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Annexin

 G3I5L3_CRIGR            Unreviewed;       346 AA.
G3I5L3;
16-NOV-2011, integrated into UniProtKB/TrEMBL.
16-NOV-2011, sequence version 1.
20-JUN-2018, entry version 41.
RecName: Full=Annexin {ECO:0000256|RuleBase:RU003540};
ORFNames=H671_3g10393 {ECO:0000313|EMBL:ERE78391.1},
I79_018766 {ECO:0000313|EMBL:EGW02515.1};
Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Cricetidae; Cricetinae; Cricetulus.
NCBI_TaxID=10029 {ECO:0000313|EMBL:EGW02515.1, ECO:0000313|Proteomes:UP000001075};
[1] {ECO:0000313|Proteomes:UP000001075}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=CHO K1 cell line {ECO:0000313|Proteomes:UP000001075};
PubMed=21804562; DOI=10.1038/nbt.1932;
Xu X., Nagarajan H., Lewis N.E., Pan S., Cai Z., Liu X., Chen W.,
Xie M., Wang W., Hammond S., Andersen M.R., Neff N., Passarelli B.,
Koh W., Fan H.C., Wang J., Gui Y., Lee K.H., Betenbaugh M.J.,
Quake S.R., Famili I., Palsson B.O., Wang J.;
"The genomic sequence of the Chinese hamster ovary (CHO)-K1 cell
line.";
Nat. Biotechnol. 29:735-741(2011).
[2] {ECO:0000313|EMBL:EGW02515.1}
NUCLEOTIDE SEQUENCE.
Xu X., Nagarajan H., Lewis N.E., Pan S., Cai Z., Liu X., Chen W.,
Xie M., Wang W., Hammond S., Andersen M.R., Neff N., Passarelli B.,
Koh W., Fan C.H., Wang J., Gui Y., Lee K.H., Betenbaugh M.J.,
Quake S.R., Famili I., Palsson B.O., Wang J.;
"The genomic sequence of the Chinese hamster ovary CHO-K1 cell line.";
Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
[3] {ECO:0000313|Proteomes:UP000030759}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=17A/GY {ECO:0000313|Proteomes:UP000030759};
PubMed=23929341; DOI=10.1038/nbt.2645;
Brinkrolf K., Rupp O., Laux H., Kollin F., Ernst W., Linke B.,
Kofler R., Romand S., Hesse F., Budach W.E., Galosy S., Muller D.,
Noll T., Wienberg J., Jostock T., Leonard M., Grillari J., Tauch A.,
Goesmann A., Helk B., Mott J.E., Puhler A., Borth N.;
"Chinese hamster genome sequenced from sorted chromosomes.";
Nat. Biotechnol. 31:694-695(2013).
[4] {ECO:0000313|EMBL:ERE78391.1}
NUCLEOTIDE SEQUENCE.
STRAIN=17A/GY {ECO:0000313|EMBL:ERE78391.1};
Brinkrolf K., Rupp O., Laux H., Kollin F., Ernst W., Linke B.,
Kofler R., Romand S., Hesse F., Budach W.E., Galosy S., Muller D.,
Noll T., Wienberg J., Jostock T., Leonard M., Grillari J., Tauch A.,
Goesmann A., Helk B., Mott J.E., Puehler A., Borth N.;
"Chinese hamster genome sequenced from sorted chromosomes.";
Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
-!- DOMAIN: The full-length protein can bind eight Ca(2+) ions via the
annexin repeats. Calcium binding causes a major conformation
change that modifies dimer contacts and leads to surface exposure
of the N-terminal phosphorylation sites; in the absence of Ca(2+),
these sites are buried in the interior of the protein core. The N-
terminal region becomes disordered in response to calcium-binding.
{ECO:0000256|RuleBase:RU003540}.
-!- SIMILARITY: Belongs to the annexin family.
{ECO:0000256|RuleBase:RU003540}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; JH001310; EGW02515.1; -; Genomic_DNA.
EMBL; KE673090; ERE78391.1; -; Genomic_DNA.
RefSeq; XP_003510519.1; XM_003510471.2.
RefSeq; XP_007620413.1; XM_007622223.1.
PRIDE; G3I5L3; -.
GeneID; 100768079; -.
KEGG; cge:100768079; -.
CTD; 301; -.
KO; K17091; -.
Proteomes; UP000001075; Unassembled WGS sequence.
Proteomes; UP000030759; Unassembled WGS sequence.
GO; GO:0005884; C:actin filament; IEA:Ensembl.
GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
GO; GO:0001533; C:cornified envelope; IEA:Ensembl.
GO; GO:0005829; C:cytosol; IEA:Ensembl.
GO; GO:0005768; C:endosome; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
GO; GO:0031232; C:extrinsic component of external side of plasma membrane; IEA:Ensembl.
GO; GO:0016328; C:lateral plasma membrane; IEA:Ensembl.
GO; GO:0031514; C:motile cilium; IEA:Ensembl.
GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
GO; GO:0042383; C:sarcolemma; IEA:Ensembl.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0005544; F:calcium-dependent phospholipid binding; IEA:UniProtKB-KW.
GO; GO:0048306; F:calcium-dependent protein binding; IEA:Ensembl.
GO; GO:0019834; F:phospholipase A2 inhibitor activity; IEA:Ensembl.
GO; GO:0030674; F:protein binding, bridging; IEA:Ensembl.
GO; GO:0005198; F:structural molecule activity; IEA:Ensembl.
GO; GO:0031532; P:actin cytoskeleton reorganization; IEA:Ensembl.
GO; GO:0046632; P:alpha-beta T cell differentiation; IEA:Ensembl.
GO; GO:0050482; P:arachidonic acid secretion; IEA:Ensembl.
GO; GO:0071385; P:cellular response to glucocorticoid stimulus; IEA:Ensembl.
GO; GO:0035924; P:cellular response to vascular endothelial growth factor stimulus; IEA:Ensembl.
GO; GO:0007187; P:G-protein coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger; IEA:Ensembl.
GO; GO:0071621; P:granulocyte chemotaxis; IEA:Ensembl.
GO; GO:0006954; P:inflammatory response; IEA:Ensembl.
GO; GO:0030216; P:keratinocyte differentiation; IEA:Ensembl.
GO; GO:0002548; P:monocyte chemotaxis; IEA:Ensembl.
GO; GO:0014839; P:myoblast migration involved in skeletal muscle regeneration; IEA:Ensembl.
GO; GO:0045920; P:negative regulation of exocytosis; IEA:Ensembl.
GO; GO:2000483; P:negative regulation of interleukin-8 secretion; IEA:Ensembl.
GO; GO:0045629; P:negative regulation of T-helper 2 cell differentiation; IEA:Ensembl.
GO; GO:0097350; P:neutrophil clearance; IEA:Ensembl.
GO; GO:0018149; P:peptide cross-linking; IEA:Ensembl.
GO; GO:0006909; P:phagocytosis; IEA:Ensembl.
GO; GO:0090050; P:positive regulation of cell migration involved in sprouting angiogenesis; IEA:Ensembl.
GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; IEA:Ensembl.
GO; GO:0032743; P:positive regulation of interleukin-2 production; IEA:Ensembl.
GO; GO:0033031; P:positive regulation of neutrophil apoptotic process; IEA:Ensembl.
GO; GO:0042102; P:positive regulation of T cell proliferation; IEA:Ensembl.
GO; GO:0045627; P:positive regulation of T-helper 1 cell differentiation; IEA:Ensembl.
GO; GO:0031340; P:positive regulation of vesicle fusion; IEA:Ensembl.
GO; GO:0090303; P:positive regulation of wound healing; IEA:Ensembl.
GO; GO:0008360; P:regulation of cell shape; IEA:Ensembl.
GO; GO:0046883; P:regulation of hormone secretion; IEA:Ensembl.
GO; GO:0050727; P:regulation of inflammatory response; IEA:Ensembl.
GO; GO:0032652; P:regulation of interleukin-1 production; IEA:Ensembl.
GO; GO:0002685; P:regulation of leukocyte migration; IEA:Ensembl.
Gene3D; 1.10.220.10; -; 4.
InterPro; IPR001464; Annexin.
InterPro; IPR018502; Annexin_repeat.
InterPro; IPR018252; Annexin_repeat_CS.
InterPro; IPR037104; Annexin_sf.
InterPro; IPR002388; ANX1.
PANTHER; PTHR10502:SF17; PTHR10502:SF17; 1.
Pfam; PF00191; Annexin; 4.
PRINTS; PR00196; ANNEXIN.
PRINTS; PR00197; ANNEXINI.
SMART; SM00335; ANX; 4.
PROSITE; PS00223; ANNEXIN; 3.
3: Inferred from homology;
Annexin {ECO:0000256|RuleBase:RU003540,
ECO:0000256|SAAS:SAAS00869627};
Calcium {ECO:0000256|RuleBase:RU003540};
Calcium/phospholipid-binding {ECO:0000256|RuleBase:RU003540};
Complete proteome {ECO:0000313|Proteomes:UP000001075};
Reference proteome {ECO:0000313|Proteomes:UP000001075};
Repeat {ECO:0000256|RuleBase:RU003540, ECO:0000256|SAAS:SAAS00429366}.
SEQUENCE 346 AA; 38862 MW; EF7751BC70910308 CRC64;
MAMVSEFLKQ AWFIDNQEQE YVQAVKSSKG GPGSAVSPYP SFNPSSDVAA LHKAIMVKGV
DEATIIDILT KRTNAQRQQI KAAYLQETGK PLDEMLRKAL TGHLEEVVLA LLKTPAQFDA
DELRAAMKGL GTDEDTLIEI LVSRNNREIR EINRVYREEL KRDLAKDITS DTSGDFRKAL
LSLAKGDRCE DLSVNQDLAD TDARALYEAG ERRKGTDTNV FITILTTRSK SHLRKVFQNY
RKYSEHDMNK VLDLEMKGDI EKCLTALVKC STSTPAFFAE KLYEAMKGAG TRHKALIRIM
VSRSEIDMNE IKAFYLKKYG ISLCQAILDE TKGDYEKILV ALCDGN


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