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Protein

Cartilage oligomeric matrix protein

Gene

Comp

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.By similarity1 Publication

Cofactori

Ca2+By similarityNote: Binds 11-14 calcium ions per subunit.By similarity

GO - Molecular functioni

  • calcium ion binding Source: InterPro
  • extracellular matrix structural constituent Source: RGD
  • fibronectin binding Source: RGD
  • heparin binding Source: UniProtKB-KW
  • vitamin D binding Source: RGD

GO - Biological processi

  • apoptotic process Source: UniProtKB-KW
  • cell adhesion Source: UniProtKB-KW
  • extracellular matrix organization Source: RGD
Complete GO annotation...

Keywords - Biological processi

Apoptosis, Cell adhesion

Keywords - Ligandi

Calcium, Heparin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Cartilage oligomeric matrix protein
Short name:
COMP
Gene namesi
Name:Comp
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2378. Comp.

Subcellular locationi

GO - Cellular componenti

  • extracellular matrix Source: RGD
  • proteinaceous extracellular matrix Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 19Sequence analysisAdd BLAST19
ChainiPRO_000003585920 – 755Cartilage oligomeric matrix proteinAdd BLAST736

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi68Interchain (with C-71)Combined sources1 Publication
Disulfide bondi71Interchain (with C-68)Combined sources1 Publication
Disulfide bondi89 ↔ 100PROSITE-ProRule annotation
Disulfide bondi94 ↔ 109PROSITE-ProRule annotation
Disulfide bondi112 ↔ 123PROSITE-ProRule annotation
Glycosylationi119N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi129 ↔ 140PROSITE-ProRule annotation
Disulfide bondi134 ↔ 149PROSITE-ProRule annotation
Disulfide bondi152 ↔ 176PROSITE-ProRule annotation
Disulfide bondi182 ↔ 195PROSITE-ProRule annotation
Disulfide bondi189 ↔ 204PROSITE-ProRule annotation
Disulfide bondi207 ↔ 219PROSITE-ProRule annotation
Disulfide bondi227 ↔ 241PROSITE-ProRule annotation
Disulfide bondi235 ↔ 251PROSITE-ProRule annotation
Disulfide bondi253 ↔ 264PROSITE-ProRule annotation
Disulfide bondi280 ↔ 285PROSITE-ProRule annotation
Disulfide bondi290 ↔ 310PROSITE-ProRule annotation
Disulfide bondi326 ↔ 346PROSITE-ProRule annotation
Disulfide bondi349 ↔ 369PROSITE-ProRule annotation
Disulfide bondi385 ↔ 405PROSITE-ProRule annotation
Modified residuei394PhosphoserineBy similarity1
Disulfide bondi408 ↔ 428PROSITE-ProRule annotation
Disulfide bondi446 ↔ 466PROSITE-ProRule annotation
Disulfide bondi482 ↔ 502PROSITE-ProRule annotation
Disulfide bondi518 ↔ 739PROSITE-ProRule annotation
Glycosylationi740N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP35444.
PRIDEiP35444.

Expressioni

Tissue specificityi

Expressed in differentiated and de-differentiated vascular smooth muscle cells (VSMCs) (at protein level).1 Publication

Interactioni

Subunit structurei

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.By similarity1 Publication

GO - Molecular functioni

  • fibronectin binding Source: RGD

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000067037.

Structurei

Secondary structure

1755
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi30 – 66Combined sources37

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FBMX-ray2.70A/B/C/D/E28-72[»]
1VDFX-ray2.05A/B/C/D/E28-72[»]
ProteinModelPortaliP35444.
SMRiP35444.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP35444.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini85 – 124EGF-like 1PROSITE-ProRule annotationAdd BLAST40
Domaini125 – 177EGF-like 2; calcium-bindingPROSITE-ProRule annotationAdd BLAST53
Domaini178 – 220EGF-like 3; calcium-bindingPROSITE-ProRule annotationAdd BLAST43
Domaini223 – 265EGF-like 4PROSITE-ProRule annotationAdd BLAST43
Repeati266 – 298TSP type-3 1Add BLAST33
Repeati299 – 334TSP type-3 2Add BLAST36
Repeati335 – 357TSP type-3 3Add BLAST23
Repeati358 – 393TSP type-3 4Add BLAST36
Repeati394 – 416TSP type-3 5Add BLAST23
Repeati417 – 454TSP type-3 6Add BLAST38
Repeati455 – 490TSP type-3 7Add BLAST36
Repeati491 – 526TSP type-3 8Add BLAST36
Domaini530 – 744TSP C-terminalPROSITE-ProRule annotationAdd BLAST215

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni21 – 84COMP N-terminalAdd BLAST64
Regioni525 – 755Mediates cell survival and induction of the IAP family of survival proteinsBy similarityAdd BLAST231

Domaini

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).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).By similarity

Sequence similaritiesi

Belongs to the thrombospondin family.Curated
Contains 4 EGF-like domains.PROSITE-ProRule annotation
Contains 1 TSP C-terminal (TSPC) domain.PROSITE-ProRule annotation
Contains 8 TSP type-3 repeats.PROSITE-ProRule annotation

Keywords - Domaini

EGF-like domain, Repeat, Signal

Phylogenomic databases

eggNOGiENOG410IFQQ. Eukaryota.
ENOG410XQKE. LUCA.
HOVERGENiHBG000636.
InParanoidiP35444.
KOiK04659.
PhylomeDBiP35444.

