ANX2A_XENLA
ID ANX2A_XENLA Reviewed; 340 AA.
AC P27006; Q5D0C8;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Annexin A2-A;
DE AltName: Full=Annexin II type I;
DE AltName: Full=Annexin-2-A;
DE AltName: Full=Calpactin I heavy chain;
DE AltName: Full=Calpactin-1 heavy chain;
DE AltName: Full=Lipocortin II;
GN Name=anxa2-a;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Kidney;
RX PubMed=1833269; DOI=10.1016/0378-1119(91)90259-e;
RA Gerke V., Koch W., Thiel C.;
RT "Primary structure and expression of the Xenopus laevis gene encoding
RT annexin II.";
RL Gene 104:259-264(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Tail bud;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JAN-2003) 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.
CC -!- SUBUNIT: Tetramer of 2 light chains (p10 proteins) and 2 heavy chains
CC (p36 proteins).
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}.
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DR EMBL; M60768; AAA49885.1; -; mRNA.
DR EMBL; BC042238; AAH42238.1; -; mRNA.
DR PIR; JQ1297; JQ1297.
DR RefSeq; NP_001081284.1; NM_001087815.1.
DR AlphaFoldDB; P27006; -.
DR SMR; P27006; -.
DR BioGRID; 99093; 1.
DR DNASU; 397754; -.
DR GeneID; 397754; -.
DR KEGG; xla:397754; -.
DR CTD; 397754; -.
DR Xenbase; XB-GENE-6252603; anxa2.S.
DR OMA; EVDLMRI; -.
DR Proteomes; UP000186698; Chromosome 3S.
DR Bgee; 397754; Expressed in zone of skin and 19 other tissues.
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; -; 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 Annexin; Basement membrane; Calcium; Calcium/phospholipid-binding;
KW Extracellular matrix; Phosphoprotein; Reference proteome; Repeat; Secreted.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..340
FT /note="Annexin A2-A"
FT /id="PRO_0000067475"
FT REPEAT 34..105
FT /note="Annexin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT REPEAT 106..177
FT /note="Annexin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT REPEAT 190..262
FT /note="Annexin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT REPEAT 266..337
FT /note="Annexin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT REGION 2..25
FT /note="P10 binding site"
FT /evidence="ECO:0000255"
SQ SEQUENCE 340 AA; 38545 MW; 6FAABBEBB9BBF7AF CRC64;
MALIHEILGK LSLEGNQSCA RQSALGTVKA STNFDAEKDA AAIETAIKTK GVDELTIINI
LTNRSNDQRQ DIAFAYHRRT KKDLASALKG ALSGNLETVM LGLIKTRPQY DASELKASMK
GLGTDEDTLI EIICSRTNKE LLDIQNAYRE LYKTELEKDI VSDTSGDFRK LMVALAKGKR
QEEGSVVDYE KIDQDARELY EAGVKRKGTD VGKWITIMTE RSTPHLQKVF ERYKSYSPYD
MEESIKKEVK GDLENAFLNL VQCIQNKPLY FADRLYESMK GRGTKDKILI RTMVSRSELD
MLKIRKEFKK KYGKSLHYFI GQDTKGDYQR ALFNLCGGDD
