CAVN3_BOVIN
ID CAVN3_BOVIN Reviewed; 260 AA.
AC A4FV37;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Caveolae-associated protein 3;
DE AltName: Full=Cavin-3;
DE AltName: Full=Protein kinase C delta-binding protein;
GN Name=CAVIN3; Synonyms=PRKCDBP;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hippocampus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
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.
CC {ECO:0000250|UniProtKB:Q91VJ2, ECO:0000250|UniProtKB:Q969G5}.
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 -!- 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; BC123692; AAI23693.1; -; mRNA.
DR RefSeq; NP_001076870.1; NM_001083401.1.
DR AlphaFoldDB; A4FV37; -.
DR SMR; A4FV37; -.
DR STRING; 9913.ENSBTAP00000026323; -.
DR PaxDb; A4FV37; -.
DR PeptideAtlas; A4FV37; -.
DR PRIDE; A4FV37; -.
DR Ensembl; ENSBTAT00000026323; ENSBTAP00000026323; ENSBTAG00000019754.
DR GeneID; 510203; -.
DR KEGG; bta:510203; -.
DR CTD; 112464; -.
DR VEuPathDB; HostDB:ENSBTAG00000019754; -.
DR VGNC; VGNC:26804; CAVIN3.
DR eggNOG; ENOG502QQCA; Eukaryota.
DR GeneTree; ENSGT00950000182910; -.
DR HOGENOM; CLU_093512_0_0_1; -.
DR InParanoid; A4FV37; -.
DR OMA; DLKCFAV; -.
DR OrthoDB; 1532835at2759; -.
DR TreeFam; TF331031; -.
DR Proteomes; UP000009136; Chromosome 15.
DR Bgee; ENSBTAG00000019754; Expressed in myometrium and 106 other tissues.
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; IEA:Ensembl.
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 2: Evidence at transcript 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_0000331411"
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..201
FT /note="Interaction with CAV1"
FT /evidence="ECO:0000250|UniProtKB:Q91VJ2"
FT REGION 140..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 167..184
FT /note="Basic and acidic 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 162
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q969G5"
FT MOD_RES 163
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q969G5"
FT MOD_RES 171
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:0000250|UniProtKB:Q969G5"
SQ SEQUENCE 260 AA; 27487 MW; 5F8C4AB4636A39AA CRC64;
MGESALESGP VPGAPAGGPV HAVTVVTLLE KLATMLETLR ERQGGLAQRQ GGLAGSVRRI
QSNLGALSRS HDTTSNTLAQ LLAKAERVGS HADAAQERAV RRAAQVQRLE ANHGLLVARG
KLHVLLFKEE AEIPAKAFQK APEPLGPVEL GPQLPEAEAE ESSDEEEPVE SRARRLRRTG
LEKVQSLRRA LSGRKGHAAP TPTPVKPPRL GPGRSAEGQW EAQPALESKL EPEPPQDTEE
DPGRPGAAEA AAVLQVESAA
