GIA5_GIAIN
ID GIA5_GIAIN Reviewed; 302 AA.
AC Q4VPQ4;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 52.
DE RecName: Full=Giardin subunit alpha-5;
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=ATCC 50803 / WB-C6;
RX PubMed=15862575; DOI=10.1016/j.ijpara.2004.12.009;
RA Weiland M.E.-L., McArthur A.G., Morrison H.G., Sogin M.L., Svard S.G.;
RT "Annexin-like alpha giardins: a new cytoskeletal gene family in Giardia
RT lamblia.";
RL Int. J. Parasitol. 35:617-626(2005).
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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the annexin family. Giardin subunit alpha
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU01245}.
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DR EMBL; AY781318; AAX07969.1; -; Genomic_DNA.
DR RefSeq; XP_001706959.1; XM_001706907.1.
DR AlphaFoldDB; Q4VPQ4; -.
DR SMR; Q4VPQ4; -.
DR PRIDE; Q4VPQ4; -.
DR GeneID; 5699854; -.
DR KEGG; gla:GL50803_007797; -.
DR VEuPathDB; GiardiaDB:DHA2_7797; -.
DR VEuPathDB; GiardiaDB:GL50581_1671; -.
DR VEuPathDB; GiardiaDB:GL50803_007797; -.
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 SUPFAM; SSF47874; SSF47874; 1.
DR PROSITE; PS51897; ANNEXIN_2; 4.
PE 3: Inferred from homology;
KW Annexin; Cytoplasm; Cytoskeleton; Microtubule; Repeat.
FT CHAIN 1..302
FT /note="Giardin subunit alpha-5"
FT /id="PRO_0000288028"
FT REPEAT 1..72
FT /note="Annexin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT REPEAT 74..144
FT /note="Annexin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT REPEAT 153..226
FT /note="Annexin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT REPEAT 230..298
FT /note="Annexin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
SQ SEQUENCE 302 AA; 33921 MW; 8138A25161A194D5 CRC64;
MTSTVAQICS DLKGAIDKKD ELRIAFIASE YSSPSRLKIA QSYEATYKTP ITEAIKKSLK
GGTAEDLLVN MWVSRHEHRA ELINKALGGS SDEEAIRELV FLCNPEDWHE TASVYNQKYQ
KIMQDAVTKA IGSKSHWAKL VAGWMEHKRE DRGSVENDVK YLKELIDAPV TDGNALAQFF
ASTTPDEYTQ IADKFCEEYN LSIDQALVRP LKENEDDLEA YAAAHFALHG LPVLAAQLIN
KACRPKNGNE RSICRITTLM VDQCLAAKYA YKLYGDMGAD LSRCFDERMA PILRTLWRVT
DA