Cartilage oligomeric matrix protein precursor

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Q9R0G6 (COMP_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 107. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Cartilage oligomeric matrix protein
Short name=COMP

Gene names

Name:

Comp

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	755 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	May play a role in the structural integrity of cartilage via its interaction with other extracellular matrix proteins such as the collagens and fibronectin. Can mediate the interaction of chondrocytes with the cartilage extracellular matrix through interaction with cell surface integrin receptors. Could play a role in the pathogenesis of osteoarthritis. Potent suppressor of apoptosis in both primary chondrocytes and transformed cells. Suppresses apoptosis by blocking the activation of caspase-3 and by inducing the IAP family of survival proteins (BIRC3, BIRC2, BIRC5 and XIAP). Essential for maintaining a vascular smooth muscle cells (VSMCs) contractile/differentiated phenotype under physiological and pathological stimuli. Maintains this phenotype of VSMCs by interacting with ITGA7 By similarity.
Cofactor	Binds 11-14 calcium ions per subunit By similarity.
Subunit structure	Pentamer; disulfide-linked. Exists in a more compact conformation in the presence of calcium and shows a more extended conformation in the absence of calcium. Interacts with ITGB3, ITGA5 and FN1. Binding to FN1 requires the presence of divalent cations (Ca²⁺, Mg²⁺ or Mn²⁺). The greatest amount of binding is seen in the presence of Mn²⁺. Interacts with MATN1, MATN3, MATN4 and ACAN. Binds heparin, heparan sulfate and chondroitin sulfate. EDTA dimishes significantly its binding to ACAN and abolishes its binding to MATN3, MATN4 and chondroitin sulfate. Interacts with collagen I, II and IX and interaction with these collagens is dependent on the presence of zinc ions. Interacts with ADAMTS12. Interacts with ITGA7 By similarity.
Subcellular location	Secreted › extracellular space › extracellular matrix By similarity.
Domain	The cell attachment motif mediates the attachment to chondrocytes. It mediates the induction of both the IAP family of survival proteins and the antiapoptotic response By similarity. The TSP C-terminal domain mediates interaction with FN1 and ACAN By similarity. Each of the eight TSP type-3 repeats binds two calcium ions. The TSP C-terminal domain binds three calcium ions By similarity.
Sequence similarities	Belongs to the thrombospondin family. Contains 4 EGF-like domains. Contains 1 TSP C-terminal (TSPC) domain. Contains 8 TSP type-3 repeats.

Ontologies

Keywords
Biological process	Apoptosis Cell adhesion
Cellular component	Extracellular matrix Secreted
Domain	EGF-like domain Repeat Signal
Ligand	Calcium Heparin-binding
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	apoptotic process Inferred from electronic annotation. Source: UniProtKB-KW cell adhesion Inferred from electronic annotation. Source: UniProtKB-KW growth plate cartilage development Inferred from mutant phenotype PubMed 18467703. Source: MGI limb development Inferred from electronic annotation. Source: Compara negative regulation of apoptotic process Inferred from electronic annotation. Source: Compara
Cellular_component	extracellular space Inferred from electronic annotation. Source: Compara proteinaceous extracellular matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	calcium ion binding Inferred from electronic annotation. Source: InterPro heparin binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 19

Potential

Chain

20 – 755

736

Cartilage oligomeric matrix protein

PRO_0000035858

Regions

Domain

85 – 124

EGF-like 1

Domain

125 – 177

EGF-like 2; calcium-binding Potential

Domain

178 – 220

EGF-like 3; calcium-binding Potential

Domain

223 – 265

EGF-like 4

Repeat

266 – 298

TSP type-3 1

Repeat

299 – 334

TSP type-3 2

Repeat

335 – 357

TSP type-3 3

Repeat

358 – 393

TSP type-3 4

Repeat

394 – 416

TSP type-3 5

Repeat

417 – 454

TSP type-3 6

Repeat

455 – 490

TSP type-3 7

Repeat

491 – 526

TSP type-3 8

Domain

530 – 744

215

TSP C-terminal

Region

21 – 84

COMP N-terminal

Region

525 – 755

231

Mediates cell survival and induction of the IAP family of survival proteins By similarity

Amino acid modifications

Glycosylation

119

N-linked (GlcNAc...) Potential

Glycosylation

740

N-linked (GlcNAc...) Potential

Disulfide bond

Interchain

Disulfide bond

Interchain

Disulfide bond

89 ↔ 100

By similarity

Disulfide bond

94 ↔ 109

By similarity

Disulfide bond

112 ↔ 123

By similarity

Disulfide bond

129 ↔ 140

By similarity

Disulfide bond

134 ↔ 149

By similarity

Disulfide bond

152 ↔ 176

By similarity

Disulfide bond

182 ↔ 195

By similarity

Disulfide bond

189 ↔ 204

By similarity

Disulfide bond

207 ↔ 219

By similarity

Disulfide bond

227 ↔ 241

By similarity

Disulfide bond

235 ↔ 251

By similarity

Disulfide bond

253 ↔ 264

By similarity

Disulfide bond

280 ↔ 285

By similarity

Disulfide bond

290 ↔ 310

By similarity

Disulfide bond

326 ↔ 346

By similarity

Disulfide bond

349 ↔ 369

By similarity

Disulfide bond

385 ↔ 405

By similarity

Disulfide bond

408 ↔ 428

By similarity

Disulfide bond

446 ↔ 466

By similarity

Disulfide bond

482 ↔ 502

By similarity

Disulfide bond

518 ↔ 739

By similarity

Experimental info

Sequence conflict

53 – 54

QQ → HE in AAD01972. Ref.1

Secondary structure

755

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

Q9R0G6 [UniParc].

Last modified October 3, 2012. Version 2.
Checksum: 24C2F113E7945C0F
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FASTA

755

82,342

        10         20         30         40         50         60 
MGPTACVLVL ALAILRATGQ GQIPLGGDLA PQMLRELQET NAALQDVREL LRQQVKEITF 

        70         80         90        100        110        120 
LKNTVMECDA CGMQPARTPG LSVRPVPLCA PGSCFPGVVC SETATGARCG PCPPGYTGNG 

       130        140        150        160        170        180 
SHCTDVNECN AHPCFPRVRC INTSPGFHCE ACPPGFSGPT HEGVGLTFAK SNKQVCTDIN 

       190        200        210        220        230        240 
ECETGQHNCV PNSVCVNTRG SFQCGPCQPG FVGDQTSGCQ RRGQHFCPDG SPSPCHEKAN 

       250        260        270        280        290        300 
CVLERDGSRS CVCAVGWAGN GLLCGRDTDL DGFPDEKLRC SERQCRKDNC VTVPNSGQED 

       310        320        330        340        350        360 
VDRDGIGDAC DPDADGDGVP NEQDNCPLVR NPDQRNSDSD KWGDACDNCR SKKNDDQKDT 

       370        380        390        400        410        420 
DLDGRGDACD DDIDGDRIRN VADNCPRVPN FDQSDSDGDG VGDACDNCPQ KDNPDQRDVD 

       430        440        450        460        470        480 
HDFVGDACDS DQDQDGDGHQ DSRDNCPTVP NSAQQDSDHD GKGDACDDDD DNDGVPDSRD 

       490        500        510        520        530        540 
NCRLVPNPGQ EDNDRDGVGD ACQGDFDADK VIDKIDVCPE NAEVTLTDFR AFQTVVLDPE 

       550        560        570        580        590        600 
GDAQIDPNWV VLNQGMEIVQ TMNSDPGLAV GYTAFNGVDF EGTFHVNTAT DDDYAGFIFG 

       610        620        630        640        650        660 
YQDSSSFYVV MWKQMEQTYW QANPFRAVAE PGIQLKAVKS STGPGEQLRN ALWHTGDTAS 

       670        680        690        700        710        720 
QVRLLWKDPR NVGWKDKTSY RWFLQHRPQV GYIRVRFYEG PELVADSNVV LDTAMRGGRL 

       730        740        750 
GVFCFSQENI IWANLRYRCN DTIPEDYESH RLQRV

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning, sequencing, and tissue and developmental expression of mouse cartilage oligomeric matrix protein (COMP)." Fang C., Carlson C.S., Leslie M.P., Tulli H., Stolerman E., Perris R., Ni L., Di Cesare P.E. J. Orthop. Res. 18:593-603(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Cartilage.
[2]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[3]	Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"Storage function of cartilage oligomeric matrix protein: the crystal structure of the coiled-coil domain in complex with vitamin D(3)." Ozbek S., Engel J., Stetefeld J. EMBO J. 21:5960-5968(2002) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 28-71.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF033530 mRNA. Translation: AAD01972.1.
AC158553 Genomic DNA. No translation available.
CH466569 Genomic DNA. Translation: EDL28815.1.

IPI

IPI00127506.

RefSeq

NP_057894.2. NM_016685.2.

UniGene

Mm.45071.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1MZ9	X-ray	1.70	A/B/C/D/E	28-71	[»]
3V2N	X-ray	1.80	A/B/C/D/E	28-71	[»]
3V2P	X-ray	1.87	A/B/C/D/E	28-71	[»]
3V2Q	X-ray	2.20	A/B/C/D/E	28-71	[»]
3V2R	X-ray	2.75	A/B/C/D/E	28-71	[»]

ProteinModelPortal

Q9R0G6.

SMR

Q9R0G6. Positions 28-72, 89-754.

ModBase

Search...

Protein-protein interaction databases

STRING

10090.ENSMUSP00000003659.

PTM databases

PhosphoSite

Q9R0G6.

Proteomic databases

PaxDb

Q9R0G6.

PRIDE

Q9R0G6.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000003659; ENSMUSP00000003659; ENSMUSG00000031849.

GeneID

12845.

KEGG

mmu:12845.

Organism-specific databases

CTD

1311.

MGI

MGI:88469. Comp.

Phylogenomic databases

eggNOG

NOG12793.

GeneTree

ENSGT00550000074507.

HOVERGEN

HBG000636.

InParanoid

Q9R0G6.

K04659.

OMA

CRPRAQR.

OrthoDB

EOG48GW2R.

Gene expression databases

CleanEx

MM_COMP.

Genevestigator

Q9R0G6.

GermOnline

ENSMUSG00000031849. Mus musculus.

Family and domain databases

Gene3D

2.60.120.200. 1 hit.

InterPro

IPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
IPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd.
IPR013032. EGF-like_CS.
IPR018097. EGF_Ca-bd_CS.
IPR024665. Thbs/COMP_coiled-coil.
IPR003367. Thrombospondin_3-like_rpt.
IPR017897. Thrombospondin_3_rpt.
IPR008859. Thrombospondin_C.
[Graphical view]

Pfam

PF11598. COMP. 1 hit.
PF07645. EGF_CA. 2 hits.
PF02412. TSP_3. 6 hits.
PF05735. TSP_C. 1 hit.
[Graphical view]

SMART

SM00181. EGF. 2 hits.
SM00179. EGF_CA. 2 hits.
[Graphical view]

SUPFAM

SSF49899. ConA_like_lec_gl. 1 hit.

PROSITE

PS00018. EF_HAND_1. 1 hit.
PS00022. EGF_1. False negative.
PS01186. EGF_2. 1 hit.
PS50026. EGF_3. 3 hits.
PS01187. EGF_CA. 2 hits.
PS51234. TSP3. 8 hits.
PS51236. TSP_CTER. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q9R0G6.

NextBio

282384.

SOURCE

Search...

Entry information

Entry name

COMP_MOUSE

Accession

Primary (citable) accession number: Q9R0G6
Secondary accession number(s): G3X8Q4

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 10, 2003
Last sequence update:	October 3, 2012
Last modified:	May 1, 2013
This is version 107 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents