CAVN3_HUMAN
ID CAVN3_HUMAN Reviewed; 261 AA.
AC Q969G5;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 3.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Caveolae-associated protein 3 {ECO:0000312|HGNC:HGNC:9400};
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;
DE Short=hSRBC;
GN Name=CAVIN3 {ECO:0000312|HGNC:HGNC:9400}; Synonyms=PRKCDBP, SRBC;
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 [GENOMIC DNA / MRNA], INDUCTION, TISSUE SPECIFICITY,
RP AND VARIANT PRO-8.
RC TISSUE=Epithelium;
RX PubMed=11691816;
RA Xu X.L., Wu L.C., Du F., Davis A., Peyton M., Tomizawa Y., Maitra A.,
RA Tomlinson G., Gazdar A.F., Weissman B.E., Bowcock A.M., Baer R.,
RA Minna J.D.;
RT "Inactivation of human SRBC, located within the 11p15.5-p15.4 tumor
RT suppressor region, in breast and lung cancers.";
RL Cancer Res. 61:7943-7949(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT PRO-8.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT PRO-8.
RC TISSUE=Skin;
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165 AND SER-166, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, DOMAIN LEUCINE ZIPPER, INTERACTION WITH
RP CAV1 AND EPS15L1, AND TISSUE SPECIFICITY.
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165 AND SER-166, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165 AND SER-166, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62 AND SER-70, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62; SER-165 AND SER-166, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [14]
RP REVIEW.
RX PubMed=26614875; DOI=10.1016/bs.ircmb.2015.07.009;
RA Nassar Z.D., Parat M.O.;
RT "Cavin family: new players in the biology of caveolae.";
RL Int. Rev. Cell Mol. Biol. 320:235-305(2015).
RN [15]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-128, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- FUNCTION: Regulates the traffic and/or budding of caveolae
CC (PubMed:19262564). Plays a role in caveola formation in a tissue-
CC specific manner. Required for the formation of caveolae in smooth
CC muscle but not in the lung and heart endothelial cells. Regulates the
CC equilibrium between cell surface-associated and cell surface-
CC dissociated caveolae by promoting the rapid release of caveolae from
CC the cell surface. Plays a role in the regulation of the circadian
CC clock. Modulates the period length and phase of circadian gene
CC expression and also regulates expression and interaction of the core
CC clock components PER1/2 and CRY1/2 (By similarity).
CC {ECO:0000250|UniProtKB:Q91VJ2, ECO:0000250|UniProtKB:Q9Z1H9,
CC ECO:0000269|PubMed:19262564}.
CC -!- SUBUNIT: Component of the CAVIN complex composed of CAVIN1, CAVIN2,
CC CAVIN3 and CAVIN4. Interacts with PRKCD and with phosphatidylserine.
CC Phosphatidylserine may form a bridge between PKC and PKC-binding
CC partners and stabilize the binding. Interacts with PER2. Interacts with
CC CAVIN1 (By similarity). Interacts (via leucine-zipper domain) with CAV1
CC in a cholesterol-sensitive manner (PubMed:19262564). Interacts with
CC EPS15L1 (PubMed:19262564). {ECO:0000250|UniProtKB:Q91VJ2,
CC ECO:0000269|PubMed:19262564}.
CC -!- INTERACTION:
CC Q969G5; Q03135: CAV1; NbExp=11; IntAct=EBI-3893101, EBI-603614;
CC Q969G5; Q6NZI2: CAVIN1; NbExp=11; IntAct=EBI-3893101, EBI-2559016;
CC Q969G5; Q8NHQ1: CEP70; NbExp=3; IntAct=EBI-3893101, EBI-739624;
CC Q969G5; Q8TAP6: CEP76; NbExp=3; IntAct=EBI-3893101, EBI-742887;
CC Q969G5; Q9UBC2: EPS15L1; NbExp=2; IntAct=EBI-3893101, EBI-2556746;
CC Q969G5; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-3893101, EBI-5916454;
CC Q969G5; Q96D09: GPRASP2; NbExp=3; IntAct=EBI-3893101, EBI-473189;
CC Q969G5; P43364: MAGEA11; NbExp=3; IntAct=EBI-3893101, EBI-739552;
CC Q969G5; Q9Y605: MRFAP1; NbExp=5; IntAct=EBI-3893101, EBI-995714;
CC Q969G5; Q96HT8: MRFAP1L1; NbExp=6; IntAct=EBI-3893101, EBI-748896;
CC Q969G5; P37198: NUP62; NbExp=3; IntAct=EBI-3893101, EBI-347978;
CC Q969G5; Q9UBB9: TFIP11; NbExp=3; IntAct=EBI-3893101, EBI-1105213;
CC Q969G5; O60220: TIMM8A; NbExp=3; IntAct=EBI-3893101, EBI-1049822;
CC Q969G5; P06753: TPM3; NbExp=3; IntAct=EBI-3893101, EBI-355607;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q91VJ2}.
CC Membrane, caveola {ECO:0000269|PubMed:19262564}. Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q91VJ2}. Note=Localizes in the caveolae in a
CC caveolin-dependent manner. {ECO:0000269|PubMed:19262564}.
CC -!- TISSUE SPECIFICITY: Skeletal muscle, liver, stomach, lung, kidney and
CC heart (at protein level). Strongly expressed in mammary and epithelial
CC cells. {ECO:0000269|PubMed:11691816, ECO:0000269|PubMed:19262564}.
CC -!- INDUCTION: Down-regulated in breast and lung cancer cell lines.
CC {ECO:0000269|PubMed:11691816}.
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:0000269|PubMed:19262564}.
CC -!- PTM: In vitro, phosphorylated by PRKCD.
