ID H2U4H0_TAKRU Unreviewed; 317 AA.
AC H2U4H0;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 3.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=Fibromodulin {ECO:0000256|ARBA:ARBA00018230};
DE AltName: Full=Keratan sulfate proteoglycan fibromodulin {ECO:0000256|ARBA:ARBA00032216};
GN Name=FMOD {ECO:0000313|Ensembl:ENSTRUP00000031832.3};
OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000031832.3, ECO:0000313|Proteomes:UP000005226};
RN [1] {ECO:0000313|Ensembl:ENSTRUP00000031832.3, ECO:0000313|Proteomes:UP000005226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21551351;
RA Kai W., Kikuchi K., Tohari S., Chew A.K., Tay A., Fujiwara A., Hosoya S.,
RA Suetake H., Naruse K., Brenner S., Suzuki Y., Venkatesh B.;
RT "Integration of the genetic map and genome assembly of fugu facilitates
RT insights into distinct features of genome evolution in teleosts and
RT mammals.";
RL Genome Biol. Evol. 3:424-442(2011).
RN [2] {ECO:0000313|Ensembl:ENSTRUP00000031832.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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 AlphaFoldDB; H2U4H0; -.
DR STRING; 31033.ENSTRUP00000031832; -.
DR Ensembl; ENSTRUT00000031955.3; ENSTRUP00000031832.3; ENSTRUG00000012573.3.
DR eggNOG; KOG0619; Eukaryota.
DR GeneTree; ENSGT00940000157007; -.
DR HOGENOM; CLU_000288_186_4_1; -.
DR InParanoid; H2U4H0; -.
DR OMA; KLLYVRM; -.
DR TreeFam; TF334562; -.
DR Proteomes; UP000005226; Chromosome 3.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 3.
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; PF13516; LRR_6; 1.
DR Pfam; PF13855; LRR_8; 2.
DR Pfam; PF01462; LRRNT; 1.
DR SMART; SM00364; LRR_BAC; 5.
DR SMART; SM00365; LRR_SD22; 4.
DR SMART; SM00369; LRR_TYP; 8.
DR SMART; SM00013; LRRNT; 1.
DR SUPFAM; SSF52058; L domain-like; 1.
DR PROSITE; PS51450; LRR; 2.
PE 3: Inferred from homology;
KW Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW Reference proteome {ECO:0000313|Proteomes:UP000005226};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT DOMAIN 16..50
FT /note="LRRNT"
FT /evidence="ECO:0000259|SMART:SM00013"
SQ SEQUENCE 317 AA; 36254 MW; E221A3984C81EBD8 CRC64;
MAGGDMYASW RAEDAECPLE CDCPSAYPTA MYCHDRNLQH VPYVPSHIKY IYLQHNQISS
IQDGVFDNAT NLVWVVLFNN QLESDKIGKN LFSKLRNLER LLLEHNQLTR VPPNLPQSIR
DLRLAHNRIS KIPSGSFEGM TNLTSLQLQA NVLEDVRGAF KGLKSLTILD MRKNKLKKIP
NSLPEGLQQL YLEFNEIESL PARFLTVLPK LQFVRLAHNK LSDRGLPADV FNTSTLVELD
LSFNKLDKIP FVHRNLENLY LQANRIKGMT IFFTVDMTDF SKMRMLRLDG NQLSAKDIPS
EAAYCLRNPI SGIFQLF
//
