CAV3_HUMAN
ID CAV3_HUMAN Reviewed; 151 AA.
AC P56539; A8K777; Q3T1A4;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 1.
DT 03-AUG-2022, entry version 203.
DE RecName: Full=Caveolin-3;
DE AltName: Full=M-caveolin;
GN Name=CAV3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS RMD2 64-THR--THR-66 DEL AND
RP LEU-105.
RX PubMed=9537420; DOI=10.1038/ng0498-365;
RA Minetti C., Sotgia F., Bruno C., Scartezzini P., Broda P., Bado M.,
RA Masetti E., Mazzocco M., Egeo A., Donati M.A., Volonte D., Galbiati F.,
RA Cordone G., Bricarelli F.D., Lisanti M.P., Zara F.;
RT "Mutations in the caveolin-3 gene cause autosomal dominant limb-girdle
RT muscular dystrophy.";
RL Nat. Genet. 18:365-368(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Skeletal muscle;
RX PubMed=9545514; DOI=10.1016/s0925-4439(97)00095-1;
RA Biederer C., Ries S., Drobnik W., Schmitz G.;
RT "Molecular cloning of human caveolin 3.";
RL Biochim. Biophys. Acta 1406:5-9(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND VARIANTS SER-56 AND TRP-72.
RX PubMed=9536092; DOI=10.1093/hmg/7.5.871;
RA McNally E.M., de Sa Moreira E., Duggan D.J., Bonnemann C.G., Lisanti M.P.,
RA Lidov H.G.W., Vainzof M., Passos-Bueno M.R., Hoffman E.P., Zatz M.,
RA Kunkel L.M.;
RT "Caveolin-3 in muscular dystrophy.";
RL Hum. Mol. Genet. 7:871-877(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skeletal muscle;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP INTERACTION WITH DAG1.
RX PubMed=10988290; DOI=10.1074/jbc.m005321200;
RA Sotgia F., Lee J.K., Das K., Bedford M., Petrucci T.C., Macioce P.,
RA Sargiacomo M., Bricarelli F.D., Minetti C., Sudol M., Lisanti M.P.;
RT "Caveolin-3 directly interacts with the C-terminal tail of beta
RT -dystroglycan. Identification of a central WW-like domain within caveolin
RT family members.";
RL J. Biol. Chem. 275:38048-38058(2000).
RN [8]
RP INTERACTION WITH DYSF, AND VARIANT RMD2 PRO-64.
RX PubMed=11532985; DOI=10.1093/hmg/10.17.1761;
RA Matsuda C., Hayashi Y.K., Ogawa M., Aoki M., Murayama K., Nishino I.,
RA Nonaka I., Arahata K., Brown R.H. Jr.;
RT "The sarcolemmal proteins dysferlin and caveolin-3 interact in skeletal
RT muscle.";
RL Hum. Mol. Genet. 10:1761-1766(2001).
RN [9]
RP FUNCTION.
RX PubMed=19262564; DOI=10.1038/emboj.2009.46;
RA McMahon K.A., Zajicek H., Li W.P., Peyton M.J., Minna J.D., Hernandez V.J.,
RA Luby-Phelps K., Anderson R.G.;
RT "SRBC/cavin-3 is a caveolin adapter protein that regulates caveolae
RT function.";
RL EMBO J. 28:1001-1015(2009).
RN [10]
RP SUMOYLATION AT LYS-38.
RX PubMed=21362625; DOI=10.1074/jbc.m110.214270;
RA Fuhs S.R., Insel P.A.;
RT "Caveolin-3 undergoes SUMOylation by the SUMO E3 ligase PIASy: sumoylation
RT affects G-protein-coupled receptor desensitization.";
RL J. Biol. Chem. 286:14830-14841(2011).
RN [11]
RP INTERACTION WITH CAVIN1; CAVIN2 AND CAVIN4.
RX PubMed=24567387; DOI=10.1073/pnas.1315359111;
RA Ogata T., Naito D., Nakanishi N., Hayashi Y.K., Taniguchi T., Miyagawa K.,
RA Hamaoka T., Maruyama N., Matoba S., Ikeda K., Yamada H., Oh H., Ueyama T.;
RT "MURC/Cavin-4 facilitates recruitment of ERK to caveolae and concentric
RT cardiac hypertrophy induced by alpha1-adrenergic receptors.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:3811-3816(2014).
RN [12]
RP INTERACTION WITH CAVIN4.
RX PubMed=26497963; DOI=10.1152/ajpheart.00446.2015;
RA Naito D., Ogata T., Hamaoka T., Nakanishi N., Miyagawa K., Maruyama N.,
RA Kasahara T., Taniguchi T., Nishi M., Matoba S., Ueyama T.;
RT "The coiled-coil domain of MURC/cavin-4 is involved in membrane trafficking
RT of caveolin-3 in cardiomyocytes.";
RL Am. J. Physiol. 309:H2127-H2136(2015).
RN [13]
RP VARIANT RMD2 THR-46.
RX PubMed=11001938; DOI=10.1093/oxfordjournals.hmg.a018926;
RA Herrmann R., Straub V., Blank M., Kutzick C., Franke N., Jacob E.N.,
RA Lenard H.-G., Kroger S., Voit T.;
RT "Dissociation of the dystroglycan complex in caveolin-3-deficient limb
RT girdle muscular dystrophy.";
RL Hum. Mol. Genet. 9:2335-2340(2000).
RN [14]
RP VARIANT HYPCK GLN-27.
RX PubMed=10746614; DOI=10.1212/wnl.54.6.1373;
RA Carbone I., Bruno C., Sotgia F., Bado M., Broda P., Masetti E., Panella A.,
RA Zara F., Bricarelli F.D., Cordone G., Lisanti M.P., Minetti C.;
RT "Mutation in the CAV3 gene causes partial caveolin-3 deficiency and
RT hyperCKemia.";
RL Neurology 54:1373-1376(2000).
RN [15]
RP VARIANTS SER-56; TRP-72 AND HIS-126.
RX PubMed=11251997;
RX DOI=10.1002/1096-8628(2001)9999:9999<::aid-ajmg1168>3.0.co;2-o;
RA de Paula F., Vainzof M., Bernardino A.L.F., McNally E., Kunkel L.M.,
RA Zatz M.;
RT "Mutations in the caveolin-3 gene: when are they pathogenic?";
RL Am. J. Med. Genet. 99:303-307(2001).
RN [16]
RP INVOLVEMENT IN RMD2, VARIANTS RMD2 GLN-27; THR-46; VAL-46 AND LEU-105, AND
RP CHARACTERIZATION OF VARIANT RMD2 THR-46.
RX PubMed=11431690; DOI=10.1038/90050;
RA Betz R.C., Schoser B.G.H., Kasper D., Ricker K., Ramirez A., Stein V.,
RA Torbergsen T., Lee Y.-A., Nothen M.M., Wienker T.F., Malin J.-P.,
RA Propping P., Reis A., Mortier W., Jentsch T.J., Vorgerd M., Kubisch C.;
RT "Mutations in CAV3 cause mechanical hyperirritability of skeletal muscle in
RT rippling muscle disease.";
RL Nat. Genet. 28:218-219(2001).
RN [17]
RP INVOLVEMENT IN RMD2, AND VARIANT RMD2 GLN-27.
RX PubMed=11756609; DOI=10.1212/wnl.57.12.2273;
RA Vorgerd M., Ricker K., Ziemssen F., Kress W., Goebel H.H., Nix W.A.,
RA Kubisch C., Schoser B.G.H., Mortier W.;
RT "A sporadic case of rippling muscle disease caused by a de novo caveolin-3
RT mutation.";
RL Neurology 57:2273-2277(2001).
RN [18]
RP VARIANT HYPCK LEU-29.
RX PubMed=12082049; DOI=10.1136/jnnp.73.1.65;
RA Merlini L., Carbone I., Capanni C., Sabatelli P., Tortorelli S., Sotgia F.,
RA Lisanti M.P., Bruno C., Minetti C.;
RT "Familial isolated hyperCKaemia associated with a new mutation in the
RT caveolin-3 (CAV-3) gene.";
RL J. Neurol. Neurosurg. Psych. 73:65-67(2002).
RN [19]
RP ERRATUM OF PUBMED:12082049.
RA Merlini L., Carbone I., Capanni C., Sabatelli P., Tortorelli S., Sotgia F.,
RA Lisanti M.P., Bruno C., Minetti C.;
RL J. Neurol. Neurosurg. Psych. 74:142-142(2003).
RN [20]
RP VARIANT MPDT GLN-27.
RX PubMed=11805270; DOI=10.1212/wnl.58.2.323;
RA Tateyama M., Aoki M., Nishino I., Hayashi Y.K., Sekiguchi S., Shiga Y.,
RA Takahashi T., Onodera Y., Haginoya K., Kobayashi K., Iinuma K., Nonaka I.,
RA Arahata K., Itoyama Y.;
RT "Mutation in the caveolin-3 gene causes a peculiar form of distal
RT myopathy.";
RL Neurology 58:323-325(2002).
RN [21]
RP ERRATUM OF PUBMED:11805270.
RA Tateyama M., Aoki M., Nishino I., Hayashi Y.K., Sekiguchi S., Shiga Y.,
RA Takahashi T., Onodera Y., Haginoya K., Kobayashi K., Iinuma K., Nonaka I.,
RA Arahata K., Itoyama Y.;
RL Neurology 58:839-839(2002).
RN [22]
RP VARIANT RMD2 GLU-28.
RX PubMed=12557291; DOI=10.1002/ana.10442;
RA Fischer D., Schroers A., Blumcke I., Urbach H., Zerres K., Mortier W.,
RA Vorgerd M., Schroder R.;
RT "Consequences of a novel caveolin-3 mutation in a large German family.";
RL Ann. Neurol. 53:233-241(2003).
RN [23]
RP VARIANTS RMD2 PRO-87 AND THR-93.
RX PubMed=12666119; DOI=10.1002/ana.10501;
RA Kubisch C., Schoser B.G.H., von Duering M., Betz R.C., Goebel H.-H.,
RA Zahn S., Ehrbrecht A., Aasly J., Schroers A., Popovic N., Lochmueller H.,
RA Schroeder J.M., Bruening T., Malin J.-P., Fricke B., Meinck H.-M.,
RA Torbergsen T., Engels H., Voss B., Vorgerd M.;
RT "Homozygous mutations in caveolin-3 cause a severe form of rippling muscle
RT disease.";
RL Ann. Neurol. 53:512-520(2003).
