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ATP-binding cassette sub-family A member 3 (ABC-C transporter) (ATP-binding cassette transporter 3) (ATP-binding cassette 3)

 ABCA3_HUMAN             Reviewed;        1704 AA.
Q99758; B2RU09; Q54A95; Q6P5P9; Q92473;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
24-JAN-2006, sequence version 2.
12-SEP-2018, entry version 162.
RecName: Full=ATP-binding cassette sub-family A member 3;
AltName: Full=ABC-C transporter;
AltName: Full=ATP-binding cassette transporter 3;
Short=ATP-binding cassette 3;
Name=ABCA3; Synonyms=ABC3;
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=Thyroid carcinoma;
PubMed=8706931; DOI=10.1016/0014-5793(96)00700-4;
Klugbauer N., Hofmann F.;
"Primary structure of a novel ABC transporter with a chromosomal
localization on the band encoding the multidrug resistance-associated
protein.";
FEBS Lett. 391:61-65(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=9027511; DOI=10.1006/geno.1996.4500;
Connors T.D., van Raay T.J., Petry L.R., Klinger K.W., Landes G.M.,
Burn T.C.;
"The cloning of a human ABC gene (ABC3) mapping to chromosome
16p13.3.";
Genomics 39:231-234(1997).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Lung;
PubMed=11718719; DOI=10.1016/S0014-5793(01)03056-3;
Yamano G., Funahashi H., Kawanami O., Zhao L., Ban N., Uchida Y.,
Morohoshi T., Ogawa J., Shioda S., Inagaki N.;
"ABCA3 is a lamellar body membrane protein in human lung alveolar type
II cells.";
FEBS Lett. 508:221-225(2001).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS HIS-140 AND SER-766.
SeattleSNPs variation discovery resource;
Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15616553; DOI=10.1038/nature03187;
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X.,
Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A.,
Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.,
Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L.,
Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A.,
Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D.,
Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J.,
Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I.,
Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W.,
Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A.,
Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S.,
Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L.,
Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A.,
Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L.,
Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N.,
Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M.,
Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L.,
Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D.,
Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P.,
Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M.,
Rubin E.M., Pennacchio L.A.;
"The sequence and analysis of duplication-rich human chromosome 16.";
Nature 432:988-994(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Brain, and Lung;
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).
[8]
VARIANTS SMDP3 PRO-101; ASP-568; PRO-1553 AND PRO-1591.
PubMed=15044640; DOI=10.1056/NEJMoa032178;
Shulenin S., Nogee L.M., Annilo T., Wert S.E., Whitsett J.A., Dean M.;
"ABCA3 gene mutations in newborns with fatal surfactant deficiency.";
N. Engl. J. Med. 350:1296-1303(2004).
[9]
VARIANTS [LARGE SCALE ANALYSIS] MET-290; ASP-801 AND GLN-1069.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
-!- FUNCTION: Plays an important role in the formation of pulmonary
surfactant, probably by transporting lipids such as cholesterol.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
protein {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q99758-1; Sequence=Displayed;
Name=2;
IsoId=Q99758-2; Sequence=VSP_056262, VSP_056263;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Highly expressed in lung, followed by brain,
pancreas, skeletal muscle and heart. Weakly expressed in placenta,
kidney and liver. Also expressed in medullary thyroid carcinoma
cells (MTC) and in C-cell carcinoma.
-!- DOMAIN: Multifunctional polypeptide with two homologous halves,
each containing a hydrophobic membrane-anchoring domain and an ATP
binding cassette (ABC) domain. {ECO:0000250}.
-!- DISEASE: Pulmonary surfactant metabolism dysfunction 3 (SMDP3)
[MIM:610921]: A rare lung disorder due to impaired surfactant
homeostasis. It is characterized by alveolar filling with
floccular material that stains positive using the periodic acid-
Schiff method and is derived from surfactant phospholipids and
protein components. Excessive lipoproteins accumulation in the
alveoli results in severe respiratory distress.
{ECO:0000269|PubMed:15044640}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCA
family. {ECO:0000305}.
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/abca3/";
-!- WEB RESOURCE: Name=ABCMdb; Note=Database for mutations in ABC
proteins;
URL="http://abcmutations.hegelab.org/proteinDetails?uniprot_id=Q99758";
-----------------------------------------------------------------------
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EMBL; U78735; AAC50967.1; -; mRNA.
EMBL; X97187; CAA65825.1; -; mRNA.
EMBL; AB070929; BAB86781.1; -; mRNA.
EMBL; DQ073080; AAY57325.1; -; Genomic_DNA.
EMBL; CH471112; EAW85515.1; -; Genomic_DNA.
