ANXA2_BOVIN
ID ANXA2_BOVIN Reviewed; 339 AA.
AC P04272; Q3ZCC7; Q5E9B0;
DT 01-NOV-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 189.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Kidney;
RX PubMed=2945590; DOI=10.1021/bi00364a007;
RA Kristensen T., Saris C.J.M., Hunter T., Hicks L.J., Noonan D.J.,
RA Glenney J.R. Jr., Tack B.F.;
RT "Primary structure of bovine calpactin I heavy chain (p36), a major
RT cellular substrate for retroviral protein-tyrosine kinases: homology with
RT the human phospholipase A2 inhibitor lipocortin.";
RL Biochemistry 25:4497-4503(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP ACETYLATION AT SER-2.
RX PubMed=2942542; DOI=10.1016/s0021-9258(18)67409-5;
RA Glenney J.R. Jr., Boudreau M., Galyean R., Hunter T., Tack B.;
RT "Association of the S-100-related calpactin I light chain with the NH2-
RT terminal tail of the 36-kDa heavy chain.";
RL J. Biol. Chem. 261:10485-10488(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).
CC {ECO:0000250|UniProtKB:A2SW69, ECO:0000250|UniProtKB:P07355,
CC ECO:0000250|UniProtKB:P07356, ECO:0000250|UniProtKB:Q6TEQ7}.
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";
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DR EMBL; M14056; AAA30421.1; -; mRNA.
DR EMBL; BT021010; AAX09027.1; -; mRNA.
DR EMBL; BC102516; AAI02517.1; -; mRNA.
DR PIR; A03081; LUBO36.
DR RefSeq; NP_777141.1; NM_174716.1.
DR PDB; 4X9P; X-ray; 2.01 A; A=1-339.
DR PDBsum; 4X9P; -.
DR AlphaFoldDB; P04272; -.
DR SMR; P04272; -.
DR IntAct; P04272; 1.
DR STRING; 9913.ENSBTAP00000012655; -.
DR ChEMBL; CHEMBL3308972; -.
DR iPTMnet; P04272; -.
DR PaxDb; P04272; -.
DR PeptideAtlas; P04272; -.
DR PRIDE; P04272; -.
DR Ensembl; ENSBTAT00000012655; ENSBTAP00000012655; ENSBTAG00000009615.
DR GeneID; 282689; -.
DR KEGG; bta:282689; -.
DR CTD; 302; -.
DR VEuPathDB; HostDB:ENSBTAG00000009615; -.
DR eggNOG; KOG0819; Eukaryota.
DR GeneTree; ENSGT00940000154257; -.
DR HOGENOM; CLU_025300_0_0_1; -.
DR InParanoid; P04272; -.
DR OMA; EVDLMRI; -.
DR OrthoDB; 856254at2759; -.
DR TreeFam; TF105452; -.
DR Reactome; R-BTA-6798695; Neutrophil degranulation.
DR Reactome; R-BTA-75205; Dissolution of Fibrin Clot.
DR Proteomes; UP000009136; Chromosome 10.
DR Bgee; ENSBTAG00000009615; Expressed in placenta and 106 other tissues.
DR GO; GO:0005604; C:basement membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IDA:AgBase.
DR GO; GO:0005768; C:endosome; ISS:UniProtKB.
DR GO; GO:0065010; C:extracellular membrane-bounded organelle; IDA:AgBase.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:AgBase.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IDA:AgBase.
DR GO; GO:0005634; C:nucleus; IDA:AgBase.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0031982; C:vesicle; IDA:AgBase.
DR GO; GO:0005262; F:calcium channel activity; IMP:AgBase.
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; IPI:AgBase.
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; IBA:GO_Central.
DR GO; GO:0031214; P:biomineral tissue development; IDA:AgBase.
DR GO; GO:0070509; P:calcium ion import; IMP:AgBase.
DR GO; GO:0070588; P:calcium ion transmembrane transport; IDA:AgBase.
DR Gene3D; 1.10.220.10; -; 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:SF18; PTHR10502:SF18; 1.
DR Pfam; PF00191; Annexin; 4.
DR PRINTS; PR00196; ANNEXIN.
DR PRINTS; PR00198; ANNEXINII.
DR SMART; SM00335; ANX; 4.
DR SUPFAM; SSF47874; SSF47874; 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; Extracellular matrix; Isopeptide bond;
KW Phosphoprotein; Reference proteome; Repeat; Secreted; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2942542"
FT CHAIN 2..339
FT /note="Annexin A2"
FT /id="PRO_0000067469"
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:2942542"
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 149
FT /note="E -> G (in Ref. 3; AAI02517)"
FT /evidence="ECO:0000305"
FT HELIX 35..47
FT /evidence="ECO:0007829|PDB:4X9P"
FT HELIX 53..60
FT /evidence="ECO:0007829|PDB:4X9P"
FT HELIX 65..79
FT /evidence="ECO:0007829|PDB:4X9P"
FT HELIX 83..90
FT /evidence="ECO:0007829|PDB:4X9P"
FT HELIX 93..103
FT /evidence="ECO:0007829|PDB:4X9P"
FT HELIX 106..117
FT /evidence="ECO:0007829|PDB:4X9P"
FT HELIX 125..133
FT /evidence="ECO:0007829|PDB:4X9P"
FT HELIX 137..151
FT /evidence="ECO:0007829|PDB:4X9P"
FT HELIX 155..162
FT /evidence="ECO:0007829|PDB:4X9P"
FT HELIX 165..175
FT /evidence="ECO:0007829|PDB:4X9P"
FT HELIX 188..200
FT /evidence="ECO:0007829|PDB:4X9P"
FT TURN 201..204
FT /evidence="ECO:0007829|PDB:4X9P"
FT STRAND 205..207
FT /evidence="ECO:0007829|PDB:4X9P"
FT HELIX 210..219
FT /evidence="ECO:0007829|PDB:4X9P"
FT HELIX 222..235
FT /evidence="ECO:0007829|PDB:4X9P"
FT HELIX 240..247
FT /evidence="ECO:0007829|PDB:4X9P"
FT HELIX 250..264
FT /evidence="ECO:0007829|PDB:4X9P"
FT HELIX 266..278
FT /evidence="ECO:0007829|PDB:4X9P"
FT STRAND 279..282
FT /evidence="ECO:0007829|PDB:4X9P"
FT HELIX 285..295
FT /evidence="ECO:0007829|PDB:4X9P"
FT TURN 296..299
FT /evidence="ECO:0007829|PDB:4X9P"
FT HELIX 300..311
FT /evidence="ECO:0007829|PDB:4X9P"
FT HELIX 315..322
FT /evidence="ECO:0007829|PDB:4X9P"
FT HELIX 325..335
FT /evidence="ECO:0007829|PDB:4X9P"
SQ 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
