ID   CHAD_BOVIN              Reviewed;         361 AA.
AC   Q27972;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 121.
DE   RecName: Full=Chondroadherin;
DE   AltName: Full=38 kDa bone protein;
DE   AltName: Full=Cartilage leucine-rich protein;
DE   Contains:
DE     RecName: Full=Chondroadherin minor form;
DE   Flags: Precursor;
GN   Name=CHAD;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC   TISSUE=Cartilage;
RX   PubMed=8063792; DOI=10.1016/s0021-9258(17)31839-2;
RA   Neame P.J., Sommarin Y., Boynton R.E., Heinegaard D.;
RT   "The structure of a 38-kDa leucine-rich protein (chondroadherin) isolated
RT   from bovine cartilage.";
RL   J. Biol. Chem. 269:21547-21554(1994).
RN   [2]
RP   PROTEIN SEQUENCE OF 25-55 AND 77-97.
RC   TISSUE=Bone;
RX   PubMed=7814406; DOI=10.1074/jbc.270.19.11619;
RA   Hu B., Coulson L., Moyer B., Price P.A.;
RT   "Isolation and molecular cloning of a novel bone phosphoprotein related in
RT   sequence to the cystatin family of thiol protease inhibitors.";
RL   J. Biol. Chem. 270:431-436(1995).
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.
CC   -!- SUBUNIT: Mostly monomeric. Interacts with collagen type II (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix.
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; U08018; AAA21330.1; -; mRNA.
DR   PIR; A53860; A53860.
DR   RefSeq; NP_776444.1; NM_174019.2.
DR   IntAct; Q27972; 1.
DR   STRING; 9913.ENSBTAP00000028386; -.
DR   PaxDb; Q27972; -.
DR   PRIDE; Q27972; -.
DR   GeneID; 281069; -.
DR   KEGG; bta:281069; -.
DR   CTD; 1101; -.
DR   eggNOG; KOG0619; Eukaryota.
DR   InParanoid; Q27972; -.
DR   OrthoDB; 826997at2759; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
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   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Extracellular matrix;
KW   Glycoprotein; Leucine-rich repeat; Reference proteome; Repeat; Secreted;
KW   Signal.
FT   SIGNAL          1..24
FT                   /note="Or 23; in some isoform(s)"
FT                   /evidence="ECO:0000269|PubMed:7814406"
FT   CHAIN           25..361
FT                   /note="Chondroadherin"
FT                   /id="PRO_0000032771"
FT   CHAIN           25..352
FT                   /note="Chondroadherin minor form"
FT                   /id="PRO_0000032772"
FT   DOMAIN          25..54
FT                   /note="LRRNT"
FT   REPEAT          78..99
FT                   /note="LRR 1"
FT   REPEAT          102..123
FT                   /note="LRR 2"
FT   REPEAT          126..147
FT                   /note="LRR 3"
FT   REPEAT          150..171
FT                   /note="LRR 4"
FT   REPEAT          174..195
FT                   /note="LRR 5"
FT   REPEAT          198..219
FT                   /note="LRR 6"
FT   REPEAT          222..243
FT                   /note="LRR 7"
FT   REPEAT          247..268
FT                   /note="LRR 8"
FT   REPEAT          271..292
FT                   /note="LRR 9"
FT   DOMAIN          302..350
FT                   /note="LRRCT"
FT   CARBOHYD        146
FT                   /note="O-linked (GalNAc...) serine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        25..40
FT                   /evidence="ECO:0000250"
FT   DISULFID        306..348
FT   DISULFID        308..328
FT   CONFLICT        25
FT                   /note="C -> Y (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        29
FT                   /note="C -> W (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        31
FT                   /note="C -> H (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        40
FT                   /note="C -> L (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        52
FT                   /note="S -> R (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   361 AA;  40885 MW;  DA79DC98AD3DD1F8 CRC64;
     MARPMLLLXL SLGLLASLLP ALAACPQNCH CHSDLQHVIC DKVGLQKIPK VSEKTKLLNL
     QRNNFPVLAT NSFRAMPNLV SLHLQHCQIR EVAAGAFRGL KQLIYLYLSH NDIRVLRAGA
     FDDLTELTYL YLDHNKVTEL PRGLLSPLVN LFILQLNNNK IRELRSGAFQ GAKDLRWLYL
     SENSLSSLQP GALDDVENLA KFYLDRNQLS SYPSAALSKL RVVEELKLSH NPLKSIPDNA
     FQSFGRYLET LWLDNTNLEK FSDGAFLGVT TLKHVHLENN RLHQLPSNFP FDSLETLTLT
     NNPWKCTCQL RGLRRWLEAK TSRPDATCAS PAKFRGQHIR DTDAFRGCKF PTKRSKKAGR
     H