CAV2_CAEEL
ID CAV2_CAEEL Reviewed; 351 AA.
AC Q18879; E1B6T3; E1B6T4; G3MU34;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 3.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Caveolin-2;
GN Name=cav-2; ORFNames=C56A3.7;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
RC STRAIN=Bristol N2;
RX PubMed=8999956; DOI=10.1074/jbc.272.4.2437;
RA Tang Z., Okamoto T., Boontrakulpoontawee P., Katada T., Otsuka A.J.,
RA Lisanti M.P.;
RT "Identification, sequence, and expression of an invertebrate caveolin gene
RT family from the nematode Caenorhabditis elegans. Implications for the
RT molecular evolution of mammalian caveolin genes.";
RL J. Biol. Chem. 272:2437-2445(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP FUNCTION.
RX PubMed=19907693; DOI=10.4161/cib.2.5.8715;
RA Parker S., Baylis H.A.;
RT "Overexpression of caveolins in Caenorhabditis elegans induces changes in
RT egg-laying and fecundity.";
RL Commun. Integr. Biol. 2:382-384(2009).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=19158391; DOI=10.1091/mbc.e08-08-0837;
RA Parker S., Walker D.S., Ly S., Baylis H.A.;
RT "Caveolin-2 is required for apical lipid trafficking and suppresses
RT basolateral recycling defects in the intestine of Caenorhabditis elegans.";
RL Mol. Biol. Cell 20:1763-1771(2009).
CC -!- FUNCTION: May act as a scaffolding protein within caveolar membranes.
CC Interacts directly with G-protein alpha subunits and can regulate their
CC activity. Thought to have a role in the uptake of lipids and proteins
CC in the intestinal cells; operates in the apical uptake of lipid markers
CC and trafficking of yolk proteins. Affects fecundity and egg laying.
CC {ECO:0000269|PubMed:19158391, ECO:0000269|PubMed:19907693}.
CC -!- SUBUNIT: Homooligomer. {ECO:0000250}.
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:0000250}; Peripheral membrane protein {ECO:0000250}. Apical cell
CC membrane {ECO:0000269|PubMed:19158391}. Note=Potential hairpin-like
CC structure in the membrane. Membrane protein of caveolae (By
CC similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=a;
CC IsoId=Q18879-1; Sequence=Displayed;
CC Name=b;
CC IsoId=Q18879-2; Sequence=VSP_043963;
CC Name=c;
CC IsoId=Q18879-3; Sequence=VSP_043962;
CC Name=d;
CC IsoId=Q18879-4; Sequence=VSP_043964;
CC -!- TISSUE SPECIFICITY: Expressed in intracellular bodies in intestinal
CC cells. {ECO:0000269|PubMed:19158391}.
CC -!- DISRUPTION PHENOTYPE: Defective in the apical uptake of lipid and
CC protein trafficking. Reduced brood size thought to be due to attenuated
CC nutrient supply. {ECO:0000269|PubMed:19158391}.
CC -!- SIMILARITY: Belongs to the caveolin family. {ECO:0000305}.
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DR EMBL; U75587; AAB48299.1; -; mRNA.
DR EMBL; Z77655; CAB01139.1; -; Genomic_DNA.
DR EMBL; Z77655; CBW48350.1; -; Genomic_DNA.
DR EMBL; Z77655; CBW48351.1; -; Genomic_DNA.
DR EMBL; Z77655; CCD31049.1; -; Genomic_DNA.
DR PIR; T20270; T20270.
DR RefSeq; NP_001256523.1; NM_001269594.1. [Q18879-1]
DR RefSeq; NP_001256524.1; NM_001269595.1. [Q18879-4]
DR RefSeq; NP_001256525.1; NM_001269596.1. [Q18879-2]
DR RefSeq; NP_001256526.1; NM_001269597.1. [Q18879-3]
DR AlphaFoldDB; Q18879; -.
DR STRING; 6239.C56A3.7a; -.
DR iPTMnet; Q18879; -.
