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Zinc transporter 9 (ZnT-9) (Human embryonic lung protein) (HuEL) (Solute carrier family 30 member 9)

 ZNT9_HUMAN              Reviewed;         568 AA.
Q6PML9; Q4W5B6; Q7Z5I7; Q8TBB2; Q9Y6R2;
24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
05-DEC-2018, entry version 124.
RecName: Full=Zinc transporter 9;
Short=ZnT-9;
AltName: Full=Human embryonic lung protein {ECO:0000303|PubMed:10409434};
Short=HuEL {ECO:0000303|PubMed:10409434};
AltName: Full=Solute carrier family 30 member 9;
Name=SLC30A9; Synonyms=C4orf1, HUEL;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
AND VARIANTS VAL-50 AND ALA-97.
TISSUE=Lung;
PubMed=10409434; DOI=10.1006/geno.1999.5856;
Sim D.L.C., Chow V.T.K.;
"The novel human HUEL (C4orf1) gene maps to chromosome 4p12-p13 and
encodes a nuclear protein containing the nuclear receptor interaction
motif.";
Genomics 59:224-233(1999).
[2]
SEQUENCE REVISION TO 160; 174 AND 196.
TISSUE=Lung;
Chow V.T.K., Sim D.L.C.;
Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS VAL-50 AND ALA-97.
TISSUE=Testis;
Xu Z.Y., Huang X.Y., Xu M., Yin L.L., Lu L., Li J.M., Zhou Z.M.,
Sha J.H.;
"A human HUEL (C4orf1) isoform play the role in spermatogenesis.";
Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [MRNA].
Luo W., Sedehizade F., Hanck T., Reiser G.;
Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS VAL-50 AND
ALA-97.
TISSUE=Cervix, Colon, and Muscle;
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).
[7]
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).
[8]
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).
[9]
STRUCTURE BY NMR OF 124-217.
RIKEN structural genomics initiative (RSGI);
"Solution structure of a putative DNA-binding domain of the human
solute carrier family 30 (zinc transporter) protein.";
Submitted (FEB-2009) to the PDB data bank.
[10]
INVOLVEMENT IN BILAPES, VARIANT BILAPES ALA-350 DEL, CHARACTERIZATION
OF VARIANT BILAPES ALA-350 DEL, TISSUE SPECIFICITY, SUBCELLULAR
LOCATION, AND FUNCTION.
PubMed=28334855; DOI=10.1093/brain/awx013;
Perez Y., Shorer Z., Liani-Leibson K., Chabosseau P., Kadir R.,
Volodarsky M., Halperin D., Barber-Zucker S., Shalev H., Schreiber R.,
Gradstein L., Gurevich E., Zarivach R., Rutter G.A., Landau D.,
Birk O.S.;
"SLC30A9 mutation affecting intracellular zinc homeostasis causes a
novel cerebro-renal syndrome.";
Brain 140:928-939(2017).
-!- FUNCTION: Acts as a zinc transporter involved in intracellular
zinc homeostasis (PubMed:28334855). Functions as a secondary
coactivator for nuclear receptors by cooperating with p160
coactivators subtypes. Plays a role in transcriptional activation
of Wnt-responsive genes (By similarity).
{ECO:0000250|UniProtKB:Q5IRJ6, ECO:0000269|PubMed:28334855}.
-!- SUBUNIT: Interacts with GRIP1, ESR1 and AR.
{ECO:0000250|UniProtKB:Q5IRJ6}.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
protein {ECO:0000305}. Nucleus {ECO:0000269|PubMed:10409434}.
Cytoplasm {ECO:0000269|PubMed:10409434}. Cytoplasmic vesicle
{ECO:0000269|PubMed:28334855}. Endoplasmic reticulum
{ECO:0000269|PubMed:28334855}. Note=Mainly in the cytoplasm
(PubMed:10409434). Partial co-localization with endoplasmic
reticulum (PubMed:28334855). {ECO:0000269|PubMed:10409434,
ECO:0000269|PubMed:28334855}.
