ID   FILA_MOUSE              Reviewed;         336 AA.
AC   P11088;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Filaggrin;
DE   Flags: Fragment;
GN   Name=Flg;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX   PubMed=3680218; DOI=10.1016/s0021-9258(18)47775-7;
RA   Rothnagel J.A., Mehrel T., Idler W.W., Roop D.R., Steinert P.M.;
RT   "The gene for mouse epidermal filaggrin precursor. Its partial
RT   characterization, expression, and sequence of a repeating filaggrin unit.";
RL   J. Biol. Chem. 262:15643-15648(1987).
RN   [2]
RP   SEQUENCE REVISION.
RA   Rothnagel J.A.;
RL   Submitted (SEP-1988) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   TISSUE SPECIFICITY.
RX   PubMed=6174530; DOI=10.1083/jcb.92.2.387;
RA   Holbrook K.A., Dale B.A., Brown K.S.;
RT   "Abnormal epidermal keratinization in the repeated epilation mutant
RT   mouse.";
RL   J. Cell Biol. 92:387-397(1982).
RN   [4]
RP   TISSUE SPECIFICITY.
RX   PubMed=24751727; DOI=10.1038/jid.2014.197;
RA   Fischer H., Langbein L., Reichelt J., Praetzel-Wunder S., Buchberger M.,
RA   Ghannadan M., Tschachler E., Eckhart L.;
RT   "Loss of keratin K2 expression causes aberrant aggregation of K10,
RT   hyperkeratosis, and inflammation.";
RL   J. Invest. Dermatol. 134:2579-2588(2014).
CC   -!- FUNCTION: Aggregates keratin intermediate filaments and promotes
CC       disulfide-bond formation among the intermediate filaments during
CC       terminal differentiation of mammalian epidermis.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic granule {ECO:0000269|PubMed:3680218}.
CC       Note=In the stratum granulosum of the epidermis, localized within
CC       keratohyalin granules. In granular keratinocytes and in lower
CC       corneocytes, colocalizes with calpain-1/CAPN1 (By similarity).
CC       {ECO:0000250|UniProtKB:P20930}.
CC   -!- TISSUE SPECIFICITY: Expressed in the granular layer of the epidermis
CC       (at protein level) (PubMed:3680218, PubMed:6174530). Expressed in the
CC       epidermis of the ear (at protein level) (PubMed:24751727).
CC       {ECO:0000269|PubMed:24751727, ECO:0000269|PubMed:3680218,
CC       ECO:0000269|PubMed:6174530}.
CC   -!- PTM: Filaggrin is initially synthesized as a large, insoluble, highly
CC       phosphorylated precursor containing many tandem copies of 248 AA, which
CC       are not separated by large linker sequences. During terminal
CC       differentiation it is dephosphorylated and proteolytically cleaved.
CC   -!- SIMILARITY: Belongs to the S100-fused protein family. {ECO:0000305}.
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DR   EMBL; J03458; AAA75559.1; -; mRNA.
DR   PIR; A28444; A28444.
DR   AlphaFoldDB; P11088; -.
DR   PhosphoSitePlus; P11088; -.
DR   MaxQB; P11088; -.
DR   PaxDb; P11088; -.
DR   PRIDE; P11088; -.
DR   ProteomicsDB; 267588; -.
DR   MGI; MGI:95553; Flg.
DR   InParanoid; P11088; -.
DR   OrthoDB; 904682at2759; -.
DR   ChiTaRS; Flg; mouse.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; P11088; protein.
DR   GO; GO:0001533; C:cornified envelope; IDA:MGI.
DR   GO; GO:0036457; C:keratohyalin granule; IDA:MGI.
DR   GO; GO:1990254; F:keratin filament binding; IDA:MGI.
DR   GO; GO:0030280; F:structural constituent of skin epidermis; IDA:MGI.
DR   GO; GO:0008544; P:epidermis development; IMP:MGI.
DR   GO; GO:0061436; P:establishment of skin barrier; IMP:MGI.
DR   GO; GO:0045109; P:intermediate filament organization; IDA:MGI.
DR   InterPro; IPR003303; Filaggrin.
DR   Pfam; PF03516; Filaggrin; 1.
PE   1: Evidence at protein level;
KW   Developmental protein; Phosphoprotein; Reference proteome.
FT   CHAIN           <1..336
FT                   /note="Filaggrin"
FT                   /id="PRO_0000144037"
FT   REGION          1..313
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        14..57
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        72..102
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        103..117
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        153..194
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        217..255
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        264..308
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
SQ   SEQUENCE   336 AA;  35678 MW;  259F124D3AC0DB2D CRC64;
     PDGSGRSSNR RDRPRQLSPS QSSDSQVHSG VQVEGRRGHS SSANRRAGSS SGSGVQGASA
     GGLAADASRR SGARQGQASA QGRAGSQGQA QGRVSSSADR QGRRGVSESR ASDSEGHSDF
     SEGQAVGAHR QSGAGQRHEQ RSSRGQHGSG YYYEQEHSEE ESDSQHQHGH QHEQQRGHQH
     QHQHQHEHEQ PESGHRQQQS SGRGHQGAHQ EQGRDSARPR GSNQGHSSSR HQADSPRVSA
     RSGSGGRGQS PDASGRSSNR RDRPRQPSPS QSSDSQVHSG VQVEAQRGQS SSANRRAGSS
     SGSGVQGAAA SGQGGYESIF TAKHLDFNQS HSYYYY