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Filamin-C (FLN-C) (ABP-280-like protein) (ABP-L) (Actin-binding-like protein) (Filamin-2) (Gamma-filamin)

 FLNC_RAT                Reviewed;        2726 AA.
D3ZHA0;
09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
20-APR-2010, sequence version 1.
28-FEB-2018, entry version 64.
RecName: Full=Filamin-C;
Short=FLN-C;
AltName: Full=ABP-280-like protein;
AltName: Full=ABP-L;
AltName: Full=Actin-binding-like protein;
AltName: Full=Filamin-2;
AltName: Full=Gamma-filamin;
Name=Flnc; Synonyms=Abpl, Fln2;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Brown Norway;
PubMed=15057822; DOI=10.1038/nature02426;
Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T.,
Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A.,
Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M.,
Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K.,
Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S.,
Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J.,
Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y.,
Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A.,
Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J.,
D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R.,
Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A.,
Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E.,
Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E.,
Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D.,
Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M.,
Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O.,
Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O.,
Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H.,
Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S.,
Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J.,
Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E.,
Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F.,
Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K.,
Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S.,
Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M.,
Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M.,
Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A.,
Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S.,
Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G.,
Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H.,
Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R.,
Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M.,
Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H.,
Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S.,
Collins F.S.;
"Genome sequence of the Brown Norway rat yields insights into
mammalian evolution.";
Nature 428:493-521(2004).
[2]
INTERACTION WITH ANK3.
PubMed=21223964; DOI=10.1016/j.yexcr.2011.01.002;
Maiweilidan Y., Klauza I., Kordeli E.;
"Novel interactions of ankyrins-G at the costameres: the muscle-
specific Obscurin/Titin-Binding-related Domain (OTBD) binds plectin
and filamin C.";
Exp. Cell Res. 317:724-736(2011).
[3]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2234 AND SER-2237, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: Muscle-specific filamin, which plays a central role in
muscle cells, probably by functioning as a large actin-cross-
linking protein. May be involved in reorganizing the actin
cytoskeleton in response to signaling events, and may also display
structural functions at the Z lines in muscle cells. Critical for
normal myogenesis and for maintaining the structural integrity of
the muscle fibers.
-!- SUBUNIT: Homodimer; the filamin repeat 24 and the second hinge
domain are important for dimer formation (By similarity).
Interacts with FLNB, KCND2, INPPL1, ITGB1A, MYOT, MYOZ1 and MYOZ3
(By similarity). Interacts with sarcoglycans SGCD and SGCG (By
similarity). Interacts (via filament repeats 17-18, 20-21 and 24)
with USP25 (isoform USP25m only) (By similarity). Interacts with
FBLIM1 (By similarity). Interacts with KY (By similarity).
Interacts with IGFN1 (By similarity). Interacts with MICALL2 (By
similarity). Interacts with XIRP1; this interaction is mediated by
filamin 20 repeat (By similarity). Interacts with ANK3. Interacts
with SYNPO2 (By similarity). {ECO:0000250,
ECO:0000250|UniProtKB:Q14315, ECO:0000269|PubMed:21223964}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane
{ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm, myofibril,
sarcomere, Z line {ECO:0000250}. Note=A small amount localizes at
membranes. In striated muscle cells, it predominantly localizes in
myofibrillar Z lines, while a minor fraction localizes with
subsarcolemme. Targeting to developing and mature Z lines is
mediated by the intradomain insert (By similarity). {ECO:0000250}.
-!- PTM: Ubiquitinated by FBXL22, leading to proteasomal degradation.
{ECO:0000250}.
-!- SIMILARITY: Belongs to the filamin family. {ECO:0000305}.
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EMBL; AABR06030202; -; NOT_ANNOTATED_CDS; Genomic_DNA.
RefSeq; NP_001178791.1; NM_001191862.1.
UniGene; Rn.22352; -.
ProteinModelPortal; D3ZHA0; -.
SMR; D3ZHA0; -.
BioGrid; 263368; 2.
IntAct; D3ZHA0; 3.
STRING; 10116.ENSRNOP00000027237; -.
iPTMnet; D3ZHA0; -.
PhosphoSitePlus; D3ZHA0; -.
PaxDb; D3ZHA0; -.
PeptideAtlas; D3ZHA0; -.
PRIDE; D3ZHA0; -.
Ensembl; ENSRNOT00000088149; ENSRNOP00000070379; ENSRNOG00000007281.
GeneID; 362332; -.
KEGG; rno:362332; -.
CTD; 2318; -.
RGD; 1308807; Flnc.
eggNOG; KOG0518; Eukaryota.
eggNOG; COG5069; LUCA.
GeneTree; ENSGT00900000140842; -.
InParanoid; D3ZHA0; -.
KO; K04437; -.
OMA; QNIERSP; -.
TreeFam; TF313685; -.
Reactome; R-RNO-446353; Cell-extracellular matrix interactions.
PRO; PR:D3ZHA0; -.
Proteomes; UP000002494; Chromosome 4.
Bgee; ENSRNOG00000007281; -.
ExpressionAtlas; D3ZHA0; baseline and differential.
Genevisible; D3ZHA0; RN.
GO; GO:0043034; C:costamere; TAS:BHF-UCL.
GO; GO:0005737; C:cytoplasm; ISO:RGD.
GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
GO; GO:0005829; C:cytosol; IEA:Ensembl.
GO; GO:0005925; C:focal adhesion; ISO:RGD.
