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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_RAT               Reviewed;         339 AA.
Q07936;
01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
22-NOV-2017, entry version 161.
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;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
PubMed=8389036;
Ozaki T., Sakiyama S.;
"Molecular cloning of rat calpactin I heavy-chain cDNA whose
expression is induced in v-src-transformed rat culture cell lines.";
Oncogene 8:1707-1710(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
Ernst J.D.;
Submitted (MAR-1993) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
PubMed=8092993; DOI=10.1042/bj3020425;
Upton A.L., Moss S.E.;
"Molecular cloning of a novel N-terminal variant of annexin II from
rat basophilic leukaemia cells.";
Biochem. J. 302:425-428(1994).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SHORT).
TISSUE=Pituitary;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
PROTEIN SEQUENCE OF 2-10; 38-47; 50-63; 69-77; 89-115; 120-145;
158-168; 180-204; 234-245 AND 314-324, CLEAVAGE OF INITIATOR
METHIONINE, ACETYLATION AT SER-2, AND IDENTIFICATION BY MASS
SPECTROMETRY.
TISSUE=Fibroblast;
Bienvenut W.V., von Kriegsheim A., Kolch W.;
Submitted (JUN-2009) to UniProtKB.
[6]
PROTEIN SEQUENCE OF 38-47; 50-63; 89-115; 136-145; 158-168; 180-196
AND 314-324 (ISOFORMS SHORT/LONG), AND IDENTIFICATION BY MASS
SPECTROMETRY.
STRAIN=Sprague-Dawley; TISSUE=Brain, and Spinal cord;
Lubec G., Afjehi-Sadat L., Kang S.U.;
Submitted (JUL-2007) to UniProtKB.
[7]
SUBCELLULAR LOCATION.
PubMed=1618851;
Mizutani A., Usuda N., Tokumitsu H., Minami H., Yasui K.,
Kobayashi R., Hidaka H.;
"CAP-50, a newly identified annexin, localizes in nuclei of cultured
fibroblast 3Y1 cells.";
J. Biol. Chem. 267:13498-13504(1992).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- 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 {ECO:0000269|PubMed:1618851}. Melanosome
{ECO:0000250}. Note=In the lamina beneath the plasma membrane.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=Short;
IsoId=Q07936-1; Sequence=Displayed;
Name=Long;
IsoId=Q07936-2; Sequence=VSP_000287;
-!- 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";
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; X66871; CAA47343.1; -; mRNA.
EMBL; L13039; AAA40741.1; -; mRNA.
EMBL; S73559; AAB31934.2; -; mRNA.
EMBL; S73557; AAB31933.2; -; mRNA.
EMBL; BC059136; AAH59136.1; -; mRNA.
PIR; S33700; S33700.
PIR; S55277; S55277.
RefSeq; NP_063970.1; NM_019905.1. [Q07936-1]
UniGene; Rn.90546; -.
ProteinModelPortal; Q07936; -.
SMR; Q07936; -.
BioGrid; 248566; 3.
CORUM; Q07936; -.
IntAct; Q07936; 3.
MINT; MINT-4997127; -.
STRING; 10116.ENSRNOP00000038428; -.
iPTMnet; Q07936; -.
PhosphoSitePlus; Q07936; -.
PaxDb; Q07936; -.
PRIDE; Q07936; -.
Ensembl; ENSRNOT00000038677; ENSRNOP00000038428; ENSRNOG00000010362. [Q07936-1]
GeneID; 56611; -.
KEGG; rno:56611; -.
UCSC; RGD:621170; rat. [Q07936-1]
CTD; 302; -.
RGD; 621170; Anxa2.
eggNOG; KOG0819; Eukaryota.
eggNOG; ENOG410XPUN; LUCA.
GeneTree; ENSGT00760000118972; -.
HOGENOM; HOG000158803; -.
HOVERGEN; HBG061815; -.
InParanoid; Q07936; -.
KO; K17092; -.
OMA; FIQQDTK; -.
OrthoDB; EOG091G0H6H; -.
PhylomeDB; Q07936; -.
TreeFam; TF105452; -.
Reactome; R-RNO-6798695; Neutrophil degranulation.
Reactome; R-RNO-75205; Dissolution of Fibrin Clot.
PRO; PR:Q07936; -.
Proteomes; UP000002494; Chromosome 8.
Bgee; ENSRNOG00000010362; -.
Genevisible; Q07936; RN.
GO; GO:0005604; C:basement membrane; IEA:UniProtKB-SubCell.
GO; GO:0016323; C:basolateral plasma membrane; ISO:RGD.
GO; GO:0005938; C:cell cortex; IDA:RGD.
GO; GO:0009986; C:cell surface; ISO:RGD.
GO; GO:0005913; C:cell-cell adherens junction; ISO:RGD.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0005829; C:cytosol; IDA:CAFA.
GO; GO:0005769; C:early endosome; ISO:RGD.
GO; GO:0005768; C:endosome; ISO:RGD.
GO; GO:0070062; C:extracellular exosome; ISO:RGD.
GO; GO:0031012; C:extracellular matrix; ISO:RGD.
GO; GO:0005615; C:extracellular space; ISO:RGD.
GO; GO:0019897; C:extrinsic component of plasma membrane; ISO:RGD.
GO; GO:0031902; C:late endosome membrane; ISO:RGD.
GO; GO:0005811; C:lipid droplet; ISO:RGD.
GO; GO:0005765; C:lysosomal membrane; ISO:RGD.
GO; GO:0044354; C:macropinosome; IDA:RGD.
GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; ISO:RGD.
GO; GO:0045121; C:membrane raft; IDA:CAFA.
GO; GO:0030496; C:midbody; ISO:RGD.
GO; GO:0035749; C:myelin sheath adaxonal region; ISO:RGD.
GO; GO:0005634; C:nucleus; ISO:RGD.
GO; GO:1990667; C:PCSK9-AnxA2 complex; ISO:RGD.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
GO; GO:0005886; C:plasma membrane; IDA:RGD.
GO; GO:0043234; C:protein complex; IDA:RGD.
GO; GO:0001726; C:ruffle; IDA:RGD.
GO; GO:0042383; C:sarcolemma; ISO:RGD.
GO; GO:0043220; C:Schmidt-Lanterman incisure; ISO:RGD.
GO; GO:0031982; C:vesicle; IDA:RGD.
GO; GO:0051015; F:actin filament binding; TAS:RGD.
GO; GO:0044730; F:bone sialoprotein binding; IPI:RGD.
GO; GO:0098641; F:cadherin binding involved in cell-cell adhesion; ISO:RGD.
GO; GO:0005509; F:calcium ion binding; TAS:RGD.
GO; GO:0005544; F:calcium-dependent phospholipid binding; ISO:RGD.
GO; GO:0048306; F:calcium-dependent protein binding; ISO:RGD.
GO; GO:0042802; F:identical protein binding; ISO:RGD.
GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IDA:RGD.
GO; GO:0019834; F:phospholipase A2 inhibitor activity; ISO:RGD.
GO; GO:0002020; F:protease binding; ISO:RGD.
GO; GO:0017137; F:Rab GTPase binding; IPI:RGD.
GO; GO:0003723; F:RNA binding; ISO:RGD.
GO; GO:0044548; F:S100 protein binding; ISO:RGD.
GO; GO:0001525; P:angiogenesis; ISO:RGD.
GO; GO:0007589; P:body fluid secretion; IMP:RGD.
GO; GO:0052362; P:catabolism by host of symbiont protein; ISO:RGD.
GO; GO:0030199; P:collagen fibril organization; ISO:RGD.
GO; GO:0042730; P:fibrinolysis; ISO:RGD.
GO; GO:0001765; P:membrane raft assembly; ISO:RGD.
GO; GO:0052405; P:negative regulation by host of symbiont molecular function; ISO:RGD.
GO; GO:0044147; P:negative regulation of development of symbiont involved in interaction with host; ISO:RGD.
GO; GO:0032804; P:negative regulation of low-density lipoprotein particle receptor catabolic process; ISO:RGD.
GO; GO:0036035; P:osteoclast development; ISO:RGD.
GO; GO:0051099; P:positive regulation of binding; ISO:RGD.
GO; GO:0048146; P:positive regulation of fibroblast proliferation; IMP:RGD.
GO; GO:1905581; P:positive regulation of low-density lipoprotein particle clearance; ISO:RGD.
GO; GO:1905597; P:positive regulation of low-density lipoprotein particle receptor binding; ISO:RGD.
GO; GO:1905599; P:positive regulation of low-density lipoprotein receptor activity; ISO:RGD.
GO; GO:0001934; P:positive regulation of protein phosphorylation; IMP:RGD.
GO; GO:0001921; P:positive regulation of receptor recycling; ISO:RGD.
GO; GO:1905602; P:positive regulation of receptor-mediated endocytosis involved in cholesterol transport; ISO:RGD.
GO; GO:0044090; P:positive regulation of vacuole organization; ISO:RGD.
GO; GO:0031340; P:positive regulation of vesicle fusion; ISO:RGD.
GO; GO:0051290; P:protein heterotetramerization; ISO:RGD.
GO; GO:0072659; P:protein localization to plasma membrane; IMP:RGD.
GO; GO:0051917; P:regulation of fibrinolysis; TAS:RGD.
GO; GO:0097066; P:response to thyroid hormone; IEP:RGD.
GO; GO:0006900; P:vesicle budding from membrane; ISO:RGD.
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;
Acetylation; Alternative splicing; Annexin; Basement membrane;
Calcium; Calcium/phospholipid-binding; Complete proteome;
Direct protein sequencing; Extracellular matrix; Isopeptide bond;
Phosphoprotein; Reference proteome; Repeat; Secreted; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000269|Ref.5}.
CHAIN 2 339 Annexin A2.
/FTId=PRO_0000067473.
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|Ref.5}.
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}.
VAR_SEQ 16 16 D -> DSQ (in isoform Long).
{ECO:0000303|PubMed:8092993}.
/FTId=VSP_000287.
CONFLICT 103 103 L -> F (in Ref. 3; AAB31934/AAB31933).
{ECO:0000305}.
CONFLICT 322 322 D -> Y (in Ref. 3; AAB31934/AAB31933).
{ECO:0000305}.
SEQUENCE 339 AA; 38678 MW; 101E67F50C01CF8B CRC64;
MSTVHEILCK LSLEGDHSTP PSAYGSVKPY TNFDAERDAL NIETAIKTKG VDEVTIVNIL
TNRSNAQRQD IAFAYQRRTK KELPSAMKSA LSGHLETVML GLLKTPAQYD ASELKASMKG
LGTDEDSLIE IICSRTNQEL QEINRVYKEM YKTDLEKDII SDTSGEFRKL LVALAKGKRA
EDGSVIDYEL IDQDARELYD AGVKRKGTDV PKWISIMTER SVCHLQKVFE RYKSYSPYDM
LESIRKEVKG DLENAFLNLV QCIQNKPLYF ADRLYDSMKG KGTRDKVLIR IMVSRSEVDM
LKIRSEFKRK YGKSLYYFIQ QDTKGDYQKA LLYLCGGDD


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