-!- TISSUE SPECIFICITY: Ubiquitously expressed in fetal and adult
tissues and cancer cell lines. {ECO:0000269|PubMed:10409434,
ECO:0000269|PubMed:28334855}.
-!- DISEASE: Birk-Landau-Perez syndrome (BILAPES) [MIM:617595]: An
autosomal recessive syndrome characterized by early-childhood
onset of different combinations of intellectual disability, muscle
weakness, camptocormia, oculomotor apraxia, and nephropathy.
{ECO:0000269|PubMed:28334855}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the cation diffusion facilitator (CDF)
transporter (TC 2.A.4) family. SLC30A subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAP83846.1; Type=Miscellaneous discrepancy; Note=Unlikely isoform. Aberrant splice sites.; Evidence={ECO:0000305};
Sequence=AAY40966.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AF006621; AAB87763.2; -; mRNA.
EMBL; AY319413; AAP83846.1; ALT_SEQ; mRNA.
EMBL; AY594282; AAT02479.1; -; mRNA.
EMBL; AC113151; AAY40966.1; ALT_SEQ; Genomic_DNA.
EMBL; BC007732; AAH07732.1; -; mRNA.
EMBL; BC016949; AAH16949.1; -; mRNA.
EMBL; BC022981; AAH22981.1; -; mRNA.
CCDS; CCDS3465.1; -.
RefSeq; NP_006336.3; NM_006345.3.
UniGene; Hs.479634; -.
PDB; 2ENK; NMR; -; A=124-217.
PDBsum; 2ENK; -.
ProteinModelPortal; Q6PML9; -.
SMR; Q6PML9; -.
BioGrid; 115726; 18.
IntAct; Q6PML9; 6.
MINT; Q6PML9; -.
STRING; 9606.ENSP00000264451; -.
TCDB; 2.A.4.6.1; the cation diffusion facilitator (cdf) family.
iPTMnet; Q6PML9; -.
PhosphoSitePlus; Q6PML9; -.
BioMuta; SLC30A9; -.
DMDM; 74722746; -.
EPD; Q6PML9; -.
MaxQB; Q6PML9; -.
PaxDb; Q6PML9; -.
PeptideAtlas; Q6PML9; -.
PRIDE; Q6PML9; -.
ProteomicsDB; 67254; -.
Ensembl; ENST00000264451; ENSP00000264451; ENSG00000014824.
GeneID; 10463; -.
KEGG; hsa:10463; -.
UCSC; uc003gwl.4; human.
CTD; 10463; -.
DisGeNET; 10463; -.
EuPathDB; HostDB:ENSG00000014824.13; -.
GeneCards; SLC30A9; -.
H-InvDB; HIX0004181; -.
HGNC; HGNC:1329; SLC30A9.
HPA; HPA004014; -.
MalaCards; SLC30A9; -.
MIM; 604604; gene.
MIM; 617595; phenotype.
neXtProt; NX_Q6PML9; -.
OpenTargets; ENSG00000014824; -.
Orphanet; 505242; Psychomotor regression-oculomotor apraxia-movement disorder-nephropathy syndrome.
PharmGKB; PA25909; -.
eggNOG; KOG2802; Eukaryota.
eggNOG; COG0053; LUCA.
GeneTree; ENSGT00390000008346; -.
HOGENOM; HOG000242618; -.
HOVERGEN; HBG104893; -.
InParanoid; Q6PML9; -.
KO; K14696; -.
OMA; KKREYGP; -.
OrthoDB; EOG091G05KM; -.
PhylomeDB; Q6PML9; -.
TreeFam; TF314526; -.
SIGNOR; Q6PML9; -.
ChiTaRS; SLC30A9; human.
EvolutionaryTrace; Q6PML9; -.
GenomeRNAi; 10463; -.
PRO; PR:Q6PML9; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000014824; Expressed in 239 organ(s), highest expression level in forebrain.
CleanEx; HS_SLC30A9; -.
ExpressionAtlas; Q6PML9; baseline and differential.
