FLNB_RABIT
ID FLNB_RABIT Reviewed; 294 AA.
AC Q9MZD2;
DT 07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 93.
DE RecName: Full=Filamin-B;
DE Short=FLN-B;
DE AltName: Full=ABP-280-like protein;
DE AltName: Full=Actin-binding-like protein;
DE AltName: Full=Beta-filamin;
DE AltName: Full=C254;
DE Flags: Fragment;
GN Name=FLNB;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH A HTLV-I VIRAL P13
RP PROTEIN.
RC TISSUE=Lymphocyte;
RX PubMed=11062043; DOI=10.1006/viro.2000.0604;
RA Hou X., Foley S., Cueto M., Robinson M.A.;
RT "The human T-cell leukemia virus type I (HTLV-I) X region encoded protein
RT p13(II) interacts with cellular proteins.";
RL Virology 277:127-135(2000).
CC -!- FUNCTION: Connects cell membrane constituents to the actin
CC cytoskeleton. May promote orthogonal branching of actin filaments and
CC links actin filaments to membrane glycoproteins. Anchors various
CC transmembrane proteins to the actin cytoskeleton (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. Interacts with FLNA, FLNC, INPPL1, ITGB1A, ITGB1D,
CC ITGB3, ITGB6, MYOT, MYOZ1, PSEN1 and PSEN2. Interacts with MICALL2 (By
CC similarity). Interacts with RFLNA and RFLNB (By similarity). Interacts
CC with HTLV-I viral p13 protein. Interacts with ASB2; the interaction
CC targets FLNB for proteasomal degradation (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:Q80X90, ECO:0000269|PubMed:11062043}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex {ECO:0000250}. Cytoplasm,
CC cytoskeleton {ECO:0000250}. Cytoplasm, myofibril, sarcomere, Z line
CC {ECO:0000250|UniProtKB:Q80X90}.
CC -!- PTM: ISGylation prevents ability to interact with the upstream
CC activators of the JNK cascade and inhibits IFNA-induced JNK signaling.
CC {ECO:0000250}.
CC -!- PTM: Ubiquitination by a SCF-like complex containing ASB2 leads to
CC proteasomal degradation which promotes muscle differentiation.
CC {ECO:0000250|UniProtKB:O75369}.
CC -!- SIMILARITY: Belongs to the filamin family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF244365; AAF97050.1; -; mRNA.
DR AlphaFoldDB; Q9MZD2; -.
DR SMR; Q9MZD2; -.
DR STRING; 9986.ENSOCUP00000000722; -.
DR PRIDE; Q9MZD2; -.
DR eggNOG; KOG0518; Eukaryota.
DR InParanoid; Q9MZD2; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0030018; C:Z disc; IEA:UniProtKB-SubCell.
DR GO; GO:0051015; F:actin filament binding; IEA:InterPro.
DR GO; GO:0030036; P:actin cytoskeleton organization; IEA:InterPro.
DR Gene3D; 2.60.40.10; -; 3.
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; PF00630; Filamin; 3.
DR SMART; SM00557; IG_FLMN; 3.
DR SUPFAM; SSF81296; SSF81296; 3.
DR PROSITE; PS50194; FILAMIN_REPEAT; 3.
PE 1: Evidence at protein level;
KW Acetylation; Actin-binding; Cytoplasm; Cytoskeleton; Isopeptide bond;
KW Phosphoprotein; Reference proteome; Repeat; Ubl conjugation.
FT CHAIN <1..294
FT /note="Filamin-B"
FT /id="PRO_0000087300"
FT REPEAT <1..67
FT /note="Filamin 22"
FT REPEAT 71..163
FT /note="Filamin 23"
FT REPEAT 199..293
FT /note="Filamin 24"
FT REGION 164..294
FT /note="Self-association site, tail"
FT /evidence="ECO:0000250"
FT REGION 164..198
FT /note="Hinge 2"
FT /evidence="ECO:0000250"
FT MOD_RES 61
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75369"
FT MOD_RES 157
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75369"
FT MOD_RES 173
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75369"
FT MOD_RES 184
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75369"
FT MOD_RES 210
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q80X90"
FT MOD_RES 216
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q80X90"
FT MOD_RES 268
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O75369"
FT CROSSLNK 160
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ISG15)"
FT /evidence="ECO:0000250"
FT NON_TER 1
SQ SEQUENCE 294 AA; 30895 MW; 9AFDFA24DC242228 CRC64;
GTRLNGAKGK IDAKVHSPSG AVEECHVSEL EPDKYAVRFI PHENGIHTID VKFNGSHVVG
SPFKVRVGEP GQAGNPALVS AYGAGLEGGT TGIQSEFFIN TTRAGPGTLS VTIEGPSKVK
MDCQETPEGY KVMYTPMAPG NYLIGVKYGG PNHIVGSPFK AKVTGQRLVG PGSTNETSSI
LVESVTRSST ETCYSAIPKA SSDASKVTSK GAGLSKAFVG QKSSFLVDCS KAGSNMLLIG
VHGPTTPCEE VSMKHVGSQQ YNVTYVVKER GEYVLAVKWG EEHIPGSPFH VTVP
