ANX2B_XENLA
ID ANX2B_XENLA Reviewed; 340 AA.
AC P24801;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Annexin A2-B;
DE AltName: Full=Annexin II type II;
DE AltName: Full=Annexin-2-B;
DE AltName: Full=Calpactin I heavy chain;
DE AltName: Full=Calpactin-1 heavy chain;
DE AltName: Full=Lipocortin II;
GN Name=anxa2-b;
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=Oocyte;
RX PubMed=1833398; DOI=10.1016/s0021-9258(18)55099-7;
RA Izant J.G., Bryson L.J.;
RT "Xenopus annexin II (calpactin I) heavy chain has a distinct amino
RT terminus.";
RL J. Biol. Chem. 266:18560-18566(1991).
RN [2]
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).
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 -!- TISSUE SPECIFICITY: Adult brain, heart, striated muscle, liver, kidney,
CC and very high levels in skin.
CC -!- DEVELOPMENTAL STAGE: Throughout oogenesis and in mature eggs. Constant
CC levels during early embryogenesis, but decrease at 8h. After
CC midblastula transition, the steady state level increases substantially.
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; M58575; AAA49664.1; -; mRNA.
DR EMBL; M58576; AAA49665.1; -; mRNA.
DR EMBL; M60769; AAA49886.1; -; mRNA.
DR PIR; JQ1298; JQ1298.
DR RefSeq; NP_001081252.1; NM_001087783.1.
DR AlphaFoldDB; P24801; -.
DR SMR; P24801; -.
DR DNASU; 397735; -.
DR GeneID; 397735; -.
DR KEGG; xla:397735; -.
DR CTD; 397735; -.
DR Xenbase; XB-GENE-945322; anxa2.L.
DR OrthoDB; 856254at2759; -.
DR Proteomes; UP000186698; Chromosome 3L.
DR Bgee; 397735; Expressed in intestine 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-B"
FT /id="PRO_0000067476"
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"
FT MOD_RES 27
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000250"
FT VARIANT 244
FT /note="S -> R"
FT VARIANT 258
FT /note="L -> S"
FT CONFLICT 223..224
FT /note="HP -> IS (in Ref. 2; AAA49886)"
FT /evidence="ECO:0000305"
FT CONFLICT 297..298
FT /note="RN -> CE (in Ref. 2; AAA49886)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 340 AA; 38774 MW; 25ABEA0CE2F2EBCD CRC64;
MALIHEILGK LSLEGNQSSS RQSKLGSVKA ATHFDAEKDA AAIETAIKTK GVDELTIINI
LTNRSNEQRQ DIAFAFHRRT KKDLPSALKG ALSGNLETVM LGLIKTRPQY DASELKASMK
GLGTDEDTLI EIICSRTNKE LLDIQNAYRE LFKTELEKDI MSDTSGDFRK LMVALAKGRR
QEDGNMVDYE KIDQDARELY EAGVKRKGTD VTKWITIMTE RSHPHLQKVF ERYKSYSPYD
IEESIKKEVK GDLENAFLNL VQCIQNKPLY FADRLYESMK GKGTKDKILI RIMVSRRNLD
MLKIRQEFKK KYGKSLHYFI GQDTKGDYQR ALLNLCGGDD
