ZNT6_MOUSE
ID ZNT6_MOUSE Reviewed; 460 AA.
AC Q8BJM5; Q3UB35; Q6NVE0; Q8K4H6; Q8R4Z2; Q99JQ3;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Zinc transporter 6;
DE Short=ZnT-6;
DE AltName: Full=Solute carrier family 30 member 6;
GN Name=Slc30a6; Synonyms=Znt6;
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], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=C57BL/6J;
RX PubMed=11997387; DOI=10.1074/jbc.m200462200;
RA Huang L., Kirschke C.P., Gitschier J.;
RT "Functional characterization of a novel mammalian zinc transporter, ZnT6.";
RL J. Biol. Chem. 277:26389-26395(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Kidney;
RA Zhu W., Mager S.;
RT "Cloning of new mammalian zinc transporter-like genes.";
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Eye, 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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
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: Zinc-efflux transporter which allocates the cytoplasmic zinc
CC to the trans-Golgi network (TGN) as well as the vesicular compartment.
CC {ECO:0000269|PubMed:11997387}.
CC -!- SUBUNIT: Heterooligomer. Interacts with ZNT5 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC {ECO:0000269|PubMed:11997387}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:11997387}. Note=Found in vesicles.
CC -!- TISSUE SPECIFICITY: Expressed in brain and liver, and to a lower extent
CC also in lung. Highly expressed in brain (at protein level).
CC {ECO:0000269|PubMed:11997387}.
CC -!- MISCELLANEOUS: Seems to have lost most of the histidine residues in the
CC loop between the fourth and fifth transmembrane regions and appears to
CC exert transport function by forming complexes with ZNT5.
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=AAH05753.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF395840; AAM27917.1; -; mRNA.
DR EMBL; AF233346; AAL83717.1; -; mRNA.
DR EMBL; AK082907; BAC38680.1; -; mRNA.
DR EMBL; AK150342; BAE29482.1; -; mRNA.
DR EMBL; AK151120; BAE30129.1; -; mRNA.
DR EMBL; BC005753; AAH05753.1; ALT_INIT; mRNA.
DR EMBL; BC066162; AAH66162.1; -; mRNA.
DR EMBL; BC068169; AAH68169.1; -; mRNA.
DR CCDS; CCDS37691.1; -.
DR RefSeq; NP_659047.2; NM_144798.6.
DR AlphaFoldDB; Q8BJM5; -.
DR SMR; Q8BJM5; -.
DR BioGRID; 229137; 2.
DR STRING; 10090.ENSMUSP00000136503; -.
DR iPTMnet; Q8BJM5; -.
DR PhosphoSitePlus; Q8BJM5; -.
DR SwissPalm; Q8BJM5; -.
DR EPD; Q8BJM5; -.
DR MaxQB; Q8BJM5; -.
DR PaxDb; Q8BJM5; -.
DR PRIDE; Q8BJM5; -.
DR ProteomicsDB; 275310; -.
DR Antibodypedia; 29149; 167 antibodies from 24 providers.
DR DNASU; 210148; -.
DR Ensembl; ENSMUST00000024870; ENSMUSP00000024870; ENSMUSG00000024069.
DR GeneID; 210148; -.
DR KEGG; mmu:210148; -.
DR UCSC; uc008dob.2; mouse.
DR CTD; 55676; -.
DR MGI; MGI:2386741; Slc30a6.
DR VEuPathDB; HostDB:ENSMUSG00000024069; -.
DR eggNOG; KOG1484; Eukaryota.
DR GeneTree; ENSGT00940000159934; -.
DR InParanoid; Q8BJM5; -.
DR OMA; EINNYYA; -.
DR PhylomeDB; Q8BJM5; -.
DR Reactome; R-MMU-264876; Insulin processing.
DR Reactome; R-MMU-435368; Zinc efflux and compartmentalization by the SLC30 family.
DR BioGRID-ORCS; 210148; 3 hits in 71 CRISPR screens.
DR ChiTaRS; Slc30a6; mouse.
