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MGI:Cav3

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Contents

Species (Taxon ID) Mus musculus (house mouse) (taxon:10090)
Gene Name(s) Cav3 ( synonyms: Cav-3, M-caveolin )
Protein Name(s) caveolin 3,
External Links
MGI MGI:107570

Annotations

Qualifier GO ID GO term name Reference Evidence Code with/from Aspect Notes Status
GO:0005515

protein binding

MGI:MGI:1927714
PMID:10988290[1]

IPI: Inferred from Physical Interaction

UniProtKB:P51637
UniProtKB:P51638

F

From MGI

GO:0005515

protein binding

MGI:MGI:2682500
PMID:14600260[2]

IPI: Inferred from Physical Interaction

UniProtKB:P05480

F

From MGI

GO:0005515

protein binding

MGI:MGI:3505818
PMID:15541368[3]

IPI: Inferred from Physical Interaction

UniProtKB:Q9ET78

F

From MGI

GO:0005515

protein binding

MGI:MGI:3526601
PMID:15277200[4]

IPI: Inferred from Physical Interaction

UniProtKB:Q811D0
UniProtKB:Q61762

F

From MGI

GO:0005515

protein binding

MGI:MGI:3622508
PMID:16455755[5]

IPI: Inferred from Physical Interaction

UniProtKB:P15208

F

From MGI

GO:0005515

protein binding

MGI:MGI:81176
PMID:8663016[6]

IPI: Inferred from Physical Interaction

UniProtKB:P11531

F

From MGI

GO:0005624

membrane fraction

MGI:MGI:1888583
PMID:10835421[7]

IDA: Inferred from Direct Assay

C

From MGI

GO:0005624

membrane fraction

MGI:MGI:3505818
PMID:15541368[3]

IDA: Inferred from Direct Assay

C

From MGI

GO:0005624

membrane fraction

MGI:MGI:4417868

ISO: Inferred from Sequence Orthology

UniProtKB:P51638

C

From MGI

GO:0005625

soluble fraction

MGI:MGI:4417868

ISO: Inferred from Sequence Orthology

UniProtKB:P51638

C

From MGI

GO:0005737

cytoplasm

MGI:MGI:4417868

ISO: Inferred from Sequence Orthology

UniProtKB:P51638

C

From MGI

GO:0005794

Golgi apparatus

MGI:MGI:1354194

IEA: Inferred from Electronic Annotation

UniProtKB-KW:KW-0333

C

From MGI

GO:0005886

plasma membrane

MGI:MGI:1927714
PMID:10988290[1]

ISO: Inferred from Sequence Orthology

UniProtKB:P51638

C

From MGI

GO:0005886

plasma membrane

MGI:MGI:2154458

ISO: Inferred from Sequence Orthology

UniProtKB:P51638

C

From MGI

GO:0005886

plasma membrane

MGI:MGI:2682500
PMID:14600260[2]

IDA: Inferred from Direct Assay

C

From MGI

GO:0005886

plasma membrane

MGI:MGI:3526601
PMID:15277200[4]

IDA: Inferred from Direct Assay

C

From MGI

GO:0005886

plasma membrane

MGI:MGI:3695802
PMID:17200204[8]

IDA: Inferred from Direct Assay

C

From MGI

GO:0005901

caveola

MGI:MGI:2154458

ISO: Inferred from Sequence Orthology

UniProtKB:P51638

C

From MGI

GO:0005901

caveola

MGI:MGI:2388238
PMID:12138167[9]

IDA: Inferred from Direct Assay

C

From MGI

GO:0005901

caveola

MGI:MGI:3051094
PMID:15155732[10]

IDA: Inferred from Direct Assay

C

From MGI

GO:0005901

caveola

MGI:MGI:3628972
PMID:16648270[11]

IDA: Inferred from Direct Assay

C

From MGI

GO:0005901

caveola

MGI:MGI:4417868

ISO: Inferred from Sequence Orthology

UniProtKB:P51638

C

From MGI

GO:0005901

caveola

MGI:MGI:85086
PMID:9008709[12]

