ID CAV1_MOUSE Reviewed; 178 AA. AC P49817; Q8C1X7; Q8CBP4; Q9QYH3; Q9QYH4; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 27-MAR-2024, entry version 230. DE RecName: Full=Caveolin-1; GN Name=Cav1; Synonyms=Cav; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC STRAIN=BALB/cJ; RX PubMed=7926819; DOI=10.1016/0378-1119(94)90087-6; RA Tang Z., Scherer P.E., Lisanti M.P.; RT "The primary sequence of murine caveolin reveals a conserved consensus site RT for phosphorylation by protein kinase C."; RL Gene 147:299-300(1994). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2). RX PubMed=10631317; DOI=10.1016/s0014-5793(99)01730-5; RA Kogo H., Fujimoto T.; RT "Caveolin-1 isoforms are encoded in distinct mRNAs: identification of mouse RT caveolin-1 mRNA variants caused by alternative transcription initiation and RT splicing."; RL FEBS Lett. 465:119-123(2000). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC STRAIN=SWR/J; RA Zaffaroni D., Dragani T.A.; RT "Met gene is a candidate for the mouse pulmonary adenoma resistance 4 RT (Par4) locus."; RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC STRAIN=C57BL/6J; TISSUE=Embryo, Skin, and Urinary bladder; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC STRAIN=C3H/He; TISSUE=Mesenchymal cell; 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 [6] RP PROTEIN SEQUENCE OF 5-26; 47-77 AND 165-176. RX PubMed=7608210; DOI=10.1074/jbc.270.27.16395; RA Scherer P.E., Tang Z., Chun M., Sargiacomo M., Lodish H.F., Lisanti M.P.; RT "Caveolin isoforms differ in their N-terminal protein sequence and RT subcellular distribution. Identification and epitope mapping of an isoform- RT specific monoclonal antibody probe."; RL J. Biol. Chem. 270:16395-16401(1995). RN [7] RP FUNCTION. RX PubMed=10816572; DOI=10.1074/jbc.m002020200; RA Galbiati F., Volonte D., Brown A.M., Weinstein D.E., Ben-Ze'ev A., RA Pestell R.G., Lisanti M.P.; RT "Caveolin-1 expression inhibits Wnt/beta-catenin/Lef-1 signaling by RT recruiting beta-catenin to caveolae membrane domains."; RL J. Biol. Chem. 275:23368-23377(2000). RN [8] RP PHOSPHORYLATION AT TYR-14. RX PubMed=12036959; DOI=10.1074/jbc.m203375200; RA Kimura A., Mora S., Shigematsu S., Pessin J.E., Saltiel A.R.; RT "The insulin receptor catalyzes the tyrosine phosphorylation of RT caveolin-1."; RL J. Biol. Chem. 277:30153-30158(2002). RN [9] RP PHOSPHORYLATION AT TYR-14. RX PubMed=12531427; DOI=10.1016/s0898-6568(02)00090-6; RA Sanguinetti A.R., Mastick C.C.; RT "c-Abl is required for oxidative stress-induced phosphorylation of RT caveolin-1 on tyrosine 14."; RL Cell. Signal. 15:289-298(2003). RN [10] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=15592455; DOI=10.1038/nbt1046; RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., RA Zha X.-M., Polakiewicz R.D., Comb M.J.; RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."; RL Nat. Biotechnol. 23:94-101(2005). RN [11] RP INTERACTION WITH SPRY1; SPRY2; SPRY3 AND SPRY4. RX PubMed=16877379; DOI=10.1074/jbc.m603921200; RA Cabrita M.A., Jaeggi F., Widjaja S.P., Christofori G.; RT "A functional interaction between sprouty proteins and caveolin-1."; RL J. Biol. Chem. 281:29201-29212(2006). RN [12] RP FUNCTION, INTERACTION WITH CAVIN1, TISSUE SPECIFICITY, AND SUBCELLULAR RP LOCATION. RX PubMed=19546242; DOI=10.1083/jcb.200903053; RA Bastiani M., Liu L., Hill M.M., Jedrychowski M.P., Nixon S.J., Lo H.P., RA Abankwa D., Luetterforst R., Fernandez-Rojo M., Breen M.R., Gygi S.P., RA Vinten J., Walser P.J., North K.N., Hancock J.F., Pilch P.F., Parton R.G.; RT "MURC/Cavin-4 and cavin family members form tissue-specific caveolar RT complexes."; RL J. Cell Biol. 185:1259-1273(2009). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic fibroblast; RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200; RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.; RT "Large scale localization of protein phosphorylation by use of electron RT capture dissociation mass spectrometry."; RL Mol. Cell. Proteomics 8:904-912(2009). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9 AND TYR-14, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brown adipose tissue, Heart, Kidney, Lung, Pancreas, Spleen, RC and Testis; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). RN [15] RP INTERACTION WITH PACSIN2, AND SUBCELLULAR LOCATION. RX PubMed=21610094; DOI=10.1242/jcs.086264; RA Senju Y., Itoh Y., Takano K., Hamada S., Suetsugu S.; RT "Essential role of PACSIN2/syndapin-II in caveolae membrane sculpting."; RL J. Cell Sci. 124:2032-2040(2011). RN [16] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND LYS-5, CLEAVAGE OF RP INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic fibroblast; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). RN [17] RP FUNCTION. RX PubMed=30188967; DOI=10.1093/abbs/gmy105; RA Wei Z., Liu T., Lei J., Wu Y., Wang S., Liao K.; RT "Fam198a, a member of secreted kinase, secrets through caveolae biogenesis RT pathway."; RL Acta Biochim. Biophys. Sin. 50:968-975(2018). RN [18] RP FUNCTION. RX PubMed=34799735; DOI=10.1038/s41589-021-00907-2; RA Cheng Y.S., Zhang T., Ma X., Pratuangtham S., Zhang G.C., Ondrus A.A., RA Mafi A., Lomenick B., Jones J.J., Ondrus A.E.; RT "A proteome-wide map of 20(S)-hydroxycholesterol interactors in cell RT membranes."; RL Nat. Chem. Biol. 17:1271-1280(2021). CC -!- FUNCTION: May act as a scaffolding protein within caveolar membranes CC (By similarity). Forms a stable heterooligomeric complex with CAV2 that CC targets to lipid rafts and drives caveolae formation. Mediates the CC recruitment of CAVIN proteins (CAVIN1/2/3/4) to the caveolae CC (PubMed:19546242). Interacts directly with G-protein alpha subunits and CC can functionally regulate their activity (By similarity). Involved in CC the costimulatory signal essential for T-cell receptor (TCR)-mediated CC T-cell activation. Its binding to DPP4 induces T-cell proliferation and CC NF-kappa-B activation in a T-cell receptor/CD3-dependent manner (By CC similarity). Recruits CTNNB1 to caveolar membranes and may regulate CC CTNNB1-mediated signaling through the Wnt pathway (PubMed:10816572). CC Negatively regulates TGFB1-mediated activation of SMAD2/3 by mediating CC the internalization of TGFBR1 from membrane rafts leading to its CC subsequent degradation (By similarity). Binds 20(S)-hydroxycholesterol CC (20(S)-OHC) (PubMed:34799735). {ECO:0000250|UniProtKB:Q03135, CC ECO:0000269|PubMed:10816572, ECO:0000269|PubMed:19546242, CC ECO:0000269|PubMed:34799735}. CC -!