FLNC_RAT
ID FLNC_RAT Reviewed; 2726 AA.
AC D3ZHA0;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Filamin-C;
DE Short=FLN-C;
DE AltName: Full=ABP-280-like protein;
DE AltName: Full=ABP-L;
DE AltName: Full=Actin-binding-like protein;
DE AltName: Full=Filamin-2;
DE AltName: Full=Gamma-filamin;
GN Name=Flnc; Synonyms=Abpl, Fln2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP INTERACTION WITH ANK3.
RX PubMed=21223964; DOI=10.1016/j.yexcr.2011.01.002;
RA Maiweilidan Y., Klauza I., Kordeli E.;
RT "Novel interactions of ankyrins-G at the costameres: the muscle-specific
RT Obscurin/Titin-Binding-related Domain (OTBD) binds plectin and filamin C.";
RL Exp. Cell Res. 317:724-736(2011).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2234 AND SER-2237, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Muscle-specific filamin, which plays a central role in
CC sarcomere assembly and organization. Critical for normal myogenesis, it
CC probably functions as a large actin-cross-linking protein with
CC structural functions at the Z lines in muscle cells. May be involved in
CC reorganizing the actin cytoskeleton in response to signaling events.
CC {ECO:0000250|UniProtKB:Q14315}.
CC -!- SUBUNIT: Homodimer; the filamin repeat 24 and the second hinge domain
CC are important for dimer formation (By similarity). Interacts with FLNB,
CC KCND2, INPPL1, ITGB1A, MYOT, MYOZ1 and MYOZ3 (By similarity). Interacts
CC with sarcoglycans SGCD and SGCG (By similarity). Interacts (via
CC filament repeats 17-18, 20-21 and 24) with USP25 (isoform USP25m only)
CC (By similarity). Interacts with FBLIM1 (By similarity). Interacts with
CC KY (By similarity). Interacts with IGFN1 (By similarity). Interacts
CC with MICALL2 (By similarity). Interacts with XIRP1; this interaction is
CC mediated by filamin 20 repeat (By similarity). Interacts with ANK3.
CC Interacts with SYNPO2 (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:Q14315, ECO:0000269|PubMed:21223964}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}. Cytoplasm, cytoskeleton
CC {ECO:0000250}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000250}.
CC Note=A small amount localizes at membranes. In striated muscle cells,
CC it predominantly localizes in myofibrillar Z lines, while a minor
CC fraction localizes with subsarcolemme. Targeting to developing and
CC mature Z lines is mediated by the intradomain insert (By similarity).
CC {ECO:0000250}.
CC -!- PTM: Ubiquitinated by FBXL22, leading to proteasomal degradation.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the filamin family. {ECO:0000305}.
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DR EMBL; AABR06030202; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001178791.1; NM_001191862.1.
DR SMR; D3ZHA0; -.
DR BioGRID; 263368; 2.
DR IntAct; D3ZHA0; 3.
DR STRING; 10116.ENSRNOP00000027237; -.
DR iPTMnet; D3ZHA0; -.
DR PhosphoSitePlus; D3ZHA0; -.
DR jPOST; D3ZHA0; -.
DR PaxDb; D3ZHA0; -.
DR PeptideAtlas; D3ZHA0; -.
DR PRIDE; D3ZHA0; -.
DR Ensembl; ENSRNOT00000027237; ENSRNOP00000027237; ENSRNOG00000007281.
DR GeneID; 362332; -.
DR KEGG; rno:362332; -.
DR CTD; 2318; -.
DR RGD; 1308807; Flnc.
DR eggNOG; KOG0518; Eukaryota.
DR GeneTree; ENSGT00940000153588; -.
DR HOGENOM; CLU_000783_0_0_1; -.
DR InParanoid; D3ZHA0; -.
DR OMA; YPVMAGK; -.
DR OrthoDB; 35998at2759; -.
DR TreeFam; TF313685; -.
DR Reactome; R-RNO-446353; Cell-extracellular matrix interactions.