RN [24]
RP VARIANT RMD2 GLN-27.
RX PubMed=12939441; DOI=10.1212/01.wnl.0000076486.57572.5c;
RA Figarella-Branger D., Pouget J., Bernard R., Krahn M., Fernandez C.,
RA Levy N., Pellissier J.F.;
RT "Limb-girdle muscular dystrophy in a 71-year-old woman with an R27Q
RT mutation in the CAV3 gene.";
RL Neurology 61:562-564(2003).
RN [25]
RP VARIANT HYPCK PHE-97 DEL.
RX PubMed=14663034; DOI=10.1212/01.wnl.0000097320.35982.03;
RA Cagliani R., Bresolin N., Prelle A., Gallanti A., Fortunato F., Sironi M.,
RA Ciscato P., Fagiolari G., Bonato S., Galbiati S., Corti S., Lamperti C.,
RA Moggio M., Comi G.P.;
RT "A CAV3 microdeletion differentially affects skeletal muscle and
RT myocardium.";
RL Neurology 61:1513-1519(2003).
RN [26]
RP VARIANT CMH SER-64.
RX PubMed=14672715; DOI=10.1016/j.bbrc.2003.11.101;
RA Hayashi T., Arimura T., Ueda K., Shibata H., Hohda S., Takahashi M.,
RA Hori H., Koga Y., Oka N., Imaizumi T., Yasunami M., Kimura A.;
RT "Identification and functional analysis of a caveolin-3 mutation associated
RT with familial hypertrophic cardiomyopathy.";
RL Biochem. Biophys. Res. Commun. 313:178-184(2004).
RN [27]
RP VARIANT HYPCK MET-57.
RX PubMed=15099591; DOI=10.1016/j.nmd.2004.01.006;
RA Alias L., Gallano P., Moreno D., Pujol R., Martinez-Matos J.A., Baiget M.,
RA Ferrer I., Olive M.;
RT "A novel mutation in the caveolin-3 gene causing familial isolated
RT hyperCKaemia.";
RL Neuromuscul. Disord. 14:321-324(2004).
RN [28]
RP VARIANTS RMD2 LYS-33 AND GLU-44.
RX PubMed=15564037; DOI=10.1016/j.nmd.2004.08.008;
RA Sugie K., Murayama K., Noguchi S., Murakami N., Mochizuki M., Hayashi Y.K.,
RA Nonaka I., Nishino I.;
RT "Two novel CAV3 gene mutations in Japanese families.";
RL Neuromuscul. Disord. 14:810-814(2004).
RN [29]
RP VARIANT RMD2 THR-93.
RX PubMed=15668980; DOI=10.1002/ana.20350;
RA Kubisch C., Ketelsen U.-P., Goebel I., Omran H.;
RT "Autosomal recessive rippling muscle disease with homozygous CAV3
RT mutations.";
RL Ann. Neurol. 57:303-304(2005).
RN [30]
RP VARIANT HYPCK GLN-27, VARIANT RMD2 THR-46, VARIANT MPDT LYS-33, AND VARIANT
RP MYOPATHY ARG-61.
RX PubMed=15580566; DOI=10.1002/humu.20119;
RA Fulizio L., Chiara-Nascimbeni A., Fanin M., Piluso G., Politano L.,
RA Nigro V., Angelini C.;
RT "Molecular and muscle pathology in a series of caveolinopathy patients.";
RL Hum. Mutat. 25:82-89(2005).
RN [31]
RP VARIANT RMD2 GLY-53.
RX PubMed=16458928; DOI=10.1016/j.jns.2005.11.032;
RA Dotti M.T., Malandrini A., Gambelli S., Salvadori C., De Stefano N.,
RA Federico A.;
RT "A new missense mutation in caveolin-3 gene causes rippling muscle
RT disease.";
RL J. Neurol. Sci. 243:61-64(2006).
RN [32]
RP VARIANTS LQT9 MET-78; THR-85; CYS-97 AND ARG-141, VARIANTS SER-56 AND
RP TRP-72, AND CHARACTERIZATION OF VARIANTS LQT9 CYS-97 AND ARG-141.
RX PubMed=17060380; DOI=10.1161/circulationaha.106.635268;
RA Vatta M., Ackerman M.J., Ye B., Makielski J.C., Ughanze E.E., Taylor E.W.,
RA Tester D.J., Balijepalli R.C., Foell J.D., Li Z., Kamp T.J., Towbin J.A.;
RT "Mutant caveolin-3 induces persistent late sodium current and is associated
RT with long-QT syndrome.";
RL Circulation 114:2104-2112(2006).
RN [33]
RP VARIANTS LQT9/SIDS LEU-14; MET-78 AND ARG-79, AND INVOLVEMENT IN SIDS.
RX PubMed=17275750; DOI=10.1016/j.hrthm.2006.11.030;
RA Cronk L.B., Ye B., Kaku T., Tester D.J., Vatta M., Makielski J.C.,
RA Ackerman M.J.;
RT "Novel mechanism for sudden infant death syndrome: persistent late sodium
RT current secondary to mutations in caveolin-3.";
RL Heart Rhythm 4:161-166(2007).
CC -!- FUNCTION: May act as a scaffolding protein within caveolar membranes.
CC Interacts directly with G-protein alpha subunits and can functionally
CC regulate their activity. May also regulate voltage-gated potassium
CC channels. Plays a role in the sarcolemma repair mechanism of both
CC skeletal muscle and cardiomyocytes that permits rapid resealing of
CC membranes disrupted by mechanical stress (By similarity). Mediates the
CC recruitment of CAVIN2 and CAVIN3 proteins to the caveolae
CC (PubMed:19262564). {ECO:0000250|UniProtKB:P51637,
CC ECO:0000269|PubMed:19262564}.
CC -!- SUBUNIT: Homooligomer. Interacts with DLG1 and KCNA5; forms a ternary
CC complex. Interacts with TRIM72. Interacts with MUSK; may regulate MUSK
CC signaling. Interacts with DAG1 (via its C-terminal); the interaction
CC prevents binding of DAG1 with DMD (PubMed:10988290). Interacts with
CC DYSF (PubMed:11532985). Interacts with BVES (By similarity). Interacts
CC with CAVIN1 and CAVIN2 (PubMed:24567387). Interacts with CAVIN4
CC (PubMed:24567387, PubMed:11251997). {ECO:0000250|UniProtKB:P51637,
CC ECO:0000250|UniProtKB:P51638, ECO:0000269|PubMed:10988290,
CC ECO:0000269|PubMed:11251997, ECO:0000269|PubMed:11532985,
CC ECO:0000269|PubMed:24567387}.
CC -!- INTERACTION:
CC P56539; Q6NZI2: CAVIN1; NbExp=3; IntAct=EBI-3905936, EBI-2559016;
CC P56539; Q8NE08: COL25A1; NbExp=3; IntAct=EBI-3905936, EBI-25836642;
CC P56539; Q96AL5: PBX3; NbExp=3; IntAct=EBI-3905936, EBI-741171;
CC P56539; Q8N0V3: RBFA; NbExp=3; IntAct=EBI-3905936, EBI-3232108;
CC P56539; P0DOE7: M; Xeno; NbExp=2; IntAct=EBI-3905936, EBI-10042882;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}. Cell membrane
CC {ECO:0000250|UniProtKB:P51638}; Peripheral membrane protein
CC {ECO:0000250}. Membrane, caveola {ECO:0000250|UniProtKB:P51637};
CC Peripheral membrane protein {ECO:0000250}. Cell membrane, sarcolemma
CC {ECO:0000250|UniProtKB:P51637}. Note=Potential hairpin-like structure
CC in the membrane. Membrane protein of caveolae (By similarity).
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed predominantly in muscle.
CC {ECO:0000269|PubMed:9545514}.
CC -!- PTM: Sumoylation with SUMO3 by PIAS4 may reduce agonist-induced
CC internalization and desensitization of adrenergic receptor ABRD2.
CC {ECO:0000269|PubMed:21362625}.
CC -!- DISEASE: HyperCKmia (HYPCK) [MIM:123320]: Characterized by persistent
CC elevated levels of serum creatine kinase without muscle weakness.
CC {ECO:0000269|PubMed:10746614, ECO:0000269|PubMed:12082049,
CC ECO:0000269|PubMed:14663034, ECO:0000269|PubMed:15099591,
CC ECO:0000269|PubMed:15580566}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Rippling muscle disease 2 (RMD2) [MIM:606072]: A disorder
CC characterized by mechanically triggered contractions of skeletal
CC muscle. Mechanical stimulation leads to electrically silent muscle
CC contractions that spread to neighboring fibers and cause visible
CC ripples to move over the muscle. RMD2 inheritance is autosomal dominant
CC or autosomal recessive. {ECO:0000269|PubMed:11001938,
CC ECO:0000269|PubMed:11431690, ECO:0000269|PubMed:11532985,
CC ECO:0000269|PubMed:11756609, ECO:0000269|PubMed:12557291,
CC ECO:0000269|PubMed:12666119, ECO:0000269|PubMed:12939441,
CC ECO:0000269|PubMed:15564037, ECO:0000269|PubMed:15580566,
CC ECO:0000269|PubMed:15668980, ECO:0000269|PubMed:16458928,
CC ECO:0000269|PubMed:9537420}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Cardiomyopathy, familial hypertrophic (CMH) [MIM:192600]: A
CC hereditary heart disorder characterized by ventricular hypertrophy,
CC which is usually asymmetric and often involves the interventricular
CC septum. The symptoms include dyspnea, syncope, collapse, palpitations,
CC and chest pain. They can be readily provoked by exercise. The disorder
CC has inter- and intrafamilial variability ranging from benign to
CC malignant forms with high risk of cardiac failure and sudden cardiac
CC death. {ECO:0000269|PubMed:14672715}. Note=The disease is caused by
CC variants affecting the gene represented in this entry.
CC -!- DISEASE: Long QT syndrome 9 (LQT9) [MIM:611818]: A heart disorder
CC characterized by a prolonged QT interval on the ECG and polymorphic
CC ventricular arrhythmias. They cause syncope and sudden death in
CC response to exercise or emotional stress, and can present with a
CC sentinel event of sudden cardiac death in infancy.
CC {ECO:0000269|PubMed:17060380, ECO:0000269|PubMed:17275750}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Sudden infant death syndrome (SIDS) [MIM:272120]: SIDS is the
CC sudden death of an infant younger than 1 year that remains unexplained
CC after a thorough case investigation, including performance of a
CC complete autopsy, examination of the death scene, and review of
CC clinical history. Pathophysiologic mechanisms for SIDS may include
CC respiratory dysfunction, cardiac dysrhythmias, cardiorespiratory
CC instability, and inborn errors of metabolism, but definitive pathogenic
CC mechanisms precipitating an infant sudden death remain elusive.
CC {ECO:0000269|PubMed:17275750}. Note=Disease susceptibility is
CC associated with variants affecting the gene represented in this entry.
CC -!- DISEASE: Myopathy, distal, Tateyama type (MPDT) [MIM:614321]: A
CC disorder characterized by progressive muscular atrophy and muscle
CC weakness beginning in the hands, the legs, or the feet. Muscle atrophy
CC may be restricted to the small muscles of the hands and feet.
CC {ECO:0000269|PubMed:11805270, ECO:0000269|PubMed:15580566}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the caveolin family. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-2 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC14931.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAF84581.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=CAV3/LGMD1C; Note=Caveolin-3/LGMD-1C page;
CC URL="https://www.dmd.nl/cav3_home.html";
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Caveolin entry;
CC URL="https://en.wikipedia.org/wiki/Caveolin";
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DR EMBL; AF043101; AAC14931.1; ALT_INIT; mRNA.
DR EMBL; Y14747; CAA75042.1; -; mRNA.
DR EMBL; AF036367; AAC39758.1; -; Genomic_DNA.
DR EMBL; AF036366; AAC39758.1; JOINED; Genomic_DNA.
DR EMBL; AF036365; AAC39756.1; -; mRNA.
DR EMBL; AK291892; BAF84581.1; ALT_INIT; mRNA.
DR EMBL; AC068312; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC069368; AAH69368.1; -; mRNA.
DR EMBL; BC102033; AAI02034.1; -; mRNA.
DR EMBL; BC102036; AAI02037.1; -; mRNA.
DR EMBL; BC102037; AAI02038.1; -; mRNA.
DR CCDS; CCDS2569.1; -.
DR RefSeq; NP_001225.1; NM_001234.4.
DR RefSeq; NP_203123.1; NM_033337.2.
DR AlphaFoldDB; P56539; -.
DR SMR; P56539; -.
DR BioGRID; 107307; 66.
DR CORUM; P56539; -.
DR IntAct; P56539; 41.
DR MINT; P56539; -.
DR STRING; 9606.ENSP00000341940; -.
DR TCDB; 1.F.1.2.1; the synaptosomal vesicle fusion pore (svf-pore) family.
DR PhosphoSitePlus; P56539; -.
DR SwissPalm; P56539; -.
DR BioMuta; CAV3; -.
DR DMDM; 3182930; -.
DR jPOST; P56539; -.
DR MassIVE; P56539; -.
DR MaxQB; P56539; -.
DR PaxDb; P56539; -.
DR PeptideAtlas; P56539; -.
DR PRIDE; P56539; -.
DR ProteomicsDB; 56922; -.
DR Antibodypedia; 4305; 293 antibodies from 39 providers.
DR DNASU; 859; -.
DR Ensembl; ENST00000343849.3; ENSP00000341940.2; ENSG00000182533.7.
DR Ensembl; ENST00000397368.2; ENSP00000380525.2; ENSG00000182533.7.
DR GeneID; 859; -.
DR KEGG; hsa:859; -.
DR MANE-Select; ENST00000343849.3; ENSP00000341940.2; NM_033337.3; NP_203123.1.
DR UCSC; uc003bra.4; human.
DR CTD; 859; -.
DR DisGeNET; 859; -.
DR GeneCards; CAV3; -.
DR GeneReviews; CAV3; -.
DR HGNC; HGNC:1529; CAV3.
DR HPA; ENSG00000182533; Group enriched (skeletal muscle, tongue).
DR MalaCards; CAV3; -.
DR MIM; 123320; phenotype.
DR MIM; 192600; phenotype.
DR MIM; 272120; phenotype.
DR MIM; 601253; gene.
DR MIM; 606072; phenotype.
DR MIM; 611818; phenotype.
DR MIM; 614321; phenotype.
DR neXtProt; NX_P56539; -.
DR OpenTargets; ENSG00000182533; -.
DR Orphanet; 488650; Distal myopathy, Tateyama type.
DR Orphanet; 206599; Isolated asymptomatic elevation of creatine phosphokinase.
DR Orphanet; 155; NON RARE IN EUROPE: Familial isolated hypertrophic cardiomyopathy.
DR Orphanet; 97238; Rippling muscle disease.
DR Orphanet; 101016; Romano-Ward syndrome.
DR PharmGKB; PA26109; -.
DR VEuPathDB; HostDB:ENSG00000182533; -.
DR eggNOG; ENOG502RYU9; Eukaryota.
DR GeneTree; ENSGT00950000183006; -.
DR HOGENOM; CLU_102582_0_0_1; -.
DR InParanoid; P56539; -.
DR OMA; QYNINEE; -.
DR OrthoDB; 1468974at2759; -.
DR PhylomeDB; P56539; -.
DR TreeFam; TF315736; -.
DR PathwayCommons; P56539; -.
DR Reactome; R-HSA-445355; Smooth Muscle Contraction.
DR SignaLink; P56539; -.
DR SIGNOR; P56539; -.
DR BioGRID-ORCS; 859; 10 hits in 1073 CRISPR screens.
DR GeneWiki; Caveolin_3; -.
DR GenomeRNAi; 859; -.
DR Pharos; P56539; Tbio.
DR PRO; PR:P56539; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; P56539; protein.
DR Bgee; ENSG00000182533; Expressed in hindlimb stylopod muscle and 129 other tissues.
DR Genevisible; P56539; HS.
DR GO; GO:0005901; C:caveola; ISS:UniProtKB.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0016010; C:dystrophin-associated glycoprotein complex; IDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0014704; C:intercalated disc; IEA:Ensembl.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0045121; C:membrane raft; ISS:BHF-UCL.
DR GO; GO:0031594; C:neuromuscular junction; ISS:BHF-UCL.
DR GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
DR GO; GO:0042383; C:sarcolemma; IDA:BHF-UCL.
DR GO; GO:0030315; C:T-tubule; ISS:BHF-UCL.
DR GO; GO:0031982; C:vesicle; IEA:Ensembl.
DR GO; GO:0030018; C:Z disc; IEA:Ensembl.
DR GO; GO:0043014; F:alpha-tubulin binding; IEA:Ensembl.
DR GO; GO:0005246; F:calcium channel regulator activity; IDA:BHF-UCL.
DR GO; GO:0071253; F:connexin binding; IDA:BHF-UCL.
DR GO; GO:0060090; F:molecular adaptor activity; IPI:BHF-UCL.
DR GO; GO:0050998; F:nitric-oxide synthase binding; IEA:Ensembl.
DR GO; GO:0019870; F:potassium channel inhibitor activity; ISS:BHF-UCL.
DR GO; GO:0008022; F:protein C-terminus binding; IDA:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:UniProtKB.
DR GO; GO:0017080; F:sodium channel regulator activity; IDA:BHF-UCL.
DR GO; GO:0044325; F:transmembrane transporter binding; IPI:BHF-UCL.
DR GO; GO:0007015; P:actin filament organization; IEA:Ensembl.
DR GO; GO:0006816; P:calcium ion transport; IEA:Ensembl.
DR GO; GO:0055013; P:cardiac muscle cell development; IEA:Ensembl.
DR GO; GO:0003300; P:cardiac muscle hypertrophy; IEA:Ensembl.
DR GO; GO:0070836; P:caveola assembly; IDA:MGI.
DR GO; GO:0030154; P:cell differentiation; ISS:BHF-UCL.
DR GO; GO:0071417; P:cellular response to organonitrogen compound; IEA:Ensembl.
DR GO; GO:0042632; P:cholesterol homeostasis; ISS:BHF-UCL.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; IEA:Ensembl.
DR GO; GO:0035995; P:detection of muscle stretch; ISS:BHF-UCL.
DR GO; GO:0006897; P:endocytosis; ISS:BHF-UCL.
DR GO; GO:0051649; P:establishment of localization in cell; IEA:Ensembl.
DR GO; GO:0042593; P:glucose homeostasis; ISS:BHF-UCL.
DR GO; GO:0060347; P:heart trabecula formation; IEA:Ensembl.
DR GO; GO:0000165; P:MAPK cascade; IEA:Ensembl.
DR GO; GO:0031579; P:membrane raft organization; ISS:BHF-UCL.
DR GO; GO:0046716; P:muscle cell cellular homeostasis; IEA:InterPro.
DR GO; GO:0007517; P:muscle organ development; TAS:UniProtKB.
DR GO; GO:0007520; P:myoblast fusion; IEA:Ensembl.
DR GO; GO:0051926; P:negative regulation of calcium ion transport; IDA:MGI.
DR GO; GO:0010614; P:negative regulation of cardiac muscle hypertrophy; IMP:BHF-UCL.
DR GO; GO:0061052; P:negative regulation of cell growth involved in cardiac muscle cell development; IEA:Ensembl.
DR GO; GO:0045792; P:negative regulation of cell size; IMP:BHF-UCL.
DR GO; GO:0043407; P:negative regulation of MAP kinase activity; IMP:BHF-UCL.
DR GO; GO:0043409; P:negative regulation of MAPK cascade; ISS:BHF-UCL.
DR GO; GO:1900826; P:negative regulation of membrane depolarization during cardiac muscle cell action potential; IEA:Ensembl.
DR GO; GO:0051001; P:negative regulation of nitric-oxide synthase activity; ISS:BHF-UCL.
DR GO; GO:1901380; P:negative regulation of potassium ion transmembrane transport; ISS:BHF-UCL.
DR GO; GO:1901017; P:negative regulation of potassium ion transmembrane transporter activity; ISS:BHF-UCL.
DR GO; GO:0006469; P:negative regulation of protein kinase activity; ISS:BHF-UCL.
DR GO; GO:2000009; P:negative regulation of protein localization to cell surface; NAS:BHF-UCL.
DR GO; GO:0060299; P:negative regulation of sarcomere organization; IMP:BHF-UCL.
DR GO; GO:0051647; P:nucleus localization; IEA:Ensembl.
DR GO; GO:0007009; P:plasma membrane organization; ISS:BHF-UCL.
