FMOD_BOVIN
ID FMOD_BOVIN Reviewed; 376 AA.
AC P13605; A7E3X1; Q3SWX6;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 2.
DT 03-AUG-2022, entry version 152.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 91-106 AND 275-282.
RX PubMed=2531085; DOI=10.1002/j.1460-2075.1989.tb08399.x;
RA Oldberg A., Antonsson P., Lindblom K., Heinegaard D.;
RT "A collagen-binding 59-kd protein (fibromodulin) is structurally related to
RT the small interstitial proteoglycans PG-S1 and PG-S2 (decorin).";
RL EMBO J. 8:2601-2604(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Ascending colon;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP GLYCOSYLATION AT ASN-127; ASN-166; ASN-201 AND ASN-291.
RX PubMed=2243109; DOI=10.1016/s0021-9258(17)30550-1;
RA Plaas A.H.K., Neame P.J., Nivens C.M., Reiss L.;
RT "Identification of the keratan sulfate attachment sites on bovine
RT fibromodulin.";
RL J. Biol. Chem. 265:20634-20640(1990).
RN [5]
RP STRUCTURE OF CARBOHYDRATES.
RX PubMed=8973659; DOI=10.1111/j.1432-1033.1996.0402r.x;
RA Lauder R.M., Huckerby T.N., Nieduszynski I.A.;
RT "The structure of the keratan sulphate chains attached to fibromodulin
RT isolated from articular cartilage.";
RL Eur. J. Biochem. 242:402-409(1996).
RN [6]
RP SULFATION AT TYR-20; TYR-38; TYR-45; TYR-47; TYR-50; TYR-53; TYR-55; TYR-63
RP AND TYR-65, PYROGLUTAMATE FORMATION AT GLN-19, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=14551184; DOI=10.1074/jbc.m308689200;
RA Onnerfjord P., Heathfield T.F., Heinegaard D.;
RT "Identification of tyrosine sulfation in extracellular leucine-rich repeat
RT proteins using mass spectrometry.";
RL J. Biol. Chem. 279:26-33(2004).
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.
CC -!- INTERACTION:
CC P13605; P08603: CFH; Xeno; NbExp=4; IntAct=EBI-5281124, EBI-1223708;
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix.
CC -!- PTM: Binds keratan sulfate chains. {ECO:0000269|PubMed:14551184}.
CC -!- SIMILARITY: Belongs to the small leucine-rich proteoglycan (SLRP)
CC family. SLRP class II subfamily. {ECO:0000305}.
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DR EMBL; X16485; CAA34503.1; -; mRNA.
DR EMBL; BT030742; ABS45058.1; -; mRNA.
DR EMBL; BC104615; AAI04616.1; -; mRNA.
DR PIR; S05390; S05390.
DR RefSeq; NP_776483.1; NM_174058.2.
DR AlphaFoldDB; P13605; -.
DR SMR; P13605; -.
DR IntAct; P13605; 4.
DR STRING; 9913.ENSBTAP00000019854; -.
DR iPTMnet; P13605; -.
DR PaxDb; P13605; -.
DR PeptideAtlas; P13605; -.
DR PRIDE; P13605; -.
DR Ensembl; ENSBTAT00000019854; ENSBTAP00000019854; ENSBTAG00000014912.
DR GeneID; 281168; -.
DR KEGG; bta:281168; -.
DR CTD; 2331; -.
DR VEuPathDB; HostDB:ENSBTAG00000014912; -.
DR VGNC; VGNC:29054; FMOD.
DR eggNOG; KOG0619; Eukaryota.
DR GeneTree; ENSGT00940000157007; -.
DR HOGENOM; CLU_000288_186_4_1; -.
DR InParanoid; P13605; -.
DR OMA; YVRMSHN; -.
DR OrthoDB; 826997at2759; -.
DR TreeFam; TF334562; -.
DR Reactome; R-BTA-2022854; Keratan sulfate biosynthesis.
DR Reactome; R-BTA-2022857; Keratan sulfate degradation.
DR Proteomes; UP000009136; Chromosome 16.
DR Bgee; ENSBTAG00000014912; Expressed in trachea and 103 other tissues.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IEA:InterPro.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0030199; P:collagen fibril organization; IEA:Ensembl.
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; 10.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Extracellular matrix;
KW Glycoprotein; Leucine-rich repeat; Proteoglycan;
KW Pyrrolidone carboxylic acid; Reference proteome; Repeat; Secreted; Signal;
KW Sulfation.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..376
FT /note="Fibromodulin"
FT /id="PRO_0000032738"
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..365
FT /note="LRR 11"
FT MOD_RES 19
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:14551184"
FT MOD_RES 20
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000269|PubMed:14551184"
FT MOD_RES 38
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000269|PubMed:14551184"
FT MOD_RES 45
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000305|PubMed:14551184"
FT MOD_RES 47
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000305|PubMed:14551184"
FT MOD_RES 50
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000305|PubMed:14551184"
FT MOD_RES 53
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000269|PubMed:14551184"
FT MOD_RES 55
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000269|PubMed:14551184"
FT MOD_RES 63
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000269|PubMed:14551184"
FT MOD_RES 65
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000269|PubMed:14551184"
FT CARBOHYD 127
FT /note="N-linked (GlcNAc...) (keratan sulfate) asparagine"
FT /evidence="ECO:0000269|PubMed:2243109"
FT CARBOHYD 166
FT /note="N-linked (GlcNAc...) (keratan sulfate) asparagine"
FT /evidence="ECO:0000269|PubMed:2243109"
FT CARBOHYD 201
FT /note="N-linked (GlcNAc...) (keratan sulfate) asparagine"
FT /evidence="ECO:0000269|PubMed:2243109"
FT CARBOHYD 291
FT /note="N-linked (GlcNAc...) (keratan sulfate) asparagine"
FT /evidence="ECO:0000269|PubMed:2243109"
FT CARBOHYD 341
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 334..367
FT /evidence="ECO:0000250"
FT CONFLICT 55..56
FT /note="YG -> T (in Ref. 1; CAA34503)"
FT /evidence="ECO:0000305"
FT CONFLICT 348
FT /note="L -> Q (in Ref. 1; CAA34503)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 376 AA; 43038 MW; CC4AA5B0AC79907B CRC64;
MQWASILLLA GLCSLSWAQY EEDSHWWFQF LRNQQSTYDD PYDPYPYEPY EPYPYGGEEG
PAYAYGSPPQ PEPRDCPQEC DCPPNFPTAM YCDNRNLKYL PFVPSRMKYV YFQNNQISSI
QEGVFDNATG LLWIALHGNQ ITSDKVGKKV FSKLRHLERL YLDHNNLTRI PSPLPRSLRE
LHLDHNQISR VPNNALEGLE NLTALYLHHN EIQEVGSSMK GLRSLILLDL SYNHLRKVPD
GLPSALEQLY LEHNNVFSVP DSYFRGSPKL LYVRLSHNSL TNNGLASNTF NSSSLLELDL
SYNQLQKIPP VSTNLENLYL QGNRINEFSI SSFCTVVDVM NFSKLQVLRL DGNEIKRSAM
PADAPLCLRL ASLIEI
