMAN Reviewed; 373 AA.
AC Q8WUP2; B3KNY0; Q5VVE0; Q5VVE1; Q8IX23; Q96T00; Q9UFD6;
DT 07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 2.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Filamin-binding LIM protein 1;
DE Short=FBLP-1;
DE AltName: Full=Migfilin;
DE AltName: Full=Mitogen-inducible 2-interacting protein;
DE Short=MIG2-interacting protein;
GN Name=FBLIM1; Synonyms=FBLP1;
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] (ISOFORMS 1 AND 3), VARIANT PHE-191, FUNCTION,
RP ALTERNATIVE SPLICING, SUBCELLULAR LOCATION, INTERACTION WITH FERMT2; FLNA
RP AND FLNC, AND MUTAGENESIS OF 7-LYS-ARG-8.
RC TISSUE=Lung;
RX PubMed=12679033; DOI=10.1016/s0092-8674(03)00163-6;
RA Tu Y., Wu S., Shi X., Chen K., Wu C.;
RT "Migfilin and Mig-2 link focal adhesions to filamin and the actin
RT cytoskeleton and function in cell shape modulation.";
RL Cell 113:37-47(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), VARIANT PHE-191,
RP FUNCTION, SUBCELLULAR LOCATION, ALTERNATIVE SPLICING, TISSUE SPECIFICITY,
RP AND INTERACTION WITH FNLB.
RC TISSUE=Placenta;
RX PubMed=12496242; DOI=10.1074/jbc.m209339200;
RA Takafuta T., Saeki M., Fujimoto T.-T., Fujimura K., Shapiro S.S.;
RT "A new member of the LIM protein family binds to filamin B and localizes at
RT stress fibers.";
RL J. Biol. Chem. 278:12175-12181(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND VARIANT
RP PHE-191.
RC TISSUE=Brain, and Teratocarcinoma;
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 GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT PHE-191.
RC TISSUE=Cervix adenocarcinoma;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 174-373 (ISOFORM 1).
RC TISSUE=Testis;
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 [7]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 5-19 IN COMPLEX WITH FLNA,
RP INTERACTION WITH FLNA; FLNB AND FLNC, FUNCTION, SUBCELLULAR LOCATION, AND
RP DOMAIN.
RX PubMed=18829455; DOI=10.1074/jbc.m802592200;
RA Lad Y., Jiang P., Ruskamo S., Harburger D.S., Ylanne J., Campbell I.D.,
RA Calderwood D.A.;
RT "Structural basis of the migfilin-filamin interaction and competition with
RT integrin beta tails.";
RL J. Biol. Chem. 283:35154-35163(2008).
RN [8]
RP STRUCTURE BY NMR OF 1-24 IN COMPLEX WITH FLNC, INTERACTION WITH FLNA AND
RP FLNC, AND FUNCTION.
RX PubMed=19074766; DOI=10.1074/jbc.m807719200;
RA Ithychanda S.S., Das M., Ma Y.Q., Ding K., Wang X., Gupta S., Wu C.,
RA Plow E.F., Qin J.;
RT "Migfilin, a molecular switch in regulation of integrin activation.";
RL J. Biol. Chem. 284:4713-4722(2009).
CC -!- FUNCTION: Serves as an anchoring site for cell-ECM adhesion proteins
CC and filamin-containing actin filaments. Is implicated in cell shape
CC modulation (spreading) and motility. May participate in the regulation
CC of filamin-mediated cross-linking and stabilization of actin filaments.
CC May also regulate the assembly of filamin-containing signaling
CC complexes that control actin assembly. Promotes dissociation of FLNA
CC from ITGB3 and ITGB7. Promotes activation of integrins and regulates
CC integrin-mediated cell-cell adhesion. {ECO:0000269|PubMed:12496242,
CC ECO:0000269|PubMed:12679033, ECO:0000269|PubMed:18829455,
CC ECO:0000269|PubMed:19074766}.
CC -!- SUBUNIT: Interacts with NKX2-5 (By similarity). Isoform 1 and isoform 3
CC interact with FERMT2, FLNA, FLNB and FLNC. Isoform 2 interacts with
CC FLNB. {ECO:0000250, ECO:0000269|PubMed:12496242,
CC ECO:0000269|PubMed:12679033, ECO:0000269|PubMed:18829455,
CC ECO:0000269|PubMed:19074766}.