DR GO; GO:0001778; P:plasma membrane repair; IEA:Ensembl.
DR GO; GO:2001288; P:positive regulation of caveolin-mediated endocytosis; IEA:Ensembl.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:Ensembl.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISS:BHF-UCL.
DR GO; GO:0031116; P:positive regulation of microtubule polymerization; ISS:BHF-UCL.
DR GO; GO:0010831; P:positive regulation of myotube differentiation; IEA:Ensembl.
DR GO; GO:2000060; P:positive regulation of ubiquitin-dependent protein catabolic process; NAS:BHF-UCL.
DR GO; GO:0008104; P:protein localization; ISS:BHF-UCL.
DR GO; GO:0072659; P:protein localization to plasma membrane; ISS:BHF-UCL.
DR GO; GO:0060762; P:regulation of branching involved in mammary gland duct morphogenesis; IEA:Ensembl.
DR GO; GO:0090279; P:regulation of calcium ion import; IDA:BHF-UCL.
DR GO; GO:1901019; P:regulation of calcium ion transmembrane transporter activity; IDA:BHF-UCL.
DR GO; GO:0098909; P:regulation of cardiac muscle cell action potential involved in regulation of contraction; IMP:BHF-UCL.
DR GO; GO:0055117; P:regulation of cardiac muscle contraction; IMP:BHF-UCL.
DR GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; IBA:GO_Central.
DR GO; GO:0008016; P:regulation of heart contraction; ISS:BHF-UCL.
DR GO; GO:0002027; P:regulation of heart rate; IMP:BHF-UCL.
DR GO; GO:1900825; P:regulation of membrane depolarization during cardiac muscle cell action potential; IMP:BHF-UCL.
DR GO; GO:0042391; P:regulation of membrane potential; IDA:BHF-UCL.
DR GO; GO:0051394; P:regulation of nerve growth factor receptor activity; IMP:MGI.
DR GO; GO:1900744; P:regulation of p38MAPK cascade; IEA:Ensembl.
DR GO; GO:0051896; P:regulation of protein kinase B signaling; IEA:Ensembl.
DR GO; GO:0038009; P:regulation of signal transduction by receptor internalization; IMP:MGI.
DR GO; GO:0014819; P:regulation of skeletal muscle contraction; IMP:BHF-UCL.
DR GO; GO:2000649; P:regulation of sodium ion transmembrane transporter activity; IDA:BHF-UCL.
DR GO; GO:0017015; P:regulation of transforming growth factor beta receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0060373; P:regulation of ventricular cardiac muscle cell membrane depolarization; IDA:BHF-UCL.
DR GO; GO:0060307; P:regulation of ventricular cardiac muscle cell membrane repolarization; IMP:BHF-UCL.
DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
DR GO; GO:0002931; P:response to ischemia; IEA:Ensembl.
DR GO; GO:0033292; P:T-tubule organization; TAS:BHF-UCL.
DR GO; GO:0006641; P:triglyceride metabolic process; ISS:BHF-UCL.
DR GO; GO:0086005; P:ventricular cardiac muscle cell action potential; ISS:BHF-UCL.
DR InterPro; IPR031091; CAV-3.
DR InterPro; IPR001612; Caveolin.
DR InterPro; IPR018361; Caveolin_CS.
DR PANTHER; PTHR10844; PTHR10844; 1.
DR PANTHER; PTHR10844:SF16; PTHR10844:SF16; 1.
DR Pfam; PF01146; Caveolin; 1.
DR PROSITE; PS01210; CAVEOLIN; 1.
PE 1: Evidence at protein level;
KW Cardiomyopathy; Cell membrane; Disease variant; Golgi apparatus;
KW Isopeptide bond; Limb-girdle muscular dystrophy; Long QT syndrome;
KW Membrane; Reference proteome; Ubl conjugation.
