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P35444

- COMP_RAT

UniProt

P35444 - COMP_RAT

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Protein

Cartilage oligomeric matrix protein

Gene

Comp

Organism
Rattus norvegicus (Rat)
Status
Reviewed - 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

Binds 11-14 calcium ions per subunit.By similarity

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. extracellular matrix structural constituent Source: RGD
  3. fibronectin binding Source: RGD
  4. heparin binding Source: UniProtKB-KW
  5. vitamin D binding Source: RGD

GO - Biological processi

  1. apoptotic process Source: UniProtKB-KW
  2. cell adhesion Source: UniProtKB-KW
  3. 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
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi2378. Comp.

Subcellular locationi

GO - Cellular componenti

  1. extracellular matrix Source: RGD
  2. proteinaceous extracellular matrix Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Sequence AnalysisAdd
BLAST
Chaini20 – 755736Cartilage oligomeric matrix proteinPRO_0000035859Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi68 – 68Interchain
Disulfide bondi71 – 71Interchain
Disulfide bondi89 ↔ 100PROSITE-ProRule annotation
Disulfide bondi94 ↔ 109PROSITE-ProRule annotation
Disulfide bondi112 ↔ 123PROSITE-ProRule annotation
Glycosylationi119 – 1191N-linked (GlcNAc...)Sequence Analysis
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
Disulfide bondi408 ↔ 428PROSITE-ProRule annotation
Disulfide bondi446 ↔ 466PROSITE-ProRule annotation
Disulfide bondi482 ↔ 502PROSITE-ProRule annotation
Disulfide bondi518 ↔ 739PROSITE-ProRule annotation
Glycosylationi740 – 7401N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PRIDEiP35444.

Expressioni

Tissue specificityi

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

Gene expression databases

GenevestigatoriP35444.

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

Structurei

Secondary structure

1
755
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi30 – 6637

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FBMX-ray2.70A/B/C/D/E28-72[»]
1VDFX-ray2.05A/B/C/D/E28-72[»]
ProteinModelPortaliP35444.
SMRiP35444. Positions 28-72, 406-741.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP35444.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini85 – 12440EGF-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini125 – 17753EGF-like 2; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini178 – 22043EGF-like 3; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini223 – 26543EGF-like 4PROSITE-ProRule annotationAdd
BLAST
Repeati266 – 29833TSP type-3 1Add
BLAST
Repeati299 – 33436TSP type-3 2Add
BLAST
Repeati335 – 35723TSP type-3 3Add
BLAST
Repeati358 – 39336TSP type-3 4Add
BLAST
Repeati394 – 41623TSP type-3 5Add
BLAST
Repeati417 – 45438TSP type-3 6Add
BLAST
Repeati455 – 49036TSP type-3 7Add
BLAST
Repeati491 – 52636TSP type-3 8Add
BLAST
Domaini530 – 744215TSP C-terminalPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni21 – 8464COMP N-terminalAdd
BLAST
Regioni525 – 755231Mediates cell survival and induction of the IAP family of survival proteinsBy similarityAdd
BLAST

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

HOVERGENiHBG000636.
InParanoidiP35444.
KOiK04659.
PhylomeDBiP35444.

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
4.10.1080.10. 2 hits.
InterProiIPR028492. Comp.
IPR013320. ConA-like_dom.
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]
PANTHERiPTHR10199:SF81. PTHR10199:SF81. 1 hit.
PfamiPF11598. COMP. 1 hit.
PF07645. EGF_CA. 2 hits.
PF02412. TSP_3. 6 hits.
PF05735. TSP_C. 1 hit.
[Graphical view]
SMARTiSM00181. EGF. 2 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:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
X72914 mRNA. Translation: CAA51419.1 .
PIRi A44315.
RefSeqi NP_036966.1. NM_012834.1.
UniGenei Rn.10343.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali P35444.
SMRi P35444. Positions 28-72, 406-741.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi P35444.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 25304.
KEGGi rno:25304.

Organism-specific databases

CTDi 1311.
RGDi 2378. Comp.

Phylogenomic databases

HOVERGENi HBG000636.
InParanoidi P35444.
KOi K04659.
PhylomeDBi P35444.

Miscellaneous databases

EvolutionaryTracei P35444.
NextBioi 606093.
PROi P35444.

Gene expression databases

Genevestigatori P35444.

Family and domain databases

Gene3Di 2.60.120.200. 1 hit.
4.10.1080.10. 2 hits.
InterProi IPR028492. Comp.
IPR013320. ConA-like_dom.
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 ]
PANTHERi PTHR10199:SF81. PTHR10199:SF81. 1 hit.
Pfami PF11598. COMP. 1 hit.
PF07645. EGF_CA. 2 hits.
PF02412. TSP_3. 6 hits.
PF05735. TSP_C. 1 hit.
[Graphical view ]
SMARTi SM00181. EGF. 2 hits.
SM00179. EGF_CA. 2 hits.
[Graphical view ]
SUPFAMi SSF103647. SSF103647. 3 hits.
SSF49899. SSF49899. 1 hit.
SSF57184. SSF57184. 1 hit.
PROSITEi 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 ]
ProtoNeti Search...

Publicationsi

  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.

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: October 29, 2014
This is version 120 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

External Data

Dasty 3