CC -!- INTERACTION:
CC Q8WUP2; Q96EY9: ADAT3; NbExp=3; IntAct=EBI-3864120, EBI-3922811;
CC Q8WUP2; Q5BKX5-3: C19orf54; NbExp=3; IntAct=EBI-3864120, EBI-11976299;
CC Q8WUP2; O60888: CUTA; NbExp=4; IntAct=EBI-3864120, EBI-1051556;
CC Q8WUP2; O60888-3: CUTA; NbExp=3; IntAct=EBI-3864120, EBI-10979071;
CC Q8WUP2; Q6NXT2: H3-5; NbExp=3; IntAct=EBI-3864120, EBI-2868501;
CC Q8WUP2; P68431: H3C12; NbExp=3; IntAct=EBI-3864120, EBI-79722;
CC Q8WUP2; Q8TAP4: LMO3; NbExp=5; IntAct=EBI-3864120, EBI-742259;
CC Q8WUP2; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-3864120, EBI-11742507;
CC Q8WUP2; Q6ZSJ9: SHISA6; NbExp=3; IntAct=EBI-3864120, EBI-12037847;
CC -!- SUBCELLULAR LOCATION: Cell junction, focal adhesion
CC {ECO:0000269|PubMed:12679033, ECO:0000269|PubMed:18829455}. Cytoplasm,
CC cytoskeleton, stress fiber {ECO:0000269|PubMed:12496242,
CC ECO:0000269|PubMed:12679033, ECO:0000269|PubMed:18829455}.
CC Note=Associated with actin stress fiber at cell-ECM focal adhesion
CC sites (PubMed:12679033, PubMed:18829455). Isoform 1 and isoform 3 are
CC recruited and localized at actin stress fibers and clustered at cell-
CC EMC adhesion sites through interaction with FERMT2 (PubMed:12679033).
CC Isoform 2 is localized at actin stress fibers (PubMed:12496242).
CC {ECO:0000269|PubMed:12496242, ECO:0000269|PubMed:12679033,
CC ECO:0000269|PubMed:18829455}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=FBLP-1A;
CC IsoId=Q8WUP2-1; Sequence=Displayed;
CC Name=2; Synonyms=FBLP-1;
CC IsoId=Q8WUP2-2; Sequence=VSP_008782;
CC Name=3; Synonyms=FBLP-1B;
CC IsoId=Q8WUP2-3; Sequence=VSP_008781;
CC -!- TISSUE SPECIFICITY: Isoform 1 and isoform 3 are expressed in heart,
CC kidney, lung, pancreas, placenta and platelets. Isoform 2 is expressed
CC in brain, heart, kidney, lung, pancreas, placenta, skeletal muscle and
CC platelets. {ECO:0000269|PubMed:12496242}.
CC -!- DOMAIN: The N-terminal region is intrinsically disordered.
CC {ECO:0000269|PubMed:18829455}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to competing donor splice site.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 3]: May be due to exon skipping. {ECO:0000305}.
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DR EMBL; AY180161; AAO49012.1; -; mRNA.
DR EMBL; AF459643; AAO15549.1; -; mRNA.
DR EMBL; AK027444; BAB55115.1; -; mRNA.
DR EMBL; AK055259; BAG51492.1; -; mRNA.
DR EMBL; AL450998; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC019895; AAH19895.1; -; mRNA.
DR EMBL; AL133035; CAB61365.1; -; mRNA.
DR CCDS; CCDS163.1; -. [Q8WUP2-1]
DR CCDS; CCDS30609.1; -. [Q8WUP2-3]
DR CCDS; CCDS44064.1; -. [Q8WUP2-2]
DR PIR; T42678; T42678.
DR RefSeq; NP_001019386.1; NM_001024215.1. [Q8WUP2-2]
DR RefSeq; NP_001019387.1; NM_001024216.1. [Q8WUP2-3]
DR RefSeq; NP_060026.2; NM_017556.2. [Q8WUP2-1]
DR RefSeq; XP_005245957.1; XM_005245900.1. [Q8WUP2-2]
DR RefSeq; XP_005245958.1; XM_005245901.1. [Q8WUP2-2]
DR RefSeq; XP_005245959.1; XM_005245902.1. [Q8WUP2-2]
DR RefSeq; XP_005245960.1; XM_005245903.1. [Q8WUP2-2]
DR RefSeq; XP_005245966.1; XM_005245909.3.
