Reviewed, UniProtKB/Swiss-Prot P19620 (ANXA2_PIG)

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

Organism

Sus scrofa (Pig)

Taxonomic identifier

9823 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

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 ATP1B1 and DYSF 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.

Ontologies

Keywords
Cellular component	Basement membrane Extracellular matrix Secreted
Domain	Annexin Repeat
Ligand	Calcium Calcium/phospholipid-binding
PTM	Acetylation Phosphoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Cellular component	basement membrane Inferred from electronic annotation. Source: UniProtKB-SubCell melanosome Inferred from electronic annotation. Source: UniProtKB-SubCell
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...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.2 Ref.3 Ref.4
	Chain	2 – 339	338	Annexin A2		PRO_0000067472
Regions
	Repeat	42 – 102	61	Annexin 1
	Repeat	114 – 174	61	Annexin 2
	Repeat	199 – 259	61	Annexin 3
	Repeat	274 – 334	61	Annexin 4
	Region	2 – 24	23	S100A10-binding site
Amino acid modifications
	Modified residue	2	1	N-acetylserine Ref.2
	Modified residue	18	1	Phosphoserine By similarity
	Modified residue	19	1	Phosphothreonine By similarity
	Modified residue	24	1	Phosphotyrosine; by SRC By similarity
	Modified residue	26	1	Phosphoserine; by PKC By similarity
	Modified residue	30	1	Phosphotyrosine By similarity
	Modified residue	104	1	N6-acetyllysine By similarity
	Modified residue	115	1	N6-acetyllysine By similarity
	Modified residue	148	1	N6-acetyllysine By similarity
	Modified residue	152	1	N6-acetyllysine By similarity
	Modified residue	157	1	N6-acetyllysine By similarity
	Modified residue	188	1	Phosphotyrosine By similarity
	Modified residue	199	1	Phosphotyrosine By similarity
	Modified residue	227	1	N6-acetyllysine By similarity
	Modified residue	238	1	Phosphotyrosine By similarity
	Modified residue	275	1	Phosphotyrosine By similarity
	Modified residue	279	1	N6-acetyllysine By similarity
	Modified residue	302	1	N6-acetyllysine By similarity
	Modified residue	313	1	N6-acetyllysine By similarity
	Modified residue	316	1	Phosphotyrosine By similarity
	Modified residue	318	1	Phosphotyrosine By similarity
Experimental info
	Sequence conflict	223	1	C → P AA sequence Ref.5
	Sequence conflict	229	1	F → S AA sequence Ref.2
	Sequence conflict	230	1	E → S AA sequence Ref.5

Sequences

	Sequence		Length	Mass (Da)
	P19620-1 [UniParc]. Last modified May 29, 2007. Version 4. Checksum: FAC554639119900D	FASTA	339	38,534
	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

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: 16263068] [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: 17607745] [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: 2456953] [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: 2973411] [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: 2937654] [Abstract] Cited for: PROTEIN SEQUENCE OF 213-234.

Web resources

Protein Spotlight

Red velvet - Issue 86 of September 2007

Cross-references

Sequence databases
EMBLGenBankDDBJ	AY706383 mRNA. Translation: AAU85387.1.
PIR	S01128.
RefSeq	NP_001005726.1.
UniGene	Ssc.12241
3D structure databases
SMR	P19620. Positions 22-339.
ModBase	Search...
Genome annotation databases
Ensembl	ENSSSCT00000005057; ENSSSCP00000004935; ENSSSCG00000004578; Sus scrofa. [Genome view]
GeneID	406192.
KEGG	ssc:406192.
Organism-specific databases
CTD	406192.
Phylogenomic databases
HOVERGEN	P19620.
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. 2 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...

Entry information

Entry name

ANXA2_PIG

Accession

Primary (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:	November 24, 2009
This is version 92 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)