ZNT9_HUMAN
ID ZNT9_HUMAN Reviewed; 568 AA.
AC Q6PML9; Q4W5B6; Q7Z5I7; Q8TBB2; Q9Y6R2;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Zinc transporter 9;
DE Short=ZnT-9;
DE AltName: Full=Human embryonic lung protein {ECO:0000303|PubMed:10409434};
DE Short=HuEL {ECO:0000303|PubMed:10409434};
DE AltName: Full=Solute carrier family 30 member 9;
GN Name=SLC30A9; Synonyms=C4orf1, HUEL;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP VARIANTS VAL-50 AND ALA-97.
RC TISSUE=Lung;
RX PubMed=10409434; DOI=10.1006/geno.1999.5856;
RA Sim D.L.C., Chow V.T.K.;
RT "The novel human HUEL (C4orf1) gene maps to chromosome 4p12-p13 and encodes
RT a nuclear protein containing the nuclear receptor interaction motif.";
RL Genomics 59:224-233(1999).
RN [2]
RP SEQUENCE REVISION TO 160; 174 AND 196.
RC TISSUE=Lung;
RA Chow V.T.K., Sim D.L.C.;
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS VAL-50 AND ALA-97.
RC TISSUE=Testis;
RA Xu Z.Y., Huang X.Y., Xu M., Yin L.L., Lu L., Li J.M., Zhou Z.M., Sha J.H.;
RT "A human HUEL (C4orf1) isoform play the role in spermatogenesis.";
RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Luo W., Sedehizade F., Hanck T., Reiser G.;
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
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., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., 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., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., 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., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS VAL-50 AND ALA-97.
RC TISSUE=Cervix, Colon, and Muscle;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [9]
RP STRUCTURE BY NMR OF 124-217.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of a putative DNA-binding domain of the human solute
RT carrier family 30 (zinc transporter) protein.";
RL Submitted (FEB-2009) to the PDB data bank.
RN [10]
RP INVOLVEMENT IN BILAPES, VARIANT BILAPES ALA-350 DEL, CHARACTERIZATION OF
RP VARIANT BILAPES ALA-350 DEL, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND
RP FUNCTION.
RX PubMed=28334855; DOI=10.1093/brain/awx013;
RA Perez Y., Shorer Z., Liani-Leibson K., Chabosseau P., Kadir R.,
RA Volodarsky M., Halperin D., Barber-Zucker S., Shalev H., Schreiber R.,
RA Gradstein L., Gurevich E., Zarivach R., Rutter G.A., Landau D., Birk O.S.;
RT "SLC30A9 mutation affecting intracellular zinc homeostasis causes a novel
RT cerebro-renal syndrome.";
RL Brain 140:928-939(2017).
CC -!- FUNCTION: Acts as a zinc transporter involved in intracellular zinc
CC homeostasis (PubMed:28334855). Functions as a secondary coactivator for
CC nuclear receptors by cooperating with p160 coactivators subtypes. Plays
CC a role in transcriptional activation of Wnt-responsive genes (By
CC similarity). {ECO:0000250|UniProtKB:Q5IRJ6,
CC ECO:0000269|PubMed:28334855}.
CC -!- SUBUNIT: Interacts with GRIP1, ESR1 and AR.
CC {ECO:0000250|UniProtKB:Q5IRJ6}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}. Nucleus {ECO:0000269|PubMed:10409434}. Cytoplasm
CC {ECO:0000269|PubMed:10409434}. Cytoplasmic vesicle
CC {ECO:0000269|PubMed:28334855}. Endoplasmic reticulum
CC {ECO:0000269|PubMed:28334855}. Note=Mainly in the cytoplasm
CC (PubMed:10409434). Partial co-localization with endoplasmic reticulum
CC (PubMed:28334855). {ECO:0000269|PubMed:10409434,
CC ECO:0000269|PubMed:28334855}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed in fetal and adult tissues
CC and cancer cell lines. {ECO:0000269|PubMed:10409434,
CC ECO:0000269|PubMed:28334855}.
CC -!- DISEASE: Birk-Landau-Perez syndrome (BILAPES) [MIM:617595]: An
CC autosomal recessive syndrome characterized by early-childhood onset of
CC different combinations of intellectual disability, muscle weakness,
CC camptocormia, oculomotor apraxia, and nephropathy.
CC {ECO:0000269|PubMed:28334855}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the cation diffusion facilitator (CDF)
CC transporter (TC 2.A.4) family. SLC30A subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAP83846.1; Type=Miscellaneous discrepancy; Note=Unlikely isoform. Aberrant splice sites.; Evidence={ECO:0000305};
CC Sequence=AAY40966.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF006621; AAB87763.2; -; mRNA.
