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Protein

Caveolae-associated protein 2

Gene

Cavin2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Plays an important role in caveolar biogenesis and morphology. Regulates caveolae morphology by inducing membrane curvature within caveolae (By similarity). Plays a role in caveola formation in a tissue-specific manner. Required for the formation of caveolae in the lung and fat endothelia but not in the heart endothelia. Negatively regulates the size or stability of CAVIN complexes in the lung endothelial cells (PubMed:23652019). May play a role in targeting PRKCA to caveolae (By similarity).By similarity1 Publication

Miscellaneous

Binds phosphatidylserine (PS) in a calcium-independent manner. PS-binding is inhibited by phosphotidic acid and phosphatidylinositol. Does not bind phosphatidylcholine (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Keywordsi

LigandLipid-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Caveolae-associated protein 2
Alternative name(s):
Cavin-2
Phosphatidylserine-binding protein
Serum deprivation-response protein
Gene namesi
Name:Cavin2
Synonyms:SdprImported, Sdr1 Publication
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:99513. Cavin2.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Membrane

Pathology & Biotechi

Disruption phenotypei

Mice show loss of endothelial caveolae in lung and adipose tissue but no effect on the abundance of endothelial caveolae in the heart.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00002389192 – 418Caveolae-associated protein 2Add BLAST417

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylglycineBy similarity1
Modified residuei27PhosphoserineCombined sources1
Modified residuei35PhosphoserineCombined sources1
Modified residuei37PhosphoserineCombined sources1
Modified residuei51PhosphoserineBy similarity1
Modified residuei196PhosphothreonineBy similarity1
Modified residuei203PhosphoserineCombined sources1
Modified residuei204PhosphoserineCombined sources1
Modified residuei218PhosphoserineCombined sources1
Modified residuei283PhosphoserineCombined sources1
Modified residuei284PhosphoserineCombined sources1
Modified residuei287PhosphoserineCombined sources1
Modified residuei288PhosphoserineCombined sources1
Modified residuei293PhosphoserineCombined sources1
Modified residuei296PhosphoserineCombined sources1
Modified residuei327PhosphoserineCombined sources1
Modified residuei336PhosphoserineCombined sources1
Modified residuei359PhosphoserineCombined sources1
Modified residuei363PhosphoserineCombined sources1
Modified residuei368PhosphothreonineCombined sources1
Modified residuei388PhosphotyrosineCombined sources1
Modified residuei390PhosphoserineCombined sources1
Modified residuei396PhosphoserineBy similarity1

Post-translational modificationi

The N-terminus is blocked.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ63918.
PaxDbiQ63918.
PeptideAtlasiQ63918.
PRIDEiQ63918.

PTM databases

iPTMnetiQ63918.
PhosphoSitePlusiQ63918.
SwissPalmiQ63918.

Expressioni

Tissue specificityi

Heart, adipose tissue, lung and endothelial cells (at protein level). Highly expressed in kidney and expressed at lower levels in liver, spleen, thymus, stomach, intestine and uterus.3 Publications

Developmental stagei

Expression gradually increases during embryonic stages and reaches a maximum in neonates.1 Publication

Inductioni

Up-regulated in response to cardiac hypertrophy and in serum-starved but not in density-dependent growth-arrested NIH3T3 cells. Down-regulated within 6 hours after the addition of serum or epidermal growth factor to serum-starved cells.2 Publications

Gene expression databases

BgeeiENSMUSG00000045954.
CleanExiMM_SDPR.
GenevisibleiQ63918. MM.

Interactioni

Subunit structurei

Component of the CAVIN complex composed of CAVIN1, CAVIN2, CAVIN3 and CAVIN4 (PubMed:19546242). Binds to PRKCA in the presence of phosphatidylserine. Interacts with CAVIN4; this augments the transactivation of NPPA by CAVIN4 (By similarity). Interacts with CAVIN1 (PubMed:25588833, PubMed:19546242). Interacts with CAV3 (By similarity).By similarity2 Publications

GO - Molecular functioni

Protein-protein interaction databases

IntActiQ63918. 3 interactors.
MINTiMINT-4114971.
STRINGi10090.ENSMUSP00000055694.

