ID   ANXA2_CHICK             Reviewed;         339 AA.
AC   P17785;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   24-JAN-2024, entry version 182.
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   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2143014; DOI=10.1093/nar/18.14.4246;
RA   Gerke V., Koch W.;
RT   "The cDNA sequence of chicken annexin II.";
RL   Nucleic Acids Res. 18:4246-4246(1990).
RN   [2]
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   [3]
RP   PROTEIN SEQUENCE OF 2-30, AND ACETYLATION AT SER-2.
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   [4]
RP   PROTEIN SEQUENCE OF 2-63; 69-77 AND 314-324, CLEAVAGE OF INITIATOR
RP   METHIONINE, ACETYLATION AT SER-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=B-cell lymphoma;
RA   Bienvenut W.V., Black E.J., Gillespie D.A.;
RL   Submitted (JAN-2007) to UniProtKB.
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.
CC   -!- SUBUNIT: Heterotetramer containing 2 light chains of S100A10/p11 and 2
CC       heavy chains of ANXA2/p36.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix, basement membrane. Note=In the lamina beneath the plasma
CC       membrane.
CC   -!- DOMAIN: A pair of annexin repeats may form one binding site for calcium
CC       and phospholipid.
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";
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DR   EMBL; X53334; CAA37421.1; -; mRNA.
DR   PIR; S10501; LUCH2.
DR   RefSeq; NP_990682.1; NM_205351.1.
DR   RefSeq; XP_015134249.1; XM_015278763.1.
DR   PDB; 1BT6; X-ray; 2.40 A; C/D=2-14.
DR   PDBsum; 1BT6; -.
DR   AlphaFoldDB; P17785; -.
DR   SMR; P17785; -.
DR   STRING; 9031.ENSGALP00000048954; -.
DR   iPTMnet; P17785; -.
DR   PaxDb; 9031-ENSGALP00000005971; -.
DR   Ensembl; ENSGALT00000083426; ENSGALP00000060891; ENSGALG00000003770.
DR   Ensembl; ENSGALT00010060304.1; ENSGALP00010037063.1; ENSGALG00010024693.1.
DR   Ensembl; ENSGALT00015042178; ENSGALP00015024698; ENSGALG00015017245.
DR   GeneID; 396297; -.
DR   KEGG; gga:396297; -.
DR   CTD; 302; -.
DR   VEuPathDB; HostDB:geneid_396297; -.
DR   eggNOG; KOG0819; Eukaryota.
DR   GeneTree; ENSGT00940000154257; -.
DR   HOGENOM; CLU_025300_0_0_1; -.
DR   InParanoid; P17785; -.
DR   OMA; DLMRIRT; -.
DR   OrthoDB; 1500773at2759; -.
DR   PhylomeDB; P17785; -.
DR   TreeFam; TF105452; -.
DR   Reactome; R-GGA-6798695; Neutrophil degranulation.
DR   Reactome; R-GGA-75205; Dissolution of Fibrin Clot.
DR   EvolutionaryTrace; P17785; -.
DR   PRO; PR:P17785; -.
DR   Proteomes; UP000000539; Chromosome 10.
DR   Bgee; ENSGALG00000003770; Expressed in ovary and 14 other cell types or tissues.
DR   ExpressionAtlas; P17785; baseline and differential.
DR   GO; GO:0005604; C:basement membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0034704; C:calcium channel complex; TAS:AgBase.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; IDA:AgBase.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IDA:AgBase.
DR   GO; GO:0032991; C:protein-containing complex; IDA:AgBase.
DR   GO; GO:0031982; C:vesicle; IDA:AgBase.
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:0046790; F:virion binding; IDA:AgBase.
DR   GO; GO:0099511; F:voltage-gated calcium channel activity involved in regulation of cytosolic calcium levels; IDA:AgBase.
DR   GO; GO:0030282; P:bone mineralization; TAS:AgBase.
DR   GO; GO:0055074; P:calcium ion homeostasis; TAS:AgBase.
DR   GO; GO:0060956; P:endocardial cell differentiation; IDA:AgBase.
DR   GO; GO:0003417; P:growth plate cartilage development; IDA:AgBase.
DR   GO; GO:0051928; P:positive regulation of calcium ion transport; IDA:AgBase.
DR   GO; GO:0032332; P:positive regulation of chondrocyte differentiation; IDA:AgBase.
DR   GO; GO:0010755; P:regulation of plasminogen activation; IDA:AgBase.
DR   GO; GO:0036366; P:transforming growth factor beta3 activation; IDA:AgBase.
DR   GO; GO:0032907; P:transforming growth factor beta3 production; IDA: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   3D-structure; Acetylation; Annexin; Basement membrane; Calcium;
KW   Calcium/phospholipid-binding; Direct protein sequencing;
KW   Extracellular matrix; Phosphoprotein; Reference proteome; Repeat; Secreted.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:2456953,
FT                   ECO:0000269|PubMed:2973411, ECO:0000269|Ref.4"
FT   CHAIN           2..339
FT                   /note="Annexin A2"
FT                   /id="PRO_0000067474"
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                   /evidence="ECO:0000255"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000269|PubMed:2973411, ECO:0000269|Ref.4"
FT   MOD_RES         24
FT                   /note="Phosphotyrosine; by SRC"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         26
FT                   /note="Phosphothreonine; by PKC"
FT                   /evidence="ECO:0000250"
FT   HELIX           3..11
FT                   /evidence="ECO:0007829|PDB:1BT6"
SQ   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
//