CHADL_MOUSE
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 03-AUG-2022, entry version 74.
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}.
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DR EMBL; AC102262; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS49677.1; -.
DR RefSeq; NP_001157792.1; NM_001164320.1.
DR AlphaFoldDB; E9Q7T7; -.
DR SMR; E9Q7T7; -.
DR STRING; 10090.ENSMUSP00000072682; -.
DR GlyConnect; 2212; 1 N-Linked glycan (1 site).
DR GlyGen; E9Q7T7; 2 sites, 1 N-linked glycan (1 site).
DR PhosphoSitePlus; E9Q7T7; -.
DR MaxQB; E9Q7T7; -.
DR PaxDb; E9Q7T7; -.
DR PRIDE; E9Q7T7; -.
DR ProteomicsDB; 281122; -.
DR Antibodypedia; 332; 80 antibodies from 18 providers.
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 VEuPathDB; HostDB:ENSMUSG00000063765; -.
DR eggNOG; KOG0619; Eukaryota.
DR GeneTree; ENSGT00940000154464; -.
DR HOGENOM; CLU_022061_0_0_1; -.
DR InParanoid; E9Q7T7; -.
DR OMA; EAQHATC; -.
DR OrthoDB; 826997at2759; -.
DR PhylomeDB; E9Q7T7; -.
DR TreeFam; TF337463; -.
DR BioGRID-ORCS; 214685; 3 hits in 73 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 96 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 REGION 352..389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 728..748
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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
