GIA1_GIAIN
ID GIA1_GIAIN Reviewed; 295 AA.
AC P17063;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Giardin subunit alpha-1;
OS Giardia intestinalis (Giardia lamblia).
OC Eukaryota; Metamonada; Diplomonadida; Hexamitidae; Giardiinae; Giardia.
OX NCBI_TaxID=5741;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 3-31.
RC STRAIN=Portland-1;
RX PubMed=2808530; DOI=10.1083/jcb.109.5.2323;
RA Peattie D.A., Alonso R.A., Hein A., Caulfield J.P.;
RT "Ultrastructural localization of giardins to the edges of disk microribbons
RT of Giarida lamblia and the nucleotide and deduced protein sequence of alpha
RT giardin.";
RL J. Cell Biol. 109:2323-2335(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Portland-1;
RX PubMed=1542319; DOI=10.1016/0166-6851(92)90247-h;
RA Alonso R.A., Peattie D.A.;
RT "Nucleotide sequence of a second alpha giardin gene and molecular analysis
RT of the alpha giardin genes and transcripts in Giardia lamblia.";
RL Mol. Biochem. Parasitol. 50:95-104(1992).
CC -!- FUNCTION: Giardins are involved in parasite attachment to the
CC intestinal mucosa and in the cytoskeletal disassembly and reassembly
CC that marks the transition from infectious trophozoite to transmissible
CC cyst. They may interact with other cytoskeletal proteins such as
CC microtubules in the microribbons or crossbridges, to maintain the
CC integrity of the ventral disk.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Note=Most likely in the
CC edges of the ventral disk microribbons.
CC -!- SIMILARITY: Belongs to the annexin family. Giardin subunit alpha
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU01245}.
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DR EMBL; X52485; CAA36727.1; -; Genomic_DNA.
DR PIR; A33735; A33735.
DR RefSeq; XP_001704310.1; XM_001704258.1.
DR PDB; 4EVF; X-ray; 1.90 A; A=1-295.
DR PDB; 4EVH; X-ray; 2.60 A; A=1-295.
DR PDBsum; 4EVF; -.
DR PDBsum; 4EVH; -.
DR AlphaFoldDB; P17063; -.
DR SMR; P17063; -.
DR PRIDE; P17063; -.
DR GeneID; 5697168; -.
DR KEGG; gla:GL50803_0011654; -.
DR VEuPathDB; GiardiaDB:DHA2_11654; -.
DR VEuPathDB; GiardiaDB:GL50581_1672; -.
DR VEuPathDB; GiardiaDB:GL50803_0011654; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005544; F:calcium-dependent phospholipid binding; IEA:InterPro.
DR GO; GO:0007010; P:cytoskeleton organization; IEA:InterPro.
DR Gene3D; 1.10.220.10; -; 4.
DR InterPro; IPR008088; Alpha_giardin.
DR InterPro; IPR018502; Annexin_repeat.
DR InterPro; IPR037104; Annexin_sf.
DR Pfam; PF00191; Annexin; 1.
DR PRINTS; PR01712; ALPHAGIARDIN.
DR SMART; SM00335; ANX; 1.
DR SUPFAM; SSF47874; SSF47874; 1.
DR PROSITE; PS51897; ANNEXIN_2; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Annexin; Cytoplasm; Cytoskeleton; Direct protein sequencing;
KW Microtubule; Repeat.
FT CHAIN 1..295
FT /note="Giardin subunit alpha-1"
FT /id="PRO_0000067522"
FT REPEAT 2..71
FT /note="Annexin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT REPEAT 73..143
FT /note="Annexin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT REPEAT 153..223
FT /note="Annexin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT REPEAT 226..293
FT /note="Annexin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT HELIX 4..16
FT /evidence="ECO:0007829|PDB:4EVF"
FT HELIX 20..28
FT /evidence="ECO:0007829|PDB:4EVF"
FT HELIX 32..46
FT /evidence="ECO:0007829|PDB:4EVF"
FT HELIX 50..57
FT /evidence="ECO:0007829|PDB:4EVF"
FT HELIX 62..70
FT /evidence="ECO:0007829|PDB:4EVF"
FT HELIX 74..87
FT /evidence="ECO:0007829|PDB:4EVF"
FT HELIX 92..99
FT /evidence="ECO:0007829|PDB:4EVF"
FT HELIX 104..118
FT /evidence="ECO:0007829|PDB:4EVF"
FT HELIX 122..130
FT /evidence="ECO:0007829|PDB:4EVF"
FT STRAND 132..134
FT /evidence="ECO:0007829|PDB:4EVF"
FT HELIX 135..145
FT /evidence="ECO:0007829|PDB:4EVF"
FT HELIX 155..167
FT /evidence="ECO:0007829|PDB:4EVF"
FT HELIX 171..180
FT /evidence="ECO:0007829|PDB:4EVF"
FT HELIX 183..196
FT /evidence="ECO:0007829|PDB:4EVF"
FT STRAND 197..199
FT /evidence="ECO:0007829|PDB:4EVF"
FT HELIX 201..208
FT /evidence="ECO:0007829|PDB:4EVF"
FT HELIX 211..225
FT /evidence="ECO:0007829|PDB:4EVF"
FT HELIX 227..240
FT /evidence="ECO:0007829|PDB:4EVF"
FT HELIX 245..255
FT /evidence="ECO:0007829|PDB:4EVF"
FT HELIX 256..258
FT /evidence="ECO:0007829|PDB:4EVF"
FT HELIX 262..265
FT /evidence="ECO:0007829|PDB:4EVF"
FT HELIX 266..268
FT /evidence="ECO:0007829|PDB:4EVF"
FT HELIX 272..279
FT /evidence="ECO:0007829|PDB:4EVF"
FT HELIX 284..292
FT /evidence="ECO:0007829|PDB:4EVF"
SQ SEQUENCE 295 AA; 33890 MW; 9DA8F7318E7E4C50 CRC64;
MPKVTDIANE LKQAIDAKDE VQIAFIASEY SAESREKIAK AYVASYGKEL PDDIKKALKG
GSEESLLMDL FSDRHEVRAQ HIRDALSGRN DHMAFFDTVI LCTPEDWHET VAAYTRMFKK
PLVEDFMKDV GRKEDWCLLM EKWMAHERVS RPGSPEDEAQ RLDQAFDQKN TAYLIDFFGT
VPSAEYRPIA EAFKAQNGKS IEQAIATIYT KTDYYTFYCA HFALLGMHRL AAYLINCACN
DKGDEKRMRR ITGMMVDKCL GAKHAYKIYG DMGTDIERCF DKRMAPILRT LWRVK
