ID CHADL_MOUSE Reviewed; 748 AA. AC E9Q7T7; DT 29-APR-2015, integrated into UniProtKB/Swiss-Prot. DT 05-APR-2011, sequence version 1. DT 17-JUN-2020, entry version 66. DE RecName: Full=Chondroadherin-like protein; DE Flags: Precursor; GN Name=Chadl; Synonyms=SLRR4B; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S., RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., RA Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of the RT mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [2] RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND TISSUE RP SPECIFICITY. RX PubMed=25451920; DOI=10.1074/jbc.m114.593541; RA Tillgren V., Ho J.C., Oennerfjord P., Kalamajski S.; RT "The novel small leucine-rich protein chondroadherin-like (CHADL) is RT expressed in cartilage and modulates chondrocyte differentiation."; RL J. Biol. Chem. 290:918-925(2015). CC -!- FUNCTION: Potential negative modulator of chondrocyte differentiation. CC Inhibits collagen fibrillogenesis in vitro. May influence chondrocyte's CC differentiation by acting on its cellular collagenous microenvironment. CC {ECO:0000269|PubMed:25451920}. CC -!- SUBUNIT: Associates with collagen and binds to collagen fibrils. CC {ECO:0000250|UniProtKB:Q6NUI6}. CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular CC matrix {ECO:0000269|PubMed:25451920}. CC -!- TISSUE SPECIFICITY: Expressed in cartilage, including articular knee CC cartilage, where it localizes to the extracellular space in the area CC immediately surrounding the chondrocytes, not detected in any other CC tissues (at protein level). {ECO:0000269|PubMed:25451920}. CC -!- DEVELOPMENTAL STAGE: Not detected before 13.5 dpc. From 13.5 dpc on, CC prominently expressed only in mesenchymal condensations and in CC cartilaginous tissues. In the ATDC5 cell line model, up-regulated CC during chondrocyte differentiation, absent in precondrogenic, non- CC differentiating stage (at protein level). CC {ECO:0000269|PubMed:25451920}. CC -!- SIMILARITY: Belongs to the small leucine-rich proteoglycan (SLRP) CC family. SLRP class IV subfamily. {ECO:0000305}. 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 EMBL; AC102262; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR CCDS; CCDS49677.1; -. DR RefSeq; NP_001157792.1; NM_001164320.1. DR STRING; 10090.ENSMUSP00000072682; -. DR GlyConnect; 2212; -. DR PhosphoSitePlus; E9Q7T7; -. DR MaxQB; E9Q7T7; -. DR PaxDb; E9Q7T7; -. DR PRIDE; E9Q7T7; -. DR Antibodypedia; 332; 77 antibodies. DR Ensembl; ENSMUST00000072910; ENSMUSP00000072682; ENSMUSG00000063765. DR GeneID; 214685; -. DR KEGG; mmu:214685; -. DR UCSC; uc007wwy.2; mouse. DR CTD; 150356; -. DR MGI; MGI:3036284; Chadl. DR eggNOG; KOG0619; Eukaryota. DR eggNOG; COG4886; LUCA. DR GeneTree; ENSGT00940000154464; -. DR HOGENOM; CLU_022061_0_0_1; -. DR InParanoid; E9Q7T7; -. DR OMA; VYLPDMV; -. DR OrthoDB; 826997at2759; -. DR TreeFam; TF337463; -. DR BioGRID-ORCS; 214685; 0 hits in 12 CRISPR screens. DR ChiTaRS; Chadl; mouse. DR PRO; PR:E9Q7T7; -. DR Proteomes; UP000000589; Chromosome 15. DR RNAct; E9Q7T7; protein. DR Bgee; ENSMUSG00000063765; Expressed in humerus cartilage element and 90 other tissues. DR ExpressionAtlas; E9Q7T7; baseline and differential. DR Genevisible; E9Q7T7; MM. DR GO; GO:0062023; C:collagen-containing extracellular matrix; IDA:UniProtKB. DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central. DR GO; GO:0005615; C:extracellular space; IBA:GO_Central. DR GO; GO:0005518; F:collagen binding; ISS:UniProtKB. DR GO; GO:0098633; F:collagen fibril binding; ISS:UniProtKB. DR GO; GO:0032331; P:negative regulation of chondrocyte differentiation; IMP:UniProtKB. DR GO; GO:1904027; P:negative regulation of collagen fibril organization; ISS:UniProtKB. DR Gene3D; 3.80.10.10; -; 3. DR InterPro; IPR000483; Cys-rich_flank_reg_C. 