EMBL; BC020724; AAH20724.1; -; mRNA.
EMBL; BC062779; AAH62779.1; -; mRNA.
EMBL; AC009065; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC098805; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC106820; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC140895; AAI40896.1; -; mRNA.
EMBL; BC146866; AAI46867.1; -; mRNA.
CCDS; CCDS10466.1; -. [Q99758-1]
PIR; A59188; A59188.
PIR; S71363; S71363.
RefSeq; NP_001080.2; NM_001089.2. [Q99758-1]
UniGene; Hs.26630; -.
ProteinModelPortal; Q99758; -.
SMR; Q99758; -.
BioGrid; 106539; 26.
IntAct; Q99758; 2.
MINT; Q99758; -.
STRING; 9606.ENSP00000301732; -.
DrugBank; DB00619; Imatinib.
TCDB; 3.A.1.211.5; the atp-binding cassette (abc) superfamily.
iPTMnet; Q99758; -.
PhosphoSitePlus; Q99758; -.
BioMuta; ABCA3; -.
DMDM; 85700402; -.
MaxQB; Q99758; -.
PaxDb; Q99758; -.
PeptideAtlas; Q99758; -.
PRIDE; Q99758; -.
ProteomicsDB; 78463; -.
Ensembl; ENST00000301732; ENSP00000301732; ENSG00000167972. [Q99758-1]
Ensembl; ENST00000567910; ENSP00000454397; ENSG00000167972. [Q99758-2]
GeneID; 21; -.
KEGG; hsa:21; -.
UCSC; uc002cpy.2; human. [Q99758-1]
CTD; 21; -.
DisGeNET; 21; -.
EuPathDB; HostDB:ENSG00000167972.13; -.
GeneCards; ABCA3; -.
HGNC; HGNC:33; ABCA3.
HPA; HPA007884; -.
MalaCards; ABCA3; -.
MIM; 601615; gene.
MIM; 610921; phenotype.
neXtProt; NX_Q99758; -.
OpenTargets; ENSG00000167972; -.
Orphanet; 264675; Congenital pulmonary alveolar proteinosis.
Orphanet; 217563; Neonatal acute respiratory distress with surfactant metabolism deficiency.
PharmGKB; PA24378; -.
eggNOG; KOG0059; Eukaryota.
eggNOG; COG1131; LUCA.
GeneTree; ENSGT00760000118965; -.
HOGENOM; HOG000006613; -.
HOVERGEN; HBG050435; -.
InParanoid; Q99758; -.
KO; K05643; -.
OMA; WDILLAE; -.
OrthoDB; EOG091G009X; -.
PhylomeDB; Q99758; -.
TreeFam; TF105191; -.
Reactome; R-HSA-1369062; ABC transporters in lipid homeostasis.
Reactome; R-HSA-5683678; Defective ABCA3 causes pulmonary surfactant metabolism dysfunction type 3 (SMDP3).
Reactome; R-HSA-5683826; Surfactant metabolism.
Reactome; R-HSA-5688399; Defective ABCA3 causes pulmonary surfactant metabolism dysfunction 3 (SMDP3).
SIGNOR; Q99758; -.
ChiTaRS; ABCA3; human.
GeneWiki; ABCA3; -.
GenomeRNAi; 21; -.
PRO; PR:Q99758; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000167972; Expressed in 176 organ(s), highest expression level in right lung.
CleanEx; HS_ABCA3; -.
ExpressionAtlas; Q99758; baseline and differential.
Genevisible; Q99758; HS.
GO; GO:0097208; C:alveolar lamellar body; IDA:MGI.
GO; GO:0097233; C:alveolar lamellar body membrane; IEA:Ensembl.
GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; TAS:ProtInc.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
GO; GO:0097232; C:lamellar body membrane; TAS:Reactome.
GO; GO:0016020; C:membrane; TAS:ProtInc.
GO; GO:0005886; C:plasma membrane; IDA:MGI.
GO; GO:0005524; F:ATP binding; TAS:ProtInc.
GO; GO:0042626; F:ATPase activity, coupled to transmembrane movement of substances; TAS:ProtInc.
GO; GO:0005319; F:lipid transporter activity; TAS:Reactome.
GO; GO:0005215; F:transporter activity; TAS:ProtInc.
GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
GO; GO:0006869; P:lipid transport; IBA:GO_Central.
GO; GO:0042493; P:response to drug; TAS:ProtInc.
GO; GO:0051384; P:response to glucocorticoid; IEA:Ensembl.
GO; GO:0055085; P:transmembrane transport; TAS:Reactome.
