ID   S39A7_PONAB             Reviewed;         469 AA.
AC   Q5RFD5;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 64.
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:0000250|UniProtKB:Q92504};
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1] {ECO:0000312|EMBL:CAH89522.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney {ECO:0000312|EMBL:CAH89522.1};
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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; CR857223; CAH89522.1; -; mRNA.
DR   RefSeq; NP_001127161.1; NM_001133689.2.
DR   AlphaFoldDB; Q5RFD5; -.
DR   SMR; Q5RFD5; -.
DR   STRING; 9601.ENSPPYP00000019325; -.
DR   GeneID; 100174212; -.
DR   KEGG; pon:100174212; -.
DR   CTD; 7922; -.
DR   eggNOG; KOG2693; Eukaryota.
DR   InParanoid; Q5RFD5; -.
DR   OrthoDB; 657777at2759; -.
DR   Proteomes; UP000001595; 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:0046873; F:metal ion transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0006829; P:zinc ion transport; IEA:UniProtKB-KW.
DR   InterPro; IPR003689; ZIP.
DR   Pfam; PF02535; Zip; 1.
PE   2: Evidence at transcript 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..469
FT                   /note="Zinc transporter SLC39A7"
FT                   /id="PRO_0000213691"
FT   TRANSMEM        10..30
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        410..430
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        448..468
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          42..121
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          242..310
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        56..115
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        242..259
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        260..288
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;  49944 MW;  3E862EB1C798FFB4 CRC64;
     MARGLGAPHW VAVGLLTWAT LGLLVAELGG HDDLHDDLQE DFHGHSHRHS HEDFHHGHSH
     AHGHGHTHES IWHGHTHGHD HGHSHGDLHH GHSHGHSHES LYHRGHGHDN EHSRGGYGES
     GAPGIKQDLD AVTLWAYALG ATVLISAAPF FVLFLIPVES NSPRHRSLLQ ILLSFASGGL
     LGDAFLHLIP HALEPHSHHT LEQPGHGHSH SGQGPILSVG LWVLSGIVAF LVVEKFVRHV
     KGGHGHSHGH GHAHSHTHGS HGHGRQECST KEKQSSEEEE KETRGVQKRR GGSTVPKDGP
     VRPQNAEEEK RGLDLRVSGY LNLAADLAHN FTDGLAIGAS FRGGRGLGIL TTMTVLLHEV
     PHEVGDFAIL VQSGCSKKQA MRLQLLTAVG ALAGTACALL TEGGAVGSEI AGGAGPGWVL
     PFTAGGFIYV ATVSVLPELL REASPLQSLL EVLGLLGGVV MMVLIAHLE