- SUBUNIT: Homooligomer. Interacts (via the N-terminus) with DPP4; the CC interaction is direct. Forms a stable heterooligomeric complex with CC CAV2 that targets to lipid rafts and drives caveolae formation. CC Interacts with BMX, BTK, CTNNB1, CDH1, GLIPR2, JUP, NOSTRIN, SNAP25 and CC STX1A. Interacts with SLC7A9. Interacts with TGFBR1 (By similarity). CC Interacts with CTNNB1, CDH1 and JUP. Interacts with PACSIN2; this CC interaction induces membrane tubulation (PubMed:21610094). Interacts CC with CAVIN3 (via leucine-zipper domain) in a cholesterol-sensitive CC manner. Interacts with EHD2 in a cholesterol-dependent manner (By CC similarity). Interacts with CAVIN1 (PubMed:19546242). Forms a ternary CC complex with UBXN6 and VCP; mediates CAV1 targeting to lysosomes for CC degradation (By similarity). Interacts with ABCG1; this interaction CC regulates ABCG1-mediated cholesterol efflux (By similarity). Interacts CC with NEU3; this interaction enhances NEU3 sialidase activity within CC caveola. Interacts (via C-terminus) with SPRY1, SPRY2 (via C-terminus), CC SPRY3, and SPRY4 (PubMed:16877379). {ECO:0000250|UniProtKB:P41350, CC ECO:0000250|UniProtKB:Q03135, ECO:0000250|UniProtKB:Q2IBA5, CC ECO:0000269|PubMed:16877379, ECO:0000269|PubMed:19546242, CC ECO:0000269|PubMed:21610094}. CC -!- INTERACTION: CC P49817; P15208: Insr; NbExp=2; IntAct=EBI-1161338, EBI-6999015; CC P49817; Q64729: Tgfbr1; NbExp=4; IntAct=EBI-1161338, EBI-2899393; CC P49817; Q07820: MCL1; Xeno; NbExp=3; IntAct=EBI-1161338, EBI-1003422; CC P49817; P22307: SCP2; Xeno; NbExp=3; IntAct=EBI-1161338, EBI-1050999; CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; CC Peripheral membrane protein {ECO:0000250}. Cell membrane {ECO:0000250}; CC Peripheral membrane protein {ECO:0000250}. Membrane, caveola CC {ECO:0000269|PubMed:19546242, ECO:0000269|PubMed:21610094}; Peripheral CC membrane protein {ECO:0000269|PubMed:21610094}. Membrane raft CC {ECO:0000250|UniProtKB:Q03135}. Golgi apparatus, trans-Golgi network CC {ECO:0000250|UniProtKB:P33724}. Note=Colocalized with DPP4 in membrane CC rafts. Potential hairpin-like structure in the membrane. Membrane CC protein of caveolae (By similarity). {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative initiation; Named isoforms=2; CC Name=1; CC IsoId=P49817-1; Sequence=Displayed; CC Name=2; CC IsoId=P49817-2; Sequence=VSP_018693; CC -!- TISSUE SPECIFICITY: Adipose tissue, lung, heart, skeletal muscle, CC stomach, small bowel, kidney, spleen and testis (at protein level). CC {ECO:0000269|PubMed:19546242}. CC -!- PTM: The N-terminus of both isoforms are blocked. CC -!- PTM: Phosphorylated at Tyr-14 by ABL1 in response to oxidative stress. CC {ECO:0000269|PubMed:12036959, ECO:0000269|PubMed:12531427}. CC -!- PTM: Ubiquitinated. Undergo monoubiquitination and multi- and/or CC polyubiquitination. Monoubiquitination of N-terminal lysines promotes CC integration in a ternary complex with UBXN6 and VCP which promotes CC oligomeric CAV1 targeting to lysosomes for degradation. Ubiquitinated CC by ZNRF1; leading to degradation and modulation of the TLR4-mediated CC immune response. {ECO:0000250|UniProtKB:Q03135}. CC -!