DR PRO; PR:D3ZHA0; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000007281; Expressed in skeletal muscle tissue and 14 other tissues.
DR ExpressionAtlas; D3ZHA0; baseline and differential.
DR Genevisible; D3ZHA0; RN.
DR GO; GO:0043034; C:costamere; TAS:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0042383; C:sarcolemma; IDA:BHF-UCL.
DR GO; GO:0016528; C:sarcoplasm; IDA:BHF-UCL.
DR GO; GO:0030018; C:Z disc; IEA:UniProtKB-SubCell.
DR GO; GO:0051015; F:actin filament binding; IEA:InterPro.
DR GO; GO:0030506; F:ankyrin binding; IPI:BHF-UCL.
DR GO; GO:0008092; F:cytoskeletal protein binding; ISO:RGD.
DR GO; GO:0055001; P:muscle cell development; ISO:RGD.
DR GO; GO:0045214; P:sarcomere organization; ISS:UniProtKB.
DR CDD; cd00014; CH; 2.
DR Gene3D; 1.10.418.10; -; 2.
DR Gene3D; 2.60.40.10; -; 24.
DR InterPro; IPR001589; Actinin_actin-bd_CS.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR036872; CH_dom_sf.
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; 2.
DR Pfam; PF00307; CH; 2.
DR Pfam; PF00630; Filamin; 23.
DR SMART; SM00033; CH; 2.
DR SMART; SM00557; IG_FLMN; 24.
DR SUPFAM; SSF47576; SSF47576; 1.
DR SUPFAM; SSF81296; SSF81296; 24.
DR PROSITE; PS00019; ACTININ_1; 1.
DR PROSITE; PS00020; ACTININ_2; 1.
DR PROSITE; PS50021; CH; 2.
DR PROSITE; PS50194; FILAMIN_REPEAT; 24.
PE 1: Evidence at protein level;
KW Actin-binding; Cytoplasm; Cytoskeleton; Membrane; Methylation;
KW Phosphoprotein; Reference proteome; Repeat; Ubl conjugation.
FT CHAIN 1..2726
FT /note="Filamin-C"
FT /id="PRO_0000429633"
FT DOMAIN 37..143
FT /note="Calponin-homology (CH) 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 160..263
FT /note="Calponin-homology (CH) 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT REPEAT 271..369
FT /note="Filamin 1"
FT REPEAT 371..469
FT /note="Filamin 2"
FT REPEAT 470..566
FT /note="Filamin 3"
FT REPEAT 567..659
FT /note="Filamin 4"
FT REPEAT 663..759
FT /note="Filamin 5"
FT REPEAT 760..862
FT /note="Filamin 6"
FT REPEAT 863..961
FT /note="Filamin 7"
FT REPEAT 962..1057
FT /note="Filamin 8"
FT REPEAT 1058..1150
FT /note="Filamin 9"
FT REPEAT 1151..1245
FT /note="Filamin 10"
FT REPEAT 1246..1345
FT /note="Filamin 11"
FT REPEAT 1346..1438
FT /note="Filamin 12"
FT REPEAT 1439..1534
FT /note="Filamin 13"
FT REPEAT 1535..1631
FT /note="Filamin 14"
FT REPEAT 1636..1735
FT /note="Filamin 15"
FT REPEAT 1760..1854
FT /note="Filamin 16"
FT REPEAT 1855..1947
FT /note="Filamin 17"
FT REPEAT 1948..2034
FT /note="Filamin 18"
FT REPEAT 2037..2129
