CAVN3_MOUSE
ID CAVN3_MOUSE Reviewed; 260 AA.
AC Q91VJ2; Q8C064; Q9CRW1;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Caveolae-associated protein 3;
DE AltName: Full=Cavin-3;
DE AltName: Full=Protein kinase C delta-binding protein;
DE AltName: Full=Serum deprivation response factor-related gene product that binds to C-kinase;
GN Name=Cavin3; Synonyms=Prkcdbp, Srbc;
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 [LARGE SCALE MRNA].
RC TISSUE=Mammary tumor;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 62-260.
RC STRAIN=C57BL/6J; TISSUE=Head, and Olfactory bulb;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 156-260, INDUCTION, INTERACTION
RP WITH PRKCD AND PHOSPHATIDYLSERINE, PHOSPHORYLATION BY PRKCD, AND TISSUE
RP SPECIFICITY.
RX PubMed=9054438; DOI=10.1074/jbc.272.11.7381;
RA Izumi Y., Hirai S., Tamai Y., Fujise-Matsuoka A., Nishimura Y., Ohno S.;
RT "A protein kinase Cdelta-binding protein SRBC whose expression is induced
RT by serum starvation.";
RL J. Biol. Chem. 272:7381-7389(1997).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165 AND SER-166, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP IDENTIFICATION IN THE CAVIN COMPLEX, INTERACTION WITH CAVIN1, TISSUE
RP SPECIFICITY, AND SUBCELLULAR 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165; SER-166 AND SER-173, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Lung, Pancreas, Spleen, and
RC 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 [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PER2.
RX PubMed=23079727; DOI=10.1038/embor.2012.158;
RA Schneider K., Kocher T., Andersin T., Kurzchalia T., Schibler U.,
RA Gatfield D.;
RT "CAVIN-3 regulates circadian period length and PER:CRY protein abundance
RT and interactions.";
RL EMBO Rep. 13:1138-1144(2012).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=23652019; DOI=10.1038/ncomms2808;
RA Hansen C.G., Shvets E., Howard G., Riento K., Nichols B.J.;
RT "Deletion of cavin genes reveals tissue-specific mechanisms for
RT morphogenesis of endothelial caveolae.";
RL Nat. Commun. 4:1831-1831(2013).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, AND INTERACTION WITH CAVIN1 AND
RP CAV1.
RX PubMed=25588833; DOI=10.1242/jcs.161463;
RA Mohan J., Moren B., Larsson E., Holst M.R., Lundmark R.;
RT "Cavin3 interacts with cavin1 and caveolin1 to increase surface dynamics of
RT caveolae.";
RL J. Cell Sci. 128:979-991(2015).
RN [10]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=28285351; DOI=10.1007/s00441-017-2587-y;
RA Zhu B., Swaerd K., Ekman M., Uvelius B., Rippe C.;
RT "Cavin-3 (PRKCDBP) deficiency reduces the density of caveolae in smooth
RT muscle.";
RL Cell Tissue Res. 368:591-602(2017).
CC -!- FUNCTION: Regulates the traffic and/or budding of caveolae (By
CC similarity). Plays a role in caveola formation in a tissue-specific
CC manner. Required for the formation of caveolae in smooth muscle but not
CC in the lung and heart endothelial cells (PubMed: 28285351,
CC PubMed:23652019). Regulates the equilibrium between cell surface-
CC associated and cell surface-dissociated caveolae by promoting the rapid
CC release of caveolae from the cell surface (PubMed:25588833). Plays a
CC role in the regulation of the circadian clock. Modulates the period
CC length and phase of circadian gene expression and also regulates
CC expression and interaction of the core clock components PER1/2 and
CC CRY1/2 (PubMed:23079727). {ECO:0000250|UniProtKB:Q969G5,
CC ECO:0000269|PubMed:23079727, ECO:0000269|PubMed:23652019,
CC ECO:0000269|PubMed:25588833, ECO:0000269|PubMed:28285351}.
CC -!- SUBUNIT: Component of the CAVIN complex composed of CAVIN1, CAVIN2,
CC CAVIN3 and CAVIN4 (PubMed:19546242). Interacts with PRKCD and with
CC phosphatidylserine. Phosphatidylserine may form a bridge between PKC
CC and PKC-binding partners and stabilize the binding (PubMed:9054438).
CC Interacts with PER2 (PubMed:23079727). Interacts with CAVIN1
CC (PubMed:19546242, PubMed:25588833). Interacts (via leucine-zipper
CC domain) with CAV1 in a cholesterol-sensitive manner (PubMed:25588833).
CC Interacts with EPS15L1 (By similarity). {ECO:0000250|UniProtKB:Q969G5,
CC ECO:0000269|PubMed:19546242, ECO:0000269|PubMed:23079727,
CC ECO:0000269|PubMed:25588833, ECO:0000269|PubMed:9054438}.
CC -!- INTERACTION:
CC Q91VJ2; O54943: Per2; NbExp=4; IntAct=EBI-8094261, EBI-1266779;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23079727}.
CC Cytoplasm, cytosol {ECO:0000269|PubMed:19546242}. Membrane, caveola
CC {ECO:0000269|PubMed:19546242, ECO:0000269|PubMed:25588833}.
CC Note=Localizes in the caveolae in a caveolin-dependent manner.
CC {ECO:0000269|PubMed:19546242, ECO:0000269|PubMed:25588833}.
CC -!- TISSUE SPECIFICITY: Lung, heart, skeletal muscle, liver, brain,
CC vascular and urinary bladder smooth muscle (at protein level). Strongly
CC expressed in uterus, ovary, mammary and epithelial cells. Also
CC expressed in spleen, intestine, kidney and testis.