DR EMBL; AY319413; AAP83846.1; ALT_SEQ; mRNA.
DR EMBL; AY594282; AAT02479.1; -; mRNA.
DR EMBL; AC113151; AAY40966.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC007732; AAH07732.1; -; mRNA.
DR EMBL; BC016949; AAH16949.1; -; mRNA.
DR EMBL; BC022981; AAH22981.1; -; mRNA.
DR CCDS; CCDS3465.1; -.
DR RefSeq; NP_006336.3; NM_006345.3.
DR PDB; 2ENK; NMR; -; A=124-217.
DR PDBsum; 2ENK; -.
DR AlphaFoldDB; Q6PML9; -.
DR SMR; Q6PML9; -.
DR BioGRID; 115726; 174.
DR IntAct; Q6PML9; 20.
DR MINT; Q6PML9; -.
DR STRING; 9606.ENSP00000264451; -.
DR DrugBank; DB14533; Zinc chloride.
DR DrugBank; DB14548; Zinc sulfate, unspecified form.
DR TCDB; 2.A.4.6.1; the cation diffusion facilitator (cdf) family.
DR iPTMnet; Q6PML9; -.
DR PhosphoSitePlus; Q6PML9; -.
DR BioMuta; SLC30A9; -.
DR DMDM; 74722746; -.
DR EPD; Q6PML9; -.
DR jPOST; Q6PML9; -.
DR MassIVE; Q6PML9; -.
DR MaxQB; Q6PML9; -.
DR PaxDb; Q6PML9; -.
DR PeptideAtlas; Q6PML9; -.
DR PRIDE; Q6PML9; -.
DR ProteomicsDB; 67254; -.
DR Antibodypedia; 1339; 158 antibodies from 27 providers.
DR DNASU; 10463; -.
DR Ensembl; ENST00000264451.12; ENSP00000264451.6; ENSG00000014824.14.
DR GeneID; 10463; -.
DR KEGG; hsa:10463; -.
DR MANE-Select; ENST00000264451.12; ENSP00000264451.6; NM_006345.4; NP_006336.3.
DR UCSC; uc003gwl.4; human.
DR CTD; 10463; -.
DR DisGeNET; 10463; -.
DR GeneCards; SLC30A9; -.
DR HGNC; HGNC:1329; SLC30A9.
DR HPA; ENSG00000014824; Low tissue specificity.
DR MalaCards; SLC30A9; -.
DR MIM; 604604; gene.
DR MIM; 617595; phenotype.
DR neXtProt; NX_Q6PML9; -.
DR OpenTargets; ENSG00000014824; -.
DR Orphanet; 505242; Psychomotor regression-oculomotor apraxia-movement disorder-nephropathy syndrome.
DR PharmGKB; PA25909; -.
DR VEuPathDB; HostDB:ENSG00000014824; -.
DR eggNOG; KOG2802; Eukaryota.
DR GeneTree; ENSGT00390000008346; -.
DR HOGENOM; CLU_021126_3_0_1; -.
DR InParanoid; Q6PML9; -.
DR OMA; IMVRAIH; -.
DR OrthoDB; 667718at2759; -.
DR PhylomeDB; Q6PML9; -.
DR TreeFam; TF314526; -.
DR PathwayCommons; Q6PML9; -.
DR SignaLink; Q6PML9; -.
DR SIGNOR; Q6PML9; -.
DR BioGRID-ORCS; 10463; 103 hits in 1092 CRISPR screens.
DR ChiTaRS; SLC30A9; human.
DR EvolutionaryTrace; Q6PML9; -.
DR GenomeRNAi; 10463; -.
DR Pharos; Q6PML9; Tbio.
DR PRO; PR:Q6PML9; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q6PML9; protein.
DR Bgee; ENSG00000014824; Expressed in cortical plate and 212 other tissues.
DR ExpressionAtlas; Q6PML9; baseline and differential.
DR Genevisible; Q6PML9; HS.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0008324; F:cation transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR GO; GO:0016922; F:nuclear receptor binding; IEA:Ensembl.
DR GO; GO:0030374; F:nuclear receptor coactivator activity; IBA:GO_Central.
DR GO; GO:0006882; P:cellular zinc ion homeostasis; IMP:UniProtKB.
DR GO; GO:0006289; P:nucleotide-excision repair; TAS:BHF-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006829; P:zinc ion transport; IMP:UniProtKB.
DR Gene3D; 1.20.1510.10; -; 1.
DR Gene3D; 3.90.530.10; -; 1.