FT /note="Filamin 19"
FT REPEAT 2245..2307
FT /note="Filamin 20; mediates interaction with XIRP1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00087"
FT REPEAT 2310..2402
FT /note="Filamin 21"
FT REPEAT 2404..2497
FT /note="Filamin 22"
FT REPEAT 2501..2593
FT /note="Filamin 23"
FT REPEAT 2631..2725
FT /note="Filamin 24"
FT REGION 1..260
FT /note="Actin-binding"
FT REGION 1736..1759
FT /note="Hinge 1"
FT REGION 2163..2244
FT /note="Intradomain insert; mediate targeting to Z lines"
FT /evidence="ECO:0000250"
FT REGION 2194..2214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2241..2261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2404..2725
FT /note="Interaction with INPPL1"
FT /evidence="ECO:0000250"
FT REGION 2594..2726
FT /note="Self-association site, tail"
FT /evidence="ECO:0000250"
FT REGION 2594..2630
FT /note="Hinge 2"
FT COMPBIAS 2194..2211
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 5
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14315"
FT MOD_RES 1003
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q8VHX6"
FT MOD_RES 1162
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14315"
FT MOD_RES 1339
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14315"
FT MOD_RES 2043
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14315"
FT MOD_RES 2234
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 2237
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 2239
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14315"
FT MOD_RES 2587
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14315"
FT MOD_RES 2618
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14315"
FT MOD_RES 2621
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14315"
FT MOD_RES 2633
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14315"
FT MOD_RES 2715
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14315"
FT MOD_RES 2719
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14315"
SQ SEQUENCE 2726 AA; 290986 MW; A91CE65E935EC2CD CRC64;
MMNNSNYSDA SGLGLLDEAD EMPSTEKDLA EDAPWKKIQQ NTFTRWCNEH LKCVGKRLTD
LQRDLSDGLR LIALLEVLSQ KRMYRKFHPR PNFRQMKLEN VSVALEFLER EHIKLVSIDS
KAIVDGNLKL ILGLIWTLIL HYSISMPMWE DEDDEDARKQ TPKQRLLGWI QNKVPQLPIT
NFNRDWQDGK ALGALVDNCA PGLCPDWEAW DPNQPVQNAR EAMQQADDWL GVPQVIAPEE
IVDPNVDEHS VMTYLSQFPK AKLKPGAPVR SKQLNPKKAI AYGPGIEPQG NTVLQPAHFT
VQTVDAGVGE VLVYIEDPEG HTEEAKVVPN NDKDRTYAVS YVPKVAGLHK VTVLFAGQNI
ERSPFEVNVG MALGDANKVS ARGPGLEPVG NVANKPTYFD IYTAGAGTGD VAVVIVDPQG
RRDTVEVALE DKGDNTFRCT YRPVMEGPHT VHVAFAGAPI TRSPFPVHVA EACNPNACRA
