Annexin A2 - Mus musculus (Mouse)

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P07356 (ANXA2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 136. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

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 names

Name:	Anxa2
Synonyms:	Anx2, Cal1h

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	339 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Calcium-regulated membrane-binding protein whose affinity for calcium is greatly enhanced by anionic phospholipids. It binds two calcium ions with high affinity.
Subunit structure	Heterotetramer containing 2 light chains of S100A10/p11 and 2 heavy chains of ANXA2/p36. Interacts with DYSF. Interacts with ATP1B1 By similarity. Interacts with COCH By similarity. Ref.5
Subcellular location	Secreted › extracellular space › extracellular matrix › basement membrane. Melanosome By similarity. Note: In the lamina beneath the plasma membrane.
Domain	A pair of annexin repeats may form one binding site for calcium and phospholipid.
Post-translational modification	ISGylated. Ref.6
Miscellaneous	It may cross-link plasma membrane phospholipids with actin and the cytoskeleton and be involved with exocytosis.
Sequence similarities	Belongs to the annexin family. Contains 4 annexin repeats.

Ontologies

Keywords
Cellular component	Basement membrane Extracellular matrix Secreted
Domain	Annexin Repeat
Ligand	Calcium Calcium/phospholipid-binding
PTM	Acetylation Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	angiogenesis Inferred from mutant phenotype PubMed 14702107. Source: MGI body fluid secretion Inferred from electronic annotation. Source: Compara cellular response to acid Inferred from direct assay PubMed 17690254. Source: MGI collagen fibril organization Inferred from mutant phenotype PubMed 14702107. Source: MGI fibrinolysis Inferred from mutant phenotype PubMed 14702107. Source: MGI positive regulation of binding Inferred from mutant phenotype PubMed 17690254. Source: MGI positive regulation of vesicle fusion Inferred from electronic annotation. Source: Compara
Cellular_component	Schmidt-Lanterman incisure Inferred from direct assay PubMed 20237282. Source: BHF-UCL basement membrane Inferred from electronic annotation. Source: UniProtKB-SubCell early endosome Inferred from direct assay PubMed 15078881. Source: MGI extrinsic to plasma membrane Inferred from direct assay PubMed 17690254. Source: MGI lipid particle Inferred from electronic annotation. Source: Compara melanosome Inferred from electronic annotation. Source: UniProtKB-SubCell midbody Inferred from electronic annotation. Source: Compara myelin sheath adaxonal region Inferred from direct assay PubMed 20237282. Source: BHF-UCL perinuclear region of cytoplasm Inferred from electronic annotation. Source: Compara protein complex Inferred from electronic annotation. Source: Compara sarcolemma Inferred from direct assay Ref.5. Source: MGI
Molecular_function	calcium ion binding Inferred from electronic annotation. Source: InterPro calcium-dependent phospholipid binding Inferred from electronic annotation. Source: UniProtKB-KW phosphatidylinositol-4,5-bisphosphate binding Inferred from electronic annotation. Source: Compara phospholipase inhibitor activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed By similarity

Chain

2 – 339

338

Annexin A2

PRO_0000067471

Regions

Repeat

42 – 102

Annexin 1

Repeat

114 – 174

Annexin 2

Repeat

199 – 259

Annexin 3

Repeat

274 – 334

Annexin 4

Region

2 – 24

S100A10-binding site Potential

Amino acid modifications

Modified residue

N-acetylserine By similarity

Modified residue

Phosphotyrosine; by SRC By similarity

Modified residue

Phosphoserine; by PKC By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

P07356 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 4407E572097FB2C0
Show »

FASTA

339

38,676

        10         20         30         40         50         60 
MSTVHEILCK LSLEGDHSTP PSAYGSVKPY TNFDAERDAL NIETAVKTKG VDEVTIVNIL 

        70         80         90        100        110        120 
TNRSNVQRQD IAFAYQRRTK KELPSALKSA LSGHLETVIL GLLKTPAQYD ASELKASMKG 

       130        140        150        160        170        180 
LGTDEDSLIE IICSRTNQEL QEINRVYKEM YKTDLEKDII SDTSGDFRKL MVALAKGRRA 

       190        200        210        220        230        240 
EDGSVIDYEL IDQDARELYD AGVKRKGTDV PKWISIMTER SVCHLQKVFE RYKSYSPYDM 

       250        260        270        280        290        300 
LESIKKEVKG DLENAFLNLV QCIQNKPLYF ADRLYDSMKG KGTRDKVLIR IMVSRSEVDM 

       310        320        330 
LKIRSEFKRK YGKSLYYYIQ QDTKGDYQKA LLYLCGGDD

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The cDNA sequence for the protein-tyrosine kinase substrate p36 (calpactin I heavy chain) reveals a multidomain protein with internal repeats." Saris C.J.M., Tack B.F., Kristensen T., Glenney J.R. Jr., Hunter T. Cell 46:201-212(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]	"Structure and chromosome assignment of the murine p36 (calpactin I heavy chain) gene." Amiguet P., D'Eustachio P., Kristensen T., Wetsel R.A., Saris C.J.M., Hunter T., Chaplin D.D., Tack B.F. Biochemistry 29:1226-1232(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-16 AND 322-339.
[4]	"Complete structure of the murine p36 (annexin II) gene. Identification of mRNAs for both the murine and the human gene with alternatively spliced 5' noncoding exons." Fey M.F., Moffat G.J., Vik D.P., Meisenhelder J., Saris C.J., Hunter T., Tack B.F. Biochim. Biophys. Acta 1306:160-170(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-16.
[5]	"Dysferlin interacts with annexins A1 and A2 and mediates sarcolemmal wound-healing." Lennon N.J., Kho A., Bacskai B.J., Perlmutter S.L., Hyman B.T., Brown R.H. Jr. J. Biol. Chem. 278:50466-50473(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH DYSF.
[6]	"Proteomic identification of proteins conjugated to ISG15 in mouse and human cells." Giannakopoulos N.V., Luo J.K., Papov V., Zou W., Lenschow D.J., Jacobs B.S., Borden E.C., Li J., Virgin H.W., Zhang D.E. Biochem. Biophys. Res. Commun. 336:496-506(2005) [PubMed] [Europe PMC] [Abstract] Cited for: ISGYLATION.
+	Additional computationally mapped references.

Web resources

Protein Spotlight

Red velvet - Issue 86 of September 2007

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00468203.

PIR

LUMS36. A23943.

RefSeq

NP_031611.1. NM_007585.3.

UniGene

Mm.238343.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
4HRE	X-ray	2.79	A/B/C/D	1-339	[»]

ProteinModelPortal

P07356.

SMR

P07356. Positions 32-339.

ModBase

Search...

Protein-protein interaction databases

IntAct

P07356. 4 interactions.

MINT

MINT-274998.

Protein family/group databases

TCDB

9.A.48.1.1. unconventional protein secretion (UPS) system.

PTM databases

PhosphoSite

P07356.

2D gel databases

REPRODUCTION-2DPAGE

IPI00468203.
P07356.

SWISS-2DPAGE

P07356.

Proteomic databases

PaxDb

P07356.

PRIDE

P07356.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000034756; ENSMUSP00000034756; ENSMUSG00000032231.

GeneID

12306.

KEGG

mmu:12306.

Organism-specific databases

CTD

302.

MGI

MGI:88246. Anxa2.

Phylogenomic databases

eggNOG

NOG259189.

HOGENOM

HOG000158803.

HOVERGEN

HBG061815.

InParanoid

P07356.

OMA

FIQQDTK.

OrthoDB

EOG4KD6MM.

Gene expression databases

ArrayExpress

P07356.

Bgee

P07356.

CleanEx

MM_ANXA2.

Genevestigator

P07356.

GermOnline

ENSMUSG00000032231. Mus musculus.

Family and domain databases

Gene3D

1.10.220.10. 4 hits.

InterPro

IPR001464. Annexin.
IPR018502. Annexin_repeat.
IPR018252. Annexin_repeat_CS.
IPR002389. AnnexinII.
[Graphical view]

PANTHER

PTHR10502. PTHR10502. 1 hit.
PTHR10502:SF18. PTHR10502:SF18. 1 hit.

Pfam

PF00191. Annexin. 4 hits.
[Graphical view]

PRINTS

PR00196. ANNEXIN.
PR00198. ANNEXINII.

SMART

SM00335. ANX. 4 hits.
[Graphical view]

SUPFAM

SSF47874. Annexin. 1 hit.

PROSITE

PS00223. ANNEXIN. 4 hits.
[Graphical view]

ProtoNet

Search...

Other

NextBio

280840.

SOURCE

Search...

Entry information

Entry name

ANXA2_MOUSE

Accession

Primary (citable) accession number: P07356

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1988
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 136 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Protein Spotlight

Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Sequences

References

Web resources

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

PTM databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents