FMOD_MOUSE
ID FMOD_MOUSE Reviewed; 376 AA.
AC P50608;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Fibromodulin;
DE Short=FM;
DE AltName: Full=Collagen-binding 59 kDa protein;
DE AltName: Full=Keratan sulfate proteoglycan fibromodulin;
DE Short=KSPG fibromodulin;
DE Flags: Precursor;
GN Name=Fmod;
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].
RC STRAIN=C57BL/6J; TISSUE=Cartilage;
RX PubMed=11311118; DOI=10.1042/bj3550577;
RA Saeaemaenen A.-M.K., Salminen H.J., Rantakokko A.J., Heinegaard D.,
RA Vuorio E.I.;
RT "Murine fibromodulin: cDNA and genomic structure, and age-related
RT expression and distribution in the knee joint.";
RL Biochem. J. 355:577-585(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C3H/He; TISSUE=Osteoblast;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Affects the rate of fibrils formation. May have a primary
CC role in collagen fibrillogenesis.
CC -!- SUBUNIT: Binds to type I and type II collagen.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix.
CC -!- TISSUE SPECIFICITY: Highest levels observed in knee epiphysis, in
CC calvarial and diaphyseal bone, in nasal and costal cartilage, in the
CC eye, and in bladder. In mature knee joint it is mostly present in the
CC proliferating zone of growth plate. It is also observed in ligaments,
CC especially at insertion sites, in the junction between meniscus and
CC joint capsule, in the perimysium of skeletal muscle and in the
CC periosteum.
CC -!- DEVELOPMENTAL STAGE: Highest levels between 5 days and 1 month of age.
CC Thereafter, the expression of declined to a level of approx. 35% of
CC maximum, and remained constant throughout the rest of the observation
CC period.
CC -!- PTM: Binds keratan sulfate chains. {ECO:0000250}.
CC -!- PTM: Sulfated on tyrosine residue(s). {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the small leucine-rich proteoglycan (SLRP)
CC family. SLRP class II subfamily. {ECO:0000305}.
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DR EMBL; X94998; CAA64454.1; -; mRNA.
DR EMBL; BC064779; AAH64779.1; -; mRNA.
DR CCDS; CCDS15301.1; -.
DR RefSeq; NP_067330.1; NM_021355.3.
DR AlphaFoldDB; P50608; -.
DR SMR; P50608; -.
DR BioGRID; 199715; 1.
DR STRING; 10090.ENSMUSP00000035489; -.
DR GlyGen; P50608; 5 sites.
DR iPTMnet; P50608; -.
DR PhosphoSitePlus; P50608; -.
DR PaxDb; P50608; -.
DR PeptideAtlas; P50608; -.
DR PRIDE; P50608; -.
DR ProteomicsDB; 267606; -.
DR Antibodypedia; 34544; 294 antibodies from 28 providers.
DR DNASU; 14264; -.
DR Ensembl; ENSMUST00000048183; ENSMUSP00000035489; ENSMUSG00000041559.
DR GeneID; 14264; -.
DR KEGG; mmu:14264; -.
DR UCSC; uc007crd.1; mouse.
DR CTD; 2331; -.
DR MGI; MGI:1328364; Fmod.
DR VEuPathDB; HostDB:ENSMUSG00000041559; -.
DR eggNOG; KOG0619; Eukaryota.
DR GeneTree; ENSGT00940000157007; -.
DR HOGENOM; CLU_000288_186_4_1; -.
DR InParanoid; P50608; -.
DR OMA; YVRMSHN; -.
DR OrthoDB; 826997at2759; -.
DR PhylomeDB; P50608; -.
DR TreeFam; TF334562; -.
DR Reactome; R-MMU-2022854; Keratan sulfate biosynthesis.
DR Reactome; R-MMU-2022857; Keratan sulfate degradation.
DR BioGRID-ORCS; 14264; 3 hits in 71 CRISPR screens.
DR PRO; PR:P50608; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; P50608; protein.
