ZNT7_MOUSE
ID ZNT7_MOUSE Reviewed; 378 AA.
AC Q9JKN1; Q80Y27;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Zinc transporter 7;
DE Short=ZnT-7;
DE AltName: Full=Solute carrier family 30 member 7;
DE AltName: Full=Znt-like transporter 2;
GN Name=Slc30a7; Synonyms=Znt7, Zntl2;
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], PROTEIN SEQUENCE OF 299-315, FUNCTION,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J; TISSUE=Kidney;
RX PubMed=12446736; DOI=10.1074/jbc.m207644200;
RA Kirschke C.P., Huang L.;
RT "ZnT7, a novel mammalian zinc transporter, accumulates zinc in the Golgi
RT apparatus.";
RL J. Biol. Chem. 278:4096-4102(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
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=Pancreas, and Tongue;
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=FVB/N; TISSUE=Embryo, and Salivary gland;
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 FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=17954933; DOI=10.1074/jbc.m706631200;
RA Huang L., Yu Y.Y., Kirschke C.P., Gertz E.R., Lloyd K.K.;
RT "Znt7 (Slc30a7)-deficient mice display reduced body zinc status and body
RT fat accumulation.";
RL J. Biol. Chem. 282:37053-37063(2007).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Liver, Lung, Pancreas, Spleen, 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: Seems to facilitate zinc transport from the cytoplasm into
CC the Golgi apparatus. Partly regulates cellular zinc homeostasis.
CC Required with ZNT5 for the activation of zinc-requiring enzymes,
CC alkaline phosphatases (ALPs). Transports zinc into the lumens of the
CC Golgi apparatus and the vesicular compartments where ALPs locate, thus,
CC converting apoALPs to holoALPs. Required with ZNT5 and ZNT6 for the
CC activation of TNAP (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:12446736, ECO:0000269|PubMed:17954933}.
CC -!- SUBUNIT: Homooligomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC {ECO:0000269|PubMed:12446736}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:12446736}.
CC -!- TISSUE SPECIFICITY: Highly expressed in liver, spleen, duodenum and
CC part of the jejunum of small intestine (at protein level). Moderately
CC expressed in kidney, lung, and brain. Barely detectable in heart.
CC {ECO:0000269|PubMed:12446736, ECO:0000269|PubMed:17954933}.
CC -!- DISRUPTION PHENOTYPE: Null mutants are viable, fertile, and display no
CC obvious morphological abnormalities. However, reduced food intake
CC (anorexia) and poor growth were observed.
CC {ECO:0000269|PubMed:17954933}.
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; AF529196; AAO17323.1; -; mRNA.
DR EMBL; AF233322; AAF43423.1; -; mRNA.
DR EMBL; AK010008; BAB26639.1; -; mRNA.
DR EMBL; AK075802; BAC35970.1; -; mRNA.
DR EMBL; BC017136; AAH17136.1; -; mRNA.
DR EMBL; BC050193; AAH50193.1; -; mRNA.
DR CCDS; CCDS17783.1; -.
DR RefSeq; NP_075703.1; NM_023214.7.
DR AlphaFoldDB; Q9JKN1; -.
DR SMR; Q9JKN1; -.
DR BioGRID; 211520; 2.
DR IntAct; Q9JKN1; 2.
DR MINT; Q9JKN1; -.
DR STRING; 10090.ENSMUSP00000065254; -.
DR iPTMnet; Q9JKN1; -.
DR PhosphoSitePlus; Q9JKN1; -.
DR EPD; Q9JKN1; -.
DR MaxQB; Q9JKN1; -.
DR PaxDb; Q9JKN1; -.
DR PeptideAtlas; Q9JKN1; -.
DR PRIDE; Q9JKN1; -.
DR ProteomicsDB; 275311; -.
DR Antibodypedia; 20006; 81 antibodies from 18 providers.
DR DNASU; 66500; -.
DR Ensembl; ENSMUST00000067485; ENSMUSP00000065254; ENSMUSG00000054414.
DR GeneID; 66500; -.
DR KEGG; mmu:66500; -.
DR UCSC; uc008rbt.2; mouse.
DR CTD; 148867; -.
DR MGI; MGI:1913750; Slc30a7.
DR VEuPathDB; HostDB:ENSMUSG00000054414; -.
DR eggNOG; KOG1484; Eukaryota.
DR GeneTree; ENSGT00940000159571; -.
DR HOGENOM; CLU_013430_0_3_1; -.
DR InParanoid; Q9JKN1; -.
DR OMA; WKRLIFS; -.
DR OrthoDB; 1507860at2759; -.
DR PhylomeDB; Q9JKN1; -.
DR TreeFam; TF315217; -.
DR BioGRID-ORCS; 66500; 4 hits in 72 CRISPR screens.
DR ChiTaRS; Slc30a7; mouse.
DR PRO; PR:Q9JKN1; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q9JKN1; protein.
DR Bgee; ENSMUSG00000054414; Expressed in lacrimal gland and 238 other tissues.
DR Genevisible; Q9JKN1; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:MGI.
DR GO; GO:0005794; C:Golgi apparatus; IDA:BHF-UCL.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:BHF-UCL.
DR GO; GO:0031982; C:vesicle; ISO:MGI.
DR GO; GO:0046873; F:metal ion transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IC:MGI.
DR GO; GO:0005385; F:zinc ion transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0006882; P:cellular zinc ion homeostasis; IBA:GO_Central.
DR GO; GO:0030001; P:metal ion transport; IBA:GO_Central.
DR GO; GO:0032119; P:sequestering of zinc ion; IEP:BHF-UCL.
DR GO; GO:1904257; P:zinc ion import into Golgi apparatus; IBA:GO_Central.
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 InterPro; IPR045316; Msc2-like.
DR PANTHER; PTHR45755; PTHR45755; 2.
DR Pfam; PF01545; Cation_efflux; 1.
DR SUPFAM; SSF161111; SSF161111; 1.
DR TIGRFAMs; TIGR01297; CDF; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Golgi apparatus; Ion transport; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport; Zinc;
KW Zinc transport.
FT CHAIN 1..378
FT /note="Zinc transporter 7"
FT /id="PRO_0000314300"
FT TOPO_DOM 1..37
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 38..58
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 59..67
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 68..88
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 89..102
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 103..123
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 124..140
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 141..161
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 162..238
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 239..259
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 260..264
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 265..285
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 286..378
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 161..220
FT /note="His-rich loop"
FT REGION 186..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 186..221
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 257
FT /note="A -> G (in Ref. 4; AAH50193)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 378 AA; 41790 MW; B98AC19C9A045006 CRC64;
MLPLSIKDDE YKPPKFNLFG KISGWFRSIL SDKTSRNLFF FLCLNLSFAF VELLYGIWSN
CLGLISDSFH MFFDSTAILA GLAASVISKW RDNDAFSYGY VRAEVLAGFV NGLFLIFTAF
FIFSEGVERA LAPPDVHHER LLLVSILGFV VNLVGIFVFN HGGHGHSHGS GHGHSHSLFN
GALDHSHGHE DHCHSHEAKH GAAHSHDHDH AHGHGHLHSH DGPSFKATAG PSRQILQGVF
LHILADTLGS IGVIASAIMM QNFGLMIADP ICSILIAILI VVSVIPLLRE SVGILMQRTP
PSLENTLPQC YQRVQQLQGV YNLQEQHFWT LCSDVYVGTL KLVVAPDADA RWILSQTHNI
FTQAGVRQLY VQIDFAAM