DR RefSeq; XP_006710767.1; XM_006710704.3. [Q8WUP2-2]
DR RefSeq; XP_006710768.1; XM_006710705.1. [Q8WUP2-2]
DR RefSeq; XP_011539918.1; XM_011541616.2. [Q8WUP2-2]
DR RefSeq; XP_011539919.1; XM_011541617.2. [Q8WUP2-1]
DR RefSeq; XP_016857008.1; XM_017001519.1. [Q8WUP2-2]
DR RefSeq; XP_016857009.1; XM_017001520.1. [Q8WUP2-2]
DR RefSeq; XP_016857010.1; XM_017001521.1. [Q8WUP2-2]
DR RefSeq; XP_016857011.1; XM_017001522.1.
DR RefSeq; XP_016857012.1; XM_017001523.1. [Q8WUP2-2]
DR RefSeq; XP_016857013.1; XM_017001524.1. [Q8WUP2-2]
DR RefSeq; XP_016857014.1; XM_017001525.1. [Q8WUP2-1]
DR PDB; 2K9U; NMR; -; B=1-24.
DR PDB; 2W0P; X-ray; 1.90 A; C=5-19.
DR PDB; 4P3W; X-ray; 2.00 A; G/H/I/J/K/L=5-28.
DR PDBsum; 2K9U; -.
DR PDBsum; 2W0P; -.
DR PDBsum; 4P3W; -.
DR AlphaFoldDB; Q8WUP2; -.
DR BMRB; Q8WUP2; -.
DR SMR; Q8WUP2; -.
DR BioGRID; 120128; 47.
DR IntAct; Q8WUP2; 16.
DR STRING; 9606.ENSP00000416387; -.
DR iPTMnet; Q8WUP2; -.
DR MetOSite; Q8WUP2; -.
DR PhosphoSitePlus; Q8WUP2; -.
DR SwissPalm; Q8WUP2; -.
DR BioMuta; FBLIM1; -.
DR DMDM; 125987829; -.
DR EPD; Q8WUP2; -.
DR jPOST; Q8WUP2; -.
DR MassIVE; Q8WUP2; -.
DR MaxQB; Q8WUP2; -.
DR PaxDb; Q8WUP2; -.
DR PeptideAtlas; Q8WUP2; -.
DR PRIDE; Q8WUP2; -.
DR ProteomicsDB; 74698; -. [Q8WUP2-1]
DR ProteomicsDB; 74699; -. [Q8WUP2-2]
DR ProteomicsDB; 74700; -. [Q8WUP2-3]
DR Antibodypedia; 14407; 244 antibodies from 27 providers.
DR DNASU; 54751; -.
DR Ensembl; ENST00000332305.5; ENSP00000364920.2; ENSG00000162458.13. [Q8WUP2-3]
DR Ensembl; ENST00000375766.8; ENSP00000364921.3; ENSG00000162458.13. [Q8WUP2-1]
DR Ensembl; ENST00000375771.5; ENSP00000364926.1; ENSG00000162458.13. [Q8WUP2-1]
DR Ensembl; ENST00000441801.6; ENSP00000416387.2; ENSG00000162458.13. [Q8WUP2-2]
DR GeneID; 54751; -.
DR KEGG; hsa:54751; -.
DR MANE-Select; ENST00000375766.8; ENSP00000364921.3; NM_017556.4; NP_060026.2.
DR UCSC; uc001axd.2; human. [Q8WUP2-1]
DR CTD; 54751; -.
DR DisGeNET; 54751; -.
DR GeneCards; FBLIM1; -.
DR HGNC; HGNC:24686; FBLIM1.
DR HPA; ENSG00000162458; Low tissue specificity.
DR MIM; 607747; gene.
DR neXtProt; NX_Q8WUP2; -.
DR OpenTargets; ENSG00000162458; -.
DR PharmGKB; PA142671776; -.
DR VEuPathDB; HostDB:ENSG00000162458; -.
DR eggNOG; KOG1701; Eukaryota.
DR GeneTree; ENSGT00940000159003; -.
DR HOGENOM; CLU_062552_0_0_1; -.
DR InParanoid; Q8WUP2; -.
DR OMA; CYQATLE; -.
DR OrthoDB; 642235at2759; -.
DR PhylomeDB; Q8WUP2; -.
DR TreeFam; TF320310; -.
DR PathwayCommons; Q8WUP2; -.
DR Reactome; R-HSA-446353; Cell-extracellular matrix interactions.
DR SignaLink; Q8WUP2; -.
DR SIGNOR; Q8WUP2; -.
DR BioGRID-ORCS; 54751; 187 hits in 1076 CRISPR screens.
DR ChiTaRS; FBLIM1; human.
DR EvolutionaryTrace; Q8WUP2; -.
DR GeneWiki; FBLIM1; -.
