ANXE1_GIAIN
ID ANXE1_GIAIN Reviewed; 337 AA.
AC Q9NFS4; Q24981;
DT 11-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Annexin E1;
DE AltName: Full=Annexin 21;
DE AltName: Full=Annexin XXI;
GN Name=ANXE1; Synonyms=ANX21;
OS Giardia intestinalis (Giardia lamblia).
OC Eukaryota; Metamonada; Diplomonadida; Hexamitidae; Giardiinae; Giardia.
OX NCBI_TaxID=5741;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Upcroft P., Healey A., Upcroft J.A., Townson S.M.;
RL Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SUBCELLULAR LOCATION.
RX PubMed=12006598; DOI=10.1074/jbc.m203260200;
RA Szkodowska A., Mueller M.C.M., Linke C., Scholze H.;
RT "Annexin XXI (ANX21) of Giardia lamblia has sequence motifs uniquely shared
RT by giardial annexins and is specifically localized in the flagella.";
RL J. Biol. Chem. 277:25703-25706(2002).
CC -!- FUNCTION: May function as a calcium-regulated structural element
CC linking phospholipid bilayer and underlying axoneme.
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium, flagellum
CC {ECO:0000269|PubMed:12006598}.
CC -!- DOMAIN: A pair of annexin repeats may form one binding site for calcium
CC and phospholipid.
CC -!- SIMILARITY: Belongs to the annexin family. {ECO:0000255|PROSITE-
CC ProRule:PRU01245}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA74893.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; L27221; AAA74893.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AJ271737; CAB86987.1; -; Genomic_DNA.
DR PIR; T18527; T18527.
DR PDB; 3CHJ; X-ray; 1.60 A; A=1-337.
DR PDB; 3CHK; X-ray; 1.65 A; A=1-337.
DR PDB; 3CHL; X-ray; 1.90 A; A=1-337.
DR PDBsum; 3CHJ; -.
DR PDBsum; 3CHK; -.
DR PDBsum; 3CHL; -.
DR AlphaFoldDB; Q9NFS4; -.
DR SMR; Q9NFS4; -.
DR PRIDE; Q9NFS4; -.
DR VEuPathDB; GiardiaDB:DHA2_15097; -.
DR VEuPathDB; GiardiaDB:GL50581_4146; -.
DR VEuPathDB; GiardiaDB:GL50803_0015097; -.
DR eggNOG; KOG0819; Eukaryota.
DR EvolutionaryTrace; Q9NFS4; -.
DR GO; GO:0031514; C:motile cilium; IEA:UniProtKB-SubCell.
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:0030030; P:cell projection organization; IEA:UniProtKB-KW.
DR Gene3D; 1.10.220.10; -; 4.
DR InterPro; IPR001464; Annexin.
DR InterPro; IPR018502; Annexin_repeat.
DR InterPro; IPR037104; Annexin_sf.
DR Pfam; PF00191; Annexin; 2.
DR PRINTS; PR00196; ANNEXIN.
DR SMART; SM00335; ANX; 2.
DR SUPFAM; SSF47874; SSF47874; 1.
DR PROSITE; PS51897; ANNEXIN_2; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Annexin; Calcium; Calcium/phospholipid-binding;
KW Cell projection; Cilium; Cilium biogenesis/degradation; Flagellum; Repeat.
FT CHAIN 1..337
FT /note="Annexin E1"
FT /id="PRO_0000067521"
FT REPEAT 10..80
FT /note="Annexin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT REPEAT 81..154
FT /note="Annexin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT REPEAT 161..238
FT /note="Annexin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT REPEAT 242..312
FT /note="Annexin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT HELIX 12..24
FT /evidence="ECO:0007829|PDB:3CHJ"
FT HELIX 26..30
FT /evidence="ECO:0007829|PDB:3CHJ"
FT HELIX 31..38
FT /evidence="ECO:0007829|PDB:3CHJ"
FT HELIX 41..55
FT /evidence="ECO:0007829|PDB:3CHJ"
FT HELIX 59..64
FT /evidence="ECO:0007829|PDB:3CHJ"
FT HELIX 69..78
FT /evidence="ECO:0007829|PDB:3CHJ"
FT HELIX 82..94
FT /evidence="ECO:0007829|PDB:3CHJ"
FT STRAND 95..98
FT /evidence="ECO:0007829|PDB:3CHJ"
FT HELIX 101..108
FT /evidence="ECO:0007829|PDB:3CHJ"
FT HELIX 113..127
FT /evidence="ECO:0007829|PDB:3CHJ"
FT HELIX 131..139
FT /evidence="ECO:0007829|PDB:3CHJ"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:3CHJ"
FT HELIX 144..154
FT /evidence="ECO:0007829|PDB:3CHJ"
FT HELIX 162..177
FT /evidence="ECO:0007829|PDB:3CHJ"
FT STRAND 178..180
FT /evidence="ECO:0007829|PDB:3CHJ"
FT HELIX 183..185
FT /evidence="ECO:0007829|PDB:3CHJ"
FT HELIX 186..195
FT /evidence="ECO:0007829|PDB:3CHJ"
FT HELIX 198..211
FT /evidence="ECO:0007829|PDB:3CHJ"
FT TURN 212..214
FT /evidence="ECO:0007829|PDB:3CHJ"
FT HELIX 217..224
FT /evidence="ECO:0007829|PDB:3CHJ"
FT HELIX 227..241
FT /evidence="ECO:0007829|PDB:3CHJ"
FT HELIX 243..254
FT /evidence="ECO:0007829|PDB:3CHJ"
FT STRAND 257..259
FT /evidence="ECO:0007829|PDB:3CHJ"
FT HELIX 262..272
FT /evidence="ECO:0007829|PDB:3CHJ"
FT TURN 273..275
FT /evidence="ECO:0007829|PDB:3CHJ"
FT HELIX 279..287
FT /evidence="ECO:0007829|PDB:3CHJ"
FT HELIX 291..298
FT /evidence="ECO:0007829|PDB:3CHJ"
FT HELIX 301..310
FT /evidence="ECO:0007829|PDB:3CHJ"
SQ SEQUENCE 337 AA; 38584 MW; 617CC6FC93DC629B CRC64;
MANKNYQMST GVTAVVQKVV EACQDESKRL DLIEIARSYP PNQLRNMQRT FQAITGTFLD
AFLKKHLSKD FESLVLMLYK PRAQLLCELI RGATKGAGTD EKCLVDVLLT IETHEVREIR
QLYYQLYNDS LGDVVRKDCG DKYMWAKLIN AVATGDRIPR DTHELEEDLV LVRKAIETKG
VKKDEVSTWI RIFATYTRAD FRQLHKMYSA KYNGDSLRAG VEDEFQGLDE YAFKLAHDFL
YDPCCAAAFS MNVAFAGSGS DSNRLNRITA MHFRECKGCK YYYKKVYGQA FDERCATELK
GVYGDAIKLL WEPVTVPLLS MDDYQGSEQH RPMTLEL
