FMOD_RABIT
ID FMOD_RABIT Reviewed; 147 AA.
AC O46378;
DT 20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 25-MAY-2022, entry version 96.
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: Fragment;
GN Name=FMOD;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=New Zealand white;
RX PubMed=9822203; DOI=10.1016/s0945-053x(98)90089-0;
RA Boykiw R.H., Sciore P., Reno C.R., Marchuk L., Frank C., Hart D.A.;
RT "Altered levels of extracellular matrix molecules mRNA in healing rabbit
RT ligaments.";
RL Matrix Biol. 17:371-378(1998).
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 -!- PTM: Sulfated on tyrosine residues. {ECO:0000250}.
CC -!- PTM: The N-terminus is blocked by a pyrrolidone carboxylic acid
CC generated by post-translational modification of N-terminal glutamine.
CC {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; AF020291; AAC39516.1; -; mRNA.
DR AlphaFoldDB; O46378; -.
DR SMR; O46378; -.
DR STRING; 9986.ENSOCUP00000007954; -.
DR eggNOG; KOG0619; Eukaryota.
DR InParanoid; O46378; -.
DR Proteomes; UP000001811; 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; -; 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 Pyrrolidone carboxylic acid; Reference proteome; Repeat; Secreted;
KW Sulfation.
FT CHAIN <1..>147
FT /note="Fibromodulin"
FT /id="PRO_0000180086"
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...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 40
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 130
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT NON_TER 1
FT NON_TER 147
SQ SEQUENCE 147 AA; 16701 MW; 570A998EF7E72EE1 CRC64;
LDHNNLTRMP GPLPRSLREL HLDHNQISRV PNNALEGLEN LTALYLQHNE IQEVGSSMRG
LRSLILLDLS YNHLRRVPDG LPSALEQLYL EHNNVYTVPD SYFRGSPKLL YVRLSHNSLT
NSGLASNTFN SSSLLELDLS YNQLQKI
