CAVN3_RAT
ID CAVN3_RAT Reviewed; 263 AA.
AC Q9Z1H9; P97585;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Caveolae-associated protein 3 {ECO:0000312|RGD:628755};
DE AltName: Full=Cavin-3;
DE AltName: Full=D3T-inducible gene 2 protein;
DE Short=DIG-2;
DE AltName: Full=Dithiolethione-inducible gene 2 protein;
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 {ECO:0000312|RGD:628755}; Synonyms=Dig2, Prkcdbp, Srbc;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PHOSPHORYLATION BY PRKCD.
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-79, AND INDUCTION BY DITHIOLETHIONE.
RC STRAIN=Fischer 344;
RX PubMed=8968041; DOI=10.1093/carcin/17.11.2297;
RA Primiano T., Gastel J.A., Kensler T.W., Sutter T.R.;
RT "Isolation of cDNAs representing dithiolethione-responsive genes.";
RL Carcinogenesis 17:2297-2303(1996).
RN [4]
RP FUNCTION.
RX PubMed=15197346; DOI=10.4161/cbt.3.8.969;
RA Bhattacharjee M., Sarkar S., Dutta S., Begum Z., Roy U.R., Chaudhuri S.,
RA Chaudhuri S.;
RT "Differential regulation of the protein tyrosine kinase activity following
RT interleukin-2 (IL-2), interferron gamma (IFN-gamma) and SRBC administration
RT in brain tumor-induced conditions: SRBC acting as a dual potentiator in
RT regulating the cytokine profile.";
RL Cancer Biol. Ther. 3:755-760(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62 AND SER-199, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Regulates the traffic and/or budding of caveolae. Plays a
CC role in caveola formation in a tissue-specific manner. Required for the
CC formation of caveolae in smooth muscle but not in the lung and heart
CC endothelial cells. 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. Plays a role in the
CC regulation of the circadian clock. Modulates the period length and
CC phase of circadian gene expression and also regulates expression and
CC interaction of the core clock components PER1/2 and CRY1/2 (By
CC similarity). Seems to have an immune potentiation function, especially
CC in the glioma (PubMed:15197346). {ECO:0000250|UniProtKB:Q91VJ2,
CC ECO:0000250|UniProtKB:Q969G5, ECO:0000269|PubMed:15197346}.
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 and EPS15L1. Interacts (via leucine-zipper domain) with CAV1 in
CC a cholesterol-sensitive manner. {ECO:0000250|UniProtKB:Q91VJ2,
CC ECO:0000250|UniProtKB:Q969G5}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q91VJ2}.
CC Membrane, caveola {ECO:0000250|UniProtKB:Q91VJ2}. Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q91VJ2}. Note=Localizes in the caveolae in a
CC caveolin-dependent manner. {ECO:0000250|UniProtKB:Q91VJ2}.
CC -!- INDUCTION: Up-regulated by 1,2-dithiole-3-thione (D3T).
CC {ECO:0000269|PubMed:8968041}.
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:0000250|UniProtKB:Q91VJ2}.
CC -!- SIMILARITY: Belongs to the CAVIN family. {ECO:0000305}.
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DR EMBL; D85435; BAA36277.1; -; mRNA.
DR EMBL; BC101398; AAI01399.1; -; mRNA.
DR EMBL; U66323; AAB39982.1; -; mRNA.
DR RefSeq; NP_604444.1; NM_134449.1.
DR AlphaFoldDB; Q9Z1H9; -.
DR SMR; Q9Z1H9; -.
DR STRING; 10116.ENSRNOP00000024119; -.
DR iPTMnet; Q9Z1H9; -.
DR PhosphoSitePlus; Q9Z1H9; -.
DR jPOST; Q9Z1H9; -.
DR PaxDb; Q9Z1H9; -.
DR PRIDE; Q9Z1H9; -.
DR GeneID; 85332; -.
DR KEGG; rno:85332; -.
DR UCSC; RGD:628755; rat.
DR CTD; 112464; -.
DR RGD; 628755; Cavin3.
DR VEuPathDB; HostDB:ENSRNOG00000017914; -.
DR eggNOG; ENOG502QQCA; Eukaryota.
DR HOGENOM; CLU_093512_0_0_1; -.
DR InParanoid; Q9Z1H9; -.
DR OMA; DLKCFAV; -.
DR OrthoDB; 1532835at2759; -.
DR PhylomeDB; Q9Z1H9; -.
DR TreeFam; TF331031; -.
DR PRO; PR:Q9Z1H9; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000017914; Expressed in heart and 20 other tissues.
DR Genevisible; Q9Z1H9; RN.
DR GO; GO:0005901; C:caveola; ISS: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; ISO:RGD.
DR GO; GO:0005080; F:protein kinase C binding; IDA:RGD.
DR GO; GO:0032922; P:circadian regulation of gene expression; ISS:UniProtKB.
DR GO; GO:0030866; P:cortical actin cytoskeleton organization; ISO:RGD.
DR GO; GO:1901003; P:negative regulation of fermentation; ISO:RGD.
DR GO; GO:0051898; P:negative regulation of protein kinase B signaling; ISO:RGD.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISO:RGD.
DR GO; GO:0001558; P:regulation of cell growth; NAS:RGD.
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..263
FT /note="Caveolae-associated protein 3"
FT /id="PRO_0000331414"
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:0000250|UniProtKB:Q969G5"
FT REGION 135..203
FT /note="Interaction with CAV1"
FT /evidence="ECO:0000250|UniProtKB:Q91VJ2"
FT REGION 141..263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..201
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 62
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 70
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q969G5"
FT MOD_RES 165
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q969G5"
FT MOD_RES 166
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q969G5"
FT MOD_RES 173
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q91VJ2"
FT MOD_RES 199
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
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 5
FT /note="A -> V (in Ref. 3; AAB39982)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 263 AA; 27910 MW; 3F2FE5E3DCB1F750 CRC64;
MGESALEPGP VPGAPAGGPV HAVTVVTLLE KLATMLEALR ERQGGLAERQ GGLAGSVRRI
QSGLGALSRS HDTTSNTLAQ LLAKAERVGS HADAAQERAV HRAAQVQRLE ANHGLLVARG
KLHVLLFKEE TEIPARAFQK APELLGPEDQ LVLGPEQPED EVGESSDEEP VESRAQRLRR
TGLQKVQSLK RAFSSRKGSE AAQPTPVKPP RLGPVRNSEG PAEGQPAAQP AMEPVLPSAL
EPEPPQPTKE DPERPVLQIE SAA