Genevisible; Q6PML9; HS.
GO; GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB.
GO; GO:0005856; C:cytoskeleton; IDA:UniProtKB.
GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0008324; F:cation transmembrane transporter activity; IEA:InterPro.
GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
GO; GO:0003700; F:DNA-binding transcription factor activity; NAS:UniProtKB.
GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISM:NTNU_SB.
GO; GO:0016922; F:nuclear receptor binding; IBA:GO_Central.
GO; GO:0030374; F:nuclear receptor transcription coactivator activity; IBA:GO_Central.
GO; GO:0006882; P:cellular zinc ion homeostasis; IMP:UniProtKB.
GO; GO:0006289; P:nucleotide-excision repair; TAS:BHF-UCL.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
GO; GO:0006829; P:zinc ion transport; IMP:UniProtKB.
Gene3D; 1.20.1510.10; -; 1.
Gene3D; 3.90.530.10; -; 1.
InterPro; IPR002524; Cation_efflux.
InterPro; IPR027469; Cation_efflux_TMD_sf.
InterPro; IPR009061; DNA-bd_dom_put_sf.
InterPro; IPR040177; SLC30A9.
InterPro; IPR037129; XPA_sf.
PANTHER; PTHR13414; PTHR13414; 1.
Pfam; PF01545; Cation_efflux; 1.
SUPFAM; SSF161111; SSF161111; 1.
SUPFAM; SSF46955; SSF46955; 1.
TIGRFAMs; TIGR01297; CDF; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Cytoplasm; Cytoplasmic vesicle;
Disease mutation; Endoplasmic reticulum; Ion transport; Membrane;
Nucleus; Polymorphism; Reference proteome; Transcription;
Transcription regulation; Transmembrane; Transmembrane helix;
Transport; Zinc; Zinc transport.
CHAIN 1 568 Zinc transporter 9.
/FTId=PRO_0000295805.
TRANSMEM 239 259 Helical. {ECO:0000255}.
TRANSMEM 314 334 Helical. {ECO:0000255}.
TRANSMEM 342 362 Helical. {ECO:0000255}.
TRANSMEM 392 412 Helical. {ECO:0000255}.
TRANSMEM 424 444 Helical. {ECO:0000255}.
MOTIF 462 466 LXXLL motif.
VARIANT 50 50 M -> V (in dbSNP:rs1047626).
{ECO:0000269|PubMed:10409434,
ECO:0000269|PubMed:15489334,
ECO:0000269|Ref.3}.
/FTId=VAR_052003.
VARIANT 97 97 T -> A (in dbSNP:rs2581423).
{ECO:0000269|PubMed:10409434,
ECO:0000269|PubMed:15489334,
ECO:0000269|Ref.3}.
/FTId=VAR_052004.
VARIANT 350 350 Missing (in BILAPES; no effect on Wnt-
signaling; no change in cytoplasmic
vesicle subcellular location; decrease in
cytosolic free zinc levels).
{ECO:0000269|PubMed:28334855}.
/FTId=VAR_079365.
VARIANT 353 353 L -> S (in dbSNP:rs1801962).
/FTId=VAR_052005.
CONFLICT 141 141 C -> Y (in Ref. 3; AAP83846).
{ECO:0000305}.
CONFLICT 356 356 E -> V (in Ref. 3; AAP83846).
{ECO:0000305}.
CONFLICT 401 401 V -> A (in Ref. 6; AAH22981).
{ECO:0000305}.
STRAND 129 132 {ECO:0000244|PDB:2ENK}.
HELIX 133 139 {ECO:0000244|PDB:2ENK}.
HELIX 144 149 {ECO:0000244|PDB:2ENK}.
STRAND 167 169 {ECO:0000244|PDB:2ENK}.
HELIX 170 180 {ECO:0000244|PDB:2ENK}.
STRAND 181 183 {ECO:0000244|PDB:2ENK}.
HELIX 184 209 {ECO:0000244|PDB:2ENK}.
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


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