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Database: UniProt
Entry: W5NHY1_LEPOC
LinkDB: W5NHY1_LEPOC
Original site: W5NHY1_LEPOC 
ID   W5NHY1_LEPOC            Unreviewed;       344 AA.
AC   W5NHY1;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   RecName: Full=Lumican {ECO:0000256|ARBA:ARBA00013370};
OS   Lepisosteus oculatus (Spotted gar).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC   Lepisosteus.
OX   NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000020240.1, ECO:0000313|Proteomes:UP000018468};
RN   [1] {ECO:0000313|Proteomes:UP000018468}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA   MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT   "The Draft Genome of Lepisosteus oculatus.";
RL   Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSLOCP00000020240.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBUNIT: Binds to laminin. {ECO:0000256|ARBA:ARBA00011719}.
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; AHAT01008628; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_015208177.1; XM_015352691.1.
DR   AlphaFoldDB; W5NHY1; -.
DR   STRING; 7918.ENSLOCP00000020240; -.
DR   Ensembl; ENSLOCT00000020274.1; ENSLOCP00000020240.1; ENSLOCG00000016388.1.
DR   GeneID; 107078028; -.
DR   KEGG; loc:107078028; -.
DR   CTD; 4060; -.
DR   eggNOG; KOG0619; Eukaryota.
DR   GeneTree; ENSGT00940000158177; -.
DR   HOGENOM; CLU_000288_186_4_1; -.
DR   InParanoid; W5NHY1; -.
DR   OMA; DCPINFP; -.
DR   OrthoDB; 521898at2759; -.
DR   Proteomes; UP000018468; Linkage group LG8.
DR   Bgee; ENSLOCG00000016388; Expressed in embryo and 13 other cell types or tissues.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
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:SF6; LUMICAN; 1.
DR   Pfam; PF13855; LRR_8; 3.
DR   Pfam; PF01462; LRRNT; 1.
DR   PRINTS; PR00019; LEURICHRPT.
DR   SMART; SM00364; LRR_BAC; 5.
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:ARBA00022974};
KW   Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW   Proteoglycan {ECO:0000256|ARBA:ARBA00022974};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018468};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP};
KW   Sulfation {ECO:0000256|ARBA:ARBA00022641}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..344
FT                   /note="Lumican"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004867798"
FT   DOMAIN          40..74
FT                   /note="LRRNT"
FT                   /evidence="ECO:0000259|SMART:SM00013"
SQ   SEQUENCE   344 AA;  38761 MW;  7F512721A7899DF9 CRC64;
     MNHFHLPLFA ALLSSVLCQY YDYGAYYDHP SPVLGPSGPN CPQECNCPVS FPSAMYCDNR
     KLKYIPIVPS GIKYLYLQNN QIDSIKSGIF DNATELSWLI LDNNQIVNSN IGKNTFSKLK
     SLQKLYISYN NLTEPVGPLP KTMNELKIVG NKLSKFPSSL LDGLENLTAI HLQENQLKDD
     AIAGAFKGVK SLAYLDLSHN KIKRLPMDLP SSLEMFYIDH NNVTSIPSGY FQKFPKLQYL
     RISHNQLVDS GIPQNVFNIS SLIELDLSFN KLQSVPAINE NLENLYVQVN NINKIDLSSF
     CKITGPLNYS RLRHLRLDGN NLTRNNLPVD MANCLRQASE VILD
//
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