Cartilage oligomeric matrix protein precursor

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P35444 (COMP_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 111. History...

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

Documents (2) |

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

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

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

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) By similarity. 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. Ref.2
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 By similarity. Interacts with ADAMTS12 By similarity. Interacts with ITGA7. Ref.2
Subcellular location	Secreted › extracellular space › extracellular matrix By similarity.
Tissue specificity	Expressed in differentiated and de-differentiated vascular smooth muscle cells (VSMCs) (at protein level). Ref.2
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 extracellular matrix organization Inferred from mutant phenotype PubMed 12225811. Source: RGD
Cellular_component	proteinaceous extracellular matrix Inferred from direct assay PubMed 12225811. Source: RGD
Molecular_function	calcium ion binding Inferred from electronic annotation. Source: InterPro extracellular matrix structural constituent Inferred from mutant phenotype PubMed 12225811. Source: RGD fibronectin binding Inferred from mutant phenotype PubMed 12225811. Source: RGD heparin binding Inferred from electronic annotation. Source: UniProtKB-KW vitamin D binding Inferred from mutant phenotype PubMed 12426368. Source: RGD
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_0000035859

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

Secondary structure

755

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P35444 [UniParc].

Last modified June 1, 1994. Version 1.
Checksum: AB48888FE093C598
Show »

FASTA

755

82,664

        10         20         30         40         50         60 
MSPTACVLVL ALAALRATGQ GQIPLGGDLA PQMLRELQET NAALQDVREL LRHRVKEITF 

        70         80         90        100        110        120 
LKNTVMECDA CGMQPARTPG LSVRPVALCA PGSCFPGVVC TETATGARCG PCPPGYTGNG 

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

       190        200        210        220        230        240 
ECETGQHNCV PNSVCVNTRG SFQCGPCQPG FVGDQRSGCQ RRGQHFCPDG SPSPCHEKAD 

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

       310        320        330        340        350        360 
VDRDRIGDAC DPDADGDGVP NEQDNCPLVR NPDQRNSDKD KWGDACDNCR SQKNDDQKDT 

       370        380        390        400        410        420 
DRDGQGDACD 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 DTIPEDYERH RLRRA

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References

[1]	"COMP (cartilage oligomeric matrix protein) is structurally related to the thrombospondins." Oldberg A., Antonsson P., Lindblom K., Heinegaard D. J. Biol. Chem. 267:22346-22350(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Cartilage.
[2]	"Cartilage oligomeric matrix protein maintains the contractile phenotype of vascular smooth muscle cells by interacting with alpha(7)beta(1) integrin." Wang L., Zheng J., Du Y., Huang Y., Li J., Liu B., Liu C.J., Zhu Y., Gao Y., Xu Q., Kong W., Wang X. Circ. Res. 106:514-525(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH ITGA7.
[3]	"The crystal structure of a five-stranded coiled coil in COMP: a prototype ion channel?" Malashkevich V.N., Kammerer R.A., Efimov V.P., Schulthess T., Engel J. Science 274:761-765(1996) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 27-72.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X72914 mRNA. Translation: CAA51419.1.

IPI

IPI00198640.

PIR

A44315.

RefSeq

NP_036966.1. NM_012834.1.

UniGene

Rn.10343.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1FBM	X-ray	2.70	A/B/C/D/E	28-72	[»]
1VDF	X-ray	2.05	A/B/C/D/E	28-72	[»]

ProteinModelPortal

P35444.

SMR

P35444. Positions 28-72, 406-741.

ModBase

Search...

Proteomic databases

PRIDE

P35444.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

25304.

KEGG

rno:25304.

Organism-specific databases

CTD

1311.

RGD

2378. Comp.

Phylogenomic databases

HOVERGEN

HBG000636.

K04659.

Gene expression databases

Genevestigator

P35444.

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

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

P35444.

NextBio

606093.

Entry information

Entry name

COMP_RAT

Accession

Primary (citable) accession number: P35444

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	June 1, 1994
Last modified:	April 3, 2013
This is version 111 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

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

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure 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