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UniProtKB - O95810 (CAVN2_HUMAN)

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Protein

Caveolae-associated protein 2

Gene

CAVIN2

Organism
Homo sapiens (Human)
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 (PubMed:19525939). 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. 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.

GO - Molecular functioni

  • phosphatidylserine binding Source: UniProtKB
  • phospholipid binding Source: ProtInc
  • protein kinase C binding Source: GO_Central
Complete GO annotation...

Keywordsi

LigandLipid-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Caveolae-associated protein 2Imported
Alternative name(s):
Cavin-2
PS-p68
Phosphatidylserine-binding protein
Serum deprivation-response protein
Gene namesi
Name:CAVIN2Imported
Synonyms:SDPRImported
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:10690. CAVIN2.

Subcellular locationi

GO - Cellular componenti

  • caveola Source: GO_Central
  • cytoplasm Source: MGI
  • cytosol Source: UniProtKB
  • membrane raft Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi86L → E: Loss of localization in caveolae; when associated with E-93 or E-100. 1 Publication1
Mutagenesisi93I → E: Loss of localization in caveolae; when associated with E-86 or E-100. 1 Publication1
Mutagenesisi100L → E: Loss of localization in caveolae; when associated with E-86 or E-93. 1 Publication1

Organism-specific databases

DisGeNETi8436.
OpenTargetsiENSG00000168497.
PharmGKBiPA35615.

Polymorphism and mutation databases

BioMutaiSDPR.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00002389182 – 425Caveolae-associated protein 2Add BLAST424

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylglycine1 Publication1
Modified residuei27PhosphoserineBy similarity1
Modified residuei35PhosphoserineCombined sources1
Modified residuei37PhosphoserineBy similarity1
Modified residuei51PhosphoserineBy similarity1
Modified residuei196PhosphothreonineCombined sources1
Modified residuei199PhosphothreonineCombined sources1
Modified residuei203PhosphoserineCombined sources1
Modified residuei204PhosphoserineCombined sources1
Modified residuei218PhosphoserineCombined sources1
Modified residuei283PhosphoserineBy similarity1
Modified residuei284PhosphoserineBy similarity1
Modified residuei287PhosphoserineCombined sources1
Modified residuei288PhosphoserineCombined sources1
Modified residuei293PhosphoserineCombined sources1
Modified residuei332PhosphoserineBy similarity1
Modified residuei341PhosphoserineBy similarity1
Modified residuei366PhosphoserineBy similarity1
Modified residuei370PhosphoserineBy similarity1
Modified residuei375PhosphothreonineBy similarity1
Modified residuei395PhosphotyrosineBy similarity1
Modified residuei403PhosphoserineBy similarity1

Post-translational modificationi

Phosphorylated on Ser residues.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiO95810.
MaxQBiO95810.
PaxDbiO95810.
PeptideAtlasiO95810.
PRIDEiO95810.
TopDownProteomicsiO95810.

2D gel databases

OGPiO95810.

PTM databases

iPTMnetiO95810.
PhosphoSitePlusiO95810.
SwissPalmiO95810.

Expressioni

Tissue specificityi

Highly expressed in heart and lung, and expressed at lower levels in brain, kidney, liver, pancreas, placenta, and skeletal muscle.1 Publication

Inductioni

Up-regulated in asyncronously growing fibroblasts following serum deprivation but not following contact inhibition. Down-regulated during synchronous cell cycle re-entry.1 Publication

Gene expression databases

BgeeiENSG00000168497.
CleanExiHS_SDPR.
GenevisibleiO95810. HS.

Organism-specific databases

HPAiHPA039325.
HPA062122.