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 Pfam; PF13855; LRR_8; 6. DR Pfam; PF01463; LRRCT; 2. DR SMART; SM00369; LRR_TYP; 19. DR SMART; SM00082; LRRCT; 2. DR SMART; SM00013; LRRNT; 2. DR PROSITE; PS51450; LRR; 19. PE 1: Evidence at protein level; KW Disulfide bond; Extracellular matrix; Glycoprotein; Leucine-rich repeat; KW Reference proteome; Repeat; Secreted; Signal. FT SIGNAL 1..29 FT /evidence="ECO:0000255" FT CHAIN 30..748 FT /note="Chondroadherin-like protein" FT /evidence="ECO:0000255" FT /id="PRO_0000432866" FT DOMAIN 30..61 FT /note="LRRNT 1" FT /evidence="ECO:0000255" FT REPEAT 85..107 FT /note="LRR 1" FT /evidence="ECO:0000255" FT REPEAT 108..131 FT /note="LRR 2" FT /evidence="ECO:0000255" FT REPEAT 132..155 FT /note="LRR 3" FT /evidence="ECO:0000255" FT REPEAT 156..179 FT /note="LRR 4" FT /evidence="ECO:0000255" FT REPEAT 181..203 FT /note="LRR 5" FT /evidence="ECO:0000255" FT REPEAT 204..227 FT /note="LRR 6" FT /evidence="ECO:0000255" FT REPEAT 229..252 FT /note="LRR 7" FT /evidence="ECO:0000255" FT REPEAT 253..275 FT /note="LRR 8" FT /evidence="ECO:0000255" FT REPEAT 276..299 FT /note="LRR 9" FT /evidence="ECO:0000255" FT DOMAIN 309..357 FT /note="LRRCT 1" FT /evidence="ECO:0000255" FT DOMAIN 394..428 FT /note="LRRNT 2" FT /evidence="ECO:0000255" FT REPEAT 423..446 FT /note="LRR 10" FT /evidence="ECO:0000255" FT REPEAT 448..470 FT /note="LRR 11" FT /evidence="ECO:0000255" FT REPEAT 471..494 FT /note="LRR 12" FT /evidence="ECO:0000255" FT REPEAT 496..518 FT /note="LRR 13" FT /evidence="ECO:0000255" FT REPEAT 519..542 FT /note="LRR 14" FT /evidence="ECO:0000255" FT REPEAT 544..566 FT /note="LRR 15" FT /evidence="ECO:0000255" FT REPEAT 567..590 FT /note="LRR 16" FT /evidence="ECO:0000255" FT REPEAT 591..614 FT /note="LRR 17" FT /evidence="ECO:0000255" FT REPEAT 616..639 FT /note="LRR 18" FT /evidence="ECO:0000255" FT REPEAT 641..665 FT /note="LRR 19" FT /evidence="ECO:0000255" FT DOMAIN 674..722 FT /note="LRRCT 2" FT /evidence="ECO:0000255" FT CARBOHYD 51 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 625 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 395..410 FT /evidence="ECO:0000250" FT DISULFID 678..721 FT /evidence="ECO:0000250" FT DISULFID 680..700 FT /evidence="ECO:0000250" SQ SEQUENCE 748 AA; 81361 MW; AF8C566BB6AD4675 CRC64; MERPQSSIWV FMLLLFMVLL QSPAWHVAAQ RCPQTCVCDN SRRHVTCRHQ NLTEVPNTIP ELTQRLDLQG NILKVLPAAA FQDLPHLTHL DLRNCQVEMV AEGAFRGLGR LLLLNLASNR LSTLPQEALD GLGSLRRLEL EGNMLEELRP GTFGALGSLT TLNLAHNALV YLPAMAFQGL LRTRWLQLSH NALSVLAPEA LAGLPALRRL SLHHNELQAL PGAALSQARS LARLELGHNP LTYTGEEDGL ALPGLRELAL DHGSLQALGP RAFAHCPRLH TLDLRGNQLT TLPPLQVPGQ LRRLRLQGNP LWCACHARPL LEWLVRARVR SDGACRGPRR LRGEALDTLR PSDLRCPGDA AAGDGDGDED EDRPAGPRAP PLRSPHGEAA WATPCPPACA CVAETRHSTC DGRGLQAVPR GFPNDTQLLD LRRNHFPSVP RAAFPGLRHL VSLHLQHCGV AELEPGALAG LDRLLYLYLS HNQLSGLSAA ALEGAPNLGY LYLEHNRFLR IPGTALRALP TLVSLHLQDN AVDRLAPGDL AGARALRCLY LSGNHITQVS PGALGPAREL EKLHLDRNRL REVPTGALEG LPALKELQLS GNPLRALPDG AFQPVGRSLQ QLFLNSSDLE QISPRAFSGL GKGLRSLYLH KNQLQSLPAP LGLSGLELVD LSGNPFHCDC QLLPLHRWLT GLNLRVGATC ATPPSVRGQK VKVAAPVFEA CPGWTARKAK RTPTSRGSAR RTPSLSRH //