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Annexin A11 (56 kDa autoantigen) (Annexin XI) (Annexin-11) (Calcyclin-associated annexin 50) (CAP-50)

 ANX11_HUMAN             Reviewed;         505 AA.
P50995; B4DVE7;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
27-SEP-2017, entry version 162.
RecName: Full=Annexin A11;
AltName: Full=56 kDa autoantigen;
AltName: Full=Annexin XI;
AltName: Full=Annexin-11;
AltName: Full=Calcyclin-associated annexin 50;
Short=CAP-50;
Name=ANXA11; Synonyms=ANX11;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Teratocarcinoma;
PubMed=7508441;
Misaki Y., Pruijn G.J.M., van der Kemp A.W., van Venrooij W.J.;
"The 56K autoantigen is identical to human annexin XI.";
J. Biol. Chem. 269:4240-4246(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=11013079; DOI=10.1006/geno.2000.6309;
Bances P., Fernandez M.R., Rodriguez-Garcia M.I., Morgan R.O.,
Fernandez M.-P.;
"Annexin A11 (ANXA11) gene structure as the progenitor of paralogous
annexins and source of orthologous cDNA isoforms.";
Genomics 69:95-103(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Spleen;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164054; DOI=10.1038/nature02462;
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Lymph;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
INTERACTION WITH PDCD6.
PubMed=11883939; DOI=10.1006/bbrc.2002.6600;
Satoh H., Shibata H., Nakano Y., Kitaura Y., Maki M.;
"ALG-2 interacts with the amino-terminal domain of annexin XI in a
Ca(2+)-dependent manner.";
Biochem. Biophys. Res. Commun. 291:1166-1172(2002).
[7]
SUBCELLULAR LOCATION.
PubMed=12601007; DOI=10.1074/jbc.M212669200;
Tomas A., Moss S.E.;
"Calcium- and cell cycle-dependent association of annexin 11 with the
nuclear envelope.";
J. Biol. Chem. 278:20210-20216(2003).
[8]
SUBCELLULAR LOCATION.
PubMed=12805373; DOI=10.1074/jbc.M210852200;
Farnaes L., Ditzel H.J.;
"Dissecting the cellular functions of annexin XI using recombinant
human annexin XI-specific autoantibodies cloned by phage display.";
J. Biol. Chem. 278:33120-33126(2003).
[9]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH KIF23.
PubMed=15197175; DOI=10.1083/jcb.200311054;
Tomas A., Futter C., Moss S.E.;
"Annexin 11 is required for midbody formation and completion of the
terminal phase of cytokinesis.";
J. Cell Biol. 165:813-822(2004).
[10]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
TISSUE=Melanoma;
PubMed=17081065; DOI=10.1021/pr060363j;
Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H.,
Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R.,
Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E.,
Hunt D.F.;
"Proteomic and bioinformatic characterization of the biogenesis and
function of melanosomes.";
J. Proteome Res. 5:3135-3144(2006).
[11]
INTERACTION WITH PDCD6.
PubMed=18256029; DOI=10.1074/jbc.M800717200;
Shibata H., Suzuki H., Kakiuchi T., Inuzuka T., Yoshida H., Mizuno T.,
Maki M.;
"Identification of Alix-type and non-Alix-type ALG-2-binding sites in
human phospholipid scramblase 3: differential binding to an
alternatively spliced isoform and amino acid-substituted mutants.";
J. Biol. Chem. 283:9623-9632(2008).
[12]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-248; LYS-255 AND LYS-479,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
-!- FUNCTION: Binds specifically to calcyclin in a calcium-dependent
manner (By similarity). Required for midbody formation and
completion of the terminal phase of cytokinesis. {ECO:0000250,
ECO:0000269|PubMed:15197175}.
-!- SUBUNIT: Interacts with S100A6 (By similarity). Interacts with
PDCD6 in a calcium-dependent manner. Interacts with KIF23 during
cytokinesis. {ECO:0000250, ECO:0000269|PubMed:11883939,
ECO:0000269|PubMed:15197175, ECO:0000269|PubMed:18256029}.
-!- INTERACTION:
Q53EZ4:CEP55; NbExp=5; IntAct=EBI-715243, EBI-747776;
O75340:PDCD6; NbExp=4; IntAct=EBI-715243, EBI-352915;
Q92734:TFG; NbExp=3; IntAct=EBI-715243, EBI-357061;
-!- SUBCELLULAR LOCATION: Cytoplasm. Melanosome. Nucleus envelope.
Nucleus, nucleoplasm. Cytoplasm, cytoskeleton, spindle. Note=Found
throughout the nucleoplasm at interphase and during mitosis
concentrates around the mitotic apparatus (By similarity).
Elevation of intracellular calcium causes relocalization from the
nucleoplasm to the nuclear envelope, with little effect on the
cytoplasmic pool. Localization to the nuclear envelope is cell-
cycle dependent. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P50995-1; Sequence=Displayed;
Name=2;
IsoId=P50995-2; Sequence=VSP_054553;
Note=No experimental confirmation available.;
-!- DOMAIN: A pair of annexin repeats may form one binding site for
calcium and phospholipid.
-!- SIMILARITY: Belongs to the annexin family. {ECO:0000305}.
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EMBL; L19605; AAA19734.1; -; mRNA.
EMBL; AJ278463; CAB94995.1; -; mRNA.
EMBL; AJ278464; CAB94996.1; -; mRNA.
EMBL; AJ278465; CAB94997.1; -; mRNA.
EMBL; AK301047; BAG62659.1; -; mRNA.
EMBL; AL356095; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL513174; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC007564; AAH07564.1; -; mRNA.
CCDS; CCDS60576.1; -. [P50995-2]
CCDS; CCDS7364.1; -. [P50995-1]
PIR; A53152; A53152.
RefSeq; NP_001148.1; NM_001157.2. [P50995-1]
RefSeq; NP_001265336.1; NM_001278407.1. [P50995-1]
RefSeq; NP_001265337.1; NM_001278408.1. [P50995-1]
RefSeq; NP_001265338.1; NM_001278409.1. [P50995-2]
RefSeq; NP_665875.1; NM_145868.1. [P50995-1]
RefSeq; NP_665876.1; NM_145869.1. [P50995-1]
RefSeq; XP_011538038.1; XM_011539736.2. [P50995-1]
UniGene; Hs.530291; -.
ProteinModelPortal; P50995; -.
SMR; P50995; -.
BioGrid; 106808; 49.
ELM; P50995; -.
IntAct; P50995; 21.
MINT; MINT-4998941; -.
STRING; 9606.ENSP00000265447; -.
TCDB; 3.A.5.9.1; the general secretory pathway (sec) family.
iPTMnet; P50995; -.
PhosphoSitePlus; P50995; -.
SwissPalm; P50995; -.
BioMuta; ANXA11; -.
DMDM; 1703322; -.
REPRODUCTION-2DPAGE; P50995; -.
EPD; P50995; -.
PaxDb; P50995; -.
PeptideAtlas; P50995; -.
PRIDE; P50995; -.
DNASU; 311; -.
Ensembl; ENST00000265447; ENSP00000265447; ENSG00000122359. [P50995-2]
Ensembl; ENST00000372231; ENSP00000361305; ENSG00000122359. [P50995-1]
Ensembl; ENST00000422982; ENSP00000404412; ENSG00000122359. [P50995-1]
Ensembl; ENST00000438331; ENSP00000398610; ENSG00000122359. [P50995-1]
GeneID; 311; -.
KEGG; hsa:311; -.
UCSC; uc057umu.1; human. [P50995-1]
CTD; 311; -.
DisGeNET; 311; -.
EuPathDB; HostDB:ENSG00000122359.17; -.
GeneCards; ANXA11; -.
HGNC; HGNC:535; ANXA11.
HPA; CAB004851; -.
HPA; HPA027545; -.
MIM; 602572; gene.
neXtProt; NX_P50995; -.
OpenTargets; ENSG00000122359; -.
PharmGKB; PA24825; -.
eggNOG; KOG0819; Eukaryota.
eggNOG; ENOG410XPUN; LUCA.
GeneTree; ENSGT00760000118972; -.
HOVERGEN; HBG061815; -.
InParanoid; P50995; -.
KO; K17095; -.
OMA; FDAYEIK; -.
OrthoDB; EOG091G0H6H; -.
PhylomeDB; P50995; -.
TreeFam; TF105452; -.
ChiTaRS; ANXA11; human.
GeneWiki; ANXA11; -.
GenomeRNAi; 311; -.
PRO; PR:P50995; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000122359; -.
CleanEx; HS_ANXA11; -.
ExpressionAtlas; P50995; baseline and differential.
Genevisible; P50995; HS.
GO; GO:0042582; C:azurophil granule; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0030496; C:midbody; IDA:UniProtKB.
GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
GO; GO:0045335; C:phagocytic vesicle; IDA:UniProtKB.
GO; GO:0042581; C:specific granule; IDA:UniProtKB.
GO; GO:0005819; C:spindle; IDA:UniProtKB.
GO; GO:0005509; F:calcium ion binding; IEA:Ensembl.
GO; GO:0005544; F:calcium-dependent phospholipid binding; IEA:UniProtKB-KW.
GO; GO:0048306; F:calcium-dependent protein binding; IPI:UniProtKB.
GO; GO:0023026; F:MHC class II protein complex binding; IDA:UniProtKB.
GO; GO:0008429; F:phosphatidylethanolamine binding; IEA:Ensembl.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0044548; F:S100 protein binding; IPI:UniProtKB.
GO; GO:0032506; P:cytokinetic process; IMP:UniProtKB.
GO; GO:0006909; P:phagocytosis; IEP:UniProtKB.
GO; GO:0051592; P:response to calcium ion; IDA:UniProtKB.
Gene3D; 1.10.220.10; -; 4.
InterPro; IPR001464; Annexin.
InterPro; IPR018502; Annexin_repeat.
InterPro; IPR018252; Annexin_repeat_CS.
InterPro; IPR008157; ANX11.
PANTHER; PTHR10502:SF136; PTHR10502:SF136; 1.
Pfam; PF00191; Annexin; 4.
PRINTS; PR00196; ANNEXIN.
PRINTS; PR01810; ANNEXINXI.
SMART; SM00335; ANX; 4.
PROSITE; PS00223; ANNEXIN; 4.
1: Evidence at protein level;
Acetylation; Alternative splicing; Annexin; Calcium;
Calcium/phospholipid-binding; Cell cycle; Cell division;
Complete proteome; Cytoplasm; Cytoskeleton; Nucleus; Polymorphism;
Reference proteome; Repeat.
CHAIN 1 505 Annexin A11.
/FTId=PRO_0000067510.
REPEAT 209 269 Annexin 1.
REPEAT 281 341 Annexin 2.
REPEAT 365 425 Annexin 3.
REPEAT 440 500 Annexin 4.
MOD_RES 248 248 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 255 255 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 479 479 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
VAR_SEQ 1 33 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_054553.
VARIANT 191 191 R -> Q (in dbSNP:rs2229554).
/FTId=VAR_048259.
VARIANT 230 230 R -> C (in dbSNP:rs1049550).
/FTId=VAR_012006.
VARIANT 457 457 I -> V (in dbSNP:rs1802932).
/FTId=VAR_012007.
SEQUENCE 505 AA; 54390 MW; 4ADCAC8F270BFEE4 CRC64;
MSYPGYPPPP GGYPPAAPGG GPWGGAAYPP PPSMPPIGLD NVATYAGQFN QDYLSGMAAN
MSGTFGGANM PNLYPGAPGA GYPPVPPGGF GQPPSAQQPV PPYGMYPPPG GNPPSRMPSY
PPYPGAPVPG QPMPPPGQQP PGAYPGQPPV TYPGQPPVPL PGQQQPVPSY PGYPGSGTVT
PAVPPTQFGS RGTITDAPGF DPLRDAEVLR KAMKGFGTDE QAIIDCLGSR SNKQRQQILL
SFKTAYGKDL IKDLKSELSG NFEKTILALM KTPVLFDIYE IKEAIKGVGT DEACLIEILA
SRSNEHIREL NRAYKAEFKK TLEEAIRSDT SGHFQRLLIS LSQGNRDEST NVDMSLAQRD
AQELYAAGEN RLGTDESKFN AVLCSRSRAH LVAVFNEYQR MTGRDIEKSI CREMSGDLEE
GMLAVVKCLK NTPAFFAERL NKAMRGAGTK DRTLIRIMVS RSETDLLDIR SEYKRMYGKS
LYHDISGDTS GDYRKILLKI CGGND


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U1731h CLIA 35-beta calcimedin,Annexin A4,Annexin IV,Annexin-4,ANX4,ANXA4,Carbohydrate-binding protein p33_p41,Chromobindin-4,Endonexin I,Homo sapiens,Human,Lipocortin IV,P32.5,PAP-II,Placental anticoagulant 96T
E1731h ELISA 35-beta calcimedin,Annexin A4,Annexin IV,Annexin-4,ANX4,ANXA4,Carbohydrate-binding protein p33_p41,Chromobindin-4,Endonexin I,Homo sapiens,Human,Lipocortin IV,P32.5,PAP-II,Placental anticoagulan 96T
15-288-22296 Annexin A9 - Annexin-31; Annexin XXXI; Pemphaxin Polyclonal 0.1 mg
15-288-22296 Annexin A9 - Annexin-31; Annexin XXXI; Pemphaxin Polyclonal 0.05 mg
28-552 Annexin A4 (ANXA4) belongs to the annexin family of calcium-dependent phospholipid binding proteins. Although their functions are still not clearly defined, several members of the annexin family have 0.1 mg
25-366 Annexin IV (ANX4) belongs to the annexin family of calcium-dependent phospholipid binding proteins. Although their functions are still not clearly defined, several members of the annexin family have b 0.05 mg
U1731p CLIA 35-beta calcimedin,Annexin A4,Annexin IV,Annexin-4,ANX4,ANXA4,Chromobindin-4,Endonexin I,Lipocortin IV,P32.5,PAP-II,Pig,Placental anticoagulant protein II,PP4-X,Protein II,Sus scrofa 96T
E1731p ELISA 35-beta calcimedin,Annexin A4,Annexin IV,Annexin-4,ANX4,ANXA4,Chromobindin-4,Endonexin I,Lipocortin IV,P32.5,PAP-II,Pig,Placental anticoagulant protein II,PP4-X,Protein II,Sus scrofa 96T


 

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