DR Bgee; ENSMUSG00000041559; Expressed in vault of skull and 261 other tissues.
DR ExpressionAtlas; P50608; baseline and differential.
DR Genevisible; P50608; MM.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; ISO:MGI.
DR GO; GO:0005576; C:extracellular region; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR Gene3D; 3.80.10.10; -; 2.
DR InterPro; IPR027215; Fibromodulin.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR000372; LRRNT.
DR PANTHER; PTHR45712:SF4; PTHR45712:SF4; 1.
DR Pfam; PF13855; LRR_8; 3.
DR Pfam; PF01462; LRRNT; 1.
DR SMART; SM00369; LRR_TYP; 8.
DR SMART; SM00013; LRRNT; 1.
DR PROSITE; PS51450; LRR; 9.
PE 2: Evidence at transcript level;
KW Disulfide bond; Extracellular matrix; Glycoprotein; Leucine-rich repeat;
KW Proteoglycan; Pyrrolidone carboxylic acid; Reference proteome; Repeat;
KW Secreted; Signal; Sulfation.
FT SIGNAL 1..18
FT /evidence="ECO:0000250"
FT CHAIN 19..376
FT /note="Fibromodulin"
FT /id="PRO_0000032740"
FT DOMAIN 67..105
FT /note="LRRNT"
FT REPEAT 106..127
FT /note="LRR 1"
FT REPEAT 130..151
FT /note="LRR 2"
FT REPEAT 156..176
FT /note="LRR 3"
FT REPEAT 177..198
FT /note="LRR 4"
FT REPEAT 201..222
FT /note="LRR 5"
FT REPEAT 224..245
FT /note="LRR 6"
FT REPEAT 246..266
FT /note="LRR 7"
FT REPEAT 269..289
FT /note="LRR 8"
FT REPEAT 294..315
FT /note="LRR 9"
FT REPEAT 316..335
FT /note="LRR 10"
FT REPEAT 344..367
FT /note="LRR 11"
FT MOD_RES 19
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250|UniProtKB:P13605"
FT MOD_RES 20
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250"
FT MOD_RES 38
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250"
FT MOD_RES 53
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250"
FT MOD_RES 55
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250"
FT MOD_RES 63
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250"
FT MOD_RES 65
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250"
FT CARBOHYD 127
FT /note="N-linked (GlcNAc...) (keratan sulfate) asparagine"
FT /evidence="ECO:0000250"
FT CARBOHYD 166
FT /note="N-linked (GlcNAc...) (keratan sulfate) asparagine"
FT /evidence="ECO:0000250"
FT CARBOHYD 201
FT /note="N-linked (GlcNAc...) (keratan sulfate) asparagine"
FT /evidence="ECO:0000250"
FT CARBOHYD 291
FT /note="N-linked (GlcNAc...) (keratan sulfate) asparagine"
FT /evidence="ECO:0000250"
FT CARBOHYD 341
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 334..367
FT /evidence="ECO:0000250"
SQ SEQUENCE 376 AA; 43055 MW; 45A9EDDB0BADA85B CRC64;
MQWASVLLLA GLCSLSQGQY DEDSHWWIQY LRNQQSTYYD PYDPYPYEPS EPYPYGVEEG
PAYAYGAPPP PEPRDCPQEC DCPPNFPTAM YCDNRNLKYL PFVPSRMKYV YFQNNQISAI
QEGVFDNATG LLWVALHGNQ ITSDKVGRKV FSKLRHLERL YLDHNNLTRM PGPLPRSLRE
LHLDHNQISR VPNNALEGLE NLTALYLHHN EIQEVGSSMR GLRSLILLDL SYNHLRRVPD
GLPSALEQLY LEHNNVYTVP DSYFRGSPKL LYVRLSHNSL TNNGLATNTF NSSSLLELDL
SYNQLQKIPP VNTNLENLYL QGNRINEFSI SSFCTVVDVM NFSKLQVLRL DGNEIKRSAM
PVDAPLCLRL ANLIEI
