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P19620 (ANXA2_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 121. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismSus scrofa (Pig) [Reference proteome]
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus

Protein attributes

Sequence length339 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 ATP1B1 and DYSF By similarity. Interacts with COCH By similarity.

Subcellular location

Secretedextracellular spaceextracellular matrixbasement 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 By similarity.

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.2 Ref.3 Ref.4
Chain2 – 339338Annexin A2
PRO_0000067472

Regions

Repeat42 – 10261Annexin 1
Repeat114 – 17461Annexin 2
Repeat199 – 25961Annexin 3
Repeat274 – 33461Annexin 4
Region2 – 2423S100A10-binding site

Amino acid modifications

Modified residue21N-acetylserine Ref.2
Modified residue241Phosphotyrosine; by SRC By similarity
Modified residue261Phosphoserine; by PKC By similarity
Modified residue491N6-acetyllysine By similarity
Modified residue1521N6-acetyllysine By similarity
Modified residue1991Phosphotyrosine By similarity
Modified residue2271N6-acetyllysine By similarity

Experimental info

Sequence conflict2231C → P AA sequence Ref.5
Sequence conflict2291F → S AA sequence Ref.2
Sequence conflict2301E → S AA sequence Ref.5

Sequences

Sequence LengthMass (Da)Tools
P19620 [UniParc].

Last modified May 29, 2007. Version 4.
Checksum: FAC554639119900D

FASTA33938,534
        10         20         30         40         50         60 
MSTVHEILCK LSLEGDHSTP ASAYGSVKAY TNFDAERDAL NIETAIKTKG VDEVTIVNIL 

        70         80         90        100        110        120 
TNRSNEQRQD IAFAYQRRTK KELASALKSA LSGHLETVIL GLLKTPAQYD ASELKASMKG 

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

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

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

       310        320        330 
LKIRSEFKRK YGKSLYNYIQ QDTKGDYQKA LLYLCGGDD 

« Hide

References

[1]"Identification of metaphase II-specific gene transcripts in porcine oocytes and their expression in early stage embryos."
Cui X.S., Song H., Kim N.H.
Reprod. Fertil. Dev. 17:625-631(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Annexin A2 / p11 interaction: new insights into annexin A2 tetramer structure by chemical cross-linking, high-resolution mass spectrometry, and computational modeling."
Schulz D.M., Kalkhof S., Schmidt A., Ihling C., Stingl C., Mechtler K., Zschoernig O., Sinz A.
Proteins 69:254-269(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-339, ACETYLATION AT SER-2.
[3]"A discontinuous epitope on p36, the major substrate of src tyrosine-protein-kinase, brings the phosphorylation site into the neighbourhood of a consensus sequence for Ca2+/lipid-binding proteins."
Johnsson N., Johnsson K., Weber K.
FEBS Lett. 236:201-204(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-70.
[4]"p36, the major cytoplasmic substrate of src tyrosine protein kinase, binds to its p11 regulatory subunit via a short amino-terminal amphiphatic helix."
Johnsson N., Marriott G., Weber K.
EMBO J. 7:2435-2442(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-30.
[5]"Binding sites for calcium, lipid and p11 on p36, the substrate of retroviral tyrosine-specific protein kinases."
Johnsson N., Vandekerckhove J., Van Damme J., Weber K.
FEBS Lett. 198:361-364(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 213-234.
+Additional computationally mapped references.

Web resources

Protein Spotlight

Red velvet - Issue 86 of September 2007

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY706383 mRNA. Translation: AAU85387.1.
PIRS01128.
RefSeqNP_001005726.1. NM_001005726.1.
UniGeneSsc.12241.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

MINTMINT-1214816.
STRING9823.ENSSSCP00000004935.

Proteomic databases

PaxDbP19620.
PRIDEP19620.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID406192.
KEGGssc:406192.

Organism-specific databases

CTD302.

Phylogenomic databases

eggNOGNOG259189.
HOGENOMHOG000158803.
HOVERGENHBG061815.
KOK17092.

Family and domain databases

Gene3D1.10.220.10. 4 hits.
InterProIPR001464. Annexin.
IPR018502. Annexin_repeat.
IPR018252. Annexin_repeat_CS.
IPR002389. AnnexinII.
[Graphical view]
PANTHERPTHR10502:SF18. PTHR10502:SF18. 1 hit.
PfamPF00191. Annexin. 4 hits.
[Graphical view]
PRINTSPR00196. ANNEXIN.
PR00198. ANNEXINII.
SMARTSM00335. ANX. 4 hits.
[Graphical view]
PROSITEPS00223. ANNEXIN. 4 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameANXA2_PIG
AccessionPrimary (citable) accession number: P19620
Secondary accession number(s): Q5Y2C7
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: May 29, 2007
Last modified: April 16, 2014
This is version 121 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Protein Spotlight

Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries