ID   FMOD_CHICK              Reviewed;         380 AA.
AC   P51887;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=Fibromodulin;
DE            Short=FM;
DE   AltName: Full=Keratan sulfate proteoglycan fibromodulin;
DE            Short=KSPG fibromodulin;
DE   Flags: Precursor;
GN   Name=FMOD;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Tendon;
RX   PubMed=8760363; DOI=10.1042/bj3170785;
RA   Nurminskaya M.V., Birk D.E.;
RT   "Differential expression of fibromodulin mRNA associated with tendon fibril
RT   growth: isolation and characterization of a chicken fibromodulin cDNA.";
RL   Biochem. J. 317:785-789(1996).
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; U34977; AAC60016.1; -; mRNA.
DR   PIR; S71876; S71876.
DR   RefSeq; NP_990298.1; NM_204967.1.
DR   AlphaFoldDB; P51887; -.
DR   SMR; P51887; -.
DR   STRING; 9031.ENSGALP00000005598; -.
DR   PaxDb; P51887; -.
DR   GeneID; 395814; -.
DR   KEGG; gga:395814; -.
DR   CTD; 2331; -.
DR   VEuPathDB; HostDB:geneid_395814; -.
DR   eggNOG; KOG0619; Eukaryota.
DR   InParanoid; P51887; -.
DR   OrthoDB; 826997at2759; -.
DR   PhylomeDB; P51887; -.
DR   PRO; PR:P51887; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; IEA:InterPro.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   Gene3D; 3.80.10.10; -; 3.
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; Reference proteome; Repeat; Secreted; Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000250"
FT   CHAIN           19..380
FT                   /note="Fibromodulin"
FT                   /id="PRO_0000032742"
FT   DOMAIN          71..109
FT                   /note="LRRNT"
FT   REPEAT          110..131
FT                   /note="LRR 1"
FT   REPEAT          134..147
FT                   /note="LRR 2"
FT   REPEAT          160..180
FT                   /note="LRR 3"
FT   REPEAT          181..202
FT                   /note="LRR 4"
FT   REPEAT          205..227
FT                   /note="LRR 5"
FT   REPEAT          228..248
FT                   /note="LRR 6"
FT   REPEAT          249..270
FT                   /note="LRR 7"
FT   REPEAT          273..293
FT                   /note="LRR 8"
FT   REPEAT          298..317
FT                   /note="LRR 9"
FT   REPEAT          318..339
FT                   /note="LRR 10"
FT   REPEAT          348..371
FT                   /note="LRR 11"
FT   CARBOHYD        89
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        131
FT                   /note="N-linked (GlcNAc...) (keratan sulfate) asparagine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        170
FT                   /note="N-linked (GlcNAc...) (keratan sulfate) asparagine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        205
FT                   /note="N-linked (GlcNAc...) (keratan sulfate) asparagine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        295
FT                   /note="N-linked (GlcNAc...) (keratan sulfate) asparagine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        345
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        338..371
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   380 AA;  43867 MW;  F4613B3CA7FF0E4D CRC64;
     MRWANILLVA GLCRASLGQY NEEEDLAWLQ YYMRQSRMSS YNYMPYYEDE NSPYVYSYVP
     APDTEAEPVP EAQQASSWQC PQECDCPPNF SSAMYCDTRN LRYLPFVPTR MKYVYFQNNQ
     ITAIQEGAFD NATELEWLAL HNNQISSEKM GKRVFAKLKN LERLYMNNNN LTKMPSPLPR
     SLRELHLSYN QISKVPSNAL EGLENLTALY LSHNYIFEMG ASLKGLKSLI LADLSYNHLR
     KVPDGLPMAL EQLYLEYNYI NAIPDDYFKV SPKLLYVRMS HNSLTNQGLS TNTFNSSSIL
     ELDLSYNRLQ KIPRVSTNLE NLYLQGNQIN EFSISSFCTV VDVMNYSRLQ VLRLDGNEIK
     RNAMPPDAPL CLRRATVIEI