O15335 (CHAD_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Chondroadherin

Alternative name(s):
Cartilage leucine-rich protein

Gene names

Name:	CHAD
Synonyms:	SLRR4A

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	359 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Promotes attachment of chondrocytes, fibroblasts, and osteoblasts. This binding is mediated (at least for chondrocytes and fibroblasts) by the integrin alpha2beta1. May play an important role in the regulation of chondrocyte growth and proliferation By similarity.
Subunit structure	Mostly monomeric By similarity. Interacts with collagen type II.
Subcellular location	Secreted › extracellular space › extracellular matrix By similarity.
Tissue specificity	Present in chondrocytes at all ages.
Sequence similarities	Belongs to the small leucine-rich proteoglycan (SLRP) family. SLRP class IV subfamily. Contains 9 LRR (leucine-rich) repeats. Contains 1 LRRCT domain. Contains 1 LRRNT domain.

Ontologies

Keywords
Cellular component	Extracellular matrix Secreted
Coding sequence diversity	Polymorphism
Domain	Leucine-rich repeat Repeat Signal
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cartilage condensation Inferred from electronic annotation. Source: Compara regulation of cell growth Non-traceable author statement. Source: UniProtKB
Cellular_component	proteinaceous extracellular matrix Traceable author statement. Source: UniProtKB
Molecular_function	extracellular matrix structural constituent Non-traceable author statement. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 22	22	Potential
	Chain	23 – 359	337	Chondroadherin		PRO_0000032773
Regions
	Domain	23 – 52	30	LRRNT
	Repeat	76 – 97	22	LRR 1
	Repeat	100 – 121	22	LRR 2
	Repeat	124 – 145	22	LRR 3
	Repeat	148 – 169	22	LRR 4
	Repeat	172 – 193	22	LRR 5
	Repeat	196 – 217	22	LRR 6
	Repeat	220 – 241	22	LRR 7
	Repeat	245 – 266	22	LRR 8
	Repeat	269 – 290	22	LRR 9
	Domain	300 – 348	49	LRRCT
Amino acid modifications
	Glycosylation	144	1	O-linked (GalNAc...) Potential
	Disulfide bond	23 ↔ 38		By similarity
	Disulfide bond	304 ↔ 346		By similarity
	Disulfide bond	306 ↔ 326		By similarity
Natural variations
	Natural variant	312	1	R → Q. Corresponds to variant rs35218093 [ dbSNP | Ensembl ].		VAR_052019
	Natural variant	350	1	T → I. Corresponds to variant rs2231510 [ dbSNP | Ensembl ].		VAR_030631
Experimental info
	Sequence conflict	114	1	L → V in AAC13410. Ref.1
	Sequence conflict	166	1	A → P in AAC13410. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	O15335 [UniParc]. Last modified February 20, 2007. Version 2. Checksum: CF24D2B5A5DFCF0C	FASTA	359	40,476
	10 20 30 40 50 60 MVRPMLLLSL GLLAGLLPAL AACPQNCHCH SDLQHVICDK VGLQKIPKVS EKTKLLNLQR 70 80 90 100 110 120 NNFPVLAANS FRAMPNLVSL HLQHCQIREV AAGAFRGLKQ LIYLYLSHND IRVLRAGAFD 130 140 150 160 170 180 DLTELTYLYL DHNKVTELPR GLLSPLVNLF ILQLNNNKIR ELRAGAFQGA KDLRWLYLSE 190 200 210 220 230 240 NALSSLQPGA LDDVENLAKF HVDRNQLSSY PSAALSKLRV VEELKLSHNP LKSIPDNAFQ 250 260 270 280 290 300 SFGRYLETLW LDNTNLEKFS DGAFLGVTTL KHVHLENNRL NQLPSNFPFD SLETLALTNN 310 320 330 340 350 PWKCTCQLRG LRRWLEAKAS RPDATCASPA KFKGQHIRDT DAFRSCKFPT KRSKKAGRH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The structure and chromosome location of the human chondroadherin gene (CHAD)." Grover J., Chen X.-N., Korenberg J.R., Roughley P.J. Genomics 45:379-385(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Association of chondroadherin with collagen type II." Maansson B., Wenglen C., Moergelin M., Saxne T., Heinegaard D. J. Biol. Chem. 276:32883-32888(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Mammary gland.
[4]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U96769, U96767, U96768 Genomic DNA. Translation: AAC13410.1. AF371328 mRNA. Translation: AAK51556.1. AK292177 mRNA. Translation: BAF84866.1. CH471109 Genomic DNA. Translation: EAW94613.1. BC036360 mRNA. Translation: AAH36360.1. BC073974 mRNA. Translation: AAH73974.1.
IPI	IPI00014592.
RefSeq	NP_001258.2. NM_001267.2.
UniGene	Hs.97220.
3D structure databases
ProteinModelPortal	O15335.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000258969.
Proteomic databases
PaxDb	O15335.
PRIDE	O15335.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000258969; ENSP00000258969; ENSG00000136457. ENST00000508540; ENSP00000423812; ENSG00000136457.
GeneID	1101.
KEGG	hsa:1101.
UCSC	uc010dbr.3. human.
Organism-specific databases
CTD	1101.
GeneCards	GC17M048541.
HGNC	HGNC:1909. CHAD.
HPA	HPA018241.
MIM	602178. gene.
neXtProt	NX_O15335.
PharmGKB	PA26445.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG4886.
HOGENOM	HOG000013150.
HOVERGEN	HBG005324.
InParanoid	O15335.
KO	K06248.
OMA	CHCHGGD.
PhylomeDB	O15335.
Gene expression databases
Bgee	O15335.
CleanEx	HS_CHAD.
Genevestigator	O15335.
GermOnline	ENSG00000136457. Homo sapiens.
Family and domain databases
InterPro	IPR000483. Cys-rich_flank_reg_C. IPR001611. Leu-rich_rpt. IPR003591. Leu-rich_rpt_typical-subtyp. IPR000372. LRR-contain_N. [Graphical view]
Pfam	PF00560. LRR_1. 3 hits. PF01462. LRRNT. 1 hit. [Graphical view]
SMART	SM00369. LRR_TYP. 5 hits. SM00082. LRRCT. 1 hit. SM00013. LRRNT. 1 hit. [Graphical view]
PROSITE	PS51450. LRR. 10 hits. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	1101.
NextBio	4554.
SOURCE	Search...

Entry information

Entry name

CHAD_HUMAN

Accession

Primary (citable) accession number: O15335
Secondary accession number(s): A8K812, Q6GTU0, Q96RJ5

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 20, 2002
Last sequence update:	February 20, 2007
Last modified:	May 1, 2013
This is version 104 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.