CC -!- SIMILARITY: Belongs to the CAVIN family. {ECO:0000305}.
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DR EMBL; AF339881; AAK97572.1; -; mRNA.
DR EMBL; AF408198; AAK97528.1; -; Genomic_DNA.
DR EMBL; AC068733; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471064; EAW68733.1; -; Genomic_DNA.
DR EMBL; BC011585; AAH11585.1; -; mRNA.
DR CCDS; CCDS7762.1; -.
DR RefSeq; NP_659477.2; NM_145040.2.
DR AlphaFoldDB; Q969G5; -.
DR SMR; Q969G5; -.
DR BioGRID; 125187; 154.
DR DIP; DIP-60484N; -.
DR IntAct; Q969G5; 50.
DR MINT; Q969G5; -.
DR STRING; 9606.ENSP00000307292; -.
DR iPTMnet; Q969G5; -.
DR MetOSite; Q969G5; -.
DR PhosphoSitePlus; Q969G5; -.
DR BioMuta; CAVIN3; -.
DR DMDM; 317373527; -.
DR EPD; Q969G5; -.
DR jPOST; Q969G5; -.
DR MassIVE; Q969G5; -.
DR MaxQB; Q969G5; -.
DR PaxDb; Q969G5; -.
DR PeptideAtlas; Q969G5; -.
DR PRIDE; Q969G5; -.
DR ProteomicsDB; 75756; -.
DR Antibodypedia; 23796; 213 antibodies from 34 providers.
DR DNASU; 112464; -.
DR Ensembl; ENST00000303927.4; ENSP00000307292.3; ENSG00000170955.10.
DR GeneID; 112464; -.
DR KEGG; hsa:112464; -.
DR MANE-Select; ENST00000303927.4; ENSP00000307292.3; NM_145040.3; NP_659477.2.
DR UCSC; uc001mcu.2; human.
DR CTD; 112464; -.
DR DisGeNET; 112464; -.
DR GeneCards; CAVIN3; -.
DR HGNC; HGNC:9400; CAVIN3.
DR HPA; ENSG00000170955; Low tissue specificity.
DR MIM; 618303; gene.
DR neXtProt; NX_Q969G5; -.
DR OpenTargets; ENSG00000170955; -.
DR PharmGKB; PA33764; -.
DR VEuPathDB; HostDB:ENSG00000170955; -.
DR eggNOG; ENOG502QQCA; Eukaryota.
DR GeneTree; ENSGT00950000182910; -.
DR InParanoid; Q969G5; -.
DR OrthoDB; 1532835at2759; -.
DR PhylomeDB; Q969G5; -.
DR TreeFam; TF331031; -.
DR PathwayCommons; Q969G5; -.
DR SignaLink; Q969G5; -.
DR BioGRID-ORCS; 112464; 8 hits in 1074 CRISPR screens.
DR ChiTaRS; PRKCDBP; human.
DR GenomeRNAi; 112464; -.
DR Pharos; Q969G5; Tbio.
DR PRO; PR:Q969G5; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q969G5; protein.
DR Bgee; ENSG00000170955; Expressed in right coronary artery and 177 other tissues.
DR ExpressionAtlas; Q969G5; baseline and differential.
DR Genevisible; Q969G5; HS.
DR GO; GO:0005901; C:caveola; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0032991; C:protein-containing complex; IDA:MGI.
DR GO; GO:0005080; F:protein kinase C binding; IBA:GO_Central.
DR GO; GO:0032922; P:circadian regulation of gene expression; ISS:UniProtKB.
DR GO; GO:0030866; P:cortical actin cytoskeleton organization; IEA:Ensembl.
DR GO; GO:1901003; P:negative regulation of fermentation; IEA:Ensembl.
DR GO; GO:0051898; P:negative regulation of protein kinase B signaling; IEA:Ensembl.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
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..261
FT /note="Caveolae-associated protein 3"
FT /id="PRO_0000331412"
FT REGION 1..84
FT /note="Interaction with CAVIN1"
FT /evidence="ECO:0000250|UniProtKB:Q91VJ2"
FT REGION 20..78
FT /note="Leucine-zipper"
FT /evidence="ECO:0000269|PubMed:19262564"
FT REGION 135..203
FT /note="Interaction with CAV1"
FT /evidence="ECO:0000250|UniProtKB:Q91VJ2"
FT REGION 139..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 62
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 70
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 165
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 166
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 173
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q91VJ2"
FT CROSSLNK 128
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 8
FT /note="R -> P (in dbSNP:rs2682123)"
FT /evidence="ECO:0000269|PubMed:11691816,
FT ECO:0000269|PubMed:15489334, ECO:0000269|Ref.3"
FT /id="VAR_042851"
FT VARIANT 104
FT /note="A -> T (in dbSNP:rs10839551)"
FT /id="VAR_042852"
FT VARIANT 158
FT /note="L -> P (in dbSNP:rs1051992)"
FT /id="VAR_042853"
FT VARIANT 255
FT /note="L -> F (in dbSNP:rs12294600)"
FT /id="VAR_042854"
SQ SEQUENCE 261 AA; 27701 MW; E806A01DA992C53B CRC64;
MRESALERGP VPEAPAGGPV HAVTVVTLLE KLASMLETLR ERQGGLARRQ GGLAGSVRRI
QSGLGALSRS HDTTSNTLAQ LLAKAERVSS HANAAQERAV RRAAQVQRLE ANHGLLVARG
KLHVLLFKEE GEVPASAFQK APEPLGPADQ SELGPEQLEA EVGESSDEEP VESRAQRLRR
TGLQKVQSLR RALSGRKGPA APPPTPVKPP RLGPGRSAEA QPEAQPALEP TLEPEPPQDT
EEDPGRPGAA EEALLQMESV A