InterPro; IPR003593; AAA+_ATPase.
InterPro; IPR003439; ABC_transporter-like.
InterPro; IPR017871; ABC_transporter_CS.
InterPro; IPR026082; ABCA.
InterPro; IPR026969; ABCA3.
InterPro; IPR027417; P-loop_NTPase.
PANTHER; PTHR19229; PTHR19229; 1.
PANTHER; PTHR19229:SF98; PTHR19229:SF98; 1.
Pfam; PF00005; ABC_tran; 2.
SMART; SM00382; AAA; 2.
SUPFAM; SSF52540; SSF52540; 2.
PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
1: Evidence at protein level;
Alternative splicing; ATP-binding; Complete proteome;
Disease mutation; Membrane; Nucleotide-binding; Polymorphism;
Reference proteome; Repeat; Transmembrane; Transmembrane helix;
Transport.
CHAIN 1 1704 ATP-binding cassette sub-family A member
3.
/FTId=PRO_0000093293.
TRANSMEM 22 42 Helical. {ECO:0000255}.
TRANSMEM 261 283 Helical. {ECO:0000255}.
TRANSMEM 307 327 Helical. {ECO:0000255}.
TRANSMEM 344 364 Helical. {ECO:0000255}.
TRANSMEM 373 393 Helical. {ECO:0000255}.
TRANSMEM 405 425 Helical. {ECO:0000255}.
TRANSMEM 447 467 Helical. {ECO:0000255}.
TRANSMEM 925 945 Helical. {ECO:0000255}.
TRANSMEM 1100 1120 Helical. {ECO:0000255}.
TRANSMEM 1144 1164 Helical. {ECO:0000255}.
TRANSMEM 1183 1203 Helical. {ECO:0000255}.
TRANSMEM 1213 1233 Helical. {ECO:0000255}.
TRANSMEM 1245 1265 Helical. {ECO:0000255}.
TRANSMEM 1306 1326 Helical. {ECO:0000255}.
DOMAIN 530 763 ABC transporter 1. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
DOMAIN 1381 1614 ABC transporter 2. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
NP_BIND 566 573 ATP 1. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
NP_BIND 1416 1423 ATP 2. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
VAR_SEQ 206 209 YIRE -> EKLG (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_056262.
VAR_SEQ 210 1704 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_056263.
VARIANT 101 101 L -> P (in SMDP3; dbSNP:rs121909182).
{ECO:0000269|PubMed:15044640}.
/FTId=VAR_023497.
VARIANT 140 140 N -> H (in dbSNP:rs45447801).
{ECO:0000269|Ref.4}.
/FTId=VAR_025061.
VARIANT 290 290 L -> M (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035728.
VARIANT 568 568 N -> D (in SMDP3; dbSNP:rs121909184).
{ECO:0000269|PubMed:15044640}.
/FTId=VAR_023498.
VARIANT 766 766 P -> S (in dbSNP:rs45592239).
{ECO:0000269|Ref.4}.
/FTId=VAR_025062.
VARIANT 801 801 E -> D (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035729.
VARIANT 1069 1069 H -> Q (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035730.
VARIANT 1553 1553 L -> P (in SMDP3; dbSNP:rs121909183).
{ECO:0000269|PubMed:15044640}.
/FTId=VAR_023499.
VARIANT 1591 1591 Q -> P (in SMDP3; dbSNP:rs28936691).
{ECO:0000269|PubMed:15044640}.
/FTId=VAR_023500.
CONFLICT 36 36 S -> P (in Ref. 1; AAC50967).
{ECO:0000305}.
CONFLICT 196 196 P -> L (in Ref. 1; AAC50967).
{ECO:0000305}.
