ZNT9_MOUSE
ID ZNT9_MOUSE Reviewed; 567 AA.
AC Q5IRJ6; Q66L46; Q7TNE9; Q8BGX8; Q8BUR1; Q8BZP2; Q8K2E0; Q8K376; Q8R0P1;
AC Q9JK46;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Zinc transporter 9;
DE Short=ZnT-9;
DE AltName: Full=GRIP1-associated coactivator 63;
DE Short=GAC63;
DE AltName: Full=Solute carrier family 30 member 9;
GN Name=Slc30a9;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND INTERACTION WITH
RP GRIP1; ESR1 AND AR.
RX PubMed=15988012; DOI=10.1128/mcb.25.14.5965-5972.2005;
RA Chen Y.-H., Kim J.H., Stallcup M.R.;
RT "GAC63, a GRIP1-dependent nuclear receptor coactivator.";
RL Mol. Cell. Biol. 25:5965-5972(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Diencephalon, Skin, and Urinary bladder;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 35-567 (ISOFORMS 1/2).
RC STRAIN=C57BL/6J, Czech II, and FVB/N;
RC TISSUE=Brain, Kidney, and Mammary tumor;
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 104-533 (ISOFORMS 1/2), AND SUBCELLULAR
RP LOCATION.
RX PubMed=11906820; DOI=10.1016/s1357-2725(01)00156-x;
RA Sim D.L.C., Yeo W.M., Chow V.T.K.;
RT "The novel human HUEL (C4orf1) protein shares homology with the DNA-binding
RT domain of the XPA DNA repair protein and displays nuclear translocation in
RT a cell cycle-dependent manner.";
RL Int. J. Biochem. Cell Biol. 34:487-504(2002).
RN [5]
RP FUNCTION, AND INTERACTION WITH CTNNB1.
RX PubMed=17344318; DOI=10.1093/nar/gkm095;
RA Chen Y.H., Yang C.K., Xia M., Ou C.Y., Stallcup M.R.;
RT "Role of GAC63 in transcriptional activation mediated by beta-catenin.";
RL Nucleic Acids Res. 35:2084-2092(2007).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Acts as a zinc transporter involved in intracellular zinc
CC homeostasis (By similarity). Functions as a secondary coactivator for
CC nuclear receptors by cooperating with p160 coactivators subtypes
CC (PubMed:15988012). Plays a role in transcriptional activation of Wnt-
CC responsive genes (PubMed:17344318). {ECO:0000250|UniProtKB:Q6PML9,
CC ECO:0000269|PubMed:15988012, ECO:0000269|PubMed:17344318}.
CC -!- SUBUNIT: Interacts with GRIP1, ESR1, AR and CTNNB1.
CC {ECO:0000269|PubMed:15988012, ECO:0000269|PubMed:17344318}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}. Nucleus {ECO:0000269|PubMed:11906820}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q6PML9}. Cytoplasmic vesicle
CC {ECO:0000250|UniProtKB:Q6PML9}. Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:Q6PML9}. Note=Mainly in the cytoplasm. Partial
CC co-localization with endoplasmic reticulum.
CC {ECO:0000250|UniProtKB:Q6PML9}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5IRJ6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5IRJ6-2; Sequence=VSP_027088;
CC -!- SIMILARITY: Belongs to the cation diffusion facilitator (CDF)
CC transporter (TC 2.A.4) family. SLC30A subfamily. {ECO:0000305}.
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DR EMBL; AY682914; AAV85854.1; -; mRNA.
DR EMBL; AK028885; BAC26172.1; -; mRNA.
DR EMBL; AK033990; BAC28540.1; -; mRNA.
DR EMBL; AK035541; BAC29097.1; -; mRNA.
DR EMBL; AK082853; BAC38654.1; -; mRNA.
DR EMBL; BC027806; AAH27806.1; -; mRNA.
DR EMBL; BC026565; AAH26565.1; -; mRNA.
DR EMBL; BC031705; AAH31705.1; -; mRNA.
DR EMBL; BC055773; AAH55773.1; -; mRNA.
DR EMBL; BC078440; AAH78440.1; -; mRNA.
DR EMBL; AF263460; AAF73055.1; -; mRNA.
DR CCDS; CCDS39103.1; -. [Q5IRJ6-1]
DR RefSeq; NP_001297558.1; NM_001310629.1.
DR RefSeq; NP_848766.2; NM_178651.4. [Q5IRJ6-1]
DR AlphaFoldDB; Q5IRJ6; -.
DR BioGRID; 224557; 3.
DR STRING; 10090.ENSMUSP00000124047; -.
DR iPTMnet; Q5IRJ6; -.
DR PhosphoSitePlus; Q5IRJ6; -.
DR EPD; Q5IRJ6; -.
DR MaxQB; Q5IRJ6; -.
DR PaxDb; Q5IRJ6; -.
DR PeptideAtlas; Q5IRJ6; -.
DR PRIDE; Q5IRJ6; -.
DR ProteomicsDB; 275153; -. [Q5IRJ6-1]
DR ProteomicsDB; 275154; -. [Q5IRJ6-2]
DR Antibodypedia; 1339; 158 antibodies from 27 providers.
DR DNASU; 109108; -.
DR Ensembl; ENSMUST00000162372; ENSMUSP00000124047; ENSMUSG00000029221. [Q5IRJ6-1]
DR GeneID; 109108; -.
DR KEGG; mmu:109108; -.
DR UCSC; uc008xpt.1; mouse. [Q5IRJ6-1]
DR CTD; 10463; -.
DR MGI; MGI:1923690; Slc30a9.
DR VEuPathDB; HostDB:ENSMUSG00000029221; -.
DR eggNOG; KOG2802; Eukaryota.
DR GeneTree; ENSGT00390000008346; -.
DR InParanoid; Q5IRJ6; -.
DR OMA; IMVRAIH; -.
DR OrthoDB; 667718at2759; -.
DR PhylomeDB; Q5IRJ6; -.
DR TreeFam; TF314526; -.
DR BioGRID-ORCS; 109108; 16 hits in 71 CRISPR screens.
DR ChiTaRS; Slc30a9; mouse.
DR PRO; PR:Q5IRJ6; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q5IRJ6; protein.
DR Bgee; ENSMUSG00000029221; Expressed in superior frontal gyrus and 262 other tissues.
DR ExpressionAtlas; Q5IRJ6; baseline and differential.
DR Genevisible; Q5IRJ6; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISS:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0008324; F:cation transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0016922; F:nuclear receptor binding; IPI:MGI.
DR GO; GO:0030374; F:nuclear receptor coactivator activity; IGI:MGI.
DR GO; GO:0006882; P:cellular zinc ion homeostasis; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0006829; P:zinc ion transport; ISS: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 Alternative splicing; Cytoplasm; Cytoplasmic vesicle;
KW Endoplasmic reticulum; Ion transport; Membrane; Nucleus;
KW Reference proteome; Transcription; Transcription regulation; Transmembrane;
KW Transmembrane helix; Transport; Zinc; Zinc transport.
FT CHAIN 1..567
FT /note="Zinc transporter 9"
FT /id="PRO_0000295806"
FT TRANSMEM 238..258
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 313..333
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 341..361
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 391..411
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 423..443
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOTIF 461..465
FT /note="LXXLL motif"
FT VAR_SEQ 1..6
FT /note="MFPGLA -> MESVGAAGGSEAGGGVRVGASAPPGCFRAWP (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_027088"
FT CONFLICT 35..38
FT /note="GWKN -> HASD (in Ref. 3; AAH27806)"
FT /evidence="ECO:0000305"
FT CONFLICT 91
FT /note="V -> A (in Ref. 1; AAV85854 and 3; AAH27806)"
FT /evidence="ECO:0000305"
FT CONFLICT 376
FT /note="T -> S (in Ref. 3; AAH31705)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 567 AA; 62875 MW; 64105C5D7D7D9A64 CRC64;
MFPGLAAAAA AHRCSWAALC RLGGGRAATR GRSQGWKNVM TFESFTYVVP DIHPHLSIIN
QVKLYSTNVQ KGGQGSQTPK ADKVPSLTQT VENIGAELKA PLKQDPLQVR VKAVLKKRDY
GSKYTKNNFI TGVRAINEFC LKSSDLEQLR KIRRRSPHDD TESFTVFLRS DVEAKALEVW
GSLEALAREK KLRKEAEIEY RERLFRNQRI LREYGDFLGN TKPRSRAVSV FLKGPGKVVM
VAICINGLNC FFKFLAWIYT GSASMFSEAI HSLSDTCNQG LLALGISKSV QTPDPSHPYG
FSNMRYISSL ISGVGIFMMG AGLSWYHGIM GLLHPQPMES LLWAYCILAG SLVSEGATLL
VAINELRRSA QAKGTTFYKY VMESRDPSTN VILLEDTAAV LGVIIAATCM GLTSITGNPL
YDSLGSLGVG TLLGVVSAFL IYTNTEALLG RSIQPEQVQR LTELLESDPS VRAIHDVKAT
DLGLGKVRFK AEVDFDGRVV TRSYLEKQDF DQMMQEIQEV KTPEQLEAFM LKHGENIIDT
LGAEVDRLEK ELKKRNPEVR HVDLEIL
