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Annexin A2 (Annexin II) (Annexin-2) (Calpactin I heavy chain) (Calpactin-1 heavy chain) (Chromobindin-8) (Lipocortin II) (Placental anticoagulant protein IV) (PAP-IV) (Protein I) (p36)

 ANXA2_BOVIN             Reviewed;         339 AA.
P04272; Q3ZCC7; Q5E9B0;
01-NOV-1986, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
22-NOV-2017, entry version 166.
RecName: Full=Annexin A2;
AltName: Full=Annexin II;
AltName: Full=Annexin-2;
AltName: Full=Calpactin I heavy chain;
AltName: Full=Calpactin-1 heavy chain;
AltName: Full=Chromobindin-8;
AltName: Full=Lipocortin II;
AltName: Full=Placental anticoagulant protein IV;
Short=PAP-IV;
AltName: Full=Protein I;
AltName: Full=p36;
Name=ANXA2; Synonyms=ANX2;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Kidney;
PubMed=2945590; DOI=10.1021/bi00364a007;
Kristensen T., Saris C.J.M., Hunter T., Hicks L.J., Noonan D.J.,
Glenney J.R. Jr., Tack B.F.;
"Primary structure of bovine calpactin I heavy chain (p36), a major
cellular substrate for retroviral protein-tyrosine kinases: homology
with the human phospholipase A2 inhibitor lipocortin.";
Biochemistry 25:4497-4503(1986).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=16305752; DOI=10.1186/1471-2164-6-166;
Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
"Characterization of 954 bovine full-CDS cDNA sequences.";
BMC Genomics 6:166-166(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Crossbred X Angus; TISSUE=Ileum;
NIH - Mammalian Gene Collection (MGC) project;
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
[4]
ACETYLATION AT SER-2.
PubMed=2942542;
Glenney J.R. Jr., Boudreau M., Galyean R., Hunter T., Tack B.;
"Association of the S-100-related calpactin I light chain with the
NH2-terminal tail of the 36-kDa heavy chain.";
J. Biol. Chem. 261:10485-10488(1986).
-!- FUNCTION: 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. Inhibits PCSK9-enhanced LDLR degradation,
probably reduces PCSK9 protein levels via a translational
mechanism but also competes with LDLR for binding with PCSK9.
{ECO:0000250|UniProtKB:P07355}.
-!- SUBUNIT: 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 (By similarity).
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). {ECO:0000250|UniProtKB:A2SW69,
ECO:0000250|UniProtKB:P07355, ECO:0000250|UniProtKB:P07356,
ECO:0000250|UniProtKB:Q6TEQ7}.
-!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
matrix, basement membrane. Melanosome {ECO:0000250}. Note=In the
lamina beneath the plasma membrane.
-!- DOMAIN: A pair of annexin repeats may form one binding site for
calcium and phospholipid.
-!- PTM: ISGylated. {ECO:0000250}.
-!- MISCELLANEOUS: It may cross-link plasma membrane phospholipids
with actin and the cytoskeleton and be involved with exocytosis.
-!- SIMILARITY: Belongs to the annexin family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Protein Spotlight; Note=Red velvet - Issue 86
of September 2007;
URL="https://web.expasy.org/spotlight/back_issues/086";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; M14056; AAA30421.1; -; mRNA.
EMBL; BT021010; AAX09027.1; -; mRNA.
EMBL; BC102516; AAI02517.1; -; mRNA.
PIR; A03081; LUBO36.
RefSeq; NP_777141.1; NM_174716.1.
UniGene; Bt.4314; -.
PDB; 4X9P; X-ray; 2.01 A; A=1-339.
PDBsum; 4X9P; -.
ProteinModelPortal; P04272; -.
SMR; P04272; -.
IntAct; P04272; 1.
STRING; 9913.ENSBTAP00000012655; -.
iPTMnet; P04272; -.
PaxDb; P04272; -.
PeptideAtlas; P04272; -.
PRIDE; P04272; -.
Ensembl; ENSBTAT00000012655; ENSBTAP00000012655; ENSBTAG00000009615.
GeneID; 282689; -.
KEGG; bta:282689; -.
CTD; 302; -.
eggNOG; KOG0819; Eukaryota.
eggNOG; ENOG410XPUN; LUCA.
GeneTree; ENSGT00760000118972; -.
HOGENOM; HOG000158803; -.
HOVERGEN; HBG061815; -.
InParanoid; P04272; -.
KO; K17092; -.
OMA; FIQQDTK; -.
OrthoDB; EOG091G0H6H; -.
TreeFam; TF105452; -.
Reactome; R-BTA-6798695; Neutrophil degranulation.
Reactome; R-BTA-75205; Dissolution of Fibrin Clot.
Proteomes; UP000009136; Chromosome 10.
Bgee; ENSBTAG00000009615; -.
GO; GO:0005604; C:basement membrane; IEA:UniProtKB-SubCell.
GO; GO:0016323; C:basolateral plasma membrane; IEA:Ensembl.
GO; GO:0009986; C:cell surface; IEA:Ensembl.
GO; GO:0005913; C:cell-cell adherens junction; IEA:Ensembl.
GO; GO:0005829; C:cytosol; IDA:AgBase.
GO; GO:0005769; C:early endosome; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
GO; GO:0065010; C:extracellular membrane-bounded organelle; IDA:AgBase.
GO; GO:0019897; C:extrinsic component of plasma membrane; IEA:Ensembl.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:AgBase.
GO; GO:0031902; C:late endosome membrane; IEA:Ensembl.
GO; GO:0005811; C:lipid droplet; IEA:Ensembl.
GO; GO:0005765; C:lysosomal membrane; IEA:Ensembl.
GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; IDA:AgBase.
GO; GO:0045121; C:membrane raft; IEA:Ensembl.
GO; GO:0030496; C:midbody; IEA:Ensembl.
GO; GO:0035749; C:myelin sheath adaxonal region; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IDA:AgBase.
GO; GO:1990667; C:PCSK9-AnxA2 complex; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; TAS:AgBase.
GO; GO:0042383; C:sarcolemma; IEA:Ensembl.
GO; GO:0043220; C:Schmidt-Lanterman incisure; IEA:Ensembl.
GO; GO:0031982; C:vesicle; IDA:AgBase.
GO; GO:0098641; F:cadherin binding involved in cell-cell adhesion; IEA:Ensembl.
GO; GO:0005262; F:calcium channel activity; IMP:AgBase.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0005544; F:calcium-dependent phospholipid binding; IEA:UniProtKB-KW.
GO; GO:0048306; F:calcium-dependent protein binding; IEA:Ensembl.
GO; GO:0008092; F:cytoskeletal protein binding; IEA:InterPro.
GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IEA:Ensembl.
GO; GO:0001786; F:phosphatidylserine binding; IPI:AgBase.
GO; GO:0019834; F:phospholipase A2 inhibitor activity; IEA:Ensembl.
GO; GO:0002020; F:protease binding; IEA:Ensembl.
GO; GO:0003723; F:RNA binding; IEA:Ensembl.
GO; GO:0044548; F:S100 protein binding; IEA:Ensembl.
GO; GO:0001525; P:angiogenesis; IEA:Ensembl.
GO; GO:0031214; P:biomineral tissue development; IDA:AgBase.
GO; GO:0070509; P:calcium ion import; IMP:AgBase.
GO; GO:0070588; P:calcium ion transmembrane transport; IDA:AgBase.
GO; GO:0052362; P:catabolism by host of symbiont protein; IEA:Ensembl.
GO; GO:0030199; P:collagen fibril organization; IEA:Ensembl.
GO; GO:0042730; P:fibrinolysis; IEA:Ensembl.
GO; GO:0001765; P:membrane raft assembly; IEA:Ensembl.
GO; GO:0052405; P:negative regulation by host of symbiont molecular function; IEA:Ensembl.
GO; GO:0044147; P:negative regulation of development of symbiont involved in interaction with host; IEA:Ensembl.
GO; GO:0032804; P:negative regulation of low-density lipoprotein particle receptor catabolic process; IEA:Ensembl.
GO; GO:0036035; P:osteoclast development; IEA:Ensembl.
GO; GO:1905581; P:positive regulation of low-density lipoprotein particle clearance; IEA:Ensembl.
GO; GO:1905597; P:positive regulation of low-density lipoprotein particle receptor binding; IEA:Ensembl.
GO; GO:1905599; P:positive regulation of low-density lipoprotein receptor activity; IEA:Ensembl.
GO; GO:0001921; P:positive regulation of receptor recycling; IEA:Ensembl.
GO; GO:1905602; P:positive regulation of receptor-mediated endocytosis involved in cholesterol transport; IEA:Ensembl.
GO; GO:0044090; P:positive regulation of vacuole organization; IEA:Ensembl.
GO; GO:0031340; P:positive regulation of vesicle fusion; IEA:Ensembl.
GO; GO:0051290; P:protein heterotetramerization; IEA:Ensembl.
GO; GO:0006900; P:vesicle budding from membrane; IEA:Ensembl.
Gene3D; 1.10.220.10; -; 4.
InterPro; IPR001464; Annexin.
InterPro; IPR018502; Annexin_repeat.
InterPro; IPR018252; Annexin_repeat_CS.
InterPro; IPR037104; Annexin_sf.
InterPro; IPR002389; ANX2.
PANTHER; PTHR10502:SF18; PTHR10502:SF18; 1.
Pfam; PF00191; Annexin; 4.
PRINTS; PR00196; ANNEXIN.
PRINTS; PR00198; ANNEXINII.
SMART; SM00335; ANX; 4.
PROSITE; PS00223; ANNEXIN; 4.
1: Evidence at protein level;
3D-structure; Acetylation; Annexin; Basement membrane; Calcium;
Calcium/phospholipid-binding; Complete proteome; Extracellular matrix;
Isopeptide bond; Phosphoprotein; Reference proteome; Repeat; Secreted;
Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:2942542}.
CHAIN 2 339 Annexin A2.
/FTId=PRO_0000067469.
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. {ECO:0000255}.
MOD_RES 2 2 N-acetylserine.
{ECO:0000269|PubMed:2942542}.
MOD_RES 24 24 Phosphotyrosine; by SRC.
{ECO:0000250|UniProtKB:P07355}.
MOD_RES 26 26 Phosphoserine; by PKC.
{ECO:0000250|UniProtKB:P07355}.
MOD_RES 49 49 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P07356}.
MOD_RES 152 152 N6-acetyllysine.
{ECO:0000250|UniProtKB:P07356}.
MOD_RES 184 184 Phosphoserine.
{ECO:0000250|UniProtKB:P07355}.
MOD_RES 199 199 Phosphotyrosine.
{ECO:0000250|UniProtKB:P07356}.
MOD_RES 227 227 N6-acetyllysine.
{ECO:0000250|UniProtKB:P07356}.
CROSSLNK 49 49 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate.
{ECO:0000250|UniProtKB:P07355}.
CROSSLNK 49 49 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P07355}.
CONFLICT 149 149 E -> G (in Ref. 3; AAI02517).
{ECO:0000305}.
HELIX 35 47 {ECO:0000244|PDB:4X9P}.
HELIX 53 60 {ECO:0000244|PDB:4X9P}.
HELIX 65 79 {ECO:0000244|PDB:4X9P}.
HELIX 83 90 {ECO:0000244|PDB:4X9P}.
HELIX 93 103 {ECO:0000244|PDB:4X9P}.
HELIX 106 117 {ECO:0000244|PDB:4X9P}.
HELIX 125 133 {ECO:0000244|PDB:4X9P}.
HELIX 137 151 {ECO:0000244|PDB:4X9P}.
HELIX 155 162 {ECO:0000244|PDB:4X9P}.
HELIX 165 175 {ECO:0000244|PDB:4X9P}.
HELIX 188 200 {ECO:0000244|PDB:4X9P}.
TURN 201 204 {ECO:0000244|PDB:4X9P}.
STRAND 205 207 {ECO:0000244|PDB:4X9P}.
HELIX 210 219 {ECO:0000244|PDB:4X9P}.
HELIX 222 235 {ECO:0000244|PDB:4X9P}.
HELIX 240 247 {ECO:0000244|PDB:4X9P}.
HELIX 250 264 {ECO:0000244|PDB:4X9P}.
HELIX 266 278 {ECO:0000244|PDB:4X9P}.
STRAND 279 282 {ECO:0000244|PDB:4X9P}.
HELIX 285 295 {ECO:0000244|PDB:4X9P}.
TURN 296 299 {ECO:0000244|PDB:4X9P}.
HELIX 300 311 {ECO:0000244|PDB:4X9P}.
HELIX 315 322 {ECO:0000244|PDB:4X9P}.
HELIX 325 335 {ECO:0000244|PDB:4X9P}.
SEQUENCE 339 AA; 38612 MW; AA8E2500F4138B3D CRC64;
MSTVHEILCK LSLEGDHSTP PSAYGSVKAY TNFDAERDAL NIETAIKTKG VDEVTIVNIL
TNRSNEQRQD IAFAYQRRTK KELASALKSA LSGHLETVIL GLLKTPAQYD ASELKASMKG
LGTDEDSLIE IICSRTNQEL QEINRVYKEM YKTDLEKDIV SDTSGDFRKL MVALAKGRRA
EDGSVIDYEL IDQDARDLYD AGVKRKGTDV PKWISIMTER SVCHLQKVFE RYKSYSPYDM
LESIKKEVKG DLENAFLNLV QCIQNKPLYF ADRLYDSMKG KGTRDKVLIR IMVSRSEVDM
LKIRSEFKKK YGKSLYYYIQ QDTKGDYQKA LLYLCGGDD


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