- SIMILARITY: Belongs to the caveolin family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U07645; AAA85784.1; -; mRNA. DR EMBL; AB029929; BAA89461.1; -; mRNA. DR EMBL; AB029930; BAA89462.1; -; mRNA. DR EMBL; AB029931; BAA89463.1; -; Genomic_DNA. DR EMBL; AY439333; AAR99702.1; -; mRNA. DR EMBL; AK003489; BAB22817.1; -; mRNA. DR EMBL; AK028738; BAC26091.1; -; mRNA. DR EMBL; AK035592; BAC29118.1; -; mRNA. DR EMBL; AK090074; BAC41079.1; -; mRNA. DR EMBL; BC038280; AAH38280.1; -; mRNA. DR EMBL; BC052859; AAH52859.1; -; mRNA. DR CCDS; CCDS19924.1; -. [P49817-1] DR CCDS; CCDS57410.1; -. [P49817-2] DR PIR; I48976; I48976. DR RefSeq; NP_001229993.1; NM_001243064.1. [P49817-2] DR RefSeq; NP_031642.1; NM_007616.4. [P49817-1] DR RefSeq; XP_006505037.1; XM_006504974.1. DR RefSeq; XP_006505038.1; XM_006504975.1. DR RefSeq; XP_006505039.1; XM_006504976.1. DR AlphaFoldDB; P49817; -. DR SMR; P49817; -. DR BioGRID; 198514; 14. DR CORUM; P49817; -. DR DIP; DIP-35140N; -. DR IntAct; P49817; 18. DR MINT; P49817; -. DR STRING; 10090.ENSMUSP00000007799; -. DR GlyGen; P49817; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P49817; -. DR PhosphoSitePlus; P49817; -. DR SwissPalm; P49817; -. DR jPOST; P49817; -. DR MaxQB; P49817; -. DR PaxDb; 10090-ENSMUSP00000007799; -. DR PeptideAtlas; P49817; -. DR ProteomicsDB; 265553; -. [P49817-1] DR ProteomicsDB; 265554; -. [P49817-2] DR Pumba; P49817; -. DR Antibodypedia; 3530; 1356 antibodies from 47 providers. DR DNASU; 12389; -. DR Ensembl; ENSMUST00000007799.13; ENSMUSP00000007799.7; ENSMUSG00000007655.17. [P49817-1] DR Ensembl; ENSMUST00000115453.2; ENSMUSP00000111113.2; ENSMUSG00000007655.17. [P49817-2] DR Ensembl; ENSMUST00000115454.2; ENSMUSP00000111114.2; ENSMUSG00000007655.17. [P49817-2] DR Ensembl; ENSMUST00000115456.6; ENSMUSP00000111116.2; ENSMUSG00000007655.17. [P49817-1] DR GeneID; 12389; -. DR KEGG; mmu:12389; -. DR UCSC; uc009azo.2; mouse. [P49817-1] DR AGR; MGI:102709; -. DR CTD; 857; -. DR MGI; MGI:102709; Cav1. DR VEuPathDB; HostDB:ENSMUSG00000007655; -. DR eggNOG; ENOG502QUK5; Eukaryota. DR GeneTree; ENSGT00950000183006; -. DR HOGENOM; CLU_102582_0_0_1; -. DR InParanoid; P49817; -. DR OMA; HIWCLAP; -. DR OrthoDB; 3740765at2759; -. DR PhylomeDB; P49817; -. DR TreeFam; TF315736; -. DR Reactome; R-MMU-203615; eNOS activation. DR Reactome; R-MMU-203641; NOSTRIN mediated eNOS trafficking. DR Reactome; R-MMU-4641262; Disassembly of the destruction complex and recruitment of AXIN to the membrane. DR Reactome; R-MMU-5218920; VEGFR2 mediated vascular permeability. DR Reactome; R-MMU-8980692; RHOA GTPase cycle. DR Reactome; R-MMU-9009391; Extra-nuclear estrogen signaling. DR Reactome; R-MMU-9013026; RHOB GTPase cycle. DR Reactome; R-MMU-9013106; RHOC GTPase cycle. DR Reactome; R-MMU-9013148; CDC42 GTPase cycle. DR Reactome; R-MMU-9013149; RAC1 GTPase cycle. DR Reactome; R-MMU-9013404; RAC2 GTPase cycle. DR Reactome; R-MMU-9013405; RHOD GTPase cycle. DR Reactome; R-MMU-9013406; RHOQ GTPase cycle. DR Reactome; R-MMU-9013407; RHOH GTPase cycle. DR Reactome; R-MMU-9013408; RHOG GTPase cycle. DR Reactome; R-MMU-9013423; RAC3 GTPase cycle. DR Reactome; R-MMU-9035034; RHOF GTPase cycle. DR Reactome; R-MMU-9696264; RND3 GTPase cycle. DR Reactome; R-MMU-9696270; RND2 GTPase cycle. DR Reactome; R-MMU-9696273; RND1 GTPase cycle. DR BioGRID-ORCS; 12389; 0 hits in 78 CRISPR screens. DR ChiTaRS; Cav1; mouse. DR PRO; PR:P49817; -. DR Proteomes; UP000000589; Chromosome 6. DR RNAct; P49817; Protein. DR Bgee; ENSMUSG00000007655; Expressed in left lung lobe and 234 other cell types or tissues. DR ExpressionAtlas; P49817; baseline and differential. DR GO; GO:0002080; C:acrosomal membrane; IDA:MGI. DR GO; GO:0016324; C:apical plasma membrane; ISO:MGI. DR GO; GO:0009925; C:basal plasma membrane; ISO:MGI. DR GO; GO:0016323; C:basolateral plasma membrane; ISO:MGI. DR GO; GO:0005901; C:caveola; IDA:BHF-UCL. DR GO; GO:0002095; C:caveolar macromolecular signaling complex; IDA:MGI. DR GO; GO:0005938; C:cell cortex; IDA:MGI. DR GO; GO:0009986; C:cell surface; ISO:MGI. DR GO; GO:0005929; C:cilium; IDA:MGI. DR GO; GO:0031410; C:cytoplasmic vesicle; ISO:MGI. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI. DR GO; GO:0005768; C:endosome; ISS:UniProtKB. DR GO; GO:0005925; C:focal adhesion; ISO:MGI. DR GO; GO:0005794; C:Golgi apparatus; IDA:MGI. DR GO; GO:0000139; C:Golgi membrane; ISS:HGNC-UCL. DR GO; GO:0005811; C:lipid droplet; ISO:MGI. DR GO; GO:0016020; C:membrane; IDA:MGI. DR GO; GO:0045121; C:membrane raft; IDA:MGI. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:MGI. DR GO; GO:0005778; C:peroxisomal membrane; ISO:MGI. DR GO; GO:0005886; C:plasma membrane; IDA:MGI. DR GO; GO:0032991; C:protein-containing complex; IDA:BHF-UCL. DR GO; GO:0051117; F:ATPase binding; ISO:MGI. DR GO; GO:0019899; F:enzyme binding; ISO:MGI. DR GO; GO:0042802; F:identical protein binding; IPI:MGI. DR GO; GO:0070320; F:inward rectifier potassium channel inhibitor activity; ISO:MGI. DR GO; GO:0019900; F:kinase binding; ISO:MGI. DR GO; GO:0060090; F:molecular adaptor activity; IDA:BHF-UCL. DR GO; GO:0050998; F:nitric-oxide synthase binding; IPI:BHF-UCL. DR GO; GO:0008142; F:oxysterol binding; IMP:UniProtKB. DR GO; GO:0016504; F:peptidase activator activity; IMP:MGI. DR GO; GO:0046982; F:protein heterodimerization activity; IPI:BHF-UCL. DR GO; GO:0019901; F:protein kinase binding; IPI:BHF-UCL. DR GO; GO:0030292; F:protein tyrosine kinase inhibitor activity; IMP:BHF-UCL. DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI. DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IDA:BHF-UCL. DR GO; GO:0033612; F:receptor serine/threonine kinase binding; ISO:MGI. DR GO; GO:0005102; F:signaling receptor binding; ISO:MGI. DR GO; GO:0031267; F:small GTPase binding; ISO:MGI. DR GO; GO:0000149; F:SNARE binding; ISO:MGI. DR GO; GO:0019905; F:syntaxin binding; ISO:MGI. DR GO; GO:0044325; F:transmembrane transporter binding; ISO:MGI. DR GO; GO:0001525; P:angiogenesis; IGI:MGI. DR GO; GO:0038166; P:angiotensin-activated signaling pathway; IGI:BHF-UCL. DR GO; GO:0097190; P:apoptotic signaling pathway; ISO:MGI. DR GO; GO:0071711; P:basement membrane organization; IMP:MGI. DR GO; GO:0055074; P:calcium ion homeostasis; IMP:MGI. DR GO; GO:0006816; P:calcium ion transport; IMP:MGI. DR GO; GO:0070836; P:caveola assembly; IDA:MGI. DR GO; GO:0072584; P:caveolin-mediated endocytosis; IMP:MGI. DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central. DR GO; GO:0008283; P:cell population proliferation; IMP:MGI. DR GO; GO:0071360; P:cellular response to exogenous dsRNA; ISO:MGI. DR GO; GO:0071455; P:cellular response to hyperoxia; ISO:MGI. DR GO; GO:0071260; P:cellular response to mechanical stimulus; ISO:MGI. DR GO; GO:0071218; P:cellular response to misfolded protein; IEA:Ensembl. DR GO; GO:0071375; P:cellular response to peptide hormone stimulus; IGI:BHF-UCL. DR GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IMP:MGI. DR GO; GO:0090398; P:cellular senescence; ISO:MGI. DR GO; GO:0033344; P:cholesterol efflux; ISO:MGI. DR GO; GO:0042632; P:cholesterol homeostasis; IMP:MGI. DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IMP:MGI. DR GO; GO:0006897; P:endocytosis; TAS:MGI. DR GO; GO:0001935; P:endothelial cell proliferation; IMP:MGI. DR GO; GO:0051649; P:establishment of localization in cell; IMP:MGI. DR GO; GO:0048144; P:fibroblast proliferation; IMP:MGI. DR GO; GO:0002067; P:glandular epithelial cell differentiation; IMP:MGI. DR GO; GO:0038016; P:insulin receptor internalization; IMP:CACAO. DR GO; GO:0006874; P:intracellular calcium ion homeostasis; IMP:MGI. DR GO; GO:0033484; P:intracellular nitric oxide homeostasis; IMP:MGI. DR GO; GO:0007595; P:lactation; IMP:MGI. DR GO; GO:0019915; P:lipid storage; IMP:MGI. DR GO; GO:0032507; P:maintenance of protein location in cell; ISO:MGI. DR GO; GO:0030879; P:mammary gland development; IMP:MGI. DR GO; GO:0060056; P:mammary gland involution; IMP:MGI. DR GO; GO:0000165; P:MAPK cascade; IMP:MGI. DR GO; GO:0051899; P:membrane depolarization; IMP:MGI. DR GO; GO:0046785; P:microtubule polymerization; ISO:MGI. DR GO; GO:0046716; P:muscle cell cellular homeostasis; IMP:MGI. DR GO; GO:2000811; P:negative regulation of anoikis; IMP:UniProtKB. DR GO; GO:0030514; P:negative regulation of BMP signaling pathway; ISO:MGI. DR GO; GO:1905949; P:negative regulation of calcium ion import across plasma membrane; ISO:MGI. DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IDA:UniProtKB. DR GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:MGI. DR GO; GO:0001960; P:negative regulation of cytokine-mediated signaling pathway; IMP:MGI. DR GO; GO:0001937; P:negative regulation of endothelial cell proliferation; IMP:MGI. DR GO; GO:0030857; P:negative regulation of epithelial cell differentiation; IMP:MGI. DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; ISO:MGI. DR GO; GO:0048147; P:negative regulation of fibroblast proliferation; IMP:MGI. DR GO; GO:0043409; P:negative regulation of MAPK cascade; IMP:MGI. DR GO; GO:0010656; P:negative regulation of muscle cell apoptotic process; ISO:MGI. DR GO; GO:0060546; P:negative regulation of necroptotic process; IMP:CACAO. DR GO; GO:0045665; P:negative regulation of neuron differentiation; ISO:MGI. DR GO; GO:0045019; P:negative regulation of nitric oxide biosynthetic process; IMP:MGI. DR GO; GO:0033137; P:negative regulation of peptidyl-serine phosphorylation; ISO:MGI. DR GO; GO:1900085; P:negative regulation of peptidyl-tyrosine autophosphorylation; ISO:MGI. DR GO; GO:0048550; P:negative regulation of pinocytosis; ISO:MGI. DR GO; GO:1901380; P:negative regulation of potassium ion transmembrane transport; ISO:MGI. DR GO; GO:0031397; P:negative regulation of protein ubiquitination; IMP:UniProtKB. DR GO; GO:0046426; P:negative regulation of receptor signaling pathway via JAK-STAT; IDA:MGI. DR GO; GO:0009968; P:negative regulation of signal transduction; IDA:MGI. DR GO; GO:0014912; P:negative regulation of smooth muscle cell migration; ISO:MGI. DR GO; GO:0048662; P:negative regulation of smooth muscle cell proliferation; ISO:MGI. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB. DR GO; GO:0042532; P:negative regulation of tyrosine phosphorylation of STAT protein; IDA:MGI. DR GO; GO:1904706; P:negative regulation of vascular associated smooth muscle cell proliferation; ISO:MGI. DR GO; GO:0006809; P:nitric oxide biosynthetic process; IMP:MGI. DR GO; GO:0010524; P:positive regulation of calcium ion transport into cytosol; IDA:BHF-UCL. DR GO; GO:0043123; P:positive regulation of canonical NF-kappaB signal transduction; ISO:MGI. DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; ISO:MGI. DR GO; GO:0060355; P:positive regulation of cell adhesion molecule production; ISO:MGI. DR GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI. DR GO; GO:0010875; P:positive regulation of cholesterol efflux; ISO:MGI. DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; IMP:YuBioLab. DR GO; GO:0045807; P:positive regulation of endocytosis; ISO:MGI. DR GO; GO:0001938; P:positive regulation of endothelial cell proliferation; ISO:MGI. DR GO; GO:1903071; P:positive regulation of ER-associated ubiquitin-dependent protein catabolic process; ISO:MGI. DR GO; GO:2001238; P:positive regulation of extrinsic apoptotic signaling pathway; ISO:MGI. DR GO; GO:1903598; P:positive regulation of gap junction assembly; IMP:BHF-UCL. DR GO; GO:0010628; P:positive regulation of gene expression; IMP:BHF-UCL. DR GO; GO:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; ISO:MGI. DR GO; GO:0031116; P:positive regulation of microtubule polymerization; ISO:MGI. DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; ISO:MGI. DR GO; GO:0031398; P:positive regulation of protein ubiquitination; ISO:MGI. DR GO; GO:0009967; P:positive regulation of signal transduction; ISO:MGI. DR GO; GO:0034141; P:positive regulation of toll-like receptor 3 signaling pathway; ISO:MGI. DR GO; GO:0045907; P:positive regulation of vasoconstriction; IMP:MGI. DR GO; GO:0010608; P:post-transcriptional regulation of gene expression; IMP:BHF-UCL. DR GO; GO:0008104; P:protein localization; IMP:MGI. DR GO; GO:0015031; P:protein transport; IMP:MGI. DR GO; GO:0031623; P:receptor internalization; ISS:UniProtKB. DR GO; GO:2000286; P:receptor internalization involved in canonical Wnt signaling pathway; ISO:MGI. DR GO; GO:0019065; P:receptor-mediated endocytosis of virus by host cell; ISO:MGI. DR GO; GO:0030193; P:regulation of blood coagulation; ISO:MGI. DR GO; GO:1901844; P:regulation of cell communication by electrical coupling involved in cardiac conduction; IMP:BHF-UCL. DR GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; ISO:MGI. DR GO; GO:2000535; P:regulation of entry of bacterium into host cell; ISO:MGI. DR GO; GO:0019217; P:regulation of fatty acid metabolic process; IMP:MGI. DR GO; GO:0086091; P:regulation of heart rate by cardiac conduction; IMP:BHF-UCL. DR GO; GO:0098903; P:regulation of membrane repolarization during action potential; ISO:MGI. DR GO; GO:1900027; P:regulation of ruffle assembly; ISO:MGI. DR GO; GO:0006940; P:regulation of smooth muscle contraction; IMP:MGI. DR GO; GO:0002026; P:regulation of the force of heart contraction; IMP:MGI. DR GO; GO:0003057; P:regulation of the force of heart contraction by chemical signal; IGI:MGI. DR GO; GO:0098911; P:regulation of ventricular cardiac muscle cell action potential; IMP:BHF-UCL. DR GO; GO:0009617; P:response to bacterium; ISO:MGI. DR GO; GO:0051592; P:response to calcium ion; IDA:BHF-UCL. DR GO; GO:0043627; P:response to estrogen; IDA:MGI. DR GO; GO:0001666; P:response to hypoxia; IMP:MGI. DR GO; GO:0002931; P:response to ischemia; IMP:MGI. DR GO; GO:0009612; P:response to mechanical stimulus; ISO:MGI. DR GO; GO:0032570; P:response to progesterone; ISO:MGI. DR GO; GO:0007519; P:skeletal muscle tissue development; IMP:MGI. DR GO; GO:0031295; P:T cell costimulation; ISS:UniProtKB. DR