FBLI1_MOUSE
ID FBLI1_MOUSE Reviewed; 375 AA.
AC Q71FD7; Q3TDK3; Q99J35;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Filamin-binding LIM protein 1;
DE Short=FBLP-1;
DE AltName: Full=CSX-associated LIM;
GN Name=Fblim1; Synonyms=Cal;
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 [MRNA], AND INTERACTION WITH NKX2-5.
RX PubMed=14757752; DOI=10.1083/jcb.200309159;
RA Akazawa H., Kudoh S., Mochizuki N., Takekoshi N., Takano H., Nagai T.,
RA Komuro I.;
RT "A novel LIM protein Cal promotes cardiac differentiation by association
RT with CSX/NKX2-5.";
RL J. Cell Biol. 164:395-405(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=NOD;
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=NMRI; TISSUE=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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, Lung, and Spleen;
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).
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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with FERMT2, FLNA, FLNB and FLNC (By similarity).
CC Interacts with NKX2-5. {ECO:0000250, ECO:0000269|PubMed:14757752}.
CC -!- INTERACTION:
CC Q71FD7; P52952: NKX2-5; Xeno; NbExp=4; IntAct=EBI-8346526, EBI-936601;
CC -!- SUBCELLULAR LOCATION: Cell junction, focal adhesion
CC {ECO:0000250|UniProtKB:Q8WUP2}. Cytoplasm, cytoskeleton, stress fiber
CC {ECO:0000250|UniProtKB:Q8WUP2}. Note=Associated with actin stress fiber
CC at cell-ECM focal adhesion sites. Recruited and localized at actin
CC stress fibers and clustered at cell-EMC adhesion sites through
CC interaction with FERMT2. {ECO:0000250|UniProtKB:Q8WUP2}.
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DR EMBL; AF513359; AAQ08090.1; -; mRNA.
DR EMBL; AK154680; BAE32761.1; -; mRNA.
DR EMBL; AK170151; BAE41598.1; -; mRNA.
DR EMBL; AK170440; BAE41798.1; -; mRNA.
DR EMBL; AL670446; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466615; EDL13381.1; -; Genomic_DNA.
DR EMBL; CH466615; EDL13382.1; -; Genomic_DNA.
DR EMBL; CH466615; EDL13383.1; -; Genomic_DNA.
DR EMBL; CH466615; EDL13384.1; -; Genomic_DNA.
DR EMBL; CH466615; EDL13385.1; -; Genomic_DNA.
DR EMBL; CH466615; EDL13386.1; -; Genomic_DNA.
DR EMBL; BC004777; AAH04777.1; -; mRNA.
DR CCDS; CCDS18876.1; -.
DR RefSeq; NP_001156728.1; NM_001163256.1.
DR RefSeq; NP_598515.3; NM_133754.5.
DR RefSeq; XP_006539277.1; XM_006539214.3.
DR RefSeq; XP_006539278.1; XM_006539215.3.
DR RefSeq; XP_006539279.1; XM_006539216.3.
DR AlphaFoldDB; Q71FD7; -.
DR BMRB; Q71FD7; -.
DR BioGRID; 216573; 2.
DR IntAct; Q71FD7; 2.
DR MINT; Q71FD7; -.
DR STRING; 10090.ENSMUSP00000101410; -.
DR iPTMnet; Q71FD7; -.
DR PhosphoSitePlus; Q71FD7; -.
DR MaxQB; Q71FD7; -.
DR PaxDb; Q71FD7; -.
DR PeptideAtlas; Q71FD7; -.
DR PRIDE; Q71FD7; -.
DR ProteomicsDB; 271556; -.
DR Antibodypedia; 14407; 244 antibodies from 27 providers.
DR DNASU; 74202; -.
DR Ensembl; ENSMUST00000006381; ENSMUSP00000006381; ENSMUSG00000006219.
DR Ensembl; ENSMUST00000105784; ENSMUSP00000101410; ENSMUSG00000006219.
DR Ensembl; ENSMUST00000105785; ENSMUSP00000101411; ENSMUSG00000006219.
DR GeneID; 74202; -.
DR KEGG; mmu:74202; -.
DR UCSC; uc008vos.2; mouse.
DR CTD; 54751; -.
DR MGI; MGI:1921452; Fblim1.
DR VEuPathDB; HostDB:ENSMUSG00000006219; -.
DR eggNOG; KOG1701; Eukaryota.
DR GeneTree; ENSGT00940000159003; -.
DR HOGENOM; CLU_062552_0_0_1; -.
DR InParanoid; Q71FD7; -.
DR OMA; CYQATLE; -.
DR OrthoDB; 642235at2759; -.
DR PhylomeDB; Q71FD7; -.
DR TreeFam; TF320310; -.
DR Reactome; R-MMU-446353; Cell-extracellular matrix interactions.
DR BioGRID-ORCS; 74202; 3 hits in 75 CRISPR screens.
DR ChiTaRS; Fblim1; mouse.
DR PRO; PR:Q71FD7; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q71FD7; protein.
DR Bgee; ENSMUSG00000006219; Expressed in interventricular septum and 195 other tissues.
DR ExpressionAtlas; Q71FD7; baseline and differential.
DR Genevisible; Q71FD7; MM.
DR GO; GO:0030054; C:cell junction; ISO:MGI.
DR GO; GO:0071944; C:cell periphery; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0001650; C:fibrillar center; ISO:MGI.
DR GO; GO:0005925; C:focal adhesion; ISO:MGI.
DR GO; GO:0001725; C:stress fiber; ISS:UniProtKB.
DR GO; GO:0031005; F:filamin binding; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0098609; P:cell-cell adhesion; ISS:UniProtKB.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR GO; GO:0033623; P:regulation of integrin activation; ISS:UniProtKB.
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 Cell adhesion; Cell junction; Cell shape; Cytoplasm; Cytoskeleton;
KW LIM domain; Metal-binding; Reference proteome; Repeat; Zinc.
FT CHAIN 1..375
FT /note="Filamin-binding LIM protein 1"
FT /id="PRO_0000075733"
FT DOMAIN 183..244
FT /note="LIM zinc-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 245..302
FT /note="LIM zinc-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 303..372
FT /note="LIM zinc-binding 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT REGION 1..69
FT /note="Filamin-binding"
FT /evidence="ECO:0000250"
FT REGION 40..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 278..375
FT /note="FERMT2-binding"
FT /evidence="ECO:0000250"
FT COMPBIAS 61..87
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..117
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..149
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..174
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 159
FT /note="I -> R (in Ref. 1; AAQ08090)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 375 AA; 41026 MW; 601DF99A8EB1BB80 CRC64;
MASKPEKRVA SSVFITLAPP RRDVAVSEEV GQAACEARRA RPWEMLPTKT PGAAVGRSPK
TWTPSGKTNA SLSGVTPQLS NGGCSLPPPS LNEEDLDLPP PPPPPSAYLP LPEEEPPVLP
GKSLISDLEQ LHLPPPPPPP PPQAPSKGSS VHPPPGHAIP SEEELPPPPE EPVTLPEREV
STDVCGFCHK PVSPRELAVE AMKRQYHAQC FTCRTCRRQL AGQRFYQKDG RPLCEPCYQD
TLEKCGKCGE VVQEHVIRAL GKAFHPPCFT CVTCARCISD ESFALDSQNQ VYCVADFYRK
FAPVCSICEN PIIPRDGKDA FKIECMGRNF HENCYRCEDC SVLLSVEPTD QGCYPLNDHL
FCKPCHLKRS AAGCC