DR EPD; Q18879; -.
DR PaxDb; Q18879; -.
DR PeptideAtlas; Q18879; -.
DR EnsemblMetazoa; C56A3.7a.1; C56A3.7a.1; WBGene00000302. [Q18879-1]
DR EnsemblMetazoa; C56A3.7b.1; C56A3.7b.1; WBGene00000302. [Q18879-2]
DR EnsemblMetazoa; C56A3.7c.1; C56A3.7c.1; WBGene00000302. [Q18879-3]
DR EnsemblMetazoa; C56A3.7d.1; C56A3.7d.1; WBGene00000302. [Q18879-4]
DR GeneID; 179838; -.
DR KEGG; cel:CELE_C56A3.7; -.
DR UCSC; C56A3.7; c. elegans. [Q18879-1]
DR CTD; 179838; -.
DR WormBase; C56A3.7a; CE15738; WBGene00000302; cav-2. [Q18879-1]
DR WormBase; C56A3.7b; CE45292; WBGene00000302; cav-2. [Q18879-2]
DR WormBase; C56A3.7c; CE45320; WBGene00000302; cav-2. [Q18879-3]
DR WormBase; C56A3.7d; CE46485; WBGene00000302; cav-2. [Q18879-4]
DR eggNOG; ENOG502RZYX; Eukaryota.
DR GeneTree; ENSGT00950000183006; -.
DR InParanoid; Q18879; -.
DR OMA; WPMFLIY; -.
DR OrthoDB; 1380805at2759; -.
DR PRO; PR:Q18879; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00000302; Expressed in larva and 4 other tissues.
DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR GO; GO:0005901; C:caveola; TAS:WormBase.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005319; F:lipid transporter activity; IMP:UniProtKB.
DR GO; GO:0060090; F:molecular adaptor activity; IBA:GO_Central.
DR GO; GO:0070836; P:caveola assembly; IBA:GO_Central.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; TAS:WormBase.
DR GO; GO:0007567; P:parturition; IMP:UniProtKB.
DR GO; GO:0046662; P:regulation of oviposition; IGI:WormBase.
DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR CDD; cd06261; TM_PBP2; 1.
DR InterPro; IPR001612; Caveolin.
DR InterPro; IPR000515; MetI-like.
DR PANTHER; PTHR10844; PTHR10844; 1.
DR Pfam; PF01146; Caveolin; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cell membrane; Golgi apparatus; Membrane;
KW Reference proteome.
FT CHAIN 1..351
FT /note="Caveolin-2"
FT /id="PRO_0000144144"
FT TOPO_DOM 1..261
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT INTRAMEM 262..290
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 291..351
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 71..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 144..193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..87
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..188
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..191
FT /note="Missing (in isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_043962"
FT VAR_SEQ 1..32
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_043963"
FT VAR_SEQ 28..97
FT /note="Missing (in isoform d)"
FT /evidence="ECO:0000305"
FT /id="VSP_043964"
FT CONFLICT 105
FT /note="V -> F (in Ref. 1; AAB48299)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 351 AA; 40771 MW; 5D3A6841966DED0A CRC64;
MTRQNTSESD NTQRPPIPQY DTVDDIDELT DAMDKEDHHH HHHHHEHHHQ HQGIAQYDTV
EEVETLETVH HRTSLNQEVP TPQRRSHPQY DNLDDIDDQE YITEVEVKSN RGSTLTTRPH
VTIKQDEIED IGERQVTVIE IASQKGSTKR VAPRKDYAPS IPLPEHPAQQ SAPPTQQSRP
QTTSHKPPNP EMEFDIGVKN IAPVLIHKMN MDDRDPKDSA QYLNTSFFEV FNEPSEQYHS
IACVWTLSFK IFEIVRIYSY KILTLIFGLI IAFLGGILFA LFAFLNIWIF RPILILTRMA
FAQIVLIWPM FLIYIVRPFF YSVGAIFSTA RLHTSRGEQV VEVWEKHIHH V
