ANXA2_MESAU
ID ANXA2_MESAU Reviewed; 199 AA.
AC C0HJG9;
DT 19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT 19-MAR-2014, sequence version 1.
DT 25-MAY-2022, entry version 28.
DE RecName: Full=Annexin A2 {ECO:0000303|Ref.1};
DE AltName: Full=Annexin II {ECO:0000250|UniProtKB:P07355};
DE AltName: Full=Annexin-2 {ECO:0000250|UniProtKB:P07355};
DE AltName: Full=Calpactin I heavy chain {ECO:0000250|UniProtKB:P07355};
DE AltName: Full=Calpactin-1 heavy chain {ECO:0000250|UniProtKB:P07355};
DE AltName: Full=Chromobindin-8 {ECO:0000250|UniProtKB:P07355};
DE AltName: Full=Lipocortin II {ECO:0000250|UniProtKB:P07355};
DE AltName: Full=Placental anticoagulant protein IV {ECO:0000250|UniProtKB:P07355};
DE Short=PAP-IV {ECO:0000250|UniProtKB:P07355};
DE AltName: Full=Protein I {ECO:0000250|UniProtKB:P07355};
DE AltName: Full=p36 {ECO:0000250|UniProtKB:P07355};
DE Flags: Fragments;
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036;
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE, AND ACETYLATION AT SER-1.
RA Hohenester U.M., Quiskamp N., Rescher U., Koenig S.;
RT "The amino acid sequence of annexin A2 of Syrian hamster Mesocricetus
RT auratus as determined by mass spectrometry.";
RL BMMS 2:109-117(2009).
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 (By similarity).
CC {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).
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 {ECO:0000250|UniProtKB:P07355}.
CC -!- SIMILARITY: Belongs to the annexin family.
CC {ECO:0000250|UniProtKB:P07355, ECO:0000255|PROSITE-ProRule:PRU01245}.
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DR AlphaFoldDB; C0HJG9; -.
DR SMR; C0HJG9; -.
DR PRIDE; C0HJG9; -.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0005604; C:basement membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005544; F:calcium-dependent phospholipid binding; IEA:UniProtKB-KW.
DR GO; GO:0008092; F:cytoskeletal protein binding; IEA:InterPro.
DR GO; GO:0004859; F:phospholipase inhibitor activity; IEA:InterPro.
DR Gene3D; 1.10.220.10; -; 1.
DR InterPro; IPR018502; Annexin_repeat.
DR InterPro; IPR037104; Annexin_sf.
DR InterPro; IPR002389; ANX2.
DR Pfam; PF00191; Annexin; 1.
DR PRINTS; PR00198; ANNEXINII.
DR SMART; SM00335; ANX; 1.
DR SUPFAM; SSF47874; SSF47874; 1.
DR PROSITE; PS51897; ANNEXIN_2; 2.
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 CHAIN 1..>199
FT /note="Annexin A2"
FT /id="PRO_0000425700"
FT REPEAT 65..129
FT /note="Annexin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT REPEAT 140..>199
FT /note="Annexin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT MOD_RES 1
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|Ref.1"
FT MOD_RES 23
FT /note="Phosphotyrosine; by SRC"
FT /evidence="ECO:0000250|UniProtKB:P07355"
FT MOD_RES 25
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000250|UniProtKB:P07355"
FT MOD_RES 37
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P07356"
FT MOD_RES 135
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P07355"
FT MOD_RES 150
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P07356"
FT MOD_RES 171
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P07356"
FT CROSSLNK 37
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P07355"
FT CROSSLNK 37
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P07355"
FT NON_CONS 27..28
FT /evidence="ECO:0000303|Ref.1"
FT NON_CONS 37..38
FT /evidence="ECO:0000303|Ref.1"
FT NON_CONS 51..52
FT /evidence="ECO:0000303|Ref.1"
FT NON_CONS 60..61
FT /evidence="ECO:0000303|Ref.1"
FT NON_CONS 68..69
FT /evidence="ECO:0000303|Ref.1"
FT NON_CONS 79..80
FT /evidence="ECO:0000303|Ref.1"
FT NON_CONS 105..106
FT /evidence="ECO:0000303|Ref.1"
FT NON_CONS 129..130
FT /evidence="ECO:0000303|Ref.1"
FT NON_CONS 156..157
FT /evidence="ECO:0000303|Ref.1"
FT NON_CONS 171..172
FT /evidence="ECO:0000303|Ref.1"
FT NON_CONS 188..189
FT /evidence="ECO:0000303|Ref.1"
FT NON_TER 199
FT /evidence="ECO:0000303|Ref.1"
SQ SEQUENCE 199 AA; 22447 MW; 6B74F7A1FD2636E9 CRC64;
STVHEILCKL SLEGDHSTPP SAYGSVKDAL NIETAVKGVD EVTIVNILTN RQDIAFAYQR
KELPSALKTP AQYDASELKG LGTDEDSLIE IICSRTNQEL QEINRTDLEK DIISDTSGDF
RKLMVALAKR AEDGSVIDYE LIDQDARDLY DAGVKRWISI MTERSVCHLQ KDKVLIRIMV
SRSEVDMLSL YYYIQQDTK
