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Protein

Annexin A2

Gene

Anxa2

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

Functioni

Calcium-regulated membrane-binding protein whose affinity for calcium is greatly enhanced by anionic phospholipids. It binds two calcium ions with high affinity. May be involved in heat-stress response (By similarity). Inhibits PCSK9-enhanced LDLR degradation, probably reduces PCSK9 protein levels via a translational mechanism but also competes with LDLR for binding with PCSK9 (PubMed:22848640).By similarity1 Publication

Miscellaneous

It may cross-link plasma membrane phospholipids with actin and the cytoskeleton and be involved with exocytosis.

GO - Molecular functioni

GO - Biological processi

  • angiogenesis Source: MGI
  • body fluid secretion Source: MGI
  • catabolism by host of symbiont protein Source: MGI
  • collagen fibril organization Source: MGI
  • fibrinolysis Source: MGI
  • membrane raft assembly Source: MGI
  • negative regulation by host of symbiont molecular function Source: MGI
  • negative regulation of development of symbiont involved in interaction with host Source: MGI
  • negative regulation of low-density lipoprotein particle receptor catabolic process Source: BHF-UCL
  • osteoclast development Source: MGI
  • positive regulation of binding Source: MGI
  • positive regulation of fibroblast proliferation Source: MGI
  • positive regulation of low-density lipoprotein particle clearance Source: BHF-UCL
  • positive regulation of low-density lipoprotein particle receptor binding Source: BHF-UCL
  • positive regulation of low-density lipoprotein receptor activity Source: BHF-UCL
  • positive regulation of protein phosphorylation Source: MGI
  • positive regulation of receptor-mediated endocytosis involved in cholesterol transport Source: BHF-UCL
  • positive regulation of receptor recycling Source: BHF-UCL
  • positive regulation of vacuole organization Source: MGI
  • positive regulation of vesicle fusion Source: MGI
  • protein heterotetramerization Source: MGI
  • protein localization to plasma membrane Source: MGI
  • response to thyroid hormone Source: Ensembl
  • vesicle budding from membrane Source: MGI

Keywordsi

LigandCalcium, Calcium/phospholipid-binding

Enzyme and pathway databases

ReactomeiR-MMU-6798695 Neutrophil degranulation
R-MMU-75205 Dissolution of Fibrin Clot

Protein family/group databases

TCDBi9.A.48.1.1 the unconventional protein secretion (ups) system

Names & Taxonomyi

Protein namesi
Recommended name:
Annexin A2
Alternative name(s):
Annexin II
Annexin-2
Calpactin I heavy chain
Calpactin-1 heavy chain
Chromobindin-8
Lipocortin II
Placental anticoagulant protein IV
Short name:
PAP-IV
Protein I
p36
Gene namesi
Name:Anxa2
Synonyms:Anx2, Cal1h
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:88246 Anxa2

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

Basement membrane, Extracellular matrix, Secreted

Pathology & Biotechi

Disruption phenotypei

Animals show a 40% increase of LDL-cholesterol levels in plasma.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000674712 – 339Annexin A2Add BLAST338

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineBy similarity1
Modified residuei24Phosphotyrosine; by SRCBy similarity1
Modified residuei26Phosphoserine; by PKCBy similarity1
Modified residuei49N6-acetyllysine; alternateCombined sources1
Cross-linki49Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateBy similarity
Cross-linki49Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei152N6-acetyllysineCombined sources1
Modified residuei184PhosphoserineBy similarity1
Modified residuei199PhosphotyrosineCombined sources1
Modified residuei227N6-acetyllysineCombined sources1

Post-translational modificationi

ISGylated.1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP07356
PaxDbiP07356
PeptideAtlasiP07356
PRIDEiP07356

2D gel databases

REPRODUCTION-2DPAGEiIPI00468203
P07356
SWISS-2DPAGEiP07356

PTM databases

iPTMnetiP07356
PhosphoSitePlusiP07356
SwissPalmiP07356

Expressioni

Gene expression databases

BgeeiENSMUSG00000032231
CleanExiMM_ANXA2
ExpressionAtlasiP07356 baseline and differential
GenevisibleiP07356 MM

Interactioni

Subunit structurei

Heterotetramer containing 2 light chains of S100A10/p11 and 2 heavy chains of ANXA2/p36 (By similarity). Interacts with ATP1B1 (By similarity). Interacts with DYSF (PubMed:14506282). Interacts with COCH. Interacts (via repeat Annexin 1) with PCSK9 (via the C-terminal domain); the interaction inhibits the degradation of LDLR. Interacts with CEACAM1 (via the cytoplasmic domain); this interaction is regulated by phosphorylation of CEACAM1 (By similarity).By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
S100a10P082072EBI-738510,EBI-643986

GO - Molecular functioni

Protein-protein interaction databases

BioGridi198448, 23 interactors
ComplexPortaliCPX-141 ANXA2-PCSK9 complex
CPX-898 Annexin A2 - S100-A10 complex
CPX-899 SMARCA3 - Annexin A2 - S100-A10 complex
CPX-905 AHNAK - Annexin A2 - S100-A10 complex
CORUMiP07356
IntActiP07356, 18 interactors
MINTiP07356
STRINGi10090.ENSMUSP00000034756