DR GenomeRNAi; 54751; -.
DR Pharos; Q8WUP2; Tbio.
DR PRO; PR:Q8WUP2; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q8WUP2; protein.
DR Bgee; ENSG00000162458; Expressed in right coronary artery and 159 other tissues.
DR ExpressionAtlas; Q8WUP2; baseline and differential.
DR Genevisible; Q8WUP2; HS.
DR GO; GO:0030054; C:cell junction; IDA:HPA.
DR GO; GO:0071944; C:cell periphery; IDA:ARUK-UCL.
DR GO; GO:0005737; C:cytoplasm; IDA:ARUK-UCL.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0001650; C:fibrillar center; IDA:HPA.
DR GO; GO:0005925; C:focal adhesion; IDA:ARUK-UCL.
DR GO; GO:0001725; C:stress fiber; IDA:UniProtKB.
DR GO; GO:0031005; F:filamin binding; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0098609; P:cell-cell adhesion; IMP:UniProtKB.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR GO; GO:0033623; P:regulation of integrin activation; IMP:UniProtKB.
DR DisProt; DP01310; -.
DR InterPro; IPR001781; Znf_LIM.
DR Pfam; PF00412; LIM; 3.
DR SMART; SM00132; LIM; 3.
DR PROSITE; PS00478; LIM_DOMAIN_1; 3.
DR PROSITE; PS50023; LIM_DOMAIN_2; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell adhesion; Cell junction;
KW Cell shape; Cytoplasm; Cytoskeleton; LIM domain; Metal-binding;
KW Reference proteome; Repeat; Zinc.
FT CHAIN 1..373
FT /note="Filamin-binding LIM protein 1"
FT /id="PRO_0000075732"
FT DOMAIN 181..242
FT /note="LIM zinc-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 243..300
FT /note="LIM zinc-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 301..370
FT /note="LIM zinc-binding 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT REGION 1..70
FT /note="Filamin-binding"
FT REGION 41..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 135..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 276..373
FT /note="FERMT2-binding"
FT COMPBIAS 101..118
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 137..174
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 84..180
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12496242,
FT ECO:0000303|PubMed:12679033, ECO:0000303|PubMed:14702039"
FT /id="VSP_008781"
FT VAR_SEQ 298..373
FT /note="KFAPVCSICENPIIPRDGKDAFKIECMGRNFHENCYRCEDCRILLSVEPTDQ
FT GCYPLNNHLFCKPCHVKRSAAGCC -> YEKGLCTGWGAGTGRDPSRVKELSLSPGCWA
FT RVSCLLVYYKEYYRAGLGAVAHACNPSTLGGRGGWITRSGDRDHPG (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:12496242"
FT /id="VSP_008782"
FT VARIANT 39
FT /note="R -> C (in dbSNP:rs34375304)"
FT /id="VAR_050145"
FT VARIANT 191
FT /note="S -> F (in dbSNP:rs10927851)"
FT /evidence="ECO:0000269|PubMed:12496242,
FT ECO:0000269|PubMed:12679033, ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_022842"
FT MUTAGEN 7..8
FT /note="KR->TG: Localizes to cell-ECM adhesions; abolishes
FT FLNA and FLNC interactions; failed to decorate actin
FT filaments."
FT /evidence="ECO:0000269|PubMed:12679033"
FT STRAND 5..8
FT /evidence="ECO:0007829|PDB:2K9U"
FT STRAND 9..16
FT /evidence="ECO:0007829|PDB:2W0P"
SQ SEQUENCE 373 AA; 40670 MW; 06B8FB911FCCB194 CRC64;
MASKPEKRVA SSVFITLAPP RRDVAVAEEV RQAVCEARRG RPWEAPAPMK TPEAGLAGRP
SPWTTPGRAA ATVPAAPMQL FNGGCPPPPP VLDGEDVLPD LDLLPPPPPP PPVLLPSEEE
APAPMGASLI ADLEQLHLSP PPPPPQAPAE GPSVQPGPLR PMEEELPPPP AEPVEKGAST
DICAFCHKTV SPRELAVEAM KRQYHAQCFT CRTCRRQLAG QSFYQKDGRP LCEPCYQDTL
ERCGKCGEVV RDHIIRALGQ AFHPSCFTCV TCARCIGDES FALGSQNEVY CLDDFYRKFA
PVCSICENPI IPRDGKDAFK IECMGRNFHE NCYRCEDCRI LLSVEPTDQG CYPLNNHLFC
KPCHVKRSAA GCC
