P56539 (CAV3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Caveolin-3

Alternative name(s):
M-caveolin

Gene names

Name:

CAV3

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	151 AA.
Sequence status	Complete.
Protein existence	Evidence 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.5 Ref.6
Subcellular location	Golgi apparatus membrane; Peripheral membrane protein By similarity. Cell membrane; Peripheral membrane protein By similarity. Membrane › caveola; 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
Involvement in disease	Defects in CAV3 are the cause of limb-girdle muscular dystrophy type 1C (LGMD1C) [MIM:607801]. LGMD1C is a myopathy characterized by calf hypertrophy and mild to moderate proximal muscle weakness. LGMD1C inheritance can be autosomal dominant or recessive. Ref.1 Ref.6 Ref.7 Ref.16 Ref.18 Ref.22 Ref.24 Defects in CAV3 are a cause of hyperCKmia (HYPCK) [MIM:123320]. It is a disease characterized by persistent elevated levels of serum creatine kinase without muscle weakness. Ref.8 Ref.12 Ref.19 Ref.21 Ref.24 Defects in CAV3 are a cause of rippling muscle disease (RMD) [MIM:606072]. RMD is a 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. Ref.10 Ref.11 Ref.16 Ref.17 Ref.23 Ref.25 Defects in CAV3 are a cause of familial hypertrophic cardiomyopathy (CMH) [MIM:192600]; also designated FHC or HCM. Familial hypertrophic cardiomyopathy is 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. Ref.20 Defects in CAV3 are the cause of long QT syndrome type 9 (LQT9) [MIM:611818]. Long QT syndromes are heart disorders characterized by a prolonged QT interval on the ECG and polymorphic ventricular arrhythmias. They cause syncope and sudden death in response to excercise or emotional stress. They can present with a sentinel event of sudden cardiac death in infancy. Ref.26 Ref.27 Defects in CAV3 can be a cause of 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. Long QT syndromes-associated mutations can be responsible for some SIDS cases. Defects in CAV3 are the cause of 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. Ref.14 Ref.24
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.

