ID   FMOD_PIG                Reviewed;         147 AA.
AC   Q9TTB4;
DT   20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 104.
DE   RecName: Full=Fibromodulin;
DE            Short=FM;
DE   AltName: Full=Keratan sulfate proteoglycan lumican;
DE            Short=KSPG fibromodulin;
DE   Flags: Fragment;
GN   Name=FMOD;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Skin;
RA   Wang J.F., Boykiw R.H., Reno C.R., Olson M.E., Hart D.A.;
RT   "Cloning and sequencing of porcine matrix molecules.";
RL   Submitted (JUN-1999) 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   -!- MISCELLANEOUS: Incorrect gene name (LUM) has been attributed by Ref.1.
CC       LUM and FMOD are two different genes but members of the same family.
CC   -!- SIMILARITY: Belongs to the small leucine-rich proteoglycan (SLRP)
CC       family. SLRP class II subfamily. {ECO:0000305}.
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DR   EMBL; AF159383; AAF19154.1; -; mRNA.
DR   AlphaFoldDB; Q9TTB4; -.
DR   SMR; Q9TTB4; -.
DR   STRING; 9823.ENSSSCP00000016193; -.
DR   PaxDb; Q9TTB4; -.
DR   PeptideAtlas; Q9TTB4; -.
DR   eggNOG; KOG0619; Eukaryota.
DR   HOGENOM; CLU_000288_186_4_1; -.
DR   InParanoid; Q9TTB4; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
DR   Genevisible; Q9TTB4; SS.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; IEA:InterPro.
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   PANTHER; PTHR45712:SF4; PTHR45712:SF4; 1.
DR   Pfam; PF13855; LRR_8; 2.
DR   SMART; SM00369; LRR_TYP; 4.
DR   PROSITE; PS51450; LRR; 6.
PE   2: Evidence at transcript level;
KW   Extracellular matrix; Glycoprotein; Leucine-rich repeat; Proteoglycan;
KW   Reference proteome; Repeat; Secreted; Sulfation.
FT   CHAIN           <1..>147
FT                   /note="Fibromodulin"
FT                   /id="PRO_0000180084"
FT   REPEAT          <1..15
FT                   /note="LRR 1"
FT   REPEAT          16..37
FT                   /note="LRR 2"
FT   REPEAT          40..61
FT                   /note="LRR 3"
FT   REPEAT          63..84
FT                   /note="LRR 4"
FT   REPEAT          85..105
FT                   /note="LRR 5"
FT   REPEAT          108..128
FT                   /note="LRR 6"
FT   REPEAT          133..>147
FT                   /note="LRR 7"
FT   CARBOHYD        5
FT                   /note="N-linked (GlcNAc...) (keratan sulfate) asparagine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        40
FT                   /note="N-linked (GlcNAc...) (keratan sulfate) asparagine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        130
FT                   /note="N-linked (GlcNAc...) (keratan sulfate) asparagine"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
FT   NON_TER         147
SQ   SEQUENCE   147 AA;  16686 MW;  652B5231CAE27EF6 CRC64;
     LDHNNLTRMP GPLPRSLREL HLDHNQISRV PNNALEGLEN LTALYLQHNE IQEVGSSMRG
     LRSLILLDLS YNHLRKVPDG LPSALEQLYL EHNNVYSVPD SYFRGSPKLL YVRLSHNSLT
     NNGLASNTFN SSSLLELDLS YNQLQKI