CHAD_MOUSE
ID CHAD_MOUSE Reviewed; 358 AA.
AC O55226;
DT 20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Chondroadherin;
DE AltName: Full=Cartilage leucine-rich protein;
DE Flags: Precursor;
GN Name=Chad;
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 [GENOMIC DNA].
RX PubMed=9465299; DOI=10.1006/geno.1997.5085;
RA Landgren C., Beier D.R., Faessler R., Heinegaard D., Sommarin Y.;
RT "The mouse chondroadherin gene: characterization and chromosomal
RT localization.";
RL Genomics 47:84-91(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Salivary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Promotes attachment of chondrocytes, fibroblasts, and
CC osteoblasts. This binding is mediated (at least for chondrocytes and
CC fibroblasts) by the integrin alpha(2)beta(1). May play an important
CC role in the regulation of chondrocyte growth and proliferation (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Mostly monomeric. Interacts with collagen type II (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Cartilage.
CC -!- SIMILARITY: Belongs to the small leucine-rich proteoglycan (SLRP)
CC family. SLRP class IV subfamily. {ECO:0000305}.
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DR EMBL; U96626; AAC39963.1; -; Genomic_DNA.
DR EMBL; BC012672; AAH12672.1; -; mRNA.
DR CCDS; CCDS25260.1; -.
DR RefSeq; NP_031715.1; NM_007689.4.
DR AlphaFoldDB; O55226; -.
DR SMR; O55226; -.
DR STRING; 10090.ENSMUSP00000047844; -.
DR GlyGen; O55226; 1 site.
DR PhosphoSitePlus; O55226; -.
DR PaxDb; O55226; -.
DR PRIDE; O55226; -.
DR ProteomicsDB; 281123; -.
DR Antibodypedia; 18082; 126 antibodies from 27 providers.
DR DNASU; 12643; -.
DR Ensembl; ENSMUST00000040418; ENSMUSP00000047844; ENSMUSG00000039084.
DR GeneID; 12643; -.
DR KEGG; mmu:12643; -.
DR UCSC; uc007kzd.1; mouse.
DR CTD; 1101; -.
DR MGI; MGI:1096866; Chad.
DR VEuPathDB; HostDB:ENSMUSG00000039084; -.
DR eggNOG; KOG0619; Eukaryota.
DR GeneTree; ENSGT00940000154464; -.
DR HOGENOM; CLU_000288_18_6_1; -.
DR InParanoid; O55226; -.
DR OMA; FRSCKSP; -.
DR OrthoDB; 826997at2759; -.
DR PhylomeDB; O55226; -.
DR TreeFam; TF332659; -.
DR BioGRID-ORCS; 12643; 2 hits in 70 CRISPR screens.
DR PRO; PR:O55226; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; O55226; protein.
DR Bgee; ENSMUSG00000039084; Expressed in tarsal region and 119 other tissues.
DR ExpressionAtlas; O55226; baseline and differential.
DR Genevisible; O55226; MM.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0060348; P:bone development; IMP:MGI.
DR GO; GO:1900155; P:negative regulation of bone trabecula formation; IMP:MGI.
DR Gene3D; 3.80.10.10; -; 1.
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; PF00560; LRR_1; 1.
DR Pfam; PF13855; LRR_8; 3.
DR Pfam; PF01462; LRRNT; 1.
DR SMART; SM00369; LRR_TYP; 9.
DR SMART; SM00082; LRRCT; 1.
DR SMART; SM00013; LRRNT; 1.
DR PROSITE; PS51450; LRR; 10.
PE 2: Evidence at transcript level;
KW Disulfide bond; Extracellular matrix; Glycoprotein; Leucine-rich repeat;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..358
FT /note="Chondroadherin"
FT /id="PRO_0000032774"
FT DOMAIN 21..50
FT /note="LRRNT"
FT REPEAT 51..72
FT /note="LRR 1"
FT REPEAT 75..96
FT /note="LRR 2"
FT REPEAT 99..120
FT /note="LRR 3"
FT REPEAT 123..144
FT /note="LRR 4"
FT REPEAT 147..168
FT /note="LRR 5"
FT REPEAT 171..192
FT /note="LRR 6"
FT REPEAT 195..216
FT /note="LRR 7"
FT REPEAT 219..240
FT /note="LRR 8"
FT REPEAT 244..265
FT /note="LRR 9"
FT REPEAT 268..289
FT /note="LRR 10"
FT DOMAIN 299..347
FT /note="LRRCT"
FT REGION 322..358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 333..347
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 143
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000255"
FT DISULFID 22..37
FT /evidence="ECO:0000250"
FT DISULFID 303..345
FT /evidence="ECO:0000250"
FT DISULFID 305..325
FT /evidence="ECO:0000250"
SQ SEQUENCE 358 AA; 40349 MW; 6A062FCEBF84A078 CRC64;
MARALLFSLV FLAILLPALA ACPQNCHCHG DLQHVICDKV GLQKIPKVSE TTKLLNLQRN
NFPVLAANSF RTMPNLVSLH LQHCNIREVA AGAFRGLKQL IYLYLSHNDI RVLRAGAFDD
LTELTYLYLD HNKVSELPRG LLSPLVNLFI LQLNNNKIRE LRAGAFQGAK DLRWLYLSEN
ALSSLQPGSL DDVENLAKFH LDKNQLSSYP SAALSKLRVV EELKLSHNPL KSIPDNAFQS
FGRYLETLWL DNTNLEKFSD AAFSGVTTLK HVHLDNNRLN QLPSSFPFDN LETLTLTNNP
WKCTCQLRGL RRWLEAKASR PDATCSSPAK FKGQRIRDTD ALRSCKSPTK RSKKAGRH