CC {ECO:0000269|PubMed:19546242, ECO:0000269|PubMed:23652019,
CC ECO:0000269|PubMed:28285351, ECO:0000269|PubMed:9054438}.
CC -!- INDUCTION: Up-regulated in serum-starvated cells or during cell growth
CC arrest. {ECO:0000269|PubMed:9054438}.
CC -!- DOMAIN: The leucine-zipper domain is essential for its localization in
CC the caveolae and for its interaction with CAV1 and EPS15L1.
CC {ECO:0000250|UniProtKB:Q969G5}.
CC -!- PTM: In vitro, phosphorylated by PRKCD. {ECO:0000269|PubMed:9054438}.
CC -!- DISRUPTION PHENOTYPE: Mice show reduced density of membrane caveolae in
CC the arterial smooth muscle and the urinary bladder but show no loss of
CC endothelial caveolae in lung and heart. {ECO:0000269|PubMed:23652019,
CC ECO:0000269|PubMed:28285351}.
CC -!- SIMILARITY: Belongs to the CAVIN family. {ECO:0000305}.
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DR EMBL; BC009660; AAH09660.1; -; mRNA.
DR EMBL; AK014051; BAB29133.1; -; mRNA.
DR EMBL; AK032154; BAC27728.1; -; mRNA.
DR CCDS; CCDS21652.1; -.
DR RefSeq; NP_082720.1; NM_028444.1.
DR AlphaFoldDB; Q91VJ2; -.
DR BioGRID; 224532; 1.
DR IntAct; Q91VJ2; 1.
DR MINT; Q91VJ2; -.
DR STRING; 10090.ENSMUSP00000044979; -.
DR iPTMnet; Q91VJ2; -.
DR PhosphoSitePlus; Q91VJ2; -.
DR jPOST; Q91VJ2; -.
DR MaxQB; Q91VJ2; -.
DR PaxDb; Q91VJ2; -.
DR PeptideAtlas; Q91VJ2; -.
DR PRIDE; Q91VJ2; -.
DR ProteomicsDB; 265672; -.
DR Antibodypedia; 23796; 213 antibodies from 34 providers.
DR DNASU; 109042; -.
DR Ensembl; ENSMUST00000047040; ENSMUSP00000044979; ENSMUSG00000037060.
DR GeneID; 109042; -.
DR KEGG; mmu:109042; -.
DR UCSC; uc009iye.1; mouse.
DR CTD; 112464; -.
DR MGI; MGI:1923422; Cavin3.
DR VEuPathDB; HostDB:ENSMUSG00000037060; -.
DR eggNOG; ENOG502QQCA; Eukaryota.
DR GeneTree; ENSGT00950000182910; -.
DR HOGENOM; CLU_093512_0_0_1; -.
DR InParanoid; Q91VJ2; -.
DR OMA; DLKCFAV; -.
DR OrthoDB; 1532835at2759; -.
DR PhylomeDB; Q91VJ2; -.
DR TreeFam; TF331031; -.
DR BioGRID-ORCS; 109042; 0 hits in 73 CRISPR screens.
DR ChiTaRS; Cavin3; mouse.
DR PRO; PR:Q91VJ2; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q91VJ2; protein.
DR Bgee; ENSMUSG00000037060; Expressed in gonadal fat pad and 177 other tissues.
DR Genevisible; Q91VJ2; MM.
DR GO; GO:0005901; C:caveola; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0005080; F:protein kinase C binding; IPI:BHF-UCL.
DR GO; GO:0032922; P:circadian regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0030866; P:cortical actin cytoskeleton organization; IMP:MGI.
DR GO; GO:1901003; P:negative regulation of fermentation; IMP:MGI.
DR GO; GO:0051898; P:negative regulation of protein kinase B signaling; IMP:MGI.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IMP:MGI.
DR InterPro; IPR033300; CAVIN3.
DR InterPro; IPR026752; Cavin_fam.
DR PANTHER; PTHR15240; PTHR15240; 1.
DR PANTHER; PTHR15240:SF2; PTHR15240:SF2; 1.
DR Pfam; PF15237; PTRF_SDPR; 1.
PE 1: Evidence at protein level;
KW Biological rhythms; Cytoplasm; Isopeptide bond; Membrane; Phosphoprotein;
KW Reference proteome; Tumor suppressor; Ubl conjugation.
FT CHAIN 1..260
FT /note="Caveolae-associated protein 3"
FT /id="PRO_0000331413"
FT REGION 1..84
FT /note="Interaction with CAVIN1"
FT /evidence="ECO:0000269|PubMed:25588833"
FT REGION 20..78
FT /note="Leucine-zipper"
FT /evidence="ECO:0000250|UniProtKB:Q969G5"
FT REGION 135..200
FT /note="Interaction with CAV1"
FT /evidence="ECO:0000269|PubMed:25588833"
FT REGION 146..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..195
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 62
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q969G5"
FT MOD_RES 70
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q969G5"
FT MOD_RES 165
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 166
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 173
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CROSSLNK 128
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q969G5"
FT CONFLICT 225
FT /note="A -> G (in Ref. 2; BAB29133)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 260 AA; 27853 MW; C895CDCB329A9728 CRC64;
MGESALEPGP VPETPAGGPV HAVTVVTLLE KLATMLEALR ERQGGLAERQ GGLAGSVRRI
QSGLGALSRS HDTTSNTLTQ LLAKAERVGS HADAAQERAV RRAAQVQRLE ANHGLLVARG
KLHVLLFKEE TEIPARAFQK VPELLGPEDQ LVLGPDQPED EVGESSEEEP VESRAQRLRR
TGLQKVQSLK RALSSRKAAQ PTPVKPPRVG PVRSSEGPSE GQPAAQPEME SELETALEPE
PPQPTKEDPE KPVLQIESAA
