ID A0A3B3XJ84_9TELE Unreviewed; 349 AA.
AC A0A3B3XJ84;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=Fibromodulin {ECO:0000256|ARBA:ARBA00018230};
DE AltName: Full=Keratan sulfate proteoglycan fibromodulin {ECO:0000256|ARBA:ARBA00032216};
OS Poecilia mexicana.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48701 {ECO:0000313|Ensembl:ENSPMEP00000015049.1, ECO:0000313|Proteomes:UP000261480};
RN [1] {ECO:0000313|Ensembl:ENSPMEP00000015049.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_014831208.1; XM_014975722.1.
DR STRING; 48701.ENSPMEP00000015054; -.
DR Ensembl; ENSPMET00000023223.1; ENSPMEP00000015049.1; ENSPMEG00000017524.1.
DR Ensembl; ENSPMET00000032841.1; ENSPMEP00000015054.1; ENSPMEG00000017524.1.
DR GeneID; 106909369; -.
DR KEGG; pmei:106909369; -.
DR CTD; 791822; -.
DR OrthoDB; 521898at2759; -.
DR Proteomes; UP000261480; Unplaced.
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; PF13855; LRR_8; 2.
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; 2.
PE 3: Inferred from homology;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..349
FT /note="Fibromodulin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5040590432"
FT DOMAIN 48..82
FT /note="LRRNT"
FT /evidence="ECO:0000259|SMART:SM00013"
SQ SEQUENCE 349 AA; 39078 MW; D57539B98BF088C0 CRC64;
MRLETVILLS ALLPLCLSHG WDPLAWLFHR HGQAQQVGFL RADTVGWACP DECDCPPTFP
IAMYCEGRGL TAVPSIPSHI KYLYLQNNAI SAVPDAALVN ATSLVWLMLH HNQLTSDAIG
KEAFLKLVGL ERLFLHHNNL TSIPPNLPLS LRDLRLDHNR IEKVIPTDLE GMDNLTILHL
HDNEVTDMAT SLKALKSLTL LDISNNKLIK VPDALPEHLH QFYMEFNSID SLPEGFLGGL
AQLQYIRMSH NLLKDKGIPS NTFNITGLVE LDLSFNKLER IPTVSTTLQH LYLQANQIKE
FSLGSFCPVV DVTNFSRLQT LRLDGNEISQ EDIPSESALC LRWASSIQI
//