Ontologies

Keywords
Cellular component	Cell membrane Golgi apparatus Membrane
Coding sequence diversity	Polymorphism
Disease	Cardiomyopathy Disease mutation Limb-girdle muscular dystrophy Long QT syndrome
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	T-tubule organization Traceable author statement. Source: BHF-UCL cell growth Inferred from sequence or structural similarity. Source: BHF-UCL elevation of cytosolic calcium ion concentration Inferred from sequence or structural similarity. Source: BHF-UCL muscle organ development Traceable author statement Ref.5. Source: UniProtKB negative regulation of MAP kinase activity Inferred from mutant phenotype. Source: BHF-UCL negative regulation of cardiac muscle hypertrophy Inferred from mutant phenotype. Source: BHF-UCL negative regulation of cell size Inferred from mutant phenotype. Source: BHF-UCL negative regulation of sarcomere organization Inferred from mutant phenotype. Source: BHF-UCL positive regulation of microtubule polymerization Inferred from sequence or structural similarity. Source: BHF-UCL regulation of skeletal muscle contraction Inferred from mutant phenotype. Source: BHF-UCL regulation of ventricular cardiomyocyte membrane repolarization Inferred from mutant phenotype Ref.26Ref.27. Source: BHF-UCL
Cellular component	Golgi 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 dystrophin-associated glycoprotein complex Inferred from direct assay Ref.5. Source: UniProtKB neuromuscular junction Inferred from sequence or structural similarity. Source: BHF-UCL
Molecular function	protein C-terminus binding Inferred from direct assay Ref.5. Source: UniProtKB protein complex binding Inferred from direct assay Ref.5. Source: UniProtKB protein complex scaffold Inferred from sequence or structural similarity. Source: BHF-UCL sodium channel regulator activity Inferred from mutant phenotype Ref.27. Source: BHF-UCL
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 151	151	Caveolin-3		PRO_0000144140
Regions
	Topological domain	1 – 83	83	Cytoplasmic Potential
	Intramembrane	84 – 104	21	Helical; Potential
	Topological domain	105 – 151	47	Cytoplasmic Potential
	Region	64 – 114	51	Required for interaction with DAG1
Natural variations
	Natural variant	14	1	V → L in SIDS. Ref.27		VAR_043694
	Natural variant	27	1	R → Q in HYPCK, RMD, LGMD1C and MPDT. Ref.8 Ref.10 Ref.11 Ref.14 Ref.18 Ref.24		VAR_011512
	Natural variant	28	1	D → E in RMD and LGMD1C. Ref.16		VAR_015374
	Natural variant	29	1	P → L in HYPCK. Ref.12		VAR_029540
	Natural variant	33	1	N → K in LGMD1C and MPDT. Ref.22 Ref.24		VAR_021016
	Natural variant	44	1	V → E in LGMD1C. Ref.22		VAR_021017
	Natural variant	46	1	A → T in LGMD1C and RMD; decreased surface expression of the CAV3 protein. Ref.7 Ref.10 Ref.24		VAR_011513
	Natural variant	46	1	A → V in RMD. Ref.10		VAR_011514
	Natural variant	53	1	S → G in RMD. Ref.25		VAR_029541
	Natural variant	56	1	G → S. Ref.3 Ref.9 Ref.26		VAR_029542
	Natural variant	57	1	V → M in HYPCK. Ref.21		VAR_010742
	Natural variant	61	1	S → R in a patient with mild proximal myopathy. Ref.24		VAR_026696
	Natural variant	64 – 66	3	Missing in LGMD1C.		VAR_001402
	Natural variant	64	1	T → P in LGMD1C. Ref.6		VAR_021018
	Natural variant	64	1	T → S in CMH. Ref.20		VAR_029543
	Natural variant	72	1	C → W. Ref.3 Ref.9 Ref.26		VAR_010743
	Natural variant	78	1	T → M in LQT9 and SIDS. Ref.26 Ref.27		VAR_043695
	Natural variant	79	1	L → R in LQT9 and SIDS. Ref.27		VAR_043696
	Natural variant	85	1	A → T in LQT9. Ref.26		VAR_043697
	Natural variant	87	1	L → P in RMD. Ref.17 Corresponds to variant rs28936685 [ dbSNP | Ensembl ].		VAR_016207
	Natural variant	93	1	A → T in RMD. Ref.17 Ref.23 Corresponds to variant rs28936686 [ dbSNP | Ensembl ].		VAR_016208
	Natural variant	97	1	F → C in LQT9; increase in late sodium current. Ref.26		VAR_043698
	Natural variant	97	1	Missing in HYPCK.		VAR_029544
	Natural variant	105	1	P → L in LGMD1C and RMD. Ref.1 Ref.10		VAR_001403
	Natural variant	126	1	R → H. Ref.9		VAR_029545
	Natural variant	141	1	S → R in LQT9; increase in late sodium current. Ref.26		VAR_043699

Sequences

	Sequence		Length	Mass (Da)
	P56539 [UniParc]. Last modified July 15, 1998. Version 1. Checksum: C695E14F5B8F4753	FASTA	151	17,259
	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

