ID CHAD_HUMAN Reviewed; 359 AA. AC O15335; A8K812; Q6GTU0; Q96RJ5; DT 20-JUN-2002, integrated into UniProtKB/Swiss-Prot. DT 20-FEB-2007, sequence version 2. DT 27-NOV-2024, entry version 175. DE RecName: Full=Chondroadherin; DE AltName: Full=Cartilage leucine-rich protein; DE Flags: Precursor; GN Name=CHAD; Synonyms=SLRR4A; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=9344663; DOI=10.1006/geno.1997.4951; RA Grover J., Chen X.-N., Korenberg J.R., Roughley P.J.; RT "The structure and chromosome location of the human chondroadherin gene RT (CHAD)."; RL Genomics 45:379-385(1997). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=11445564; DOI=10.1074/jbc.m101680200; RA Maansson B., Wenglen C., Moergelin M., Saxne T., Heinegaard D.; RT "Association of chondroadherin with collagen type II."; RL J. Biol. Chem. 276:32883-32888(2001). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Mammary gland; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; 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 (By similarity). Interacts with collagen type CC II. {ECO:0000250}. CC -!- INTERACTION: CC O15335; Q8N129: CNPY4; NbExp=2; IntAct=EBI-21895311, EBI-723824; CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular CC matrix {ECO:0000250}. CC -!- TISSUE SPECIFICITY: Present in chondrocytes at all ages. 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; U96769; AAC13410.1; -; Genomic_DNA. DR EMBL; U96767; AAC13410.1; JOINED; Genomic_DNA. DR EMBL; U96768; AAC13410.1; JOINED; Genomic_DNA. DR EMBL; AF371328; AAK51556.1; -; mRNA. DR EMBL; AK292177; BAF84866.1; -; mRNA. DR EMBL; CH471109; EAW94613.1; -; Genomic_DNA. DR EMBL; BC036360; AAH36360.1; -; mRNA. DR EMBL; BC073974; AAH73974.1; -; mRNA. DR CCDS; CCDS11568.1; -. DR RefSeq; NP_001258.2; NM_001267.2. DR RefSeq; XP_011522516.1; XM_011524214.2. DR PDB; 5LFN; X-ray; 2.10 A; A/B/C/D=23-359. DR PDB; 5MX1; X-ray; 2.17 A; A/B=20-359. DR PDBsum; 5LFN; -. DR PDBsum; 5MX1; -. DR AlphaFoldDB; O15335; -. DR SMR; O15335; -. DR BioGRID; 107526; 3. DR CORUM; O15335; -. DR IntAct; O15335; 2. DR STRING; 9606.ENSP00000258969; -. DR GlyCosmos; O15335; 1 site, No reported glycans. DR GlyGen; O15335; 1 site. DR PhosphoSitePlus; O15335; -. DR BioMuta; CHAD; -. DR jPOST; O15335; -. DR MassIVE; O15335; -. DR PaxDb; 9606-ENSP00000423812; -. DR PeptideAtlas; O15335; -. DR ProteomicsDB; 48592; -. DR Antibodypedia; 18082; 116 antibodies from 26 providers. DR DNASU; 1101; -. DR Ensembl; ENST00000258969.4; ENSP00000258969.4; ENSG00000136457.10. DR Ensembl; ENST00000508540.6; ENSP00000423812.1; ENSG00000136457.10. DR GeneID; 1101; -. DR KEGG; hsa:1101; -. DR MANE-Select; ENST00000508540.6; ENSP00000423812.1; NM_001267.3; NP_001258.2. DR UCSC; uc010dbr.4; human. DR AGR; HGNC:1909; -. DR CTD; 1101; -. DR DisGeNET; 1101; -. DR GeneCards; CHAD; -. DR HGNC; HGNC:1909; CHAD. DR HPA; ENSG00000136457; Tissue enhanced (brain, liver, pancreas). DR MIM; 602178; gene. DR neXtProt; NX_O15335; -. DR OpenTargets; ENSG00000136457; -. DR PharmGKB; PA26445; -. DR VEuPathDB; HostDB:ENSG00000136457; -. DR eggNOG; KOG0619; Eukaryota. DR GeneTree; ENSGT00940000154464; -. DR HOGENOM; CLU_000288_18_6_1; -. DR InParanoid; O15335; -. DR OMA; FRSCKSP; -. DR OrthoDB; 3851278at2759; -. DR PhylomeDB; O15335; -. DR TreeFam; TF332659; -. DR PathwayCommons; O15335; -. DR SignaLink; O15335; -. DR BioGRID-ORCS; 1101; 15 hits in 1138 CRISPR screens. DR GenomeRNAi; 1101; -. DR Pharos; O15335; Tbio. DR PRO; PR:O15335; -. DR Proteomes; UP000005640; Chromosome 17. DR RNAct; O15335; protein. DR Bgee; ENSG00000136457; Expressed in tibia and 114 other cell types or tissues. DR ExpressionAtlas; O15335; baseline and differential. 