Structurei

Secondary structure

1339
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi4 – 8Combined sources5
Helixi35 – 46Combined sources12
Helixi53 – 61Combined sources9
Helixi65 – 79Combined sources15
Helixi83 – 90Combined sources8
Helixi93 – 103Combined sources11
Helixi106 – 118Combined sources13
Helixi125 – 134Combined sources10
Helixi137 – 151Combined sources15
Helixi155 – 162Combined sources8
Helixi165 – 175Combined sources11
Helixi188 – 201Combined sources14
Beta strandi204 – 207Combined sources4
Helixi210 – 219Combined sources10
Helixi222 – 235Combined sources14
Helixi240 – 247Combined sources8
Helixi251 – 264Combined sources14
Helixi266 – 278Combined sources13
Beta strandi279 – 282Combined sources4
Helixi285 – 294Combined sources10
Turni296 – 299Combined sources4
Helixi300 – 311Combined sources12
Helixi315 – 322Combined sources8
Helixi325 – 335Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4HREX-ray2.79A/B/C/D1-339[»]
ProteinModelPortaliP07356
SMRiP07356
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati42 – 102Annexin 1Add BLAST61
Repeati114 – 174Annexin 2Add BLAST61
Repeati199 – 259Annexin 3Add BLAST61
Repeati274 – 334Annexin 4Add BLAST61

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 24S100A10-binding siteSequence analysisAdd BLAST23

Domaini

A pair of annexin repeats may form one binding site for calcium and phospholipid.

Sequence similaritiesi

Belongs to the annexin family.Curated

Keywords - Domaini

Annexin, Repeat

Phylogenomic databases

eggNOGiKOG0819 Eukaryota
ENOG410XPUN LUCA
GeneTreeiENSGT00760000118972
HOGENOMiHOG000158803
HOVERGENiHBG061815
InParanoidiP07356
KOiK17092
OMAiFIQQDTK
OrthoDBiEOG091G0H6H
PhylomeDBiP07356
TreeFamiTF105452

Family and domain databases

Gene3Di1.10.220.10, 4 hits
InterProiView protein in InterPro
IPR001464 Annexin
IPR018502 Annexin_repeat
IPR018252 Annexin_repeat_CS
IPR037104 Annexin_sf
IPR002389 ANX2
PANTHERiPTHR10502:SF18 PTHR10502:SF18, 1 hit
PfamiView protein in Pfam
PF00191 Annexin, 4 hits
PRINTSiPR00196 ANNEXIN
PR00198 ANNEXINII
SMARTiView protein in SMART
SM00335 ANX, 4 hits
PROSITEiView protein in PROSITE
PS00223 ANNEXIN, 4 hits

Sequencei

Sequence statusi: Complete.

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

P07356-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTVHEILCK LSLEGDHSTP PSAYGSVKPY TNFDAERDAL NIETAVKTKG
60 70 80 90 100
VDEVTIVNIL TNRSNVQRQD IAFAYQRRTK KELPSALKSA LSGHLETVIL
110 120 130 140 150
GLLKTPAQYD ASELKASMKG LGTDEDSLIE IICSRTNQEL QEINRVYKEM
160 170 180 190 200
YKTDLEKDII SDTSGDFRKL MVALAKGRRA EDGSVIDYEL IDQDARELYD
210 220 230 240 250
AGVKRKGTDV PKWISIMTER SVCHLQKVFE RYKSYSPYDM LESIKKEVKG
260 270 280 290 300
DLENAFLNLV QCIQNKPLYF ADRLYDSMKG KGTRDKVLIR IMVSRSEVDM
310 320 330
LKIRSEFKRK YGKSLYYYIQ QDTKGDYQKA LLYLCGGDD
Length:339
Mass (Da):38,676
Last modified:January 23, 2007 - v2
Checksum:i4407E572097FB2C0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M14044 mRNA Translation: AAA37360.1
BC003327 mRNA Translation: AAH03327.1
BC005763 mRNA Translation: AAH05763.1
M33321 Genomic DNA Translation: AAA37361.1
M33322 Genomic DNA Translation: AAA37362.1
D10024 mRNA Translation: BAA00914.1
S82177 Genomic DNA No translation available.
CCDSiCCDS23316.1
PIRiA23943 LUMS36
RefSeqiNP_031611.1, NM_007585.3
XP_006510859.1, XM_006510796.2
UniGeneiMm.238343

Genome annotation databases

EnsembliENSMUST00000034756; ENSMUSP00000034756; ENSMUSG00000032231
GeneIDi12306
KEGGimmu:12306
UCSCiuc009qng.1 mouse

Similar proteinsi

Entry informationi

Entry nameiANXA2_MOUSE
AccessioniPrimary (citable) accession number: P07356
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: January 23, 2007
Last modified: June 20, 2018
This is version 191 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

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