FT CHAIN 1..151
FT /note="Caveolin-3"
FT /id="PRO_0000144140"
FT TOPO_DOM 1..83
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT INTRAMEM 84..104
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 105..151
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 64..114
FT /note="Required for interaction with DAG1"
FT /evidence="ECO:0000269|PubMed:10988290"
FT CROSSLNK 38
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO3)"
FT /evidence="ECO:0000269|PubMed:21362625"
FT VARIANT 14
FT /note="V -> L (in SIDS; dbSNP:rs121909281)"
FT /evidence="ECO:0000269|PubMed:17275750"
FT /id="VAR_043694"
FT VARIANT 27
FT /note="R -> Q (in HYPCK, RMD2 and MPDT; dbSNP:rs116840778)"
FT /evidence="ECO:0000269|PubMed:10746614,
FT ECO:0000269|PubMed:11431690, ECO:0000269|PubMed:11756609,
FT ECO:0000269|PubMed:11805270, ECO:0000269|PubMed:12939441,
FT ECO:0000269|PubMed:15580566"
FT /id="VAR_011512"
FT VARIANT 28
FT /note="D -> E (in RMD2; dbSNP:rs116840782)"
FT /evidence="ECO:0000269|PubMed:12557291"
FT /id="VAR_015374"
FT VARIANT 29
FT /note="P -> L (in HYPCK; dbSNP:rs116840786)"
FT /evidence="ECO:0000269|PubMed:12082049"
FT /id="VAR_029540"
FT VARIANT 33
FT /note="N -> K (in RMD2 and MPDT; dbSNP:rs1008642)"
FT /evidence="ECO:0000269|PubMed:15564037,
FT ECO:0000269|PubMed:15580566"
FT /id="VAR_021016"
FT VARIANT 44
FT /note="V -> E (in RMD2; dbSNP:rs116840788)"
FT /evidence="ECO:0000269|PubMed:15564037"
FT /id="VAR_021017"
FT VARIANT 46
FT /note="A -> T (in RMD2; decreased surface expression of the
FT CAV3 protein; dbSNP:rs116840789)"
FT /evidence="ECO:0000269|PubMed:11001938,
FT ECO:0000269|PubMed:11431690, ECO:0000269|PubMed:15580566"
FT /id="VAR_011513"
FT VARIANT 46
FT /note="A -> V (in RMD2; dbSNP:rs116840773)"
FT /evidence="ECO:0000269|PubMed:11431690"
FT /id="VAR_011514"
FT VARIANT 53
FT /note="S -> G (in RMD2; dbSNP:rs116840794)"
FT /evidence="ECO:0000269|PubMed:16458928"
FT /id="VAR_029541"
FT VARIANT 56
FT /note="G -> S (in dbSNP:rs72546667)"
FT /evidence="ECO:0000269|PubMed:11251997,
FT ECO:0000269|PubMed:17060380, ECO:0000269|PubMed:9536092"
FT /id="VAR_029542"
FT VARIANT 57
FT /note="V -> M (in HYPCK; dbSNP:rs116840795)"
FT /evidence="ECO:0000269|PubMed:15099591"
FT /id="VAR_010742"
FT VARIANT 61
FT /note="S -> R (in a patient with mild proximal myopathy;
FT dbSNP:rs116840796)"
FT /evidence="ECO:0000269|PubMed:15580566"
FT /id="VAR_026696"
FT VARIANT 64..66
FT /note="Missing (in RMD2)"
FT /evidence="ECO:0000269|PubMed:9537420"
FT /id="VAR_001402"
FT VARIANT 64
FT /note="T -> P (in RMD2; dbSNP:rs199476332)"
FT /evidence="ECO:0000269|PubMed:11532985"
FT /id="VAR_021018"
FT VARIANT 64
FT /note="T -> S (in CMH; dbSNP:rs121909280)"
FT /evidence="ECO:0000269|PubMed:14672715"
FT /id="VAR_029543"
FT VARIANT 72
FT /note="C -> W (in dbSNP:rs116840776)"
FT /evidence="ECO:0000269|PubMed:11251997,
FT ECO:0000269|PubMed:17060380, ECO:0000269|PubMed:9536092"
FT /id="VAR_010743"
FT VARIANT 78
FT /note="T -> M (in LQT9 and SIDS; dbSNP:rs72546668)"
FT /evidence="ECO:0000269|PubMed:17060380,
FT ECO:0000269|PubMed:17275750"
FT /id="VAR_043695"
FT VARIANT 79
FT /note="L -> R (in LQT9 and SIDS; dbSNP:rs121909282)"
FT /evidence="ECO:0000269|PubMed:17275750"
FT /id="VAR_043696"
FT VARIANT 85
FT /note="A -> T (in LQT9; dbSNP:rs104893715)"
FT /evidence="ECO:0000269|PubMed:17060380"
FT /id="VAR_043697"
FT VARIANT 87
FT /note="L -> P (in RMD2; dbSNP:rs28936685)"
FT /evidence="ECO:0000269|PubMed:12666119"
FT /id="VAR_016207"
FT VARIANT 93
FT /note="A -> T (in RMD2; dbSNP:rs28936686)"
FT /evidence="ECO:0000269|PubMed:12666119,
FT ECO:0000269|PubMed:15668980"
FT /id="VAR_016208"
FT VARIANT 97
FT /note="F -> C (in LQT9; increase in late sodium current;
FT dbSNP:rs104893714)"
FT /evidence="ECO:0000269|PubMed:17060380"
FT /id="VAR_043698"
FT VARIANT 97
FT /note="Missing (in HYPCK)"
FT /evidence="ECO:0000269|PubMed:14663034"
FT /id="VAR_029544"
FT VARIANT 105
FT /note="P -> L (in RMD2; dbSNP:rs116840805)"
FT /evidence="ECO:0000269|PubMed:11431690,
FT ECO:0000269|PubMed:9537420"
FT /id="VAR_001403"
FT VARIANT 126
FT /note="R -> H (in dbSNP:rs116840777)"
FT /evidence="ECO:0000269|PubMed:11251997"
FT /id="VAR_029545"
FT VARIANT 141
FT /note="S -> R (in LQT9; increase in late sodium current;
FT dbSNP:rs104893713)"
FT /evidence="ECO:0000269|PubMed:17060380"
FT /id="VAR_043699"
SQ SEQUENCE 151 AA; 17259 MW; C695E14F5B8F4753 CRC64;
MMAEEHTDLE AQIVKDIHCK EIDLVNRDPK NINEDIVKVD FEDVIAEPVG TYSFDGVWKV
SYTTFTVSKY WCYRLLSTLL GVPLALLWGF LFACISFCHI WAVVPCIKSY LIEIQCISHI
YSLCIRTFCN PLFAALGQVC SSIKVVLRKE V
