S39A7_MOUSE
ID S39A7_MOUSE Reviewed; 476 AA.
AC Q31125; Q3TVU6; Q9Z1W1;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2001, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Zinc transporter SLC39A7;
DE AltName: Full=Histidine-rich membrane protein Ke4;
DE AltName: Full=Solute carrier family 39 member 7;
DE AltName: Full=Zrt-, Irt-like protein 7 {ECO:0000303|PubMed:15705588};
DE Short=ZIP7 {ECO:0000303|PubMed:15705588};
GN Name=Slc39a7; Synonyms=H2-Ke4, Hke4;
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], AND TISSUE SPECIFICITY.
RX PubMed=2294398; DOI=10.1128/mcb.10.1.138-145.1990;
RA St Jacques B., Han T.-H., Macmurray A., Shin H.-S.;
RT "A putative transmembrane protein with histidine-rich charge clusters
RT encoded in the H-2K/tw5 region of mice.";
RL Mol. Cell. Biol. 10:138-145(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=129/SvJ;
RA Rowen L., Qin S., Madan A., Loretz C., James R., Dors M., Mix L., Hall J.,
RA Lasky S., Hood L.;
RT "Sequence of the mouse major histocompatibility complex class II region.";
RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Osteoclast;
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 FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=15705588; DOI=10.1074/jbc.m412188200;
RA Huang L., Kirschke C.P., Zhang Y., Yu Y.Y.;
RT "The ZIP7 gene (Slc39a7) encodes a zinc transporter involved in zinc
RT homeostasis of the Golgi apparatus.";
RL J. Biol. Chem. 280:15456-15463(2005).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, Pancreas, and 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 transporter, that transports Zn(2+) from the endoplasmic
CC reticulum/Golgi apparatus to the cytosol (PubMed:15705588). Transport
CC is stimulated by growth factors, such as EGF, and Ca(2+), as well as by
CC exogenous Zn(2+) (By similarity). {ECO:0000250|UniProtKB:Q92504,
CC ECO:0000269|PubMed:15705588}.
CC -!- INTERACTION:
CC Q31125; P25118: Tnfrsf1a; NbExp=3; IntAct=EBI-644519, EBI-518014;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q92504}; Multi-pass membrane protein
CC {ECO:0000255}. Golgi apparatus, cis-Golgi network membrane
CC {ECO:0000250|UniProtKB:Q92504}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:15705588,
CC ECO:0000269|PubMed:2294398}.
CC -!- PTM: Methylation at some His residue by METTL9 leads to reduced zinc-
CC binding. {ECO:0000250|UniProtKB:Q92504}.
CC -!- SIMILARITY: Belongs to the ZIP transporter (TC 2.A.5) family.
CC KE4/Catsup subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA37767.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; M32010; AAA37767.1; ALT_FRAME; mRNA.
DR EMBL; AF100956; AAC69903.1; -; Genomic_DNA.
DR EMBL; AK159968; BAE35522.1; -; mRNA.
DR CCDS; CCDS37576.1; -.
DR PIR; I49714; I49714.
DR RefSeq; NP_001071177.1; NM_001077709.1.
DR RefSeq; NP_032228.2; NM_008202.2.
DR AlphaFoldDB; Q31125; -.
DR BioGRID; 200158; 3.
DR IntAct; Q31125; 4.
DR MINT; Q31125; -.
DR STRING; 10090.ENSMUSP00000025186; -.
DR iPTMnet; Q31125; -.
DR PhosphoSitePlus; Q31125; -.
DR EPD; Q31125; -.
DR jPOST; Q31125; -.
DR MaxQB; Q31125; -.
DR PaxDb; Q31125; -.
DR PRIDE; Q31125; -.
DR ProteomicsDB; 260786; -.
DR Antibodypedia; 28954; 258 antibodies from 33 providers.
DR DNASU; 14977; -.
DR Ensembl; ENSMUST00000025186; ENSMUSP00000025186; ENSMUSG00000024327.
DR Ensembl; ENSMUST00000169397; ENSMUSP00000130102; ENSMUSG00000024327.
DR GeneID; 14977; -.
DR KEGG; mmu:14977; -.
DR UCSC; uc008cav.1; mouse.
DR CTD; 7922; -.
DR MGI; MGI:95909; Slc39a7.
DR VEuPathDB; HostDB:ENSMUSG00000024327; -.
DR eggNOG; KOG2693; Eukaryota.
DR GeneTree; ENSGT00940000160076; -.
DR HOGENOM; CLU_015114_0_1_1; -.
DR InParanoid; Q31125; -.
DR OMA; IWLHSIG; -.
DR OrthoDB; 657777at2759; -.
DR PhylomeDB; Q31125; -.
DR TreeFam; TF318470; -.
DR Reactome; R-MMU-442380; Zinc influx into cells by the SLC39 gene family.
DR BioGRID-ORCS; 14977; 12 hits in 71 CRISPR screens.
DR ChiTaRS; Slc39a7; mouse.
DR PRO; PR:Q31125; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q31125; protein.
DR Bgee; ENSMUSG00000024327; Expressed in islet of Langerhans and 65 other tissues.
DR ExpressionAtlas; Q31125; baseline and differential.
DR Genevisible; Q31125; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005654; C:nucleoplasm; ISO: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:0071577; P:zinc ion transmembrane transport; IBA:GO_Central.
DR InterPro; IPR003689; ZIP.
DR Pfam; PF02535; Zip; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Golgi apparatus; Ion transport; Membrane;
KW Methylation; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport; Zinc; Zinc transport.
FT CHAIN 1..476
FT /note="Zinc transporter SLC39A7"
FT /id="PRO_0000213689"
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 146..166
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 177..197
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 222..242
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 393..413
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 417..437
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 35..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 249..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 259..302
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 283
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92504"
FT CONFLICT 208
FT /note="A -> T (in Ref. 3; BAE35522)"
FT /evidence="ECO:0000305"
FT CONFLICT 367
FT /note="V -> L (in Ref. 1; AAA37767)"
FT /evidence="ECO:0000305"
FT CONFLICT 449..450
FT /note="EA -> DR (in Ref. 1; AAA37767)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 476 AA; 50657 MW; 48214438BE44919B CRC64;
MTMGLRAPHW VAVGLLTWAA LGLLVAGHEG HGDLHKDVEE DFHGHSHGHS HEDFHHGHSH
GHSHEDFHHG HGHTHESIWH GHAHSHDHGH SREELHHGHS HGHSHDSLHH GGHGHAHREH
SHGTSREAGA PGIKHHLDTV TLWAYALGAT VLISAAPFFV LFLIPVESNS PRHRSLLQIL
LSFASGGLLG DAFLHLIPHA LEPHSHHAPE QPGHGHSHSG QGPILSVGLW VLSGIVAFLV
VEKFVRHVKG GHGHSHGHGD RHAHGDSHTH GDRHECSSKE KPSTEEEKEV GGLRKRRGGN
TGPRDGPVKP QSPEEEKAGS DLRVSGYLNL AADLAHNFTD GLAIGASFRG GRGLGILTTM
TVLLHEVPHE VGDFAILVQS GCSKKQAMRL QLVTAIGALA GTACALLTEG GAVDSDVAGG
AGPGWVLPFT AGGFIYVATV SVLPELLREA SPLQSLLEVL GLLGGVAMMV LIAHLE
