Annexin A2 - Mus musculus (Mouse)

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Reviewed, UniProtKB/Swiss-Prot P07356 (ANXA2_MOUSE)

Last modified December 15, 2009. Version 108. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Annexin A2
Alternative name(s):
    Annexin-2
    Annexin II
    Lipocortin II
    Calpactin I heavy chain
    Chromobindin-8
    p36
    Protein I
    Placental anticoagulant protein IV
      Short name=PAP-IV

Gene names

Name:	Anxa2
Synonyms:	Anx2, Cal1h

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

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

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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.

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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.
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.
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.

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Ontologies

Keywords
Cellular component	Basement membrane Extracellular matrix Secreted
Domain	Annexin Repeat
Ligand	Calcium Calcium/phospholipid-binding
PTM	Acetylation Phosphoprotein
Gene Ontology (GO)
Biological process	angiogenesis Inferred from mutant phenotype. Source: MGI collagen fibril organization Inferred from mutant phenotype. Source: MGI fibrinolysis Inferred from mutant phenotype. Source: MGI
Cellular component	basement membrane Inferred from electronic annotation. Source: UniProtKB-SubCell early endosome Inferred from direct assay. Source: MGI melanosome Inferred from electronic annotation. Source: UniProtKB-SubCell sarcolemma Ref.5 Inferred from direct assay. Source: MGI
Molecular function	calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW calcium-dependent phospholipid binding Inferred from electronic annotation. Source: UniProtKB-KW cytoskeletal protein binding Inferred from electronic annotation. Source: InterPro phospholipase inhibitor activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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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

Phosphoserine By similarity

Modified residue

Phosphothreonine By similarity

Modified residue

Phosphotyrosine; by SRC Ref.6

Modified residue

Phosphoserine; by PKC By similarity

Modified residue

Phosphotyrosine By similarity

Modified residue

104

N6-acetyllysine By similarity

Modified residue

115

N6-acetyllysine By similarity

Modified residue

148

N6-acetyllysine By similarity

Modified residue

152

N6-acetyllysine By similarity

Modified residue

157

N6-acetyllysine By similarity

Modified residue

188

Phosphotyrosine Ref.6

Modified residue

199

Phosphotyrosine By similarity

Modified residue

227

N6-acetyllysine By similarity

Modified residue

238

Phosphotyrosine By similarity

Modified residue

275

Phosphotyrosine By similarity

Modified residue

279

N6-acetyllysine By similarity

Modified residue

302

N6-acetyllysine By similarity

Modified residue

313

N6-acetyllysine By similarity

Modified residue

316

Phosphotyrosine By similarity

Modified residue

317

Phosphotyrosine By similarity

Modified residue

318

Phosphotyrosine By similarity

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Sequences

Sequence

Length

Mass (Da)

Tools

P07356-1 [UniParc].

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

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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: 3013423] [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: 15489334] [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: 2138915] [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: 8634333] [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: 14506282] [Abstract] Cited for: INTERACTION WITH DYSF.
[6]	"Multiple reaction monitoring for robust quantitative proteomic analysis of cellular signaling networks." Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M. Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007) [PubMed: 17389395] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-24 AND TYR-188, MASS SPECTROMETRY.
+	Additional computationally mapped references.

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Web resources

Protein Spotlight

Red velvet - Issue 86 of September 2007

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Cross-references

Sequence databases
	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.
UniGene	Mm.238343
3D structure databases
SMR	P07356. Positions 21-339.
ModBase	Search...
Protein-protein interaction databases
IntAct	P07356. 2 interactions.
STRING	P07356.
Protein family/group databases
TCDB	9.A.48.1.1. unconventional protein secretion (UPS) system.
PTM databases
PhosphoSite	P07356.
2-D gel databases
SWISS-2DPAGE	P07356.
REPRODUCTION-2DPAGE	P07356.
Proteomic databases
PRIDE	P07356.
Genome annotation databases
Ensembl	ENSMUST00000034756; ENSMUSP00000034756; ENSMUSG00000032231; Mus musculus. [Genome view]
GeneID	12306.
KEGG	mmu:12306.
UCSC	uc009qng.1. mouse.
Organism-specific databases
CTD	12306.
MGI	MGI:88246. Anxa2.
Phylogenomic databases
HOGENOM	HBG745057.
HOVERGEN	P07356.
InParanoid	P07356.
OMA	CHLQKVF.
OrthoDB	EOG9B2WHD.
Gene expression databases
ArrayExpress	P07356.
Bgee	P07356.
CleanEx	MM_ANXA2.
Genevestigator	P07356.
GermOnline	ENSMUSG00000032231. Mus musculus.
Family and domain databases
InterPro	IPR001464. Annexin. IPR018502. Annexin_repeat. IPR018252. Annexin_repeat_CS. IPR002389. AnnexinII. [Graphical view]
Gene3D	G3DSA:1.10.220.10. Annexin. 4 hits.
PANTHER	PTHR10502. Annexin. 1 hit. PTHR10502:SF18. AnnexinII. 1 hit.
Pfam	PF00191. Annexin. 4 hits. [Graphical view]
PRINTS	PR00196. ANNEXIN. PR00198. ANNEXINII.
SMART	SM00335. ANX. 4 hits. [Graphical view]
PROSITE	PS00223. ANNEXIN. 4 hits. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	280840.
SOURCE	Search...

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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:	December 15, 2009
This is version 108 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

MGD cross-references

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

Protein Spotlight

Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries

SIMILARITY comments

Index of protein domains and families

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

2-D gel databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents