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Database: UniProt
Entry: A0A3B3XJ84_9TELE
LinkDB: A0A3B3XJ84_9TELE
Original site: A0A3B3XJ84_9TELE 
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}.
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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
//
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