IDA: Inferred from Direct Assay

C

From MGI

GO:0006469

negative regulation of protein kinase activity

MGI:MGI:2682500
PMID:14600260[2]

IMP: Inferred from Mutant Phenotype

P

From MGI

GO:0006641

triglyceride metabolic process

MGI:MGI:3052616
PMID:15314230[13]

IMP: Inferred from Mutant Phenotype

MGI:MGI:2684578

P

From MGI

GO:0006897

endocytosis

MGI:MGI:1339528
PMID:10373486[14]

TAS: Traceable Author Statement

P

From MGI

GO:0006897

endocytosis

MGI:MGI:2682500
PMID:14600260[2]

IMP: Inferred from Mutant Phenotype

P

From MGI

GO:0007009

plasma membrane organization

MGI:MGI:1928619
PMID:11115849[15]

IMP: Inferred from Mutant Phenotype

MGI:MGI:2684578

P

From MGI

GO:0007009

plasma membrane organization

MGI:MGI:2388238
PMID:12138167[9]

IMP: Inferred from Mutant Phenotype

MGI:MGI:2180558

P

From MGI

GO:0007009

plasma membrane organization

MGI:MGI:2682500
PMID:14600260[2]

IMP: Inferred from Mutant Phenotype

P

From MGI

GO:0007204

elevation of cytosolic calcium ion concentration

MGI:MGI:4417868

ISO: Inferred from Sequence Orthology

UniProtKB:P51638

P

From MGI

GO:0008016

regulation of heart contraction

MGI:MGI:4417868

ISO: Inferred from Sequence Orthology

UniProtKB:P51638

P

From MGI

GO:0008022

protein C-terminus binding

MGI:MGI:4834177

ISO: Inferred from Sequence Orthology

UniProtKB:P56539

F

From MGI

GO:0008104

protein localization

MGI:MGI:2135840
PMID:11259414[16]

IMP: Inferred from Mutant Phenotype

MGI:MGI:2180558

P

From MGI

GO:0008104

protein localization

MGI:MGI:2388238
PMID:12138167[9]

IMP: Inferred from Mutant Phenotype

MGI:MGI:2180558

P

From MGI

GO:0008104

protein localization

MGI:MGI:2682500
PMID:14600260[2]

IMP: Inferred from Mutant Phenotype

P

From MGI

GO:0008104

protein localization

MGI:MGI:3526601
PMID:15277200[4]

IGI: Inferred from Genetic Interaction

MGI:MGI:107231

P

From MGI

GO:0008104

protein localization

MGI:MGI:3612003
PMID:16319126[17]

IMP: Inferred from Mutant Phenotype

P

From MGI

GO:0009986

cell surface

MGI:MGI:4417868

ISO: Inferred from Sequence Orthology

UniProtKB:P51638

C

From MGI

GO:0010614

negative regulation of cardiac muscle hypertrophy

MGI:MGI:4834177

ISO: Inferred from Sequence Orthology

UniProtKB:P56539

P

From MGI

GO:0014819

regulation of skeletal muscle contraction

MGI:MGI:4834177

ISO: Inferred from Sequence Orthology

UniProtKB:P56539

P

From MGI

GO:0016010

dystrophin-associated glycoprotein complex

MGI:MGI:4834177

ISO: Inferred from Sequence Orthology

UniProtKB:P56539

C

From MGI

GO:0016020

membrane

MGI:MGI:1354194

IEA: Inferred from Electronic Annotation

UniProtKB-KW:KW-0472

C

From MGI

GO:0017080

sodium channel regulator activity

MGI:MGI:4834177

ISO: Inferred from Sequence Orthology

UniProtKB:P56539

F

From MGI

GO:0019899

enzyme binding

MGI:MGI:4417868

ISO: Inferred from Sequence Orthology

UniProtKB:P51638

F

From MGI

GO:0030315

T-tubule

MGI:MGI:2154458

ISO: Inferred from Sequence Orthology

UniProtKB:P51638

C

From MGI

GO:0030315

T-tubule

MGI:MGI:3612003
PMID:16319126[17]

