GIA2_GIAIN
ID GIA2_GIAIN Reviewed; 296 AA.
AC P19389;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Giardin subunit alpha-2;
OS Giardia intestinalis (Giardia lamblia).
OC Eukaryota; Metamonada; Diplomonadida; Hexamitidae; Giardiinae; Giardia.
OX NCBI_TaxID=5741;
RN [1]
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; M34550; AAA29150.1; -; Genomic_DNA.
DR PIR; A45645; A45645.
DR RefSeq; XP_001706958.1; XM_001706906.1.
DR AlphaFoldDB; P19389; -.
DR SMR; P19389; -.
DR PRIDE; P19389; -.
DR GeneID; 5699853; -.
DR KEGG; gla:GL50803_007796; -.
DR VEuPathDB; GiardiaDB:DHA2_7796; -.
DR VEuPathDB; GiardiaDB:GL50581_1672; -.
DR VEuPathDB; GiardiaDB:GL50803_007796; -.
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 3: Inferred from homology;
KW Annexin; Cytoplasm; Cytoskeleton; Microtubule; Repeat.
FT CHAIN 1..296
FT /note="Giardin subunit alpha-2"
FT /id="PRO_0000067523"
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"
SQ SEQUENCE 296 AA; 33936 MW; AA9C79312C716A54 CRC64;
MPKLSQIVAD MKQAIDAKDE AQIAFIASEY SADARQRIAQ GYRDQYGKEL PDDIKKALKG
GSEESLLMDL FSDRHEVRAQ HIRDALSGKN DHMAFFDTVI LCTPEDWHET VAAYTRMFKK
PLVEDFMKDV GRKENWCLFM EKWMAHERTS REGSPDEEAE KLNKAFSESD HDYISSFMAG
VPPEEYKSIN TSFKSLTGKG IDQAFATIYT GTDYYSLYCA HFALLGMHKL AAYLVNCACN
DKGDEKRMRR ITGMMVDKCL AAKYAYKTYG SMKADVERCF DKRMAPILCT LWRLRE