ID   S39A7_CANLF             Reviewed;         469 AA.
AC   Q5TJF6;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 82.
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;
DE            Short=ZIP7;
GN   Name=SLC39A7 {ECO:0000312|EMBL:CAI11432.1};
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:CAI11432.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Doberman pinscher;
RX   PubMed=15607421; DOI=10.1016/j.ygeno.2004.09.009;
RA   Debenham S.L., Hart E.A., Ashurst J.L., Howe K.L., Quail M.A.,
RA   Ollier W.E.R., Binns M.M.;
RT   "Genomic sequence of the class II region of the canine MHC: comparison with
RT   the MHC of other mammalian species.";
RL   Genomics 85:48-59(2005).
CC   -!- FUNCTION: Zinc transporter, that transports Zn(2+) from the endoplasmic
CC       reticulum/Golgi apparatus to the cytosol. Transport is stimulated by
CC       growth factors, such as EGF, and Ca(2+), as well as by exogenous
CC       Zn(2+). {ECO:0000250|UniProtKB:Q92504}.
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   -!- 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:0000255}.
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DR   EMBL; AJ630366; CAI11432.1; -; Genomic_DNA.
DR   RefSeq; NP_001041565.1; NM_001048100.1.
DR   AlphaFoldDB; Q5TJF6; -.
DR   SMR; Q5TJF6; -.
DR   STRING; 9612.ENSCAFP00000001312; -.
DR   PaxDb; Q5TJF6; -.
DR   PRIDE; Q5TJF6; -.
DR   GeneID; 481736; -.
DR   KEGG; cfa:481736; -.
DR   CTD; 7922; -.
DR   eggNOG; KOG2693; Eukaryota.
DR   InParanoid; Q5TJF6; -.
DR   Proteomes; UP000002254; Unplaced.
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: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   3: Inferred from homology;
KW   Endoplasmic reticulum; Golgi apparatus; Ion transport; Membrane;
KW   Methylation; Phosphoprotein; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport; Zinc; Zinc transport.
FT   CHAIN           1..469
FT                   /note="Zinc transporter SLC39A7"
FT                   /id="PRO_0000213687"
FT   TRANSMEM        5..25
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        138..158
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        169..189
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        214..234
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        386..406
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        417..437
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        448..468
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          43..122
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          242..313
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        43..116
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        242..257
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        266..313
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         275
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q92504"
FT   MOD_RES         276
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q92504"
SQ   SEQUENCE   469 AA;  49916 MW;  8266CA42D94D4024 CRC64;
     MARGLGAPHW VAVGLLTWAA LGLLVAGHGG HGDLHEDLHE DFHGHSHRRS HEDFHHGHSY
     AHGHGHTHES IWHGHTHGHE HGHAHEDLHH GHSHGQSHES LYHRGHGHDH EHSHGGYGES
     GAPGIKQDLD TVTLWAYALG ATVLISAAPF FVLFLIPVES NSPRHRSLLQ ILLSFASGGL
     LGDAFLHLIP HALEPHSHHP LEQPGHGHSH SGQGPILSVG LWVLSGIVAF LVVEKFVRHV
     KGGHGHSHGH GHTHGHTQGS HGHGTQKYPS KEKQSSEEEE KEANGSRKRK GGSTRLKDGP
     LRPQNSEEEK TGSDLRVSGY LNLAADLAHN FTDGLAIGAS FRGGRGLGIL TTMTVLLHEV
     PHEVGDFAIL VQSGCSKKQA MRLQLLTAIG ALAGTACALL TEGGAVGSEV AGGTGSGWVL
     PFTAGGFIYV ATVSVLPELL REASPLQSLL EVLGLLGGVV MMVLIAHLE