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P56539 (CAV3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 136. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Caveolin-3
Alternative name(s):
M-caveolin
Gene names
Name:CAV3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length151 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May act as a scaffolding protein within caveolar membranes. Interacts directly with G-protein alpha subunits and can functionally regulate their activity. May also regulate voltage-gated potassium channels. Plays a role in the sarcolemma repair mechanism of both skeletal muscle and cardiomyocytes that permits rapid resealing of membranes disrupted by mechanical stress.

Subunit structure

Homooligomer. Interacts with DLG1 and KCNA5; forms a ternary complex By similarity. Interacts with TRIM72 By similarity. Interacts with MUSK; may regulate MUSK signaling By similarity. Interacts with DAG1 (via its C-terminal); the interaction prevents binding of DAG1 with DMD. Interacts with DYSF. Ref.7 Ref.8

Subcellular location

Golgi apparatus membrane; Peripheral membrane protein By similarity. Cell membrane; Peripheral membrane protein By similarity. Membranecaveola; Peripheral membrane protein By similarity. Note: Potential hairpin-like structure in the membrane. Membrane protein of caveolae By similarity.

Tissue specificity

Expressed predominantly in muscle. Ref.2

Post-translational modification

Sumoylation with SUMO3 by PIAS4 may reduce agonist-induced internalization and desensitization of adrenergic receptor ABRD2. Ref.9

Involvement in disease

Limb-girdle muscular dystrophy 1C (LGMD1C) [MIM:607801]: A degenerative myopathy characterized by calf hypertrophy and mild to moderate proximal muscle weakness. Inheritance can be autosomal dominant or recessive.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.1 Ref.8 Ref.10 Ref.19 Ref.21 Ref.25 Ref.27

HyperCKmia (HYPCK) [MIM:123320]: Characterized by persistent elevated levels of serum creatine kinase without muscle weakness.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.11 Ref.15 Ref.22 Ref.24 Ref.27

Rippling muscle disease (RMD) [MIM:606072]: Rare disorder characterized by mechanically triggered contractions of skeletal muscle. In RMD, mechanical stimulation leads to electrically silent muscle contractions that spread to neighboring fibers that cause visible ripples to move over the muscle.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.13 Ref.14 Ref.19 Ref.20 Ref.26 Ref.28

Cardiomyopathy, familial hypertrophic (CMH) [MIM:192600]: A hereditary heart disorder characterized by ventricular hypertrophy, which is usually asymmetric and often involves the interventricular septum. The symptoms include dyspnea, syncope, collapse, palpitations, and chest pain. They can be readily provoked by exercise. The disorder has inter- and intrafamilial variability ranging from benign to malignant forms with high risk of cardiac failure and sudden cardiac death.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.23

Long QT syndrome 9 (LQT9) [MIM:611818]: A heart disorder characterized by a prolonged QT interval on the ECG and polymorphic ventricular arrhythmias. They cause syncope and sudden death in response to exercise or emotional stress, and can present with a sentinel event of sudden cardiac death in infancy.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.29 Ref.30

Sudden infant death syndrome (SIDS) [MIM:272120]: SIDS is the sudden death of an infant younger than 1 year that remains unexplained after a thorough case investigation, including performance of a complete autopsy, examination of the death scene, and review of clinical history. Pathophysiologic mechanisms for SIDS may include respiratory dysfunction, cardiac dysrhythmias, cardiorespiratory instability, and inborn errors of metabolism, but definitive pathogenic mechanisms precipitating an infant sudden death remain elusive.
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.

Myopathy, distal, Tateyama type (MPDT) [MIM:614321]: A disorder characterized by progressive muscular atrophy and muscle weakness beginning in the hands, the legs, or the feet. Muscle atrophy may be restricted to the small muscles of the hands and feet.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.17 Ref.27

Sequence similarities

Belongs to the caveolin family.

Caution

It is uncertain whether Met-1 or Met-2 is the initiator.

Sequence caution

The sequence AAC14931.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence BAF84581.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
   Cellular componentCell membrane
Golgi apparatus
Membrane
   Coding sequence diversityPolymorphism
   DiseaseCardiomyopathy
Disease mutation
Limb-girdle muscular dystrophy
Long QT syndrome
   PTMIsopeptide bond
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processT-tubule organization

Traceable author statement PubMed 12847114. Source: BHF-UCL

actin filament organization

Inferred from electronic annotation. Source: Ensembl

cardiac muscle cell development

Inferred from electronic annotation. Source: Ensembl

caveola assembly

Inferred from direct assay PubMed 18936328. Source: MGI

cell differentiation

Inferred from sequence or structural similarity. Source: BHF-UCL

cell growth

Inferred from sequence or structural similarity. Source: BHF-UCL

cholesterol homeostasis

Inferred from sequence or structural similarity. Source: BHF-UCL

cytoplasmic microtubule organization

Inferred from electronic annotation. Source: Ensembl

endocytosis

Inferred from sequence or structural similarity. Source: BHF-UCL

establishment of protein localization to plasma membrane

Inferred from electronic annotation. Source: Ensembl

glucose homeostasis

Inferred from sequence or structural similarity. Source: BHF-UCL

heart trabecula formation

Inferred from electronic annotation. Source: Ensembl

membrane raft organization

Inferred from sequence or structural similarity. Source: BHF-UCL

muscle cell cellular homeostasis

Inferred from sequence or structural similarity. Source: BHF-UCL

muscle organ development

Traceable author statement Ref.7. Source: UniProtKB

myoblast fusion

Inferred from electronic annotation. Source: Ensembl

negative regulation of MAP kinase activity

Inferred from mutant phenotype PubMed 12847114. Source: BHF-UCL

negative regulation of MAPK cascade

Inferred from sequence or structural similarity. Source: BHF-UCL

negative regulation of calcium ion transport

Inferred from direct assay PubMed 21084288. Source: MGI

negative regulation of cardiac muscle hypertrophy

Inferred from mutant phenotype PubMed 12847114. Source: BHF-UCL

negative regulation of cell growth involved in cardiac muscle cell development

Inferred from electronic annotation. Source: Ensembl

negative regulation of cell size

Inferred from mutant phenotype PubMed 12847114. Source: BHF-UCL

negative regulation of nitric-oxide synthase activity

Inferred from sequence or structural similarity. Source: BHF-UCL

negative regulation of potassium ion transmembrane transport

Inferred from sequence or structural similarity PubMed 22879586. Source: BHF-UCL

negative regulation of potassium ion transmembrane transporter activity

Inferred from sequence or structural similarity PubMed 22879586. Source: BHF-UCL

negative regulation of protein kinase activity

Inferred from sequence or structural similarity. Source: BHF-UCL

negative regulation of protein localization to cell surface

Non-traceable author statement PubMed 22879586. Source: BHF-UCL

negative regulation of sarcomere organization

Inferred from mutant phenotype PubMed 12847114. Source: BHF-UCL

nucleus localization

Inferred from electronic annotation. Source: Ensembl

plasma membrane organization

Inferred from sequence or structural similarity. Source: BHF-UCL

plasma membrane repair

Inferred from electronic annotation. Source: Ensembl

positive regulation of caveolin-mediated endocytosis

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of cytosolic calcium ion concentration

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of microtubule polymerization

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of myotube differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process

Non-traceable author statement PubMed 22879586. Source: BHF-UCL

protein localization

Inferred from sequence or structural similarity. Source: BHF-UCL

protein localization to plasma membrane

Inferred from sequence or structural similarity. Source: BHF-UCL

regulation of branching involved in mammary gland duct morphogenesis

Inferred from electronic annotation. Source: Ensembl

regulation of calcium ion import

Inferred from direct assay PubMed 21084288. Source: BHF-UCL

regulation of calcium ion transmembrane transporter activity

Inferred from direct assay PubMed 21084288. Source: BHF-UCL

regulation of cardiac muscle contraction

Inferred from mutant phenotype Ref.30. Source: BHF-UCL

regulation of heart contraction

Inferred from sequence or structural similarity. Source: BHF-UCL

regulation of heart rate

Inferred from mutant phenotype Ref.29. Source: BHF-UCL

regulation of membrane depolarization during cardiac muscle cell action potential

Inferred from mutant phenotype Ref.30. Source: BHF-UCL

regulation of membrane potential

Inferred from direct assay PubMed 21084288. Source: BHF-UCL

regulation of nerve growth factor receptor activity

Inferred from mutant phenotype PubMed 20472890. Source: MGI

regulation of p38MAPK cascade

Inferred from electronic annotation. Source: Ensembl

regulation of protein kinase B signaling

Inferred from electronic annotation. Source: Ensembl

regulation of signal transduction by receptor internalization

Inferred from mutant phenotype PubMed 20472890. Source: MGI

regulation of skeletal muscle contraction

Inferred from mutant phenotype PubMed 17524427. Source: BHF-UCL

regulation of sodium ion transmembrane transporter activity

Inferred from direct assay Ref.29Ref.30. Source: BHF-UCL

regulation of transforming growth factor beta receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

regulation of ventricular cardiac muscle cell membrane depolarization

Inferred from direct assay Ref.29. Source: BHF-UCL

regulation of ventricular cardiac muscle cell membrane repolarization

Inferred from mutant phenotype Ref.29. Source: BHF-UCL

triglyceride metabolic process

Inferred from sequence or structural similarity. Source: BHF-UCL

ventricular cardiac muscle cell action potential

Inferred from sequence or structural similarity PubMed 22879586. Source: BHF-UCL

   Cellular_componentGolgi membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

T-tubule

Inferred from sequence or structural similarity. Source: BHF-UCL

caveola

Inferred from electronic annotation. Source: UniProtKB-SubCell

cell surface

Inferred from electronic annotation. Source: Ensembl

dystrophin-associated glycoprotein complex

Inferred from direct assay Ref.7. Source: UniProtKB

endoplasmic reticulum

Inferred from direct assay PubMed 22792322. Source: MGI

membrane raft

Inferred from sequence or structural similarity. Source: BHF-UCL

neuromuscular junction

Inferred from sequence or structural similarity. Source: BHF-UCL

plasma membrane

Inferred from direct assay Ref.29. Source: BHF-UCL

sarcolemma

Inferred from direct assay PubMed 12847114Ref.29. Source: BHF-UCL

vesicle

Inferred from electronic annotation. Source: Ensembl

   Molecular_functioncalcium channel regulator activity

Inferred from direct assay PubMed 21084288. Source: BHF-UCL

connexin binding

Inferred from direct assay PubMed 19544087. Source: BHF-UCL

ion channel binding

Inferred from physical interaction Ref.29PubMed 21084288. Source: BHF-UCL

potassium channel inhibitor activity

Inferred from sequence or structural similarity PubMed 22879586. Source: BHF-UCL

protein C-terminus binding

Inferred from direct assay Ref.7. Source: UniProtKB

protein complex binding

Inferred from direct assay Ref.7. Source: UniProtKB

protein complex scaffold

Inferred from physical interaction Ref.29. Source: BHF-UCL

sodium channel regulator activity

Inferred from direct assay Ref.29. Source: BHF-UCL

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 151151Caveolin-3
PRO_0000144140

Regions

Topological domain1 – 8383Cytoplasmic Potential
Intramembrane84 – 10421Helical; Potential
Topological domain105 – 15147Cytoplasmic Potential
Region64 – 11451Required for interaction with DAG1

Amino acid modifications

Cross-link38Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO3) Ref.9

Natural variations

Natural variant141V → L in SIDS. Ref.30
Corresponds to variant rs121909281 [ dbSNP | Ensembl ].
VAR_043694
Natural variant271R → Q in HYPCK, RMD, LGMD1C and MPDT. Ref.11 Ref.13 Ref.14 Ref.17 Ref.21 Ref.27
VAR_011512
Natural variant281D → E in RMD and LGMD1C. Ref.19
VAR_015374
Natural variant291P → L in HYPCK. Ref.15
VAR_029540
Natural variant331N → K in LGMD1C and MPDT. Ref.25 Ref.27
Corresponds to variant rs1008642 [ dbSNP | Ensembl ].
VAR_021016
Natural variant441V → E in LGMD1C. Ref.25
VAR_021017
Natural variant461A → T in LGMD1C and RMD; decreased surface expression of the CAV3 protein. Ref.10 Ref.13 Ref.27
VAR_011513
Natural variant461A → V in RMD. Ref.13
VAR_011514
Natural variant531S → G in RMD. Ref.28
VAR_029541
Natural variant561G → S. Ref.3 Ref.12 Ref.29
Corresponds to variant rs72546667 [ dbSNP | Ensembl ].
VAR_029542
Natural variant571V → M in HYPCK. Ref.24
VAR_010742
Natural variant611S → R in a patient with mild proximal myopathy. Ref.27
VAR_026696
Natural variant64 – 663Missing in LGMD1C.
VAR_001402
Natural variant641T → P in LGMD1C. Ref.8
VAR_021018
Natural variant641T → S in CMH. Ref.23
VAR_029543
Natural variant721C → W. Ref.3 Ref.12 Ref.29
Corresponds to variant rs116840776 [ dbSNP | Ensembl ].
VAR_010743
Natural variant781T → M in LQT9 and SIDS. Ref.29 Ref.30
Corresponds to variant rs72546668 [ dbSNP | Ensembl ].
VAR_043695
Natural variant791L → R in LQT9 and SIDS. Ref.30
VAR_043696
Natural variant851A → T in LQT9. Ref.29
VAR_043697
Natural variant871L → P in RMD. Ref.20
Corresponds to variant rs28936685 [ dbSNP | Ensembl ].
VAR_016207
Natural variant931A → T in RMD. Ref.20 Ref.26
Corresponds to variant rs28936686 [ dbSNP | Ensembl ].
VAR_016208
Natural variant971F → C in LQT9; increase in late sodium current. Ref.29
VAR_043698
Natural variant971Missing in HYPCK. Ref.22
VAR_029544
Natural variant1051P → L in LGMD1C and RMD. Ref.1 Ref.13
VAR_001403
Natural variant1261R → H. Ref.12
VAR_029545
Natural variant1411S → R in LQT9; increase in late sodium current. Ref.29
VAR_043699

Sequences

Sequence LengthMass (Da)Tools
P56539 [UniParc].

Last modified July 15, 1998. Version 1.
Checksum: C695E14F5B8F4753

FASTA15117,259
        10         20         30         40         50         60 
MMAEEHTDLE AQIVKDIHCK EIDLVNRDPK NINEDIVKVD FEDVIAEPVG TYSFDGVWKV 

        70         80         90        100        110        120 
SYTTFTVSKY WCYRLLSTLL GVPLALLWGF LFACISFCHI WAVVPCIKSY LIEIQCISHI 

       130        140        150 
YSLCIRTFCN PLFAALGQVC SSIKVVLRKE V 

« Hide

References

« Hide 'large scale' references
[1]"Mutations in the caveolin-3 gene cause autosomal dominant limb-girdle muscular dystrophy."
Minetti C., Sotgia F., Bruno C., Scartezzini P., Broda P., Bado M., Masetti E., Mazzocco M., Egeo A., Donati M.A., Volonte D., Galbiati F., Cordone G., Bricarelli F.D., Lisanti M.P., Zara F.
Nat. Genet. 18:365-368(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS LGMD1C 64-THR--THR-66 DEL AND LEU-105.
[2]"Molecular cloning of human caveolin 3."
Biederer C., Ries S., Drobnik W., Schmitz G.
Biochim. Biophys. Acta 1406:5-9(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
Tissue: Skeletal muscle.
[3]"Caveolin-3 in muscular dystrophy."
McNally E.M., de Sa Moreira E., Duggan D.J., Bonnemann C.G., Lisanti M.P., Lidov H.G.W., Vainzof M., Passos-Bueno M.R., Hoffman E.P., Zatz M., Kunkel L.M.
Hum. Mol. Genet. 7:871-877(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], VARIANTS SER-56 AND TRP-72.
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Skeletal muscle.
[5]"The DNA sequence, annotation and analysis of human chromosome 3."
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J. expand/collapse author list , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[7]"Caveolin-3 directly interacts with the C-terminal tail of beta -dystroglycan. Identification of a central WW-like domain within caveolin family members."
Sotgia F., Lee J.K., Das K., Bedford M., Petrucci T.C., Macioce P., Sargiacomo M., Bricarelli F.D., Minetti C., Sudol M., Lisanti M.P.
J. Biol. Chem. 275:38048-38058(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DAG1.
[8]"The sarcolemmal proteins dysferlin and caveolin-3 interact in skeletal muscle."
Matsuda C., Hayashi Y.K., Ogawa M., Aoki M., Murayama K., Nishino I., Nonaka I., Arahata K., Brown R.H. Jr.
Hum. Mol. Genet. 10:1761-1766(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DYSF, VARIANT LGMD1C PRO-64.
[9]"Caveolin-3 undergoes SUMOylation by the SUMO E3 ligase PIASy: sumoylation affects G-protein-coupled receptor desensitization."
Fuhs S.R., Insel P.A.
J. Biol. Chem. 286:14830-14841(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: SUMOYLATION AT LYS-38.
[10]"Dissociation of the dystroglycan complex in caveolin-3-deficient limb girdle muscular dystrophy."
Herrmann R., Straub V., Blank M., Kutzick C., Franke N., Jacob E.N., Lenard H.-G., Kroger S., Voit T.
Hum. Mol. Genet. 9:2335-2340(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT LGMD1C THR-46.
[11]"Mutation in the CAV3 gene causes partial caveolin-3 deficiency and hyperCKemia."
Carbone I., Bruno C., Sotgia F., Bado M., Broda P., Masetti E., Panella A., Zara F., Bricarelli F.D., Cordone G., Lisanti M.P., Minetti C.
Neurology 54:1373-1376(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HYPCK GLN-27.
[12]"Mutations in the caveolin-3 gene: when are they pathogenic?"
de Paula F., Vainzof M., Bernardino A.L.F., McNally E., Kunkel L.M., Zatz M.
Am. J. Med. Genet. 99:303-307(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS SER-56; TRP-72 AND HIS-126.
[13]"Mutations in CAV3 cause mechanical hyperirritability of skeletal muscle in rippling muscle disease."
Betz R.C., Schoser B.G.H., Kasper D., Ricker K., Ramirez A., Stein V., Torbergsen T., Lee Y.-A., Nothen M.M., Wienker T.F., Malin J.-P., Propping P., Reis A., Mortier W., Jentsch T.J., Vorgerd M., Kubisch C.
Nat. Genet. 28:218-219(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS RMD GLN-27; THR-46; VAL-46 AND LEU-105, SURFACE EXPRESSION OF VARIANT RMD THR-46.
[14]"A sporadic case of rippling muscle disease caused by a de novo caveolin-3 mutation."
Vorgerd M., Ricker K., Ziemssen F., Kress W., Goebel H.H., Nix W.A., Kubisch C., Schoser B.G.H., Mortier W.
Neurology 57:2273-2277(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT RMD GLN-27.
[15]"Familial isolated hyperCKaemia associated with a new mutation in the caveolin-3 (CAV-3) gene."
Merlini L., Carbone I., Capanni C., Sabatelli P., Tortorelli S., Sotgia F., Lisanti M.P., Bruno C., Minetti C.
J. Neurol. Neurosurg. Psych. 73:65-67(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HYPCK LEU-29.
[16]Erratum
Merlini L., Carbone I., Capanni C., Sabatelli P., Tortorelli S., Sotgia F., Lisanti M.P., Bruno C., Minetti C.
J. Neurol. Neurosurg. Psych. 74:142-142(2003)
[17]"Mutation in the caveolin-3 gene causes a peculiar form of distal myopathy."
Tateyama M., Aoki M., Nishino I., Hayashi Y.K., Sekiguchi S., Shiga Y., Takahashi T., Onodera Y., Haginoya K., Kobayashi K., Iinuma K., Nonaka I., Arahata K., Itoyama Y.
Neurology 58:323-325(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MPDT GLN-27.
[18]Erratum
Tateyama M., Aoki M., Nishino I., Hayashi Y.K., Sekiguchi S., Shiga Y., Takahashi T., Onodera Y., Haginoya K., Kobayashi K., Iinuma K., Nonaka I., Arahata K., Itoyama Y.
Neurology 58:839-839(2002)
[19]"Consequences of a novel caveolin-3 mutation in a large German family."
Fischer D., Schroers A., Blumcke I., Urbach H., Zerres K., Mortier W., Vorgerd M., Schroder R.
Ann. Neurol. 53:233-241(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT RMD GLU-28, VARIANT LGMD1C GLU-28.
[20]"Homozygous mutations in caveolin-3 cause a severe form of rippling muscle disease."
Kubisch C., Schoser B.G.H., von Duering M., Betz R.C., Goebel H.-H., Zahn S., Ehrbrecht A., Aasly J., Schroers A., Popovic N., Lochmueller H., Schroeder J.M., Bruening T., Malin J.-P., Fricke B., Meinck H.-M., Torbergsen T., Engels H., Voss B., Vorgerd M.
Ann. Neurol. 53:512-520(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS RMD PRO-87 AND THR-93.
[21]"Limb-girdle muscular dystrophy in a 71-year-old woman with an R27Q mutation in the CAV3 gene."
Figarella-Branger D., Pouget J., Bernard R., Krahn M., Fernandez C., Levy N., Pellissier J.F.
Neurology 61:562-564(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT LGMD1C GLN-27.
[22]"A CAV3 microdeletion differentially affects skeletal muscle and myocardium."
Cagliani R., Bresolin N., Prelle A., Gallanti A., Fortunato F., Sironi M., Ciscato P., Fagiolari G., Bonato S., Galbiati S., Corti S., Lamperti C., Moggio M., Comi G.P.
Neurology 61:1513-1519(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HYPCK PHE-97 DEL.
[23]"Identification and functional analysis of a caveolin-3 mutation associated with familial hypertrophic cardiomyopathy."
Hayashi T., Arimura T., Ueda K., Shibata H., Hohda S., Takahashi M., Hori H., Koga Y., Oka N., Imaizumi T., Yasunami M., Kimura A.
Biochem. Biophys. Res. Commun. 313:178-184(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CMH SER-64.
[24]"A novel mutation in the caveolin-3 gene causing familial isolated hyperCKaemia."
Alias L., Gallano P., Moreno D., Pujol R., Martinez-Matos J.A., Baiget M., Ferrer I., Olive M.
Neuromuscul. Disord. 14:321-324(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HYPCK MET-57.
[25]"Two novel CAV3 gene mutations in Japanese families."
Sugie K., Murayama K., Noguchi S., Murakami N., Mochizuki M., Hayashi Y.K., Nonaka I., Nishino I.
Neuromuscul. Disord. 14:810-814(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS LGMD1C LYS-33 AND GLU-44.
[26]"Autosomal recessive rippling muscle disease with homozygous CAV3 mutations."
Kubisch C., Ketelsen U.-P., Goebel I., Omran H.
Ann. Neurol. 57:303-304(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT RMD THR-93.
[27]"Molecular and muscle pathology in a series of caveolinopathy patients."
Fulizio L., Chiara-Nascimbeni A., Fanin M., Piluso G., Politano L., Nigro V., Angelini C.
Hum. Mutat. 25:82-89(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HYPCK GLN-27, VARIANT LGMD1C THR-46, VARIANT MPDT LYS-33, VARIANT MYOPATHY ARG-61.
[28]"A new missense mutation in caveolin-3 gene causes rippling muscle disease."
Dotti M.T., Malandrini A., Gambelli S., Salvadori C., De Stefano N., Federico A.
J. Neurol. Sci. 243:61-64(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT RMD GLY-53.
[29]"Mutant caveolin-3 induces persistent late sodium current and is associated with long-QT syndrome."
Vatta M., Ackerman M.J., Ye B., Makielski J.C., Ughanze E.E., Taylor E.W., Tester D.J., Balijepalli R.C., Foell J.D., Li Z., Kamp T.J., Towbin J.A.
Circulation 114:2104-2112(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS LQT9 MET-78; THR-85; CYS-97 AND ARG-141, VARIANTS SER-56 AND TRP-72, CHARACTERIZATION OF VARIANTS LQT9 CYS-97 AND ARG-141.
[30]"Novel mechanism for sudden infant death syndrome: persistent late sodium current secondary to mutations in caveolin-3."
Cronk L.B., Ye B., Kaku T., Tester D.J., Vatta M., Makielski J.C., Ackerman M.J.
Heart Rhythm 4:161-166(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS LQT9/SIDS LEU-14; MET-78 AND ARG-79.
+Additional computationally mapped references.

Web resources

CAV3/LGMD1C

Caveolin-3/LGMD-1C page

GeneReviews
Wikipedia

Caveolin entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF043101 mRNA. Translation: AAC14931.1. Different initiation.
Y14747 mRNA. Translation: CAA75042.1.
AF036367, AF036366 Genomic DNA. Translation: AAC39758.1.
AF036365 mRNA. Translation: AAC39756.1.
AK291892 mRNA. Translation: BAF84581.1. Different initiation.
AC068312 Genomic DNA. No translation available.
BC069368 mRNA. Translation: AAH69368.1.
BC102033 mRNA. Translation: AAI02034.1.
BC102036 mRNA. Translation: AAI02037.1.
BC102037 mRNA. Translation: AAI02038.1.
RefSeqNP_001225.1. NM_001234.4.
NP_203123.1. NM_033337.2.
UniGeneHs.98303.

3D structure databases

ProteinModelPortalP56539.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107307. 17 interactions.
IntActP56539. 3 interactions.
MINTMINT-3021471.
STRING9606.ENSP00000341940.

PTM databases

PhosphoSiteP56539.

Polymorphism databases

DMDM3182930.

Proteomic databases

PaxDbP56539.
PRIDEP56539.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000343849; ENSP00000341940; ENSG00000182533.
ENST00000397368; ENSP00000380525; ENSG00000182533.
GeneID859.
KEGGhsa:859.
UCSCuc003bra.3. human.

Organism-specific databases

CTD859.
GeneCardsGC03P008775.
HGNCHGNC:1529. CAV3.
HPACAB017518.
CAB018557.
MIM123320. phenotype.
192600. phenotype.
272120. phenotype.
601253. gene.
606072. phenotype.
607801. phenotype.
611818. phenotype.
614321. phenotype.
neXtProtNX_P56539.
Orphanet265. Autosomal dominant limb-girdle muscular dystrophy type 1C.
155. Familial isolated hypertrophic cardiomyopathy.
97238. Rippling muscle disease.
101016. Romano-Ward syndrome.
PharmGKBPA26109.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG86001.
HOGENOMHOG000036550.
HOVERGENHBG003422.
InParanoidP56539.
KOK12959.
OMAHFKEIDL.
OrthoDBEOG7V1FSD.
PhylomeDBP56539.
TreeFamTF315736.

Enzyme and pathway databases

SignaLinkP56539.

Gene expression databases

BgeeP56539.
CleanExHS_CAV3.
GenevestigatorP56539.

Family and domain databases

InterProIPR001612. Caveolin.
IPR018361. Caveolin_CS.
[Graphical view]
PANTHERPTHR10844. PTHR10844. 1 hit.
PfamPF01146. Caveolin. 1 hit.
[Graphical view]
PROSITEPS01210. CAVEOLIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiCaveolin_3.
GenomeRNAi859.
NextBio3566.
PROP56539.
SOURCESearch...

Entry information

Entry nameCAV3_HUMAN
AccessionPrimary (citable) accession number: P56539
Secondary accession number(s): A8K777, Q3T1A4
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 15, 1998
Last modified: April 16, 2014
This is version 136 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM