ID ANXA2_PIG Reviewed; 339 AA. AC P19620; Q5Y2C7; DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot. DT 29-MAY-2007, sequence version 4. DT 24-JAN-2024, entry version 169. DE RecName: Full=Annexin A2; DE AltName: Full=Annexin II; DE AltName: Full=Annexin-2; DE AltName: Full=Calpactin I heavy chain; DE AltName: Full=Calpactin-1 heavy chain; DE AltName: Full=Chromobindin-8; DE AltName: Full=Lipocortin II; DE AltName: Full=Placental anticoagulant protein IV; DE Short=PAP-IV; DE AltName: Full=Protein I; DE AltName: Full=p36; GN Name=ANXA2; Synonyms=ANX2; OS Sus scrofa (Pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus. OX NCBI_TaxID=9823; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=16263068; DOI=10.1071/rd05019; RA Cui X.S., Song H., Kim N.H.; RT "Identification of metaphase II-specific gene transcripts in porcine RT oocytes and their expression in early stage embryos."; RL Reprod. Fertil. Dev. 17:625-631(2005). RN [2] RP PROTEIN SEQUENCE OF 2-339, AND ACETYLATION AT SER-2. RX PubMed=17607745; DOI=10.1002/prot.21445; RA Schulz D.M., Kalkhof S., Schmidt A., Ihling C., Stingl C., Mechtler K., RA Zschoernig O., Sinz A.; RT "Annexin A2 / p11 interaction: new insights into annexin A2 tetramer RT structure by chemical cross-linking, high-resolution mass spectrometry, and RT computational modeling."; RL Proteins 69:254-269(2007). RN [3] RP PROTEIN SEQUENCE OF 2-70. RX PubMed=2456953; DOI=10.1016/0014-5793(88)80314-4; RA Johnsson N., Johnsson K., Weber K.; RT "A discontinuous epitope on p36, the major substrate of src tyrosine- RT protein-kinase, brings the phosphorylation site into the neighbourhood of a RT consensus sequence for Ca2+/lipid-binding proteins."; RL FEBS Lett. 236:201-204(1988). RN [4] RP PROTEIN SEQUENCE OF 2-30. RX PubMed=2973411; DOI=10.1002/j.1460-2075.1988.tb03089.x; RA Johnsson N., Marriott G., Weber K.; RT "p36, the major cytoplasmic substrate of src tyrosine protein kinase, binds RT to its p11 regulatory subunit via a short amino-terminal amphipathic RT helix."; RL EMBO J. 7:2435-2442(1988). RN [5] RP PROTEIN SEQUENCE OF 213-234. RX PubMed=2937654; DOI=10.1016/0014-5793(86)80437-9; RA Johnsson N., Vandekerckhove J., Van Damme J., Weber K.; RT "Binding sites for calcium, lipid and p11 on p36, the substrate of RT retroviral tyrosine-specific protein kinases."; RL FEBS Lett. 198:361-364(1986). CC -!- FUNCTION: Calcium-regulated membrane-binding protein whose affinity for CC calcium is greatly enhanced by anionic phospholipids. It binds two CC calcium ions with high affinity. May be involved in heat-stress CC response. Inhibits PCSK9-enhanced LDLR degradation, probably reduces CC PCSK9 protein levels via a translational mechanism but also competes CC with LDLR for binding with PCSK9. {ECO:0000250|UniProtKB:P07355}. CC -!- SUBUNIT: Heterotetramer containing 2 light chains of S100A10/p11 and 2 CC heavy chains of ANXA2/p36 (By similarity). Interacts with ATP1B1 (By CC similarity). Interacts with DYSF (By similarity). Interacts with COCH. CC Interacts (via repeat Annexin 1) with PCSK9 (via the C-terminal CC domain); the interaction inhibits the degradation of LDLR. Interacts CC with CEACAM1 (via the cytoplasmic domain); this interaction is CC regulated by phosphorylation of CEACAM1 (By similarity). Interacts with CC APPL2 and APPL1; targets APPL2 to endosomes and acting in parallel to CC RAB5A (By similarity). Interacts with S100A4 (By similarity). May CC interact with UBAP2 (By similarity). {ECO:0000250|UniProtKB:A2SW69, CC ECO:0000250|UniProtKB:P07355, ECO:0000250|UniProtKB:P07356, CC ECO:0000250|UniProtKB:Q6TEQ7}. CC -!- INTERACTION: CC P19620; Q9YS30; Xeno; NbExp=3; IntAct=EBI-7437630, EBI-12522488; CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular CC matrix, basement membrane. Melanosome {ECO:0000250}. Note=In the lamina CC beneath the plasma membrane. CC -!- DOMAIN: A pair of annexin repeats may form one binding site for calcium CC and phospholipid. CC -!- PTM: ISGylated. {ECO:0000250}. CC -!- MISCELLANEOUS: It may cross-link plasma membrane phospholipids with CC actin and the cytoskeleton and be involved with exocytosis. CC -!- SIMILARITY: Belongs to the annexin family. {ECO:0000255|PROSITE- CC ProRule:PRU01245, ECO:0000305}. CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Red velvet - Issue 86 of CC September 2007; CC URL="https://web.expasy.org/spotlight/back_issues/086"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AY706383; AAU85387.1; -; mRNA. DR PIR; S01128; S01128. DR RefSeq; NP_001005726.1; NM_001005726.1. DR IntAct; P19620; 3. DR MINT; P19620; -. DR STRING; 9823.ENSSSCP00000031749; -. DR iPTMnet; P19620; -. DR PaxDb; 9823-ENSSSCP00000004935; -. DR PeptideAtlas; P19620; -. DR GeneID; 406192; -. DR KEGG; ssc:406192; -. DR CTD; 302; -. DR eggNOG; KOG0819; Eukaryota. DR InParanoid; P19620; -. DR OrthoDB; 1500773at2759; -. DR Proteomes; UP000008227; Unplaced. DR Proteomes; UP000314985; Unplaced. DR Proteomes; UP000694570; Unplaced. DR Proteomes; UP000694571; Unplaced. DR Proteomes; UP000694720; Unplaced. DR Proteomes; UP000694722; Unplaced. DR Proteomes; UP000694723; Unplaced. DR Proteomes; UP000694724; Unplaced. DR Proteomes; UP000694725; Unplaced. DR Proteomes; UP000694726; Unplaced. DR Proteomes; UP000694727; Unplaced. DR Proteomes; UP000694728; Unplaced. DR GO; GO:1990665; C:AnxA2-p11 complex; IDA:UniProtKB. DR GO; GO:0005604; C:basement membrane; IEA:UniProtKB-SubCell. DR GO; GO:0062023; C:collagen-containing extracellular matrix; IBA:GO_Central. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0005768; C:endosome; ISS:UniProtKB. DR GO; GO:0005615; C:extracellular space; IBA:GO_Central. DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0031982; C:vesicle; IBA:GO_Central. DR GO; GO:0005262; F:calcium channel activity; IBA:GO_Central. DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central. DR GO; GO:0005544; F:calcium-dependent phospholipid binding; IBA:GO_Central. DR GO; GO:0008092; F:cytoskeletal protein binding; IEA:InterPro. DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IBA:GO_Central. DR GO; GO:0001786; F:phosphatidylserine binding; IBA:GO_Central. DR GO; GO:0019834; F:phospholipase A2 inhibitor activity; IBA:GO_Central. DR GO; GO:0002020; F:protease binding; IBA:GO_Central. DR GO; GO:0044548; F:S100 protein binding; IPI:UniProtKB. DR GO; GO:0046790; F:virion binding; IBA:GO_Central. DR GO; GO:0044794; P:positive regulation by host of viral process; IMP:AgBase. DR GO; GO:1903902; P:positive regulation of viral life cycle; IMP:AgBase. DR Gene3D; 1.10.220.10; Annexin; 4. DR InterPro; IPR001464; Annexin. DR InterPro; IPR018502; Annexin_repeat. DR InterPro; IPR018252; Annexin_repeat_CS. DR InterPro; IPR037104; Annexin_sf. DR InterPro; IPR002389; ANX2. DR PANTHER; PTHR10502; ANNEXIN; 1. DR PANTHER; PTHR10502:SF18; ANNEXIN A2-RELATED; 1. DR Pfam; PF00191; Annexin; 4. DR PRINTS; PR00196; ANNEXIN. DR PRINTS; PR00198; ANNEXINII. DR SMART; SM00335; ANX; 4. DR SUPFAM; SSF47874; Annexin; 1. DR PROSITE; PS00223; ANNEXIN_1; 4. DR PROSITE; PS51897; ANNEXIN_2; 4. PE 1: Evidence at protein level; KW Acetylation; Annexin; Basement membrane; Calcium; KW Calcium/phospholipid-binding; Direct protein sequencing; KW Extracellular matrix; Isopeptide bond; Phosphoprotein; Reference proteome; KW Repeat; Secreted; Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:17607745, FT ECO:0000269|PubMed:2456953, ECO:0000269|PubMed:2973411" FT CHAIN 2..339 FT /note="Annexin A2" FT /id="PRO_0000067472" FT REPEAT 33..104 FT /note="Annexin 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245" FT REPEAT 105..176 FT /note="Annexin 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245" FT REPEAT 189..261 FT /note="Annexin 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245" FT REPEAT 265..336 FT /note="Annexin 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245" FT REGION 2..24 FT /note="S100A10-binding site" FT MOD_RES 2 FT /note="N-acetylserine" FT /evidence="ECO:0000269|PubMed:17607745" FT MOD_RES 24 FT /note="Phosphotyrosine; by SRC" FT /evidence="ECO:0000250|UniProtKB:P07355" FT MOD_RES 26 FT /note="Phosphoserine; by PKC" FT /evidence="ECO:0000250|UniProtKB:P07355" FT MOD_RES 49 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P07356" FT MOD_RES 152 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P07356" FT MOD_RES 184 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P07355" FT MOD_RES 199 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:P07356" FT MOD_RES 227 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P07356" FT CROSSLNK 49 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO1); alternate" FT /evidence="ECO:0000250|UniProtKB:P07355" FT CROSSLNK 49 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0000250|UniProtKB:P07355" FT CONFLICT 223 FT /note="C -> P (in Ref. 5; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 229 FT /note="F -> S (in Ref. 2; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 230 FT /note="E -> S (in Ref. 5; AA sequence)" FT /evidence="ECO:0000305" SQ SEQUENCE 339 AA; 38534 MW; FAC554639119900D CRC64; MSTVHEILCK LSLEGDHSTP ASAYGSVKAY TNFDAERDAL NIETAIKTKG VDEVTIVNIL TNRSNEQRQD IAFAYQRRTK KELASALKSA LSGHLETVIL GLLKTPAQYD ASELKASMKG LGTDEDSLIE IICSRTNQEL QEINRVYKEM YKTDLEKDII SDTSGDFRKL MVALAKGRRA EDGSVIDYEL IDQDARDLYD AGVKRKGTDV PKWISIMTER SVCHLQKVFE RYKSYSPYDM LESIKKEVKG DLENAFLNLV QCIQNKPLYF ADRLYDSMKG KGTRDKVLIX IMVSRSEVDM LKIRSEFKRK YGKSLYNYIQ QDTKGDYQKA LLYLCGGDD //