ID   FBLI1_BOVIN             Reviewed;         378 AA.
AC   Q1JQB5;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2006, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Filamin-binding LIM protein 1;
DE            Short=FBLP-1;
GN   Name=FBLIM1;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Ascending colon;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
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 PLEKHC1, FLNA, FLNB and FLNC. Interacts with
CC       NKX2-5. {ECO:0000250}.
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; BC116079; AAI16080.1; -; mRNA.
DR   RefSeq; NP_001070423.1; NM_001076955.1.
DR   RefSeq; XP_005217193.1; XM_005217136.3.
DR   RefSeq; XP_005217194.1; XM_005217137.3.
DR   AlphaFoldDB; Q1JQB5; -.
DR   STRING; 9913.ENSBTAP00000024926; -.
DR   PaxDb; Q1JQB5; -.
DR   Ensembl; ENSBTAT00000024926; ENSBTAP00000024926; ENSBTAG00000018725.
DR   Ensembl; ENSBTAT00000076589; ENSBTAP00000067709; ENSBTAG00000018725.
DR   GeneID; 767833; -.
DR   KEGG; bta:767833; -.
DR   CTD; 54751; -.
DR   VEuPathDB; HostDB:ENSBTAG00000018725; -.
DR   VGNC; VGNC:28880; FBLIM1.
DR   eggNOG; KOG1701; Eukaryota.
DR   GeneTree; ENSGT00940000159003; -.
DR   HOGENOM; CLU_062552_0_0_1; -.
DR   InParanoid; Q1JQB5; -.
DR   OMA; CYQATLE; -.
DR   OrthoDB; 642235at2759; -.
DR   TreeFam; TF320310; -.
DR   Proteomes; UP000009136; Chromosome 16.
DR   Bgee; ENSBTAG00000018725; Expressed in trachea and 105 other tissues.
DR   ExpressionAtlas; Q1JQB5; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005925; C:focal adhesion; IBA:GO_Central.
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   2: Evidence at transcript level;
KW   Cell adhesion; Cell junction; Cell shape; Cytoplasm; Cytoskeleton;
KW   LIM domain; Metal-binding; Reference proteome; Repeat; Zinc.
FT   CHAIN           1..378
FT                   /note="Filamin-binding LIM protein 1"
FT                   /id="PRO_0000265104"
FT   DOMAIN          186..247
FT                   /note="LIM zinc-binding 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT   DOMAIN          248..305
FT                   /note="LIM zinc-binding 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT   DOMAIN          306..375
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          38..179
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          281..378
FT                   /note="PLEKHC1-binding"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        100..117
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        136..159
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   378 AA;  41497 MW;  553951E50D1F2FB2 CRC64;
     MASKPEKRVA SSVFITLVPP RRDEAVVEEV RRAACEAWPG RPWESAPTKA PGAGSVGKLR
     SWMPPGRAAA PGPAVPPQLS NGGCSLPPPP LDVDDALPDL DLLPPPPPPP AADLPPPDEE
     PHSAMGASLI SDLEQLHLPP PPPPPQALVE GPPLQPRPSH LKPAEEELPP PPEEPVSFPE
     REASTDICAF CHKTVSPREL AVEAMKRQYH AQCFTCRVCR RQLAGQSFYQ KDGRPLCEPC
     YQDTLEKCGK CGEVVREHII RALGQAFHPS CFTCVTCARR IGDESFALDS QNEVYCLDDF
     YRKFAPVCSI CENPIIPRDG KDAFKIECMG RNFHENCYRC EDCRVLLSVE PTDQGCYPLN
     NRLFCKPCHV KRSAAGCC