ANXA2_PIG
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 23-FEB-2022, entry version 164.
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).
CC {ECO:0000250|UniProtKB:A2SW69, ECO:0000250|UniProtKB:P07355,
CC ECO:0000250|UniProtKB:P07356, 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";
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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.ENSSSCP00000004935; -.
DR iPTMnet; P19620; -.
DR PaxDb; P19620; -.
DR PeptideAtlas; P19620; -.
DR PRIDE; P19620; -.
DR GeneID; 406192; -.
DR KEGG; ssc:406192; -.
DR CTD; 302; -.
DR eggNOG; KOG0819; Eukaryota.
DR InParanoid; P19620; -.
DR OrthoDB; 856254at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:1990665; C:AnxA2-p11 complex; IDA:UniProtKB.
DR GO; GO:0005604; C:basement membrane; IEA:UniProtKB-SubCell.
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; -; 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 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
