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 13-FEB-2019, entry version 147. 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; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; 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 RT gene (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., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA 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., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., 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., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA 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 RT project: 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 CC and fibroblasts) by the integrin alpha(2)beta(1). May play an CC important role in the regulation of chondrocyte growth and CC proliferation (By similarity). {ECO:0000250}. CC -!- SUBUNIT: Mostly monomeric (By similarity). Interacts with collagen CC type II. {ECO:0000250}. 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 UniGene; Hs.97220; -. 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 ProteinModelPortal; O15335; -. DR SMR; O15335; -. DR BioGrid; 107526; 3. DR CORUM; O15335; -. DR STRING; 9606.ENSP00000258969; -. DR PhosphoSitePlus; O15335; -. DR BioMuta; CHAD; -. DR jPOST; O15335; -. DR PaxDb; O15335; -. DR PeptideAtlas; O15335; -. DR PRIDE; O15335; -. DR ProteomicsDB; 48592; -. DR Ensembl; ENST00000258969; ENSP00000258969; ENSG00000136457. DR Ensembl; ENST00000508540; ENSP00000423812; ENSG00000136457. DR GeneID; 1101; -. DR KEGG; hsa:1101; -. DR UCSC; uc010dbr.4; human. DR CTD; 1101; -. DR DisGeNET; 1101; -. DR EuPathDB; HostDB:ENSG00000136457.9; -. DR GeneCards; CHAD; -. DR HGNC; HGNC:1909; CHAD. DR HPA; HPA018241; -. DR MIM; 602178; gene. DR neXtProt; NX_O15335; -. DR OpenTargets; ENSG00000136457; -. DR PharmGKB; PA26445; -. DR eggNOG; KOG0619; Eukaryota. DR eggNOG; COG4886; LUCA. DR GeneTree; ENSGT00940000154464; -. DR HOGENOM; HOG000013150; -. DR HOVERGEN; HBG005324; -. DR InParanoid; O15335; -. DR KO; K06248; -. DR OMA; AFRGCKF; -. DR OrthoDB; 826997at2759; -. DR PhylomeDB; O15335; -. DR TreeFam; TF332659; -. DR GenomeRNAi; 1101; -. DR PRO; PR:O15335; -. DR Proteomes; UP000005640; Chromosome 17. DR Bgee; ENSG00000136457; Expressed in 132 organ(s), highest expression level in tibia. DR ExpressionAtlas; O15335; baseline and differential. DR Genevisible; O15335; HS. 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 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 3D-structure; Complete proteome; Disulfide bond; Extracellular matrix; KW Glycoprotein; Leucine-rich repeat; Polymorphism; Reference proteome; KW Repeat; Secreted; Signal. FT SIGNAL 1 22 {ECO:0000255}. FT CHAIN 23 359 Chondroadherin. FT /FTId=PRO_0000032773. FT DOMAIN 23 52 LRRNT. FT REPEAT 76 97 LRR 1. FT REPEAT 100 121 LRR 2. FT REPEAT 124 145 LRR 3. FT REPEAT 148 169 LRR 4. FT REPEAT 172 193 LRR 5. FT REPEAT 196 217 LRR 6. FT REPEAT 220 241 LRR 7. FT REPEAT 245 266 LRR 8. FT REPEAT 269 290 LRR 9. FT DOMAIN 300 348 LRRCT. FT CARBOHYD 144 144 O-linked (GalNAc...) serine. FT {ECO:0000255}. FT DISULFID 23 38 {ECO:0000250}. FT DISULFID 304 346 {ECO:0000250}. FT DISULFID 306 326 {ECO:0000250}. FT VARIANT 312 312 R -> Q (in dbSNP:rs35218093). FT /FTId=VAR_052019. FT VARIANT 350 350 T -> I (in dbSNP:rs2231510). FT /FTId=VAR_030631. FT CONFLICT 114 114 L -> V (in Ref. 1; AAC13410). FT {ECO:0000305}. FT CONFLICT 166 166 A -> P (in Ref. 1; AAC13410). FT {ECO:0000305}. FT STRAND 28 30 {ECO:0000244|PDB:5LFN}. FT TURN 31 34 {ECO:0000244|PDB:5LFN}. FT STRAND 35 37 {ECO:0000244|PDB:5LFN}. FT STRAND 55 57 {ECO:0000244|PDB:5LFN}. FT STRAND 64 66 {ECO:0000244|PDB:5LFN}. FT TURN 68 73 {ECO:0000244|PDB:5LFN}. FT STRAND 79 81 {ECO:0000244|PDB:5LFN}. FT TURN 92 97 {ECO:0000244|PDB:5LFN}. FT STRAND 103 105 {ECO:0000244|PDB:5LFN}. FT TURN 116 121 {ECO:0000244|PDB:5LFN}. FT STRAND 127 129 {ECO:0000244|PDB:5LFN}. FT TURN 140 145 {ECO:0000244|PDB:5LFN}. FT STRAND 151 153 {ECO:0000244|PDB:5LFN}. FT TURN 164 169 {ECO:0000244|PDB:5LFN}. FT STRAND 175 177 {ECO:0000244|PDB:5LFN}. FT TURN 188 191 {ECO:0000244|PDB:5LFN}. FT HELIX 192 194 {ECO:0000244|PDB:5LFN}. FT STRAND 198 201 {ECO:0000244|PDB:5LFN}. FT HELIX 212 215 {ECO:0000244|PDB:5LFN}. FT STRAND 222 225 {ECO:0000244|PDB:5LFN}. FT TURN 236 239 {ECO:0000244|PDB:5LFN}. FT HELIX 240 242 {ECO:0000244|PDB:5LFN}. FT TURN 243 245 {ECO:0000244|PDB:5LFN}. FT STRAND 248 250 {ECO:0000244|PDB:5LFN}. FT TURN 261 266 {ECO:0000244|PDB:5LFN}. FT STRAND 272 274 {ECO:0000244|PDB:5LFN}. FT STRAND 294 296 {ECO:0000244|PDB:5LFN}. FT HELIX 306 308 {ECO:0000244|PDB:5LFN}. FT HELIX 309 317 {ECO:0000244|PDB:5LFN}. FT STRAND 325 329 {ECO:0000244|PDB:5MX1}. FT HELIX 330 332 {ECO:0000244|PDB:5LFN}. FT TURN 337 339 {ECO:0000244|PDB:5LFN}. FT TURN 342 345 {ECO:0000244|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 //