CAVN2_RAT
ID CAVN2_RAT Reviewed; 417 AA.
AC Q66H98;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Caveolae-associated protein 2 {ECO:0000312|RGD:1359345};
DE AltName: Full=Cavin-2;
DE AltName: Full=Phosphatidylserine-binding protein;
DE AltName: Full=Serum deprivation-response protein;
GN Name=Cavin2 {ECO:0000312|RGD:1359345};
GN Synonyms=Sdpr {ECO:0000312|EMBL:AAH81956.1};
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 [LARGE SCALE MRNA].
RC TISSUE=Lung;
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] {ECO:0000305}
RP FUNCTION, INTERACTION WITH PRKCA, AND SUBCELLULAR LOCATION.
RX PubMed=9566962; DOI=10.1083/jcb.141.3.601;
RA Mineo C., Ying Y.-S., Chapline C., Jaken S., Anderson R.G.W.;
RT "Targeting of protein kinase Calpha to caveolae.";
RL J. Cell Biol. 141:601-610(1998).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27; SER-35; SER-51; SER-202;
RP SER-203; SER-217; SER-283; SER-292; SER-326; SER-335; SER-362; SER-389 AND
RP SER-395, AND 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: Plays an important role in caveolar biogenesis and
CC morphology. Regulates caveolae morphology by inducing membrane
CC curvature within caveolae. Plays a role in caveola formation in a
CC tissue-specific manner. Required for the formation of caveolae in the
CC lung and fat endothelia but not in the heart endothelia. Negatively
CC regulates the size or stability of CAVIN complexes in the lung
CC endothelial cells (By similarity). May play a role in targeting PRKCA
CC to caveolae (PubMed:9566962). {ECO:0000250|UniProtKB:O95810,
CC ECO:0000250|UniProtKB:Q63918, ECO:0000269|PubMed:9566962}.
CC -!- SUBUNIT: Component of the CAVIN complex composed of CAVIN1, CAVIN2,
CC CAVIN3 and CAVIN. Interacts with CAVIN4; this augments the
CC transactivation of NPPA by CAVIN4 (By similarity). Binds to PRKCA in
CC the presence of phosphatidylserine (PubMed:9566962). Interacts with
CC CAVIN1 and CAV3 (By similarity). {ECO:0000250|UniProtKB:O95810,
CC ECO:0000250|UniProtKB:Q63918, ECO:0000269|PubMed:9566962}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:O95810}. Membrane, caveola
CC {ECO:0000269|PubMed:9566962}. Note=Localizes in the caveolae in a
CC caveolin-dependent manner. {ECO:0000269|PubMed:9566962}.
CC -!- DOMAIN: The leucine-zipper domain is essential for its localization in
CC the caveolae. {ECO:0000250|UniProtKB:O95810}.
CC -!- PTM: The N-terminus is blocked. {ECO:0000250}.
CC -!- PTM: Phosphorylated on Ser residues. {ECO:0000250}.
CC -!- MISCELLANEOUS: Binds phosphatidylserine (PS) in a calcium-independent
CC manner. PS-binding is inhibited by phosphotidic acid and
CC phosphatidylinositol. Does not bind phosphatidylcholine (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the CAVIN family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC081956; AAH81956.1; -; mRNA.
DR RefSeq; NP_001007713.1; NM_001007712.1.
DR AlphaFoldDB; Q66H98; -.
DR SMR; Q66H98; -.
DR BioGRID; 261332; 1.
DR IntAct; Q66H98; 1.
DR STRING; 10116.ENSRNOP00000030025; -.
DR iPTMnet; Q66H98; -.
DR PhosphoSitePlus; Q66H98; -.
DR PaxDb; Q66H98; -.
DR PRIDE; Q66H98; -.
DR Ensembl; ENSRNOT00000028907; ENSRNOP00000030025; ENSRNOG00000025895.
DR GeneID; 316384; -.
DR KEGG; rno:316384; -.
DR UCSC; RGD:1359345; rat.
DR CTD; 8436; -.
DR RGD; 1359345; Cavin2.
DR eggNOG; ENOG502QQCA; Eukaryota.
DR GeneTree; ENSGT00950000182910; -.
DR HOGENOM; CLU_039470_1_0_1; -.
DR InParanoid; Q66H98; -.
DR OMA; QMPNDQE; -.
DR OrthoDB; 858587at2759; -.
DR PhylomeDB; Q66H98; -.
DR TreeFam; TF331031; -.
DR PRO; PR:Q66H98; -.
DR Proteomes; UP000002494; Chromosome 9.
DR Bgee; ENSRNOG00000025895; Expressed in lung and 19 other tissues.
DR Genevisible; Q66H98; RN.
DR GO; GO:0005901; C:caveola; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0045121; C:membrane raft; ISO:RGD.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0001786; F:phosphatidylserine binding; ISS:UniProtKB.
DR GO; GO:0005080; F:protein kinase C binding; IBA:GO_Central.
DR GO; GO:0097320; P:plasma membrane tubulation; ISS:UniProtKB.
DR InterPro; IPR033298; Cavin2.
DR InterPro; IPR026752; Cavin_fam.
DR PANTHER; PTHR15240; PTHR15240; 1.
DR PANTHER; PTHR15240:SF1; PTHR15240:SF1; 1.
DR Pfam; PF15237; PTRF_SDPR; 1.
PE 1: Evidence at protein level;
KW Acetylation; Coiled coil; Cytoplasm; Lipid-binding; Membrane;
KW Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O95810"
FT CHAIN 2..417
FT /note="Caveolae-associated protein 2"
FT /id="PRO_0000238920"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2..168
FT /note="Interaction with CAVIN1"
FT /evidence="ECO:0000250|UniProtKB:Q63918"
FT REGION 62..100
FT /note="Leucine-zipper"
FT /evidence="ECO:0000250|UniProtKB:O95810"
FT REGION 198..242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 256..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 61..87
FT /evidence="ECO:0000255"
FT COILED 126..267
FT /evidence="ECO:0000255"
FT COMPBIAS 219..242
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 256..275
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..290
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..328
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylglycine"
FT /evidence="ECO:0000250|UniProtKB:O95810"
FT MOD_RES 27
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 35
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 37
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63918"
FT MOD_RES 51
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 195
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O95810"
FT MOD_RES 202
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 203
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 217
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 282
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63918"
FT MOD_RES 283
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 286
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95810"
FT MOD_RES 287
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95810"
FT MOD_RES 292
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 295
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63918"
FT MOD_RES 326
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 335
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 358
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63918"
FT MOD_RES 362
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 367
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q63918"
FT MOD_RES 387
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q63918"
FT MOD_RES 389
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 395
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 417 AA; 46386 MW; CA138577B3A4A6A0 CRC64;
MGEDAAQAEK FQHPNTDMLQ EKPSNPSPMP SSTPSPSLNL GSTEEAIRDN SQVNAVTVHT
LLDKLVNMLD AVRENQHNME QRQINLEGSV KGIQNDLTKL SKYQASTSNT VSKLLEKSRK
VSAHTRAVRE RLEKQCVQVK RLENNHAQLL RRNHFKVLIF QEESEIPASV FVKEPVPSTA
EGKELADENK SLEETLHNVD LSSDDELPGD EEALEDSAEE KMEESRAEKI KRSSLKKVDS
LKKAFSRQNI EKKMNKLGTK IVSVERREKI KKSLTPNHQK ASSGKSSPFK VSPLSFGRKK
IREGESSAEN ETKLEEQVQD DHEEGSFTEG LSEASLPSGL LEGSAEDAEK SALRGNNSGV
GSNADLTIEE DEEEESVALQ QAQQVRYESG YMLNSKEMEE SSEKHVQAAV LHVDQTA
