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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_CHICK             Reviewed;         339 AA.
P17785;
01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
16-JAN-2019, entry version 157.
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;
Gallus gallus (Chicken).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes;
Phasianidae; Phasianinae; Gallus.
NCBI_TaxID=9031;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2143014; DOI=10.1093/nar/18.14.4246;
Gerke V., Koch W.;
"The cDNA sequence of chicken annexin II.";
Nucleic Acids Res. 18:4246-4246(1990).
[2]
PROTEIN SEQUENCE OF 2-70.
PubMed=2456953; DOI=10.1016/0014-5793(88)80314-4;
Johnsson N., Johnsson K., Weber K.;
"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.";
FEBS Lett. 236:201-204(1988).
[3]
PROTEIN SEQUENCE OF 2-30, AND ACETYLATION AT SER-2.
PubMed=2973411;
Johnsson N., Marriott G., Weber K.;
"p36, the major cytoplasmic substrate of src tyrosine protein kinase,
binds to its p11 regulatory subunit via a short amino-terminal
amphiphatic helix.";
EMBO J. 7:2435-2442(1988).
[4]
PROTEIN SEQUENCE OF 2-63; 69-77 AND 314-324, CLEAVAGE OF INITIATOR
METHIONINE, ACETYLATION AT SER-2, AND IDENTIFICATION BY MASS
SPECTROMETRY.
TISSUE=B-cell lymphoma;
Bienvenut W.V., Black E.J., Gillespie D.A.;
Submitted (JAN-2007) to UniProtKB.
-!- 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: Heterotetramer containing 2 light chains of S100A10/p11
and 2 heavy chains of ANXA2/p36.
-!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
matrix, basement membrane. 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.
-!- 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";
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
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EMBL; X53334; CAA37421.1; -; mRNA.
PIR; S10501; LUCH2.
RefSeq; NP_990682.1; NM_205351.1.
RefSeq; XP_015134249.1; XM_015278763.1.
UniGene; Gga.3641; -.
UniGene; Gga.56016; -.
PDB; 1BT6; X-ray; 2.40 A; C/D=2-14.
PDBsum; 1BT6; -.
ProteinModelPortal; P17785; -.
SMR; P17785; -.
STRING; 9031.ENSGALP00000038695; -.
iPTMnet; P17785; -.
PaxDb; P17785; -.
PRIDE; P17785; -.
Ensembl; ENSGALT00000005981; ENSGALP00000005971; ENSGALG00000003770.
Ensembl; ENSGALT00000050124; ENSGALP00000048954; ENSGALG00000003770.
Ensembl; ENSGALT00000083426; ENSGALP00000060891; ENSGALG00000003770.
Ensembl; ENSGALT00000085466; ENSGALP00000063929; ENSGALG00000003770.
Ensembl; ENSGALT00000089656; ENSGALP00000059946; ENSGALG00000003770.
GeneID; 396297; -.
KEGG; gga:396297; -.
CTD; 302; -.
eggNOG; KOG0819; Eukaryota.
eggNOG; ENOG410XPUN; LUCA.
GeneTree; ENSGT00940000154257; -.
HOGENOM; HOG000158803; -.
HOVERGEN; HBG061815; -.
InParanoid; P17785; -.
KO; K17092; -.
OMA; LVECFEN; -.
OrthoDB; 856254at2759; -.
PhylomeDB; P17785; -.
TreeFam; TF105452; -.
Reactome; R-GGA-6798695; Neutrophil degranulation.
Reactome; R-GGA-75205; Dissolution of Fibrin Clot.
EvolutionaryTrace; P17785; -.
PRO; PR:P17785; -.
Proteomes; UP000000539; Chromosome 10.
Bgee; ENSGALG00000003770; Expressed in 11 organ(s), highest expression level in female gonad.
ExpressionAtlas; P17785; baseline and differential.
GO; GO:0005604; C:basement membrane; IEA:UniProtKB-SubCell.
GO; GO:0016323; C:basolateral plasma membrane; IEA:Ensembl.
GO; GO:0034704; C:calcium channel complex; TAS:AgBase.
GO; GO:0009986; C:cell surface; IEA:Ensembl.
GO; GO:0062023; C:collagen-containing extracellular matrix; IDA:AgBase.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; IEA:Ensembl.
GO; GO:0005769; C:early endosome; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
GO; GO:0005615; C:extracellular space; IBA:GO_Central.
GO; GO:0019897; C:extrinsic component of plasma membrane; IEA:Ensembl.
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: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; IBA:GO_Central.
GO; GO:1990667; C:PCSK9-AnxA2 complex; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; IDA:AgBase.
GO; GO:0032991; C:protein-containing complex; IDA: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:0044730; F:bone sialoprotein binding; IBA:GO_Central.
GO; GO:0005262; F:calcium channel activity; IBA:GO_Central.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0005544; F:calcium-dependent phospholipid binding; IBA:GO_Central.
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; IBA:GO_Central.
GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IBA:GO_Central.
GO; GO:0001786; F:phosphatidylserine binding; IBA:GO_Central.
GO; GO:0019834; F:phospholipase A2 inhibitor activity; IBA:GO_Central.
GO; GO:0002020; F:protease binding; IBA:GO_Central.
GO; GO:0017137; F:Rab GTPase binding; IBA:GO_Central.
GO; GO:0044548; F:S100 protein binding; IBA:GO_Central.
GO; GO:0046790; F:virion binding; IDA:AgBase.
GO; GO:0099511; F:voltage-gated calcium channel activity involved in regulation of cytosolic calcium levels; IDA:AgBase.
GO; GO:0001525; P:angiogenesis; IBA:GO_Central.
GO; GO:0031214; P:biomineral tissue development; IBA:GO_Central.
GO; GO:0030282; P:bone mineralization; TAS:AgBase.
GO; GO:0055074; P:calcium ion homeostasis; TAS:AgBase.
GO; GO:0052362; P:catabolism by host of symbiont protein; IBA:GO_Central.
GO; GO:0030199; P:collagen fibril organization; IBA:GO_Central.
GO; GO:0060956; P:endocardial cell differentiation; IDA:AgBase.
GO; GO:0042730; P:fibrinolysis; IBA:GO_Central.
GO; GO:0003417; P:growth plate cartilage development; IDA:AgBase.
GO; GO:0001765; P:membrane raft assembly; IBA:GO_Central.
GO; GO:0052405; P:negative regulation by host of symbiont molecular function; IBA:GO_Central.
GO; GO:0044147; P:negative regulation of development of symbiont involved in interaction with host; IBA:GO_Central.
GO; GO:0032804; P:negative regulation of low-density lipoprotein particle receptor catabolic process; IBA:GO_Central.
GO; GO:0036035; P:osteoclast development; IBA:GO_Central.
GO; GO:0044794; P:positive regulation by host of viral process; IBA:GO_Central.
GO; GO:0051928; P:positive regulation of calcium ion transport; IDA:AgBase.
GO; GO:0032332; P:positive regulation of chondrocyte differentiation; IDA:AgBase.
GO; GO:0048146; P:positive regulation of fibroblast proliferation; IBA:GO_Central.
GO; GO:1905581; P:positive regulation of low-density lipoprotein particle clearance; IBA:GO_Central.
GO; GO:1905597; P:positive regulation of low-density lipoprotein particle receptor binding; IBA:GO_Central.
GO; GO:1905599; P:positive regulation of low-density lipoprotein receptor activity; IBA:GO_Central.
GO; GO:0001934; P:positive regulation of protein phosphorylation; IBA:GO_Central.
GO; GO:0001921; P:positive regulation of receptor recycling; IBA:GO_Central.
GO; GO:1905602; P:positive regulation of receptor-mediated endocytosis involved in cholesterol transport; IBA:GO_Central.
GO; GO:0044090; P:positive regulation of vacuole organization; IBA:GO_Central.
GO; GO:0031340; P:positive regulation of vesicle fusion; IBA:GO_Central.
GO; GO:1903902; P:positive regulation of viral life cycle; IBA:GO_Central.
GO; GO:0051290; P:protein heterotetramerization; IBA:GO_Central.
GO; GO:0072659; P:protein localization to plasma membrane; IBA:GO_Central.
GO; GO:0010755; P:regulation of plasminogen activation; IDA:AgBase.
GO; GO:0036366; P:transforming growth factor beta3 activation; IDA:AgBase.
GO; GO:0032907; P:transforming growth factor beta3 production; IDA:AgBase.
GO; GO:0006900; P:vesicle budding from membrane; IBA:GO_Central.
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;
Direct protein sequencing; Extracellular matrix; Phosphoprotein;
Reference proteome; Repeat; Secreted.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:2456953,
ECO:0000269|PubMed:2973411,
ECO:0000269|Ref.4}.
CHAIN 2 339 Annexin A2.
/FTId=PRO_0000067474.
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:2973411,
ECO:0000269|Ref.4}.
MOD_RES 24 24 Phosphotyrosine; by SRC. {ECO:0000250}.
MOD_RES 26 26 Phosphothreonine; by PKC. {ECO:0000250}.
HELIX 3 11 {ECO:0000244|PDB:1BT6}.
SEQUENCE 339 AA; 38640 MW; 4B621506C4BFCD73 CRC64;
MSTVHEILSK LSLEGDHSLP PSAYATVKAY SNFDADRDAA ALEAAIKTKG VDEVTIINIL
TNRSNEQRQD IAFAYQRRTK KELSAALKSA LSGHLEAVIL GLLKTPSQYD ASELKAAMKG
LGTDEDTLIE IICSRTNQEL NEINRVYREM YKTELEKDII SDTSGDFRKL MVALAKGKRC
EDTSVIDYEL IDQDARELYD AGVKRKGTDV PKWINIMTER SVPHLQKVFE RYKSYSPYDM
LESIKKEVKG DLENAFLNLV QCIQNKQLYF ADRLYDSMKG KGTRDKVLIR IMVSRCEVDM
LKIKSEFKRK YGKSLYYFIQ QDTKGDYQRA LLNLCGGED


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