ID CHAD_RAT Reviewed; 358 AA.
AC O70210;
DT 20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 24-JAN-2024, entry version 143.
DE RecName: Full=Chondroadherin;
DE AltName: Full=Cartilage leucine-rich protein;
DE Flags: Precursor;
GN Name=Chad;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Chondrosarcoma;
RX PubMed=9461555; DOI=10.1042/bj3300549;
RA Shen Z., Gantcheva S., Maansson B., Heinegaard D., Sommarin Y.;
RT "Chondroadherin expression changes in skeletal development.";
RL Biochem. J. 330:549-557(1998).
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. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Present in femoral head and rib cartilage, as well
CC as in tendon. Detected in bone marrow.
CC -!- SIMILARITY: Belongs to the small leucine-rich proteoglycan (SLRP)
CC family. SLRP class IV subfamily. {ECO:0000305}.
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DR EMBL; AF004953; AAC40060.1; -; mRNA.
DR RefSeq; NP_062037.1; NM_019164.1.
DR AlphaFoldDB; O70210; -.
DR SMR; O70210; -.
DR STRING; 10116.ENSRNOP00000004435; -.
DR GlyCosmos; O70210; 1 site, No reported glycans.
DR GlyGen; O70210; 1 site.
DR iPTMnet; O70210; -.
DR PhosphoSitePlus; O70210; -.
DR PaxDb; 10116-ENSRNOP00000004435; -.
DR GeneID; 29195; -.
DR KEGG; rno:29195; -.
DR UCSC; RGD:2336; rat.
DR AGR; RGD:2336; -.
DR CTD; 1101; -.
DR RGD; 2336; Chad.
DR eggNOG; KOG0619; Eukaryota.
DR HOGENOM; CLU_000288_18_6_1; -.
DR InParanoid; O70210; -.
DR OrthoDB; 3851278at2759; -.
DR PhylomeDB; O70210; -.
DR TreeFam; TF332659; -.
DR PRO; PR:O70210; -.
DR Proteomes; UP000002494; Unplaced.
DR Genevisible; O70210; RN.
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; ISO:RGD.
DR GO; GO:0001502; P:cartilage condensation; IEP:RGD.
DR GO; GO:1900155; P:negative regulation of bone trabecula formation; ISO:RGD.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 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 PANTHER; PTHR24373:SF277; CHONDROADHERIN; 1.
DR PANTHER; PTHR24373; SLIT RELATED LEUCINE-RICH REPEAT NEURONAL PROTEIN; 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 SUPFAM; SSF52058; L domain-like; 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_0000032775"
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 321..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; 40404 MW; 630946F96F384857 CRC64;
MARVLLLSLV FLAILLPALA ACPQNCHCHG DLQHVICDKV GLQKIPKVSE TTKLLNLQRN
NFPVLAANSF RTVPNLVSLH LQHCNIREVA AGAFRGLKQL IYLYLSHNDI RVLRAGAFDD
LTELTYLYLD HNKVSELPRG LLSPLVNLFI LQLNNNKIRE LRAGAFQGAK DLRWLYLSEN
ALTSLHPGSL DDVENLAKFH LDRNQLSSYP SAALSKLRVV EELKLSHNPL KSIPDNAFQS
FGRYLETLWL DNTNLEKFSD AAFAGVTTLK HVHLENNRLN QLPSTFPFDN LETLTLTNNP
WKCTCQLRGL RRWLEAKTSR PDATCSSPAK FKGQRIRDTD ALRSCKSPTK RSKKAGRH
//
