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P35444 (COMP_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 118. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cartilage oligomeric matrix protein

Short name=COMP
Gene names
Name:Comp
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length755 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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

Secretedextracellular spaceextracellular 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Potential
Chain20 – 755736Cartilage oligomeric matrix protein
PRO_0000035859

Regions

Domain85 – 12440EGF-like 1
Domain125 – 17753EGF-like 2; calcium-binding Potential
Domain178 – 22043EGF-like 3; calcium-binding Potential
Domain223 – 26543EGF-like 4
Repeat266 – 29833TSP type-3 1
Repeat299 – 33436TSP type-3 2
Repeat335 – 35723TSP type-3 3
Repeat358 – 39336TSP type-3 4
Repeat394 – 41623TSP type-3 5
Repeat417 – 45438TSP type-3 6
Repeat455 – 49036TSP type-3 7
Repeat491 – 52636TSP type-3 8
Domain530 – 744215TSP C-terminal
Region21 – 8464COMP N-terminal
Region525 – 755231Mediates cell survival and induction of the IAP family of survival proteins By similarity

Amino acid modifications

Glycosylation1191N-linked (GlcNAc...) Potential
Glycosylation7401N-linked (GlcNAc...) Potential
Disulfide bond68Interchain
Disulfide bond71Interchain
Disulfide bond89 ↔ 100 By similarity
Disulfide bond94 ↔ 109 By similarity
Disulfide bond112 ↔ 123 By similarity
Disulfide bond129 ↔ 140 By similarity
Disulfide bond134 ↔ 149 By similarity
Disulfide bond152 ↔ 176 By similarity
Disulfide bond182 ↔ 195 By similarity
Disulfide bond189 ↔ 204 By similarity
Disulfide bond207 ↔ 219 By similarity
Disulfide bond227 ↔ 241 By similarity
Disulfide bond235 ↔ 251 By similarity
Disulfide bond253 ↔ 264 By similarity
Disulfide bond280 ↔ 285 By similarity
Disulfide bond290 ↔ 310 By similarity
Disulfide bond326 ↔ 346 By similarity
Disulfide bond349 ↔ 369 By similarity
Disulfide bond385 ↔ 405 By similarity
Disulfide bond408 ↔ 428 By similarity
Disulfide bond446 ↔ 466 By similarity
Disulfide bond482 ↔ 502 By similarity
Disulfide bond518 ↔ 739 By similarity

Secondary structure

... 755
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P35444 [UniParc].

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

FASTA75582,664
        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 

« Hide

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.
PIRA44315.
RefSeqNP_036966.1. NM_012834.1.
UniGeneRn.10343.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1FBMX-ray2.70A/B/C/D/E28-72[»]
1VDFX-ray2.05A/B/C/D/E28-72[»]
ProteinModelPortalP35444.
SMRP35444. Positions 28-72, 406-741.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEP35444.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID25304.
KEGGrno:25304.

Organism-specific databases

CTD1311.
RGD2378. Comp.

Phylogenomic databases

HOVERGENHBG000636.
KOK04659.
PhylomeDBP35444.

Gene expression databases

GenevestigatorP35444.

Family and domain databases

Gene3D2.60.120.200. 1 hit.
4.10.1080.10. 2 hits.
InterProIPR028492. Comp.
IPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
IPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR018097. EGF_Ca-bd_CS.
IPR009030. Growth_fac_rcpt_N_dom.
IPR024665. Thbs/COMP_coiled-coil.
IPR003367. Thrombospondin_3-like_rpt.
IPR017897. Thrombospondin_3_rpt.
IPR008859. Thrombospondin_C.
IPR028974. TSP_type-3_rpt.
[Graphical view]
PANTHERPTHR10199:SF81. PTHR10199:SF81. 1 hit.
PfamPF11598. COMP. 1 hit.
PF07645. EGF_CA. 2 hits.
PF02412. TSP_3. 6 hits.
PF05735. TSP_C. 1 hit.
[Graphical view]
SMARTSM00181. EGF. 2 hits.
SM00179. EGF_CA. 2 hits.
[Graphical view]
SUPFAMSSF103647. SSF103647. 3 hits.
SSF49899. SSF49899. 1 hit.
SSF57184. SSF57184. 1 hit.
PROSITEPS01186. 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]
ProtoNetSearch...

Other

EvolutionaryTraceP35444.
NextBio606093.
PROP35444.

Entry information

Entry nameCOMP_RAT
AccessionPrimary (citable) accession number: P35444
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: June 11, 2014
This is version 118 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references