References

	« Hide 'large scale' referencesShow '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: 9537420] [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: 9545514] [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: 9536092] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], VARIANTS SER-56 AND TRP-72.
[4]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]	"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: 10988290] [Abstract] Cited for: INTERACTION WITH DAG1.
[6]	"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: 11532985] [Abstract] Cited for: INTERACTION WITH DYSF, VARIANT LGMD1C PRO-64.
[7]	"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: 11001938] [Abstract] Cited for: VARIANT LGMD1C THR-46.
[8]	"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: 10746614] [Abstract] Cited for: VARIANT HYPCK GLN-27.
[9]	"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: 11251997] [Abstract] Cited for: VARIANTS SER-56; TRP-72 AND HIS-126.
[10]	"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: 11431690] [Abstract] Cited for: VARIANTS RMD GLN-27; THR-46; VAL-46 AND LEU-105, SURFACE EXPRESSION OF VARIANT RMD THR-46.
[11]	"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: 11756609] [Abstract] Cited for: VARIANT RMD GLN-27.
[12]	"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: 12082049] [Abstract] Cited for: VARIANT HYPCK LEU-29.
[13]	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)
[14]	"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: 11805270] [Abstract] Cited for: VARIANT MPDT GLN-27.
[15]	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)
[16]	"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: 12557291] [Abstract] Cited for: VARIANT RMD GLU-28, VARIANT LGMD1C GLU-28.
[17]	"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: 12666119] [Abstract] Cited for: VARIANTS RMD PRO-87 AND THR-93.
[18]	"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: 12939441] [Abstract] Cited for: VARIANT LGMD1C GLN-27.
[19]	"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: 14663034] [Abstract] Cited for: VARIANT HYPCK PHE-97 DEL.
[20]	"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: 14672715] [Abstract] Cited for: VARIANT CMH SER-64.
[21]	"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: 15099591] [Abstract] Cited for: VARIANT HYPCK MET-57.
[22]	"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: 15564037] [Abstract] Cited for: VARIANTS LGMD1C LYS-33 AND GLU-44.
[23]	"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: 15668980] [Abstract] Cited for: VARIANT RMD THR-93.
[24]	"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: 15580566] [Abstract] Cited for: VARIANT HYPCK GLN-27, VARIANT LGMD1C THR-46, VARIANT MPDT LYS-33, VARIANT MYOPATHY ARG-61.
[25]	"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: 16458928] [Abstract] Cited for: VARIANT RMD GLY-53.
[26]	"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: 17060380] [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.
[27]	"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: 17275750] [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. BC069368 mRNA. Translation: AAH69368.1. BC102033 mRNA. Translation: AAI02034.1. BC102036 mRNA. Translation: AAI02037.1. BC102037 mRNA. Translation: AAI02038.1.
IPI	IPI00790433.
RefSeq	NP_001225.1. NM_001234.4. NP_203123.1. NM_033337.2.
UniGene	Hs.98303.
3D structure databases
ProteinModelPortal	P56539.
ModBase	Search...
Protein-protein interaction databases
IntAct	P56539. 2 interactions.
STRING	P56539.
Polymorphism databases
DMDM	3182930.
Proteomic databases
PRIDE	P56539.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000343849; ENSP00000341940; ENSG00000182533. ENST00000397368; ENSP00000380525; ENSG00000182533.
GeneID	859.
KEGG	hsa:859.
UCSC	uc003bra.1. human.
Organism-specific databases
CTD	859.
GeneCards	GC03P008775.
H-InvDB	HIX0030704.
HGNC	HGNC:1529. CAV3.
HPA	CAB017518. CAB018557.
MIM	123320. phenotype. 192600. phenotype. 272120. phenotype. 601253. gene. 606072. phenotype. 607801. phenotype. 611818. phenotype. 614321. phenotype.
neXtProt	NX_P56539.
Orphanet	265. Autosomal dominant limb-girdle muscular dystrophy type 1C. 155. Familial isolated hypertrophic cardiomyopathy. 97238. Rippling muscle disease. 101016. Romano-Ward syndrome.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG12264.
GeneTree	ENSGT00390000014924.
HOGENOM	HBG443750.
HOVERGEN	HBG003422.
InParanoid	P56539.
OMA	EDIVKVD.
OrthoDB	EOG4DFPPG.
PhylomeDB	P56539.
Enzyme and pathway databases
Pathway_Interaction_DB	pdgfrapathway. PDGFR-alpha signaling pathway.
Gene expression databases
ArrayExpress	P56539.
Bgee	P56539.
CleanEx	HS_CAV3.
Genevestigator	P56539.
GermOnline	ENSG00000182533. Homo sapiens.
Family and domain databases
InterPro	IPR001612. Caveolin. IPR018361. Caveolin_CS. [Graphical view]
KO	K12959.
PANTHER	PTHR10844. Caveolin. 1 hit.
Pfam	PF01146. Caveolin. 1 hit. [Graphical view]
PROSITE	PS01210. CAVEOLIN. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	3566.
SOURCE	Search...

Entry information

Entry name

CAV3_HUMAN

Accession

Primary (citable) accession number: P56539
Secondary accession number(s): Q3T1A4

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	July 15, 1998
Last modified:	January 25, 2012
This is version 111 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.