ANXA2_PONAB
ID ANXA2_PONAB Reviewed; 339 AA.
AC Q5R5A0;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 117.
DE RecName: Full=Annexin A2;
DE AltName: Full=Annexin-2;
GN Name=ANXA2; Synonyms=ANX2;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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). {ECO:0000250|UniProtKB:A2SW69,
CC ECO:0000250|UniProtKB:P07355, ECO:0000250|UniProtKB:P07356,
CC ECO:0000250|UniProtKB:Q6TEQ7}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix, basement membrane. Note=In the lamina beneath the plasma
CC membrane. {ECO:0000250}.
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; CR860964; CAH93066.1; -; mRNA.
DR RefSeq; NP_001126816.1; NM_001133344.1.
DR AlphaFoldDB; Q5R5A0; -.
DR SMR; Q5R5A0; -.
DR STRING; 9601.ENSPPYP00000007399; -.
DR Ensembl; ENSPPYT00000045908; ENSPPYP00000029450; ENSPPYG00000006526.
DR GeneID; 100173821; -.
DR KEGG; pon:100173821; -.
DR CTD; 302; -.
DR eggNOG; KOG0819; Eukaryota.
DR GeneTree; ENSGT00940000154257; -.
DR HOGENOM; CLU_025300_0_0_1; -.
DR InParanoid; Q5R5A0; -.
DR OMA; EVDLMRI; -.
DR OrthoDB; 856254at2759; -.
DR TreeFam; TF105452; -.
DR Proteomes; UP000001595; Chromosome 15.
DR GO; GO:1990665; C:AnxA2-p11 complex; IEA:Ensembl.
DR GO; GO:0005604; C:basement membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005768; C:endosome; ISS:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
DR GO; GO:0031902; C:late endosome membrane; IEA:Ensembl.
DR GO; GO:0005811; C:lipid droplet; IEA:Ensembl.
DR GO; GO:0005765; C:lysosomal membrane; IEA:Ensembl.
DR GO; GO:0045121; C:membrane raft; IEA:Ensembl.
DR GO; GO:0030496; C:midbody; IEA:Ensembl.
DR GO; GO:1990667; C:PCSK9-AnxA2 complex; IEA:Ensembl.
DR GO; GO:0098797; C:plasma membrane protein complex; IEA:Ensembl.
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:0048306; F:calcium-dependent protein binding; IEA:Ensembl.
DR GO; GO:0008092; F:cytoskeletal protein binding; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IEA:Ensembl.
DR GO; GO:0019834; F:phospholipase A2 inhibitor activity; IEA:Ensembl.
DR GO; GO:0002020; F:protease binding; IEA:Ensembl.
DR GO; GO:0044548; F:S100 protein binding; IEA:Ensembl.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:Ensembl.
DR GO; GO:0001525; P:angiogenesis; IEA:Ensembl.
DR GO; GO:0001765; P:membrane raft assembly; IEA:Ensembl.
DR GO; GO:0032804; P:negative regulation of low-density lipoprotein particle receptor catabolic process; IEA:Ensembl.
DR GO; GO:0002091; P:negative regulation of receptor internalization; IEA:Ensembl.
DR GO; GO:0036035; P:osteoclast development; IEA:Ensembl.
DR GO; GO:1905581; P:positive regulation of low-density lipoprotein particle clearance; IEA:Ensembl.
DR GO; GO:1905597; P:positive regulation of low-density lipoprotein particle receptor binding; IEA:Ensembl.
DR GO; GO:1905599; P:positive regulation of low-density lipoprotein receptor activity; IEA:Ensembl.
DR GO; GO:0010756; P:positive regulation of plasminogen activation; IEA:Ensembl.
DR GO; GO:0001921; P:positive regulation of receptor recycling; IEA:Ensembl.
DR GO; GO:1905602; P:positive regulation of receptor-mediated endocytosis involved in cholesterol transport; IEA:Ensembl.
DR GO; GO:0044090; P:positive regulation of vacuole organization; IEA:Ensembl.
DR GO; GO:0031340; P:positive regulation of vesicle fusion; IEA:Ensembl.
DR GO; GO:0006900; P:vesicle budding from membrane; IEA:Ensembl.
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 2: Evidence at transcript level;
KW 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:0000250|UniProtKB:P04272"
FT CHAIN 2..339
FT /note="Annexin A2"
FT /id="PRO_0000288686"
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:0000250|UniProtKB:P04272"
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"
SQ SEQUENCE 339 AA; 38604 MW; 5126E1337A0CBEA1 CRC64;
MSTVHEILCK LSLEGDHSTP PSAYGSVKAY TNFDAERDAL NIETAIKTKG VDEVTIVNIL
TNRSNAQRQD IAFAYQRRTK KELASALKSA LSGHLETVIL GLLKTPAQYD ASELKASMKG
LGTDEDSLIE IICSRTNQEL QEINRVYKEM YKTDLEKDII SDTSGDFRKL MVALAKGRRA
EDGSVIDYEL IDQDARDLYD AGVKRKGTDV PKWISIMTER SVPHLQKVFD RYKSYSPYDM
LESIRKEVKG DLENAFLNLV QCIQNKPLYF ADRLYDSMKG KGTRDKVLIR IMVSRSEVDM
LKIRSEFKRK YGKSLYYYIQ QDTKGDYQKA LLYLCGGDD
