ID   ANX4_FRAAN              Reviewed;         314 AA.
AC   P51074; Q9SBT3;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   27-MAY-2002, sequence version 2.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Annexin-like protein RJ4;
OS   Fragaria ananassa (Strawberry) (Fragaria chiloensis x Fragaria virginiana).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Rosaceae; Rosoideae; Potentilleae; Fragariinae;
OC   Fragaria.
OX   NCBI_TaxID=3747;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. All Star; TISSUE=Fruit;
RA   Yang H.Y., Wang G.L., Xia R., Fang H.J., Jing S.X.;
RT   "Cloning of the complete cDNA encoding annexin in strawberry fruit.";
RL   Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 44-314.
RC   STRAIN=cv. Pajaro; TISSUE=Fruit;
RX   PubMed=7766892; DOI=10.1007/bf00020883;
RA   Wilkinson J.Q., Lanahan M.B., Conner T.W., Klee H.J.;
RT   "Identification of mRNAs with enhanced expression in ripening strawberry
RT   fruit using polymerase chain reaction differential display.";
RL   Plant Mol. Biol. 27:1097-1108(1995).
CC   -!- TISSUE SPECIFICITY: Predominantly in developing fruit.
CC   -!- DEVELOPMENTAL STAGE: Expression is enhanced in ripening fruit.
CC   -!- DOMAIN: A pair of annexin repeats may form one binding site for calcium
CC       and phospholipid.
CC   -!- SIMILARITY: Belongs to the annexin (TC 1.A.31.1) family. {ECO:0000305}.
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DR   EMBL; AF188832; AAF01250.1; -; mRNA.
DR   EMBL; U19941; AAA79922.1; -; mRNA.
DR   PIR; S56674; S56674.
DR   AlphaFoldDB; P51074; -.
DR   SMR; P51074; -.
DR   GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR   GO; GO:0005544; F:calcium-dependent phospholipid binding; IEA:UniProtKB-KW.
DR   GO; GO:0006950; P:response to stress; IEA:UniProt.
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; IPR009118; AnnexinD_plant.
DR   Pfam; PF00191; Annexin; 4.
DR   PRINTS; PR00196; ANNEXIN.
DR   PRINTS; PR01814; ANNEXINPLANT.
DR   SMART; SM00335; ANX; 4.
DR   SUPFAM; SSF47874; SSF47874; 1.
DR   PROSITE; PS00223; ANNEXIN_1; 1.
DR   PROSITE; PS51897; ANNEXIN_2; 4.
PE   2: Evidence at transcript level;
KW   Annexin; Calcium; Calcium/phospholipid-binding; Metal-binding; Repeat.
FT   CHAIN           1..314
FT                   /note="Annexin-like protein RJ4"
FT                   /id="PRO_0000067520"
FT   REPEAT          10..81
FT                   /note="Annexin 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT   REPEAT          82..153
FT                   /note="Annexin 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT   REPEAT          165..236
FT                   /note="Annexin 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT   REPEAT          240..311
FT                   /note="Annexin 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT   BINDING         25
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P93157"
FT   BINDING         27
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P93157"
FT   BINDING         67
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P93157"
FT   BINDING         253
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P93157"
FT   BINDING         255
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P93157"
FT   BINDING         257
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P93157"
FT   BINDING         297
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P93157"
FT   BINDING         298
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:P93157"
FT   CONFLICT        44
FT                   /note="Q -> E (in Ref. 2; AAA79922)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   314 AA;  35622 MW;  E01520F22101B0F8 CRC64;
     MATLVSPPNF CAKEDAEALR KSVKGWGTNE KAIISILGHR NAGQRKEIRA AYEQLYQEDL
     LKPLESELSG DFEKAVYRWT LDPADRDAVL ANVAIKKSTD VYNVIIEISC IHSPEELLAV
     RRAYQLRYKH SVEEDLAAHT TGDIRKLLVA LVTAYRYDGH EINAKLANSE ADILHDAIKD
     KAFNHEEIIR ILSTRSKTQL MATFNKYRDD QGISISKNLL EEGANDFQKA LHTAIRCLND
     PKKYFEKVLR NAIKRVGTDE DALTRVIVTR AERDLRDIKE VYYKKNSVPL EQAVAKDTSG
     DYKAFLLTLL GKED