ID S39A8_HUMAN Reviewed; 460 AA.
AC Q9C0K1; B4E2H3; Q96SM9; Q9BVC0; Q9NSA4;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 10-MAY-2017, entry version 121.
DE RecName: Full=Zinc transporter ZIP8;
DE AltName: Full=BCG-induced integral membrane protein in monocyte clone 103 protein;
DE AltName: Full=LIV-1 subfamily of ZIP zinc transporter 6;
DE Short=LZT-Hs6;
DE AltName: Full=Solute carrier family 39 member 8;
DE AltName: Full=Zrt- and Irt-like protein 8;
DE Short=ZIP-8;
GN Name=SLC39A8; Synonyms=BIGM103, ZIP8; ORFNames=PP3105;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY,
RP SUBCELLULAR LOCATION, INDUCTION BY PHORBOL ESTER; TNFA AND
RP MYCOBACTERIUM BOVIS BCG CELL WALL, AND FUNCTION.
RX PubMed=12504855; DOI=10.1006/geno.2002.7000;
RA Begum N.A., Kobayashi M., Moriwaki Y., Matsumoto M., Toyoshima K.,
RA Seya T.;
RT "Mycobacterium bovis BCG cell wall and lipopolysaccharide induce a
RT novel gene, BIGM103, encoding a 7-TM protein: identification of a new
RT protein family having Zn-transporter and Zn-metalloprotease
RT signatures.";
RL Genomics 80:630-645(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Trachea;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=15498874; DOI=10.1073/pnas.0404089101;
RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H.,
RA Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y.,
RA Shu H., Chen X., Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S.,
RA Gu J.;
RT "Large-scale cDNA transfection screening for genes related to cancer
RT development and progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 4.";
RL Nature 434:724-731(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Cervix, and Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP VARIANT CDG2N ARG-38, AND FUNCTION.
RX PubMed=26637978; DOI=10.1016/j.ajhg.2015.11.002;
RG Care4Rare Canada Consortium;
RA Boycott K.M., Beaulieu C.L., Kernohan K.D., Gebril O.H., Mhanni A.,
RA Chudley A.E., Redl D., Qin W., Hampson S., Kuery S., Tetreault M.,
RA Puffenberger E.G., Scott J.N., Bezieau S., Reis A., Uebe S.,
RA Schumacher J., Hegele R.A., McLeod D.R., Galvez-Peralta M.,
RA Majewski J., Ramaekers V.T., Nebert D.W., Innes A.M.,
RA Parboosingh J.S., Abou Jamra R.;
RT "Autosomal-recessive intellectual disability with cerebellar atrophy
RT syndrome caused by mutation of the manganese and zinc transporter gene
RT SLC39A8.";
RL Am. J. Hum. Genet. 97:886-893(2015).
RN [8]
RP VARIANTS CDG2N MET-33; ARG-38; CYS-204; THR-335 AND ASN-340.
RX PubMed=26637979; DOI=10.1016/j.ajhg.2015.11.003;
RA Park J.H., Hogrebe M., Grueneberg M., DuChesne I.,
RA von der Heiden A.L., Reunert J., Schlingmann K.P., Boycott K.M.,
RA Beaulieu C.L., Mhanni A.A., Innes A.M., Hoertnagel K., Biskup S.,
RA Gleixner E.M., Kurlemann G., Fiedler B., Omran H., Rutsch F., Wada Y.,
RA Tsiakas K., Santer R., Nebert D.W., Rust S., Marquardt T.;
RT "SLC39A8 deficiency: a disorder of manganese transport and
RT glycosylation.";
RL Am. J. Hum. Genet. 97:894-903(2015).
CC -!- FUNCTION: Acts as a manganese and zinc influx transporter
CC (PubMed:12504855, PubMed:26637978). Plays a role in manganese
CC reabsorption in the proximal tubule of the kidney and in manganese
CC uptake into the brain (PubMed:26637978).