IDA: Inferred from Direct Assay

C

From MGI

GO:0030315

T-tubule

MGI:MGI:4417868

ISO: Inferred from Sequence Orthology

UniProtKB:P51638

C

From MGI

GO:0030315

T-tubule

MGI:MGI:85086
PMID:9008709[12]

IDA: Inferred from Direct Assay

C

From MGI

GO:0031116

positive regulation of microtubule polymerization

MGI:MGI:4417868

ISO: Inferred from Sequence Orthology

UniProtKB:P51638

P

From MGI

GO:0031579

membrane raft organization

MGI:MGI:2135840
PMID:11259414[16]

IMP: Inferred from Mutant Phenotype

MGI:MGI:2180558

P

From MGI

GO:0031579

membrane raft organization

MGI:MGI:2682500
PMID:14600260[2]

IMP: Inferred from Mutant Phenotype

P

From MGI

GO:0031594

neuromuscular junction

MGI:MGI:4417868

ISO: Inferred from Sequence Orthology

UniProtKB:P51638

C

From MGI

GO:0032403

protein complex binding

MGI:MGI:4834177

ISO: Inferred from Sequence Orthology

UniProtKB:P56539

F

From MGI

GO:0032947

protein complex scaffold

MGI:MGI:4417868

ISO: Inferred from Sequence Orthology

UniProtKB:P51638

F

From MGI

GO:0042383

sarcolemma

MGI:MGI:1928619
PMID:11115849[15]

IDA: Inferred from Direct Assay

C

From MGI

GO:0042383

sarcolemma

MGI:MGI:2388238
PMID:12138167[9]

IDA: Inferred from Direct Assay

C

From MGI

GO:0042383

sarcolemma

MGI:MGI:3612003
PMID:16319126[17]

IDA: Inferred from Direct Assay

C

From MGI

GO:0042383

sarcolemma

MGI:MGI:3622508
PMID:16455755[5]

IDA: Inferred from Direct Assay

C

From MGI

GO:0042383

sarcolemma

MGI:MGI:4417868

ISO: Inferred from Sequence Orthology

UniProtKB:P51638

C

From MGI

GO:0042383

sarcolemma

MGI:MGI:4834177

ISO: Inferred from Sequence Orthology

UniProtKB:P56539

C

From MGI

GO:0042383

sarcolemma

MGI:MGI:81176
PMID:8663016[6]

IDA: Inferred from Direct Assay

C

From MGI

GO:0042383

sarcolemma

MGI:MGI:85086
PMID:9008709[12]

IDA: Inferred from Direct Assay

C

From MGI

GO:0042391

regulation of membrane potential

MGI:MGI:3526601
PMID:15277200[4]

IGI: Inferred from Genetic Interaction

MGI:MGI:96662
MGI:MGI:107231

P

From MGI

GO:0042593

glucose homeostasis

MGI:MGI:3052616
PMID:15314230[13]

IMP: Inferred from Mutant Phenotype

MGI:MGI:2684578

P

From MGI

GO:0042598

vesicular fraction

MGI:MGI:4417868

ISO: Inferred from Sequence Orthology

UniProtKB:P51638

C

From MGI

GO:0042632

cholesterol homeostasis

MGI:MGI:3052616
PMID:15314230[13]

IMP: Inferred from Mutant Phenotype

MGI:MGI:2684578

P

From MGI

GO:0043234

protein complex

MGI:MGI:4417868

ISO: Inferred from Sequence Orthology

UniProtKB:P51638

C

From MGI

GO:0043407

negative regulation of MAP kinase activity

MGI:MGI:4834177

ISO: Inferred from Sequence Orthology

UniProtKB:P56539

P

From MGI

GO:0043409

negative regulation of MAPK cascade

MGI:MGI:2388238
PMID:12138167[9]