DR PRO; PR:Q8BJM5; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q8BJM5; protein.
DR Bgee; ENSMUSG00000024069; Expressed in interventricular septum and 249 other tissues.
DR ExpressionAtlas; Q8BJM5; baseline and differential.
DR Genevisible; Q8BJM5; MM.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005385; F:zinc ion transmembrane transporter activity; IDA:MGI.
DR GO; GO:0006895; P:Golgi to endosome transport; IDA:MGI.
DR GO; GO:0006829; P:zinc ion transport; IDA:MGI.
DR Gene3D; 1.20.1510.10; -; 1.
DR InterPro; IPR002524; Cation_efflux.
DR InterPro; IPR027469; Cation_efflux_TMD_sf.
DR Pfam; PF01545; Cation_efflux; 1.
DR SUPFAM; SSF161111; SSF161111; 1.
DR TIGRFAMs; TIGR01297; CDF; 1.
PE 1: Evidence at protein level;
KW Golgi apparatus; Ion transport; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport; Zinc; Zinc transport.
FT CHAIN 1..460
FT /note="Zinc transporter 6"
FT /id="PRO_0000312574"
FT TOPO_DOM 1..33
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 34..54
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 55..64
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 65..85
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 86..98
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 99..119
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 120..134
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 135..155
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 156..200
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 201..221
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 222..223
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 224..244
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 245..460
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 371..390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 80
FT /note="S -> R (in Ref. 3; BAE29482 and 4; AAH68169)"
FT /evidence="ECO:0000305"
FT CONFLICT 81
FT /note="Y -> H (in Ref. 1; AAM27917)"
FT /evidence="ECO:0000305"
FT CONFLICT 128
FT /note="E -> G (in Ref. 1; AAM27917)"
FT /evidence="ECO:0000305"
FT CONFLICT 161..168
FT /note="AYVSEAAS -> GRVGGRVG (in Ref. 4; AAH05753)"
FT /evidence="ECO:0000305"
FT CONFLICT 225
FT /note="F -> C (in Ref. 4; AAH68169)"
FT /evidence="ECO:0000305"
FT CONFLICT 292
FT /note="F -> L (in Ref. 1; AAM27917)"
FT /evidence="ECO:0000305"
FT CONFLICT 308
FT /note="N -> S (in Ref. 3; BAE29482 and 4; AAH68169)"
FT /evidence="ECO:0000305"
FT CONFLICT 314
FT /note="A -> T (in Ref. 2; AAL83717)"
FT /evidence="ECO:0000305"
FT CONFLICT 324..326
FT /note="VST -> ASS (in Ref. 2; AAL83717)"
FT /evidence="ECO:0000305"
FT CONFLICT 331
FT /note="I -> N (in Ref. 2; AAL83717)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 460 AA; 51027 MW; A3E910CE96D16015 CRC64;
MGTIHLFRKP QRSFFGKLLQ EFRLVAADRR SWKILLFGAI NVLCTGFLLM WCSSTNSIAL
TAYTYLTIFD LFSLITCLIS YWVMMRKPSP VYSFGFERLE VLAVFASTVL AQLGALFILK
ESAERFLEQP EIHTGRLLVG TFVALSFNLF TMLSIRNKPF AYVSEAASTS WLQEHVADLS
RSLCGLIPGL SSIFLPRMNP FVLIDLAGAF ALCITYMLIE INNYFAVDTA SAIAIALMTF
GTMYPMSVYS GKVLLQTTPP HVIGQLDKLI REVSTLDGVL EVRNEHFWTL GFGSLAGSVH
VRIRRDANEQ MVLAHVSNRL CTLVSTLTVQ IFKDDWIRPA LSSGPVAPNV LNFSDHHVIP
MPLLKNVDER TPVTSTPAKP SSPPPEFSFN TPGKNVSPVI LLNTQTRPYS LGLNRGHTPY
SSVFSQGLAF PGVGAGQGLR PTFPHIPSRY GINRMGQPRP