GO; GO:0042383; C:sarcolemma; IDA:BHF-UCL.
GO; GO:0016528; C:sarcoplasm; IDA:BHF-UCL.
GO; GO:0030018; C:Z disc; IEA:UniProtKB-SubCell.
GO; GO:0051015; F:actin filament binding; IEA:InterPro.
GO; GO:0030506; F:ankyrin binding; IPI:BHF-UCL.
GO; GO:0008092; F:cytoskeletal protein binding; ISO:RGD.
GO; GO:0042802; F:identical protein binding; ISO:RGD.
GO; GO:0048747; P:muscle fiber development; ISO:RGD.
CDD; cd00014; CH; 2.
Gene3D; 1.10.418.10; -; 2.
Gene3D; 2.60.40.10; -; 24.
InterPro; IPR001589; Actinin_actin-bd_CS.
InterPro; IPR001715; CH-domain.
InterPro; IPR036872; CH_dom_sf.
InterPro; IPR017868; Filamin/ABP280_repeat-like.
InterPro; IPR001298; Filamin/ABP280_rpt.
InterPro; IPR032461; FLN_C.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR014756; Ig_E-set.
PANTHER; PTHR43998:SF4; PTHR43998:SF4; 1.
Pfam; PF00307; CH; 2.
Pfam; PF00630; Filamin; 23.
SMART; SM00033; CH; 2.
SMART; SM00557; IG_FLMN; 24.
SUPFAM; SSF47576; SSF47576; 1.
SUPFAM; SSF81296; SSF81296; 24.
PROSITE; PS00019; ACTININ_1; 1.
PROSITE; PS00020; ACTININ_2; 1.
PROSITE; PS50021; CH; 2.
PROSITE; PS50194; FILAMIN_REPEAT; 24.
1: Evidence at protein level;
Actin-binding; Complete proteome; Cytoplasm; Cytoskeleton; Membrane;
Methylation; Phosphoprotein; Reference proteome; Repeat;
Ubl conjugation.
CHAIN 1 2726 Filamin-C.
/FTId=PRO_0000429633.
DOMAIN 37 143 Calponin-homology (CH) 1.
{ECO:0000255|PROSITE-ProRule:PRU00044}.
DOMAIN 160 263 Calponin-homology (CH) 2.
{ECO:0000255|PROSITE-ProRule:PRU00044}.
REPEAT 271 369 Filamin 1.
REPEAT 371 469 Filamin 2.
REPEAT 470 566 Filamin 3.
REPEAT 567 659 Filamin 4.
REPEAT 663 759 Filamin 5.
REPEAT 760 862 Filamin 6.
REPEAT 863 961 Filamin 7.
REPEAT 962 1057 Filamin 8.
REPEAT 1058 1150 Filamin 9.
REPEAT 1151 1245 Filamin 10.
REPEAT 1246 1345 Filamin 11.
REPEAT 1346 1438 Filamin 12.
REPEAT 1439 1534 Filamin 13.
REPEAT 1535 1631 Filamin 14.
REPEAT 1636 1735 Filamin 15.
REPEAT 1760 1854 Filamin 16.
REPEAT 1855 1947 Filamin 17.
REPEAT 1948 2034 Filamin 18.
REPEAT 2037 2129 Filamin 19.
REPEAT 2245 2307 Filamin 20; mediates interaction with
XIRP1. {ECO:0000255|PROSITE-
ProRule:PRU00087}.
REPEAT 2310 2402 Filamin 21.
REPEAT 2404 2497 Filamin 22.
REPEAT 2501 2593 Filamin 23.
REPEAT 2631 2725 Filamin 24.
REGION 1 260 Actin-binding.
REGION 1736 1759 Hinge 1.
REGION 2163 2244 Intradomain insert; mediate targeting to
Z lines. {ECO:0000250}.
REGION 2404 2725 Interaction with INPPL1. {ECO:0000250}.
REGION 2594 2726 Self-association site, tail.
{ECO:0000250}.
REGION 2594 2630 Hinge 2.
MOD_RES 5 5 Phosphoserine.
{ECO:0000250|UniProtKB:Q14315}.
MOD_RES 1003 1003 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:Q8VHX6}.
MOD_RES 1162 1162 Phosphoserine.
{ECO:0000250|UniProtKB:Q14315}.
MOD_RES 1339 1339 Phosphoserine.
{ECO:0000250|UniProtKB:Q14315}.
MOD_RES 2043 2043 Phosphoserine.
{ECO:0000250|UniProtKB:Q14315}.
MOD_RES 2234 2234 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 2237 2237 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 2239 2239 Phosphothreonine.
{ECO:0000250|UniProtKB:Q14315}.
MOD_RES 2587 2587 Phosphoserine.
{ECO:0000250|UniProtKB:Q14315}.
MOD_RES 2618 2618 Phosphoserine.
{ECO:0000250|UniProtKB:Q14315}.
MOD_RES 2621 2621 Phosphoserine.
{ECO:0000250|UniProtKB:Q14315}.
MOD_RES 2633 2633 Phosphoserine.
{ECO:0000250|UniProtKB:Q14315}.
MOD_RES 2715 2715 Phosphoserine.
{ECO:0000250|UniProtKB:Q14315}.
MOD_RES 2719 2719 Phosphoserine.
{ECO:0000250|UniProtKB:Q14315}.
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


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