IMP: Inferred from Mutant Phenotype

MGI:MGI:2180558

P

From MGI

GO:0045121

membrane raft

MGI:MGI:2135840
PMID:11259414[16]

IDA: Inferred from Direct Assay

C

From MGI

GO:0045792

negative regulation of cell size

MGI:MGI:4834177

ISO: Inferred from Sequence Orthology

UniProtKB:P56539

P

From MGI

GO:0046716

muscle cell homeostasis

MGI:MGI:1928619
PMID:11115849[15]

IMP: Inferred from Mutant Phenotype

MGI:MGI:2684578

P

From MGI

GO:0046716

muscle cell homeostasis

MGI:MGI:2388238
PMID:12138167[9]

IMP: Inferred from Mutant Phenotype

MGI:MGI:2180558

P

From MGI

GO:0046716

muscle cell homeostasis

MGI:MGI:2682500
PMID:14600260[2]

IMP: Inferred from Mutant Phenotype

P

From MGI

GO:0050998

nitric-oxide synthase binding

MGI:MGI:4417868

ISO: Inferred from Sequence Orthology

UniProtKB:P51638

F

From MGI

GO:0051001

negative regulation of nitric-oxide synthase activity

MGI:MGI:1930012
PMID:11159934[18]

IMP: Inferred from Mutant Phenotype

MGI:MGI:2180562

P

From MGI

GO:0051925

regulation of calcium ion transport via voltage-gated calcium channel activity

MGI:MGI:3628972
PMID:16648270[11]

IMP: Inferred from Mutant Phenotype

P

From MGI

GO:0055117

regulation of cardiac muscle contraction

MGI:MGI:4834177

ISO: Inferred from Sequence Orthology

UniProtKB:P56539

P

From MGI

GO:0060299

negative regulation of sarcomere organization

MGI:MGI:4834177

ISO: Inferred from Sequence Orthology

UniProtKB:P56539

P

From MGI

GO:0060307

regulation of ventricular cardiomyocyte membrane repolarization

MGI:MGI:4834177

ISO: Inferred from Sequence Orthology

UniProtKB:P56539

P

From MGI

GO:0072659

protein localization in plasma membrane

MGI:MGI:3622508
PMID:16455755[5]