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
4.10.1080.10. 2 hits.
InterProiIPR013320. ConA-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR018097. EGF_Ca-bd_CS.
IPR009030. Growth_fac_rcpt_.
IPR024665. Thbs/COMP_coiled-coil.
IPR003367. Thrombospondin_3-like_rpt.
IPR017897. Thrombospondin_3_rpt.
IPR008859. Thrombospondin_C.
IPR028974. TSP_type-3_rpt.
[Graphical view]
PfamiPF11598. COMP. 1 hit.
PF07645. EGF_CA. 2 hits.
PF02412. TSP_3. 6 hits.
PF05735. TSP_C. 1 hit.
[Graphical view]
SMARTiSM00181. EGF. 4 hits.
SM00179. EGF_CA. 2 hits.
[Graphical view]
SUPFAMiSSF103647. SSF103647. 3 hits.
SSF49899. SSF49899. 1 hit.
SSF57184. SSF57184. 1 hit.
PROSITEiPS01186. 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]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P35444-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSPTACVLVL ALAALRATGQ GQIPLGGDLA PQMLRELQET NAALQDVREL
60 70 80 90 100
LRHRVKEITF LKNTVMECDA CGMQPARTPG LSVRPVALCA PGSCFPGVVC
110 120 130 140 150
TETATGARCG PCPPGYTGNG SHCTDVNECN AHPCFPRVRC INTSPGFHCE
160 170 180 190 200
ACPPGFSGPT HEGVGLTFAK TNKQVCTDIN ECETGQHNCV PNSVCVNTRG
210 220 230 240 250
SFQCGPCQPG FVGDQRSGCQ RRGQHFCPDG SPSPCHEKAD CILERDGSRS
260 270 280 290 300
CVCAVGWAGN GLLCGRDTDL DGFPDEKLRC SERQCRKDNC VTVPNSGQED
310 320 330 340 350
VDRDRIGDAC DPDADGDGVP NEQDNCPLVR NPDQRNSDKD KWGDACDNCR
360 370 380 390 400
SQKNDDQKDT DRDGQGDACD DDIDGDRIRN VADNCPRVPN FDQSDSDGDG
410 420 430 440 450
VGDACDNCPQ KDNPDQRDVD HDFVGDACDS DQDQDGDGHQ DSRDNCPTVP
460 470 480 490 500
NSAQQDSDHD GKGDACDDDD DNDGVPDSRD NCRLVPNPGQ EDNDRDGVGD
510 520 530 540 550
ACQGDFDADK VIDKIDVCPE NAEVTLTDFR AFQTVVLDPE GDAQIDPNWV
560 570 580 590 600
VLNQGMEIVQ TMNSDPGLAV GYTAFNGVDF EGTFHVNTAT DDDYAGFIFG
610 620 630 640 650
YQDSSSFYVV MWKQMEQTYW QANPFRAVAE PGIQLKAVKS STGPGEQLRN
660 670 680 690 700
ALWHTGDTAS QVRLLWKDPR NVGWKDKTSY RWFLQHRPQV GYIRVRFYEG
710 720 730 740 750
PELVADSNVV LDTAMRGGRL GVFCFSQENI IWANLRYRCN DTIPEDYERH

RLRRA
Length:755
Mass (Da):82,664
Last modified:June 1, 1994 - v1
Checksum:iAB48888FE093C598
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X72914 mRNA. Translation: CAA51419.1.
PIRiA44315.
RefSeqiNP_036966.1. NM_012834.1.
UniGeneiRn.10343.

Genome annotation databases

GeneIDi25304.
KEGGirno:25304.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X72914 mRNA. Translation: CAA51419.1.
PIRiA44315.
RefSeqiNP_036966.1. NM_012834.1.
UniGeneiRn.10343.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FBMX-ray2.70A/B/C/D/E28-72[»]
1VDFX-ray2.05A/B/C/D/E28-72[»]
ProteinModelPortaliP35444.
SMRiP35444.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000067037.

Proteomic databases

PaxDbiP35444.
PRIDEiP35444.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi25304.
KEGGirno:25304.

Organism-specific databases

CTDi1311.
RGDi2378. Comp.

Phylogenomic databases

eggNOGiENOG410IFQQ. Eukaryota.
ENOG410XQKE. LUCA.
HOVERGENiHBG000636.
InParanoidiP35444.
KOiK04659.
PhylomeDBiP35444.

Miscellaneous databases

EvolutionaryTraceiP35444.
PROiP35444.

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
4.10.1080.10. 2 hits.
InterProiIPR013320. ConA-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR018097. EGF_Ca-bd_CS.
IPR009030. Growth_fac_rcpt_.
IPR024665. Thbs/COMP_coiled-coil.
IPR003367. Thrombospondin_3-like_rpt.
IPR017897. Thrombospondin_3_rpt.
IPR008859. Thrombospondin_C.
IPR028974. TSP_type-3_rpt.
[Graphical view]
PfamiPF11598. COMP. 1 hit.
PF07645. EGF_CA. 2 hits.
PF02412. TSP_3. 6 hits.
PF05735. TSP_C. 1 hit.
[Graphical view]
SMARTiSM00181. EGF. 4 hits.
SM00179. EGF_CA. 2 hits.
[Graphical view]
SUPFAMiSSF103647. SSF103647. 3 hits.
SSF49899. SSF49899. 1 hit.
SSF57184. SSF57184. 1 hit.
PROSITEiPS01186. 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]
ProtoNetiSearch...

Entry informationi

Entry nameiCOMP_RAT
AccessioniPrimary (citable) accession number: P35444
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: November 2, 2016
This is version 131 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.