DR InterPro; IPR002524; Cation_efflux.
DR InterPro; IPR027469; Cation_efflux_TMD_sf.
DR InterPro; IPR009061; DNA-bd_dom_put_sf.
DR InterPro; IPR040177; SLC30A9.
DR InterPro; IPR037129; XPA_sf.
DR PANTHER; PTHR13414; PTHR13414; 1.
DR Pfam; PF01545; Cation_efflux; 1.
DR SUPFAM; SSF161111; SSF161111; 1.
DR SUPFAM; SSF46955; SSF46955; 1.
DR TIGRFAMs; TIGR01297; CDF; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Cytoplasmic vesicle; Disease variant;
KW Endoplasmic reticulum; Ion transport; Membrane; Nucleus;
KW Reference proteome; Transcription; Transcription regulation; Transmembrane;
KW Transmembrane helix; Transport; Zinc; Zinc transport.
FT CHAIN 1..568
FT /note="Zinc transporter 9"
FT /id="PRO_0000295805"
FT TRANSMEM 239..259
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 314..334
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 342..362
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 392..412
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 424..444
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOTIF 462..466
FT /note="LXXLL motif"
FT VARIANT 50
FT /note="M -> V (in dbSNP:rs1047626)"
FT /evidence="ECO:0000269|PubMed:10409434,
FT ECO:0000269|PubMed:15489334, ECO:0000269|Ref.3"
FT /id="VAR_052003"
FT VARIANT 97
FT /note="T -> A (in dbSNP:rs2581423)"
FT /evidence="ECO:0000269|PubMed:10409434,
FT ECO:0000269|PubMed:15489334, ECO:0000269|Ref.3"
FT /id="VAR_052004"
FT VARIANT 350
FT /note="Missing (in BILAPES; no effect on Wnt-signaling; no
FT change in cytoplasmic vesicle subcellular location;
FT decrease in cytosolic free zinc levels)"
FT /evidence="ECO:0000269|PubMed:28334855"
FT /id="VAR_079365"
FT VARIANT 353
FT /note="L -> S (in dbSNP:rs1801962)"
FT /id="VAR_052005"
FT CONFLICT 141
FT /note="C -> Y (in Ref. 3; AAP83846)"
FT /evidence="ECO:0000305"
FT CONFLICT 356
FT /note="E -> V (in Ref. 3; AAP83846)"
FT /evidence="ECO:0000305"
FT CONFLICT 401
FT /note="V -> A (in Ref. 6; AAH22981)"
FT /evidence="ECO:0000305"
FT STRAND 129..132
FT /evidence="ECO:0007829|PDB:2ENK"
FT HELIX 133..139
FT /evidence="ECO:0007829|PDB:2ENK"
FT HELIX 144..149
FT /evidence="ECO:0007829|PDB:2ENK"
FT STRAND 167..169
FT /evidence="ECO:0007829|PDB:2ENK"
FT HELIX 170..180
FT /evidence="ECO:0007829|PDB:2ENK"
FT STRAND 181..183
FT /evidence="ECO:0007829|PDB:2ENK"
FT HELIX 184..209
FT /evidence="ECO:0007829|PDB:2ENK"
SQ SEQUENCE 568 AA; 63515 MW; CA59839CA983FDC2 CRC64;
MLPGLAAAAA HRCSWSSLCR LRLRCRAAAC NPSDRQEWQN LVTFGSFSNM VPCSHPYIGT
LSQVKLYSTN VQKEGQGSQT LRVEKVPSFE TAEGIGTELK APLKQEPLQV RVKAVLKKRE
YGSKYTQNNF ITGVRAINEF CLKSSDLEQL RKIRRRSPHE DTESFTVYLR SDVEAKSLEV
WGSPEALARE KKLRKEAEIE YRERLFRNQK ILREYRDFLG NTKPRSRTAS VFFKGPGKVV
MVAICINGLN CFFKFLAWIY TGSASMFSEA IHSLSDTCNQ GLLALGISKS VQTPDPSHPY
GFSNMRYISS LISGVGIFMM GAGLSWYHGV MGLLHPQPIE SLLWAYCILA GSLVSEGATL
LVAVNELRRN ARAKGMSFYK YVMESRDPST NVILLEDTAA VLGVIIAATC MGLTSITGNP
LYDSLGSLGV GTLLGMVSAF LIYTNTEALL GRSIQPEQVQ RLTELLENDP SVRAIHDVKA
TDLGLGKVRF KAEVDFDGRV VTRSYLEKQD FDQMLQEIQE VKTPEELETF MLKHGENIID
TLGAEVDRLE KELKKRNPEV RHVDLEIL