IMP: Inferred from Mutant Phenotype

P

From MGI

colocalizes_with

GO:0005901

caveola

MGI:MGI:4417868

ISO: Inferred from Sequence Orthology

UniProtKB:P51638

C

From MGI

colocalizes_with

GO:0030018

Z disc

MGI:MGI:4417868

ISO: Inferred from Sequence Orthology

UniProtKB:P51638

C

From MGI

colocalizes_with

GO:0042383

sarcolemma

MGI:MGI:4417868

ISO: Inferred from Sequence Orthology

UniProtKB:P51638

C

From MGI

colocalizes_with

GO:0044424

intracellular part

MGI:MGI:4417868

ISO: Inferred from Sequence Orthology

UniProtKB:P51638

C

From MGI


Notes

References

See Help:References for how to manage references in GONUTS.
  1. 1.0 1.1 Sotgia F et al. (2000) Caveolin-3 directly interacts with the C-terminal tail of beta -dystroglycan. Identification of a central WW-like domain within caveolin family members. J Biol Chem 275: 38048-58 PubMed GONUTS page
  2. 2.0 2.1 2.2 2.3 2.4 2.5 2.6 2.7 Smythe GM et al. (2003) A caveolin-3 mutant that causes limb girdle muscular dystrophy type 1C disrupts Src localization and activity and induces apoptosis in skeletal myotubes. J Cell Sci 116: 4739-49 PubMed GONUTS page
  3. 3.0 3.1 Minamisawa S et al. (2004) Junctophilin type 2 is associated with caveolin-3 and is down-regulated in the hypertrophic and dilated cardiomyopathies. Biochem Biophys Res Commun 325: 852-6 PubMed GONUTS page
  4. 4.0 4.1 4.2 4.3 Folco EJ et al. (2004) Caveolin-3 and SAP97 form a scaffolding protein complex that regulates the voltage-gated potassium channel Kv1.5. Am J Physiol Heart Circ Physiol 287: H681-90 PubMed GONUTS page
  5. 5.0 5.1 5.2 Fecchi K et al. (2006) Spatial and temporal regulation of GLUT4 translocation by flotillin-1 and caveolin-3 in skeletal muscle cells. FASEB J 20: 705-7 PubMed GONUTS page
  6. 6.0 6.1 Song KS et al. (1996) Expression of caveolin-3 in skeletal, cardiac, and smooth muscle cells. Caveolin-3 is a component of the sarcolemma and co-fractionates with dystrophin and dystrophin-associated glycoproteins. J Biol Chem 271: 15160-5 PubMed GONUTS page
  7. Biederer CH et al. (2000) The basic helix-loop-helix transcription factors myogenin and Id2 mediate specific induction of caveolin-3 gene expression during embryonic development. J Biol Chem 275: 26245-51 PubMed GONUTS page
  8. Schubert W et al. (2007) Caveolin-1(-/-)- and caveolin-2(-/-)-deficient mice both display numerous skeletal muscle abnormalities, with tubular aggregate formation. Am J Pathol 170: 316-33 PubMed GONUTS page
  9. 9.0 9.1 9.2 9.3 9.4 9.5 Woodman SE et al. (2002) Caveolin-3 knock-out mice develop a progressive cardiomyopathy and show hyperactivation of the p42/44 MAPK cascade. J Biol Chem 277: 38988-97 PubMed GONUTS page
  10. Trinidad JC & Cohen JB (2004) Neuregulin inhibits acetylcholine receptor aggregation in myotubes. J Biol Chem 279: 31622-8 PubMed GONUTS page
  11. 11.0 11.1 Balijepalli RC et al. (2006) Localization of cardiac L-type Ca(2+) channels to a caveolar macromolecular signaling complex is required for beta(2)-adrenergic regulation. Proc Natl Acad Sci U S A 103: 7500-5 PubMed GONUTS page
  12. 12.0 12.1 12.2 Parton RG et al. (1997) Caveolin-3 associates with developing T-tubules during muscle differentiation. J Cell Biol 136: 137-54 PubMed GONUTS page
  13. 13.0 13.1 13.2 Oshikawa J et al. (2004) Insulin resistance in skeletal muscles of caveolin-3-null mice. Proc Natl Acad Sci U S A 101: 12670-5 PubMed GONUTS page
  14. Das K et al. (1999) The membrane-spanning domains of caveolins-1 and -2 mediate the formation of caveolin hetero-oligomers. Implications for the assembly of caveolae membranes in vivo. J Biol Chem 274: 18721-8 PubMed GONUTS page
  15. 15.0 15.1 15.2 Hagiwara Y et al. (2000) Caveolin-3 deficiency causes muscle degeneration in mice. Hum Mol Genet 9: 3047-54 PubMed GONUTS page
  16. 16.0 16.1 16.2 Galbiati F et al. (2001) Caveolin-3 null mice show a loss of caveolae, changes in the microdomain distribution of the dystrophin-glycoprotein complex, and t-tubule abnormalities. J Biol Chem 276: 21425-33 PubMed GONUTS page
  17. 17.0 17.1 17.2 Hernández-Deviez DJ et al. (2006) Aberrant dysferlin trafficking in cells lacking caveolin or expressing dystrophy mutants of caveolin-3. Hum Mol Genet 15: 129-42 PubMed GONUTS page
  18. Sunada Y et al. (2001) Transgenic mice expressing mutant caveolin-3 show severe myopathy associated with increased nNOS activity. Hum Mol Genet 10: 173-8 PubMed GONUTS page
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