SEQUENCE 1704 AA; 191362 MW; 606735C504839D0D CRC64;
MAVLRQLALL LWKNYTLQKR KVLVTVLELF LPLLFSGILI WLRLKIQSEN VPNATIYPGQ
SIQELPLFFT FPPPGDTWEL AYIPSHSDAA KTVTETVRRA LVINMRVRGF PSEKDFEDYI
RYDNCSSSVL AAVVFEHPFN HSKEPLPLAV KYHLRFSYTR RNYMWTQTGS FFLKETEGWH
TTSLFPLFPN PGPREPTSPD GGEPGYIREG FLAVQHAVDR AIMEYHADAA TRQLFQRLTV
TIKRFPYPPF IADPFLVAIQ YQLPLLLLLS FTYTALTIAR AVVQEKERRL KEYMRMMGLS
SWLHWSAWFL LFFLFLLIAA SFMTLLFCVK VKPNVAVLSR SDPSLVLAFL LCFAISTISF
SFMVSTFFSK ANMAAAFGGF LYFFTYIPYF FVAPRYNWMT LSQKLCSCLL SNVAMAMGAQ
LIGKFEAKGM GIQWRDLLSP VNVDDDFCFG QVLGMLLLDS VLYGLVTWYM EAVFPGQFGV
PQPWYFFIMP SYWCGKPRAV AGKEEEDSDP EKALRNEYFE AEPEDLVAGI KIKHLSKVFR
VGNKDRAAVR DLNLNLYEGQ ITVLLGHNGA GKTTTLSMLT GLFPPTSGRA YISGYEISQD
MVQIRKSLGL CPQHDILFDN LTVAEHLYFY AQLKGLSRQK CPEEVKQMLH IIGLEDKWNS
RSRFLSGGMR RKLSIGIALI AGSKVLILDE PTSGMDAISR RAIWDLLQRQ KSDRTIVLTT
HFMDEADLLG DRIAIMAKGE LQCCGSSLFL KQKYGAGYHM TLVKEPHCNP EDISQLVHHH
VPNATLESSA GAELSFILPR ESTHRFEGLF AKLEKKQKEL GIASFGASIT TMEEVFLRVG
KLVDSSMDIQ AIQLPALQYQ HERRASDWAV DSNLCGAMDP SDGIGALIEE ERTAVKLNTG
LALHCQQFWA MFLKKAAYSW REWKMVAAQV LVPLTCVTLA LLAINYSSEL FDDPMLRLTL
GEYGRTVVPF SVPGTSQLGQ QLSEHLKDAL QAEGQEPREV LGDLEEFLIF RASVEGGGFN
ERCLVAASFR DVGERTVVNA LFNNQAYHSP ATALAVVDNL LFKLLCGPHA SIVVSNFPQP
RSALQAAKDQ FNEGRKGFDI ALNLLFAMAF LASTFSILAV SERAVQAKHV QFVSGVHVAS
FWLSALLWDL ISFLIPSLLL LVVFKAFDVR AFTRDGHMAD TLLLLLLYGW AIIPLMYLMN
FFFLGAATAY TRLTIFNILS GIATFLMVTI MRIPAVKLEE LSKTLDHVFL VLPNHCLGMA
VSSFYENYET RRYCTSSEVA AHYCKKYNIQ YQENFYAWSA PGVGRFVASM AASGCAYLIL
LFLIETNLLQ RLRGILCALR RRRTLTELYT RMPVLPEDQD VADERTRILA PSPDSLLHTP
LIIKELSKVY EQRVPLLAVD RLSLAVQKGE CFGLLGFNGA GKTTTFKMLT GEESLTSGDA
FVGGHRISSD VGKVRQRIGY CPQFDALLDH MTGREMLVMY ARLRGIPERH IGACVENTLR
GLLLEPHANK LVRTYSGGNK RKLSTGIALI GEPAVIFLDE PSTGMDPVAR RLLWDTVARA
RESGKAIIIT SHSMEECEAL CTRLAIMVQG QFKCLGSPQH LKSKFGSGYS LRAKVQSEGQ
QEALEEFKAF VDLTFPGSVL EDEHQGMVHY HLPGRDLSWA KVFGILEKAK EKYGVDDYSV
SQISLEQVFL SFAHLQPPTA EEGR


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E1068b ELISA kit ABCC1,ATP-binding cassette sub-family C member 1,Bos taurus,Bovine,Leukotriene C(4) transporter,LTC4 transporter,MRP1,Multidrug resistance-associated protein 1 96T
E1068b ELISA ABCC1,ATP-binding cassette sub-family C member 1,Bos taurus,Bovine,Leukotriene C(4) transporter,LTC4 transporter,MRP1,Multidrug resistance-associated protein 1 96T
E1068h ELISA kit ABCC1,ATP-binding cassette sub-family C member 1,Homo sapiens,Human,Leukotriene C(4) transporter,LTC4 transporter,MRP,MRP1,Multidrug resistance-associated protein 1 96T
E1068h ELISA ABCC1,ATP-binding cassette sub-family C member 1,Homo sapiens,Human,Leukotriene C(4) transporter,LTC4 transporter,MRP,MRP1,Multidrug resistance-associated protein 1 96T
U1068h CLIA ABCC1,ATP-binding cassette sub-family C member 1,Homo sapiens,Human,Leukotriene C(4) transporter,LTC4 transporter,MRP,MRP1,Multidrug resistance-associated protein 1 96T


 

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