CC {ECO:0000269|PubMed:12504855, ECO:0000305|PubMed:26637978}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}. Note=Associated with the
CC lysosomal/endosomal compartment following transfection.
CC {ECO:0000269|PubMed:12504855}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9C0K1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9C0K1-2; Sequence=VSP_029884, VSP_029885;
CC Note=No experimental confirmation available.;
CC Name=3;
CC IsoId=Q9C0K1-3; Sequence=VSP_043675;
CC Note=No experimental confirmation available.;
CC -!- TISSUE SPECIFICITY: Expressed in thymus, placenta, lung, liver,
CC pancreas and, to a lower extent, in spleen, testis, ovary, small
CC intestine, colon, leukocyte, heart. Highest expression is observed
CC in pancreas. {ECO:0000269|PubMed:12504855}.
CC -!- INDUCTION: By live and heat-killed Mycobacterium bovis bacterial
CC cell wall and inflammatory cytokines like TNF. Down-regulated
CC following phorbol ester treatment. {ECO:0000269|PubMed:12504855}.
CC -!- DISEASE: Congenital disorder of glycosylation 2N (CDG2N)
CC [MIM:616721]: A form of congenital disorder of glycosylation, a
CC genetically heterogeneous group of autosomal recessive,
CC multisystem disorders caused by a defect in glycoprotein
CC biosynthesis and characterized by under-glycosylated serum
CC glycoproteins. Congenital disorders of glycosylation result in a
CC wide variety of clinical features, such as defects in the nervous
CC system development, psychomotor retardation, dysmorphic features,
CC hypotonia, coagulation disorders, and immunodeficiency. The broad
CC spectrum of features reflects the critical role of N-glycoproteins
CC during embryonic development, differentiation, and maintenance of
CC cell functions. {ECO:0000269|PubMed:26637978,
CC ECO:0000269|PubMed:26637979}. Note=The disease is caused by
CC mutations affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the ZIP transporter (TC 2.A.5) family.
CC {ECO:0000305}.
CC -----------------------------------------------------------------------
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DR EMBL; AB020970; BAA96442.1; -; mRNA.
DR EMBL; AB040120; BAB21559.1; -; mRNA.
DR EMBL; AK027652; BAB55268.1; -; mRNA.
DR EMBL; AK304274; BAG65135.1; -; mRNA.
DR EMBL; AF193052; AAG22480.1; -; mRNA.
DR EMBL; AC098487; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP002023; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471057; EAX06130.1; -; Genomic_DNA.
DR EMBL; BC001320; AAH01320.1; -; mRNA.
DR EMBL; BC012125; AAH12125.1; -; mRNA.
DR CCDS; CCDS3656.1; -. [Q9C0K1-1]
DR CCDS; CCDS47117.1; -. [Q9C0K1-3]
DR RefSeq; NP_001128618.1; NM_001135146.1. [Q9C0K1-1]
DR RefSeq; NP_001128619.1; NM_001135147.1. [Q9C0K1-3]
DR RefSeq; NP_001128620.1; NM_001135148.1. [Q9C0K1-2]
DR RefSeq; NP_071437.3; NM_022154.5. [Q9C0K1-1]
DR RefSeq; XP_005263234.1; XM_005263177.1. [Q9C0K1-1]
DR RefSeq; XP_016864029.1; XM_017008540.1. [Q9C0K1-1]
DR RefSeq; XP_016864030.1; XM_017008541.1. [Q9C0K1-2]
DR UniGene; Hs.288034; -.
DR ProteinModelPortal; Q9C0K1; -.
DR SMR; Q9C0K1; -.
DR BioGrid; 122072; 26.
DR STRING; 9606.ENSP00000349174; -.
DR TCDB; 2.A.5.4.15; the zinc (zn(2+))-iron (fe(2+)) permease (zip) family.
DR iPTMnet; Q9C0K1; -.
DR PhosphoSitePlus; Q9C0K1; -.
DR BioMuta; SLC39A8; -.
DR DMDM; 74733496; -.
DR EPD; Q9C0K1; -.
DR MaxQB; Q9C0K1; -.
DR PaxDb; Q9C0K1; -.
DR PeptideAtlas; Q9C0K1; -.
DR PRIDE; Q9C0K1; -.
DR DNASU; 64116; -.
DR Ensembl; ENST00000356736; ENSP00000349174; ENSG00000138821. [Q9C0K1-1]
DR Ensembl; ENST00000394833; ENSP00000378310; ENSG00000138821. [Q9C0K1-1]
DR Ensembl; ENST00000424970; ENSP00000394548; ENSG00000138821. [Q9C0K1-3]
DR GeneID; 64116; -.
DR KEGG; hsa:64116; -.
DR UCSC; uc003hwb.2; human. [Q9C0K1-1]
DR CTD; 64116; -.
DR DisGeNET; 64116; -.
DR GeneCards; SLC39A8; -.
DR HGNC; HGNC:20862; SLC39A8.
DR HPA; HPA038832; -.
DR HPA; HPA038833; -.
DR MalaCards; SLC39A8; -.
DR MIM; 608732; gene.
DR MIM; 616721; phenotype.
DR neXtProt; NX_Q9C0K1; -.
DR OpenTargets; ENSG00000138821; -.
DR PharmGKB; PA134931507; -.
DR eggNOG; KOG2693; Eukaryota.
DR eggNOG; COG0428; LUCA.
DR GeneTree; ENSGT00760000119115; -.
DR HOGENOM; HOG000070225; -.
DR HOVERGEN; HBG108450; -.
DR InParanoid; Q9C0K1; -.
DR KO; K14714; -.
DR OMA; FFVERVL; -.
DR OrthoDB; EOG091G064Y; -.
DR PhylomeDB; Q9C0K1; -.
DR TreeFam; TF318470; -.
DR Reactome; R-HSA-442380; Zinc influx into cells by the SLC39 gene family.
DR ChiTaRS; SLC39A8; human.
DR GenomeRNAi; 64116; -.
DR PRO; PR:Q9C0K1; -.
DR Proteomes; UP000005640; Chromosome 4.
DR Bgee; ENSG00000138821; -.
DR CleanEx; HS_SLC39A8; -.
DR ExpressionAtlas; Q9C0K1; baseline and differential.
DR Genevisible; Q9C0K1; HS.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0031090; C:organelle membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0005385; F:zinc ion transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0070574; P:cadmium ion transmembrane transport; IEA:Ensembl.
DR GO; GO:0006882; P:cellular zinc ion homeostasis; IBA:GO_Central.
DR GO; GO:0071578; P:zinc II ion transmembrane import; IBA:GO_Central.
DR GO; GO:0006829; P:zinc II ion transport; IMP:UniProtKB.
DR InterPro; IPR003689; ZIP.
DR Pfam; PF02535; Zip; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Complete proteome;
KW Congenital disorder of glycosylation; Glycoprotein; Ion transport;
KW Membrane; Polymorphism; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport; Zinc; Zinc transport.
FT CHAIN 1 460 Zinc transporter ZIP8.
FT /FTId=PRO_0000312707.
FT TOPO_DOM 1 8 Extracellular. {ECO:0000255}.
FT TRANSMEM 9 29 Helical. {ECO:0000255}.
FT TOPO_DOM 30 132 Cytoplasmic. {ECO:0000255}.
FT TRANSMEM 133 153 Helical. {ECO:0000255}.
FT TOPO_DOM 154 160 Extracellular. {ECO:0000255}.
FT TRANSMEM 161 181 Helical. {ECO:0000255}.
FT TOPO_DOM 182 191 Cytoplasmic. {ECO:0000255}.
FT TRANSMEM 192 212 Helical. {ECO:0000255}.
FT TOPO_DOM 213 302 Extracellular. {ECO:0000255}.
FT TRANSMEM 303 323 Helical. {ECO:0000255}.
FT TOPO_DOM 324 365 Cytoplasmic. {ECO:0000255}.