Structurei

3D structure databases

ProteinModelPortaliQ63918.
SMRiQ63918.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 168Interaction with CAVIN11 PublicationAdd BLAST167
Regioni62 – 100Leucine-zipperBy similarityAdd BLAST39

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili61 – 87Sequence analysisAdd BLAST27
Coiled coili126 – 268Sequence analysisAdd BLAST143

Domaini

The leucine-zipper domain is essential for its localization in the caveolae.By similarity

Sequence similaritiesi

Belongs to the CAVIN family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410IEZA. Eukaryota.
ENOG410XP8W. LUCA.
GeneTreeiENSGT00530000063058.
HOGENOMiHOG000293135.
HOVERGENiHBG056807.
InParanoidiQ63918.
OMAiERMDRQC.
OrthoDBiEOG091G09Y1.
PhylomeDBiQ63918.
TreeFamiTF331031.

Family and domain databases

InterProiView protein in InterPro
IPR033298. Cavin2.
IPR026752. Cavin_fam.
PANTHERiPTHR15240. PTHR15240. 1 hit.
PTHR15240:SF1. PTHR15240:SF1. 1 hit.
PfamiView protein in Pfam
PF15237. PTRF_SDPR. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q63918-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGEDAAQAEK FQHPNTDMLQ EKPSSPSPMP SSTPSPSLNL GSTEEAIRDN
60 70 80 90 100
SQVNAVTVHT LLDKLVNMLD AVRENQHNME QRQINLEGSV KGIQNDLTKL
110 120 130 140 150
SKYQASTSNT VSKLLEKSRK VSAHTRAVRE RLERQCVQVK RLENNHAQLL
160 170 180 190 200
RRNHFKVLIF QEESEIPASV FVKEPVPSAA EGKEELADEN KSLEETLHNV
210 220 230 240 250
DLSSDDELPR DEEALEDSAE EKMEESRAEK IKRSSLKKVD SLKKAFSRQN
260 270 280 290 300
IEKKMNKLGT KIVSVERREK IKKSLTPNHQ KASSGKSSPF KVSPLSFGRK
310 320 330 340 350
KVREGESSVE NETKLEDQMQ EDREEGSFTE GLSEASLPSG LMEGSAEDAE
360 370 380 390 400
KSARRGNNSA VGSNADLTIE EDEEEEPVAL QQAQQVRYES GYMLNSEEME
410
EPSEKQVQPA VLHVDQTA
Length:418
Mass (Da):46,764
Last modified:January 23, 2007 - v3
Checksum:iEFD7B4E383785F41
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti14P → L in BAE21104 (PubMed:16141072).Curated1
Sequence conflicti76Q → L in BAC29033 (PubMed:16141072).Curated1
Sequence conflicti173K → R in BAC29033 (PubMed:16141072).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S67386 mRNA. Translation: AAB28953.1.
AK035324 mRNA. Translation: BAC29033.1.
AK084096 mRNA. Translation: BAC39116.1.
AK132324 mRNA. Translation: BAE21104.1.
BC020008 mRNA. Translation: AAH20008.1.
BC027005 mRNA. Translation: AAH27005.1.
CCDSiCCDS14940.1.
RefSeqiNP_620080.1. NM_138741.1.
UniGeneiMm.398690.

Genome annotation databases

EnsembliENSMUST00000051572; ENSMUSP00000055694; ENSMUSG00000045954.
GeneIDi20324.
KEGGimmu:20324.
UCSCiuc007axk.1. mouse.

Similar proteinsi

Entry informationi

Entry nameiCAVN2_MOUSE
AccessioniPrimary (citable) accession number: Q63918
Secondary accession number(s): Q3V1P6, Q78EC3, Q8CBT4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: January 23, 2007
Last modified: October 25, 2017
This is version 123 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families