Interactioni

Subunit structurei

Component of the CAVIN complex composed of CAVIN1, CAVIN2, CAVIN3 and CAVIN4. Binds to PRKCA in the presence of phosphatidylserine (By similarity). Interacts with CAVIN4; this augments the transactivation of NPPA by CAVIN4 (PubMed:18332105, PubMed:24567387). Interacts with CAVIN1 (PubMed:19525939, PubMed:24567387). Interacts with CAV3 (PubMed:24567387).By similarity3 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

Complete GO annotation...

Protein-protein interaction databases

BioGridi114016. 7 interactors.
DIPiDIP-56943N.
IntActiO95810. 12 interactors.
MINTiMINT-1436848.
STRINGi9606.ENSP00000305675.

Structurei

3D structure databases

ProteinModelPortaliO95810.
SMRiO95810.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 168Interaction with CAVIN1By similarityAdd BLAST167
Regioni62 – 100Leucine-zipper1 PublicationAdd BLAST39

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili61 – 82Sequence analysisAdd BLAST22
Coiled coili125 – 154Sequence analysisAdd BLAST30
Coiled coili210 – 268Sequence analysisAdd BLAST59

Domaini

The leucine-zipper domain is essential for its localization in the caveolae.1 Publication

Sequence similaritiesi

Belongs to the CAVIN family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410IEZA. Eukaryota.
ENOG410XP8W. LUCA.
GeneTreeiENSGT00530000063058.
HOGENOMiHOG000293135.
HOVERGENiHBG056807.
InParanoidiO95810.
OMAiERMDRQC.
OrthoDBiEOG091G09Y1.
PhylomeDBiO95810.
TreeFamiTF331031.

Family and domain databases

InterProiView protein in InterPro
IPR026752. Cavin_fam.
IPR033298. SDPR.
PANTHERiPTHR15240. PTHR15240. 1 hit.
PTHR15240:SF10. PTHR15240:SF10. 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.

O95810-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGEDAAQAEK FQHPGSDMRQ EKPSSPSPMP SSTPSPSLNL GNTEEAIRDN 
        60         70         80         90        100
SQVNAVTVLT LLDKLVNMLD AVQENQHKME QRQISLEGSV KGIQNDLTKL 
       110        120        130        140        150
SKYQASTSNT VSKLLEKSRK VSAHTRAVKE RMDRQCAQVK RLENNHAQLL 
       160        170        180        190        200
RRNHFKVLIF QEENEIPASV FVKQPVSGAV EGKEELPDEN KSLEETLHTV 
       210        220        230        240        250
DLSSDDDLPH DEEALEDSAE EKVEESRAEK IKRSSLKKVD SLKKAFSRQN 
       260        270        280        290        300
IEKKMNKLGT KIVSVERREK IKKSLTSNHQ KISSGKSSPF KVSPLTFGRK 
       310        320        330        340        350
KVREGESHAE NETKSEDLPS SEQMPNDQEE ESFAEGHSEA SLASALVEGE 
       360        370        380        390        400
IAEEAAEKAT SRGSNSGMDS NIDLTIVEDE EEESVALEQA QKVRYEGSYA 
       410        420 
LTSEEAERSD GDPVQPAVLQ VHQTS
Length:425
Mass (Da):47,173
Last modified:January 23, 2007 - v3
Checksum:i0631CBF4BED537F9
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_034422130E → D. Corresponds to variant dbSNP:rs35012125Ensembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF085481 mRNA. Translation: AAD17795.1.
AC098872 Genomic DNA. Translation: AAY24078.1.
BC016475 mRNA. Translation: AAH16475.1.
CCDSiCCDS2313.1.
RefSeqiNP_004648.1. NM_004657.5.
UniGeneiHs.26530.

Genome annotation databases

EnsembliENST00000304141; ENSP00000305675; ENSG00000168497.
GeneIDi8436.
KEGGihsa:8436.
UCSCiuc002utb.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.

Entry informationi

Entry nameiCAVN2_HUMAN
AccessioniPrimary (citable) accession number: O95810
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: January 23, 2007
Last modified: July 5, 2017
This is version 128 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families