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; IEA:Ensembl. DR GO; GO:1900155; P:negative regulation of bone trabecula formation; IEA:Ensembl. DR FunFam; 3.80.10.10:FF:000059; Chondroadherin like; 1. DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1. DR InterPro; IPR000483; Cys-rich_flank_reg_C. DR InterPro; IPR050328; Dev_Immune_Receptor. 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 1: Evidence at protein level; KW 3D-structure; Disulfide bond; Extracellular matrix; Glycoprotein; KW Leucine-rich repeat; Proteomics identification; Reference proteome; Repeat; KW Secreted; Signal. FT SIGNAL 1..22 FT /evidence="ECO:0000255" FT CHAIN 23..359 FT /note="Chondroadherin" FT /id="PRO_0000032773" FT DOMAIN 23..52 FT /note="LRRNT" FT REPEAT 76..97 FT /note="LRR 1" FT REPEAT 100..121 FT /note="LRR 2" FT REPEAT 124..145 FT /note="LRR 3" FT REPEAT 148..169 FT /note="LRR 4" FT REPEAT 172..193 FT /note="LRR 5" FT REPEAT 196..217 FT /note="LRR 6" FT REPEAT 220..241 FT /note="LRR 7" FT REPEAT 245..266 FT /note="LRR 8" FT REPEAT 269..290 FT /note="LRR 9" FT DOMAIN 300..348 FT /note="LRRCT" FT CARBOHYD 144 FT /note="O-linked (GalNAc...) serine" FT /evidence="ECO:0000255" FT DISULFID 23..38 FT /evidence="ECO:0000250" FT DISULFID 304..346 FT /evidence="ECO:0000250" FT DISULFID 306..326 FT /evidence="ECO:0000250" FT VARIANT 312 FT /note="R -> Q (in dbSNP:rs35218093)" FT /id="VAR_052019" FT VARIANT 350 FT /note="T -> I (in dbSNP:rs2231510)" FT /id="VAR_030631" FT CONFLICT 114 FT /note="L -> V (in Ref. 1; AAC13410)" FT /evidence="ECO:0000305" FT CONFLICT 166 FT /note="A -> P (in Ref. 1; AAC13410)" FT /evidence="ECO:0000305" FT STRAND 28..30 FT /evidence="ECO:0007829|PDB:5LFN" FT TURN 31..34 FT /evidence="ECO:0007829|PDB:5LFN" FT STRAND 35..37 FT /evidence="ECO:0007829|PDB:5LFN" FT STRAND 55..57 FT /evidence="ECO:0007829|PDB:5LFN" FT STRAND 64..66 FT /evidence="ECO:0007829|PDB:5LFN" FT TURN 68..73 FT /evidence="ECO:0007829|PDB:5LFN" FT STRAND 79..81 FT /evidence="ECO:0007829|PDB:5LFN" FT TURN 92..97 FT /evidence="ECO:0007829|PDB:5LFN" FT STRAND 103..105 FT /evidence="ECO:0007829|PDB:5LFN" FT TURN 116..121 FT /evidence="ECO:0007829|PDB:5LFN" FT STRAND 127..129 FT /evidence="ECO:0007829|PDB:5LFN" FT TURN 140..145 FT /evidence="ECO:0007829|PDB:5LFN" FT STRAND 151..153 FT /evidence="ECO:0007829|PDB:5LFN" FT TURN 164..169 FT /evidence="ECO:0007829|PDB:5LFN" FT STRAND 175..177 FT /evidence="ECO:0007829|PDB:5LFN" FT TURN 188..191 FT /evidence="ECO:0007829|PDB:5LFN" FT HELIX 192..194 FT /evidence="ECO:0007829|PDB:5LFN" FT STRAND 198..201 FT /evidence="ECO:0007829|PDB:5LFN" FT HELIX 212..215 FT /evidence="ECO:0007829|PDB:5LFN" FT STRAND 222..225 FT /evidence="ECO:0007829|PDB:5LFN" FT TURN 236..239 FT /evidence="ECO:0007829|PDB:5LFN" FT HELIX 240..242 FT /evidence="ECO:0007829|PDB:5LFN" FT TURN 243..245 FT /evidence="ECO:0007829|PDB:5LFN" FT STRAND 248..250 FT /evidence="ECO:0007829|PDB:5LFN" FT TURN 261..266 FT /evidence="ECO:0007829|PDB:5LFN" FT STRAND 272..274 FT /evidence="ECO:0007829|PDB:5LFN" FT STRAND 294..296 FT /evidence="ECO:0007829|PDB:5LFN" FT HELIX 306..308 FT /evidence="ECO:0007829|PDB:5LFN" FT HELIX 309..317 FT /evidence="ECO:0007829|PDB:5LFN" FT STRAND 325..329 FT /evidence="ECO:0007829|PDB:5MX1" FT HELIX 330..332 FT /evidence="ECO:0007829|PDB:5LFN" FT TURN 337..339 FT /evidence="ECO:0007829|PDB:5LFN" FT TURN 342..345 FT /evidence="ECO:0007829|PDB:5MX1" SQ SEQUENCE 359 AA; 40476 MW; CF24D2B5A5DFCF0C CRC64; MVRPMLLLSL GLLAGLLPAL AACPQNCHCH SDLQHVICDK VGLQKIPKVS EKTKLLNLQR NNFPVLAANS FRAMPNLVSL HLQHCQIREV AAGAFRGLKQ LIYLYLSHND IRVLRAGAFD DLTELTYLYL DHNKVTELPR GLLSPLVNLF ILQLNNNKIR ELRAGAFQGA KDLRWLYLSE NALSSLQPGA LDDVENLAKF HVDRNQLSSY PSAALSKLRV VEELKLSHNP LKSIPDNAFQ SFGRYLETLW LDNTNLEKFS DGAFLGVTTL KHVHLENNRL NQLPSNFPFD SLETLALTNN PWKCTCQLRG LRRWLEAKAS RPDATCASPA KFKGQHIRDT DAFRSCKFPT KRSKKAGRH //