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   24-JAN-2024, entry version 171.
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   -!- 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}.
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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; 136 antibodies from 27 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   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.
DR   Genevisible; O15335; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Disulfide bond; Extracellular matrix; Glycoprotein;
KW   Leucine-rich repeat; Reference proteome; Repeat; 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
//