SGRGLQPKGV RVKEVADFKV FTKGAGSGEL KVTVKGPKGT EEPVKVREAG DGVFECEYYP
VIPGKYVVTI TWGGYAIPRS PFEVQVSPEA GAQKVRAWGP GLETGQVGKS ADFVVEAIGT
EVGTLGFSIE GPSQAKIECD DRGDGSCDVR YWPTEPGEYA VHVICDDEDI RDSPFIAHIQ
PAPPDCFPDK VKAFGPGLEP TGCIVDRPAE FTIDARAAGK GDLKLYAQDA DGCPIDIKVI
PNGDGTFRCS YVPTKPIKHT VIISWGGVNV PKSPFRVNVG EGSHPERVKV YGPGVEKTGL
KANEPTYFTV DCSEAGQGDV SIGIKCAPGV VGPAEADIDF DIIKNDNDTF TVKYTPPGAG
HYTIMVLFAN QEIPASPFHI KVDPSHDASK VKAEGPGLSR TGVEVGKPTH FTVLTKGAGK
AKLDVHFAGA AKGEAVRDFE IIDNHDYSYT VKYTAVQQGN MAVTVTYGGD PVPKSPFVVN
VAPPLDLSKV KVQGLNSKVA VGEEQAFLVN TRGAGGQGQL DVRMTSPSRR PIPCKLEPGS
GAEAQAVRYM PPEEGPYKVD ITYDGHPVPG SPFAVEGVLP PDPSKVCAYG PGLKGGLVGT
PAPFSIDTKG AGTGGLGLTV EGPCEAKIEC QDNGDGSCAV SYLPTEPGEY TINILFAEAH
IPGSPFKATI QPVFDPSKVR ASGPGLERGK AGEAATFTVD CSEAGEAELT IEILSDAGVK
AEVLIHNNAD GTYHITYSPA FPGTYTITIK YGGHPIPKFP TRVHVQPAVD TSGIKVSGPG
VEPHGVLREV TTEFTVDARS LTATGGNHVT ARVLNPSGAK TDTYVTDNGD GTYRVQYTAY
EEGVHLVEVL YDEVAVPKSP FRVGVTEGCD PTRVRAFGPG LEGGLVNKAN RFTVETRGAG
TGGLGLAIEG PSEAKMSCKD NKDGSCTVEY VPFTPGDYDV NITFGGQPIP GSPFRVPVKD
VVDPGKVKCS GPGLGTGVRA RVPQTFTVDC SQAGRAPLQV AVLGPTGVAE PVEVRDNGDG
THTVHYTPAT DGPYTVAVKY ADQEVPRSPF KIKVLPAHDA SKVRASGPGL NASGIPASLP
VEFTIDARDA GEGLLTVQIL DPEGKPKKAN IRDNGDGTYT VSYLPDMSGR YTITIKYGGD
EIPYSPFRIH ALPTGDASKC LVTVSIGGHG LGACLGPRIQ IGEETVITVD AKAAGKGKVT
CTVSTPDGAE LDVDVVENHD GTFDIYYTAP EPGKYVITIR FGGEHIPNSP FHVLACDPLP
HVEEPAEVLQ LHQPYAPLRP GTCPTHWATE EPVVPVEPLE SMLRPFNLVI PFTVQKGELT
GEVRMPSGKT ARPNITDNKD GTITVRYAPT EKGLHQMGIK YDGNHIPGSP LQFYVDAINS
GHVSAYGPGL SHGMVNKPAT FTIVTKDAGE GGLSLAVEGP SKAEITCKDN KDGTCTVSYL
PTAPGDYSII VRFDDKHIPG SPFTAKITGD DSMRTSQLNV GTSTDVSLKI TEGDLSQLTA
SIRAPSGNEE PCLLKRLPNR HIGISFTPKE VGEHVVSVRK SGKHVTNSPF KILVGPSEIG
DASKVRVWGK GLSEGQTFQV AEFIVDTRNA GYGGLGLSIE GPSKVDINCE DMEDGTCKVT
YCPTEPGTYI INIKFADKHV PGSPFTVKVT GEGRMKESIT RRRQAPSIAT IGSTCDLNLK
IPGNWFQMVS AQERLTRTFT RSSHTYTRTE RTEISKTRGG ETKREVRVEE STQVGGDPFP
AVFGDFLGRE RLGSFGSITR QQEGEASSQD MTAQVTSPSG KTEAAEIVEG EDSAYSVRFV
PQEMGPHTVA VKYRGQHVPG SPFQFTVGPL GEGGAHKVRA GGTGLERGVA GVPAEFSIWT
REAGAGGLSI AVEGPSKAEI AFEDRKDGSC GVSYVVQEPG DYEVSIKFND EHIPDSPFVV
PVASLSDDAR RLTVTSLQET GLKVNQPASF AVQLNGARGV IDARVHTPSG AVEECYVSEL
DSDKHTIRFI PHENGVHSID VKFNGAHIPG SPFKIRVGEQ SQAGDPGLVS AYGPGLEGGT
TGVSSEFIVN TQNAGSGALS VTIDGPSKVQ LDCRECPEGH VVTYTPMAPG NYLIAIKYGG
PQHIVGSPFK AKVTGPRLSG GHSLHETSTV LVETVTKSSS SRGASYSSIP KFSSDASKVV
TRGPGLSQAF VGQKNSFTVD CSKAGTNMMM VGVHGPKTPC EEVYVKHMGN RVYNVTYTVK
EKGDYILIVK WGDESVPGSP FKVNVP