FT TRANSMEM 366 386 Helical. {ECO:0000255}.
FT TOPO_DOM 387 388 Extracellular. {ECO:0000255}.
FT TRANSMEM 389 409 Helical. {ECO:0000255}.
FT TOPO_DOM 410 429 Cytoplasmic. {ECO:0000255}.
FT TRANSMEM 430 450 Helical. {ECO:0000255}.
FT TOPO_DOM 451 460 Extracellular. {ECO:0000255}.
FT MOTIF 343 348 XEXPHE-motif.
FT CARBOHYD 273 273 N-linked (GlcNAc...) asparagine.
FT {ECO:0000255}.
FT VAR_SEQ 1 67 Missing (in isoform 2).
FT {ECO:0000303|PubMed:14702039}.
FT /FTId=VSP_029884.
FT VAR_SEQ 68 72 QLHFN -> MHQHA (in isoform 2).
FT {ECO:0000303|PubMed:14702039}.
FT /FTId=VSP_029885.
FT VAR_SEQ 423 460 VTGRKTDFTFFMIQNAGMLTGFTAILLITLYAGEIELE ->
FT IIKWATDDIKSQLHLLWIYTAR (in isoform 3).
FT {ECO:0000303|PubMed:14702039}.
FT /FTId=VSP_043675.
FT VARIANT 33 33 V -> M (in CDG2N; dbSNP:rs373562040).
FT {ECO:0000269|PubMed:26637979}.
FT /FTId=VAR_076241.
FT VARIANT 38 38 G -> R (in CDG2N; lowered Mn and Zn blood
FT levels and increased Mn and Zn urine
FT levels in affected individuals;
FT dbSNP:rs778210210).
FT {ECO:0000269|PubMed:26637978,
FT ECO:0000269|PubMed:26637979}.
FT /FTId=VAR_076242.
FT VARIANT 204 204 G -> C (in CDG2N; dbSNP:rs779241085).
FT {ECO:0000269|PubMed:26637979}.
FT /FTId=VAR_076243.
FT VARIANT 335 335 S -> T (in CDG2N; dbSNP:rs864309660).
FT {ECO:0000269|PubMed:26637979}.
FT /FTId=VAR_076244.
FT VARIANT 340 340 I -> N (in CDG2N; no detectable serum or
FT urinary manganese levels in an affected
FT individual who also carries R-38
FT mutation; dbSNP:rs864309659).
FT {ECO:0000269|PubMed:26637979}.
FT /FTId=VAR_076245.
FT VARIANT 391 391 A -> T (in dbSNP:rs13107325).
FT /FTId=VAR_037551.
FT CONFLICT 241 241 K -> E (in Ref. 3; BAB55268).
FT {ECO:0000305}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 127 450 ipfam:Zip [T]
SQ SEQUENCE 460 AA; 49631 MW; E5C03F4576E11E2F CRC64;
MAPGRAVAGL LLLAAAGLGG VAEGPGLAFS EDVLSVFGAN LSLSAAQLQH LLEQMGAASR
VGVPEPGQLH FNQCLTAEEI FSLHGFSNAT QITSSKFSVI CPAVLQQLNF HPCEDRPKHK
TRPSHSEVWG YGFLSVTIIN LASLLGLILT PLIKKSYFPK ILTFFVGLAI GTLFSNAIFQ
LIPEAFGFDP KVDSYVEKAV AVFGGFYLLF FFERMLKMLL KTYGQNGHTH FGNDNFGPQE
KTHQPKALPA INGVTCYANP AVTEANGHIH FDNVSVVSLQ DGKKEPSSCT CLKGPKLSEI
GTIAWMITLC DALHNFIDGL AIGASCTLSL LQGLSTSIAI LCEEFPHELG DFVILLNAGM
STRQALLFNF LSACSCYVGL AFGILVGNNF APNIIFALAG GMFLYISLAD MFPEMNDMLR
EKVTGRKTDF TFFMIQNAGM LTGFTAILLI TLYAGEIELE
//
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