ID A0A093IUA2_EURHL Unreviewed; 380 AA.
AC A0A093IUA2;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Fibromodulin {ECO:0000256|ARBA:ARBA00018230};
DE AltName: Full=Keratan sulfate proteoglycan fibromodulin {ECO:0000256|ARBA:ARBA00032216};
GN ORFNames=N326_05200 {ECO:0000313|EMBL:KFW03197.1};
OS Eurypyga helias (Sunbittern) (Ardea helias).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Eurypygimorphae; Eurypygiformes;
OC Eurypygidae; Eurypyga.
OX NCBI_TaxID=54383 {ECO:0000313|EMBL:KFW03197.1, ECO:0000313|Proteomes:UP000054232};
RN [1] {ECO:0000313|EMBL:KFW03197.1, ECO:0000313|Proteomes:UP000054232}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N326 {ECO:0000313|EMBL:KFW03197.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Affects the rate of fibrils formation. May have a primary
CC role in collagen fibrillogenesis. {ECO:0000256|ARBA:ARBA00025136}.
CC -!- SUBUNIT: Binds to type I and type II collagen.
CC {ECO:0000256|ARBA:ARBA00011226}.
CC -!- SIMILARITY: Belongs to the small leucine-rich proteoglycan (SLRP)
CC family. SLRP class II subfamily. {ECO:0000256|ARBA:ARBA00005818}.
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DR EMBL; KK564015; KFW03197.1; -; Genomic_DNA.
DR RefSeq; XP_010147708.1; XM_010149406.1.
DR AlphaFoldDB; A0A093IUA2; -.
DR GeneID; 104507957; -.
DR KEGG; ehs:104507957; -.
DR CTD; 2331; -.
DR OrthoDB; 521898at2759; -.
DR Proteomes; UP000054232; Unassembled WGS sequence.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 2.
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; AGAP008170-PA; 1.
DR PANTHER; PTHR45712:SF4; FIBROMODULIN; 1.
DR Pfam; PF00560; LRR_1; 1.
DR Pfam; PF13855; LRR_8; 3.
DR Pfam; PF01462; LRRNT; 1.
DR SMART; SM00364; LRR_BAC; 4.
DR SMART; SM00369; LRR_TYP; 8.
DR SMART; SM00013; LRRNT; 1.
DR SUPFAM; SSF52058; L domain-like; 1.
DR PROSITE; PS51450; LRR; 3.
PE 3: Inferred from homology;
KW Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW Reference proteome {ECO:0000313|Proteomes:UP000054232};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..380
FT /note="Fibromodulin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001884758"
FT DOMAIN 79..113
FT /note="LRRNT"
FT /evidence="ECO:0000259|SMART:SM00013"
SQ SEQUENCE 380 AA; 43785 MW; 09DD204C7B82F3D4 CRC64;
MSWATILIIA GLCGASLGQY NEEEDMAWLQ YYMRQSRMSS YNYMPYYEDE NTPYVYSYLP
APDREAEPGP EPQLASSWQC PQECDCPPNF SSAMYCDTRN LRYLPFVPSR MKYVYFQNNQ
ITAIQEGAFD NATELEWLAL HNNQITSEKM GKRVFAKLKS LERLYMNNNN LTRMPSPLPQ
SLRELHLSYN QISKVPSNAL EGLENLTALY LSHNYIFEMG ASLKSLKSLI LADLSYNHLR
KVPDGLPMAL EQLYLEYNYI NTIPDDYFKV SPKLLYVRMS HNSLTNQGLS TNTFNSSSIL
ELDLSYNRLQ KIPRVSTNLE NLYLQGNQIN EFSISSFCTV VDVMNYSRLQ VLRLDGNEIK
RNAVPPDAPL CLRRATIIEI
//
