ID   FBLI1_PONAB             Reviewed;         375 AA.
AC   Q5REN1;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 74.
DE   RecName: Full=Filamin-binding LIM protein 1;
DE            Short=FBLP-1;
GN   Name=FBLIM1;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Heart;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) 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 FERMT2, 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; CR857491; CAH89776.1; -; mRNA.
DR   RefSeq; NP_001127194.1; NM_001133722.1.
DR   AlphaFoldDB; Q5REN1; -.
DR   SMR; Q5REN1; -.
DR   STRING; 9601.ENSPPYP00000002131; -.
DR   GeneID; 100174248; -.
DR   KEGG; pon:100174248; -.
DR   CTD; 54751; -.
DR   eggNOG; KOG1701; Eukaryota.
DR   InParanoid; Q5REN1; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
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..375
FT                   /note="Filamin-binding LIM protein 1"
FT                   /id="PRO_0000075734"
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..70
FT                   /note="Filamin-binding"
FT                   /evidence="ECO:0000250"
FT   REGION          43..119
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          137..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        101..118
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        138..167
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   375 AA;  41108 MW;  4B36D5753213634D CRC64;
     MASKPEKRVA SSVFITLAPL RRDVAMAEEV RQAVCEARRG RPWEAPAPMK TPEAGLEGRP
     SPWTPPGRAA ATVPAAPMQL SNGGCPPPPP VLDGEDALPD LDLFPPPPPP PPVLLPSEEE
     APAPMGASLI ADLEQLHLSP PLPPPPPQAP AERPSVQPSP LRPMEEELPP PPAERVEKGA
     STDICAFCHK TVSPRELAVE AMKRQYHAQC FTCRTCRRQL AGQSFYQKDG RPLCEPCYQD
     TLERCGKCGE VVRDHIIRAL GQAFHPSCFT CVTCARCIGD ESFALGSQNE VYCLDDFYRK
     FAPVCSICEN PIIPRDGKDA FKIECMGRSF HENCYRCEDC RILLSVEPTD QGCYPLNNRL
     FCKPCHVKRS AAGCC