GO; GO:0006641; P:triglyceride metabolic process; IMP:MGI. DR GO; GO:0001570; P:vasculogenesis; IMP:MGI. DR GO; GO:0042310; P:vasoconstriction; IMP:MGI. DR InterPro; IPR001612; Caveolin. DR InterPro; IPR018361; Caveolin_CS. DR PANTHER; PTHR10844; CAVEOLIN; 1. DR PANTHER; PTHR10844:SF18; CAVEOLIN-1; 1. DR Pfam; PF01146; Caveolin; 1. DR PROSITE; PS01210; CAVEOLIN; 1. DR Genevisible; P49817; MM. PE 1: Evidence at protein level; KW Acetylation; Alternative initiation; Cell membrane; KW Direct protein sequencing; Golgi apparatus; Isopeptide bond; Lipoprotein; KW Membrane; Palmitate; Phosphoprotein; Reference proteome; Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:23806337" FT CHAIN 2..178 FT /note="Caveolin-1" FT /id="PRO_0000004766" FT TOPO_DOM 2..104 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT INTRAMEM 105..125 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 126..178 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT REGION 2..94 FT /note="Required for homooligomerization" FT /evidence="ECO:0000250|UniProtKB:Q03135" FT REGION 82..94 FT /note="Interaction with CAVIN3" FT /evidence="ECO:0000250|UniProtKB:Q03135" FT REGION 131..142 FT /note="Interacts with SPRY1, SPRY2, SPRY3 and SPRY4" FT /evidence="ECO:0000269|PubMed:16877379" FT REGION 149..160 FT /note="Interacts with SPRY1, SPRY2, and SPRY4" FT /evidence="ECO:0000269|PubMed:16877379" FT REGION 167..178 FT /note="Interacts with SPRY1, SPRY2, SPRY3 and SPRY4" FT /evidence="ECO:0000269|PubMed:16877379" FT MOD_RES 2 FT /note="N-acetylserine" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 2 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P41350" FT MOD_RES 5 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 6 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:Q03135" FT MOD_RES 9 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 14 FT /note="Phosphotyrosine; by ABL1 and INSR" FT /evidence="ECO:0000269|PubMed:12036959, FT ECO:0000269|PubMed:12531427, ECO:0007744|PubMed:21183079" FT MOD_RES 25 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:Q03135" FT LIPID 133 FT /note="S-palmitoyl cysteine" FT /evidence="ECO:0000250" FT LIPID 143 FT /note="S-palmitoyl cysteine" FT /evidence="ECO:0000250" FT LIPID 156 FT /note="S-palmitoyl cysteine" FT /evidence="ECO:0000250" FT CROSSLNK 5 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin); alternate" FT /evidence="ECO:0000250|UniProtKB:Q03135" FT CROSSLNK 26 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0000250|UniProtKB:Q03135" FT CROSSLNK 30 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0000250|UniProtKB:Q03135" FT CROSSLNK 39 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0000250|UniProtKB:Q03135" FT CROSSLNK 47 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0000250|UniProtKB:Q03135" FT CROSSLNK 57 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0000250|UniProtKB:Q03135" FT VAR_SEQ 1..31 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:10631317, FT ECO:0000303|PubMed:16141072" FT /id="VSP_018693" FT CONFLICT 170 FT /note="I -> F (in Ref. 4; BAC29118)" FT /evidence="ECO:0000305" SQ SEQUENCE 178 AA; 20539 MW; CF88FE9B1D3D67AE CRC64; MSGGKYVDSE GHLYTVPIRE QGNIYKPNNK AMADEVTEKQ VYDAHTKEID LVNRDPKHLN DDVVKIDFED VIAEPEGTHS FDGIWKASFT TFTVTKYWFY RLLSTIFGIP MALIWGIYFA ILSFLHIWAV VPCIKSFLIE IQCISRVYSI YVHTFCDPLF EAIGKIFSNI RISTQKEI //