FMOD_RAT
ID FMOD_RAT Reviewed; 376 AA.
AC P50609;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 128.
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 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 [MRNA].
RC STRAIN=Sprague-Dawley;
RA Krull N.;
RL Submitted (DEC-1994) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Affects the rate of fibrils formation. May have a primary
CC role in collagen fibrillogenesis (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Binds to type I and type II collagen. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix.
CC -!- PTM: Binds keratan sulfate chains. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the small leucine-rich proteoglycan (SLRP)
CC family. SLRP class II subfamily. {ECO:0000305}.
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DR EMBL; X82152; CAA57648.1; -; mRNA.
DR RefSeq; NP_542429.1; NM_080698.1.
DR AlphaFoldDB; P50609; -.
DR SMR; P50609; -.
DR BioGRID; 249092; 1.
DR IntAct; P50609; 1.
DR STRING; 10116.ENSRNOP00000004382; -.
DR GlyGen; P50609; 5 sites.
DR PaxDb; P50609; -.
DR PRIDE; P50609; -.
DR GeneID; 64507; -.
DR KEGG; rno:64507; -.
DR UCSC; RGD:619769; rat.
DR CTD; 2331; -.
DR RGD; 619769; Fmod.
DR eggNOG; KOG0619; Eukaryota.
DR InParanoid; P50609; -.
DR OrthoDB; 826997at2759; -.
DR PhylomeDB; P50609; -.
DR Reactome; R-RNO-2022854; Keratan sulfate biosynthesis.
DR Reactome; R-RNO-2022857; Keratan sulfate degradation.
DR PRO; PR:P50609; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IDA:RGD.
DR GO; GO:0005576; C:extracellular region; IDA:RGD.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0042476; P:odontogenesis; IEP:RGD.
DR GO; GO:0043588; P:skin development; IEP:RGD.
DR GO; GO:0042060; P:wound healing; IEP:RGD.
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_0000032741"
FT DOMAIN 67..105
FT /note="LRRNT"
FT REPEAT 106..127
FT /note="LRR 1"
FT REPEAT 130..143
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; 43219 MW; 9C3298675CE3714A CRC64;
MQWASILLLR GLCSLSQGQY EEDSHWWLQY LRNQQSTYYD PYDTYPYETS DPYPYEVEEG
PAYAYGAPPP PEPRDCPQEC DCPPNFPTAM YCDNRNLKYL PFVPSRMKYV YFQNNQIAAI
QEGVFDNATG LLWIALHGNQ ITSDKIGRKV FSKLRHLERL YLDHNNLTRM PGPLPRSLRE
LHLDHNQISR VPNNALEGLE NLTALYLHHN EIQEVGSSMR GLRSLILLDL SYNHLRRVPD
GLPSALEQLY LEHNNVYTVP DSYFRGSPKL LYVRLSHNSL TNNGLATNTF NSSSLLELDL
SYNQLQKIPP VNTNLENLYL QGNRINEFSI SSFCTVVDVM NFSKLQVLRL DGNEIKRSAM
PVDAPLCLRL ASLIEI
