ZNT7_CHICK
ID ZNT7_CHICK Reviewed; 378 AA.
AC Q5MNV6;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Zinc transporter 7;
DE Short=ZnT-7;
DE AltName: Full=Solute carrier family 30 member 7;
GN Name=SLC30A7; Synonyms=ZNT7;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX PubMed=15525635; DOI=10.1074/jbc.m411247200;
RA Suzuki T., Ishihara K., Migaki H., Matsuura W., Kohda A., Okumura K.,
RA Nagao M., Yamaguchi-Iwai Y., Kambe T.;
RT "Zinc transporters, ZnT5 and ZnT7, are required for the activation of
RT alkaline phosphatases, zinc-requiring enzymes that are
RT glycosylphosphatidylinositol-anchored to the cytoplasmic membrane.";
RL J. Biol. Chem. 280:637-643(2005).
RN [2]
RP FUNCTION.
RX PubMed=15994300; DOI=10.1074/jbc.m506902200;
RA Suzuki T., Ishihara K., Migaki H., Ishihara K., Nagao M.,
RA Yamaguchi-Iwai Y., Kambe T.;
RT "Two different zinc transport complexes of cation diffusion facilitator
RT proteins localized in the secretory pathway operate to activate alkaline
RT phosphatases in vertebrate cells.";
RL J. Biol. Chem. 280:30956-30962(2005).
CC -!- FUNCTION: Seems to facilitate zinc transport from the cytoplasm into
CC the Golgi apparatus. Partly regulates cellular zinc homeostasis (By
CC similarity). Required with ZNT5 for the activation of zinc-requiring
CC enzymes, alkaline phosphatases (ALPs). Transports zinc into the lumens
CC of the Golgi apparatus and the vesicular compartments where ALPs
CC locate, thus, converting apoALPs to holoALPs. Required with ZNT5 and
CC ZNT6 for the activation of TNAP. {ECO:0000250,
CC ECO:0000269|PubMed:15525635, ECO:0000269|PubMed:15994300}.
CC -!- SUBUNIT: Homooligomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
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; AY703477; AAV98202.1; -; mRNA.
DR RefSeq; NP_001008788.1; NM_001008788.1.
DR AlphaFoldDB; Q5MNV6; -.
DR SMR; Q5MNV6; -.
DR STRING; 9031.ENSGALP00000032851; -.
DR PaxDb; Q5MNV6; -.
DR GeneID; 424464; -.
DR KEGG; gga:424464; -.
DR CTD; 148867; -.
DR VEuPathDB; HostDB:geneid_424464; -.
DR eggNOG; KOG1484; Eukaryota.
DR InParanoid; Q5MNV6; -.
DR OrthoDB; 1507860at2759; -.
DR PhylomeDB; Q5MNV6; -.
DR PRO; PR:Q5MNV6; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0046873; F:metal ion transmembrane transporter activity; IBA:GO_Central.
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; IEA:Ensembl.
DR GO; GO:1904257; P:zinc ion import into Golgi apparatus; IBA:GO_Central.
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; 1.
DR Pfam; PF01545; Cation_efflux; 1.
DR SUPFAM; SSF161111; SSF161111; 1.
DR TIGRFAMs; TIGR01297; CDF; 1.
PE 2: Evidence at transcript level;
KW Golgi apparatus; Ion transport; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport; Zinc; Zinc transport.
FT CHAIN 1..378
FT /note="Zinc transporter 7"
FT /id="PRO_0000314302"
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..223
FT /note="His-rich loop"
FT REGION 185..214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..207
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 378 AA; 41989 MW; E49508ACB14C2686 CRC64;
MLPLSIKDDE YKPPRLNLFR KMSGWFRSIL ADKTSRNLFF FLCLNLSFAF VELLYGVWSN
SLGLISDSFH MFFDCTALLA GLAASVISKW RSNDAFSYGY VRAEVLAGFV NGLFLIFTAF
FIFSEGVERA LEPPDVHHER LLPVSILGFI VNLIGIFVFQ HGGHGHSHGS GHEHSHSLFN
GGLSHGHSHR GHGHSHEHKH GHTHDHGHSH GLSHGQDYCH DDHCLEGMTG SSKQILQGVF
LHIVADTLGS IGVIISAILM QNYGLMIADP ICSMLIALLI GVSIVPLLKE SIGILMQRTP
PSLENALPQC YQRVQQLQGV YSLHDPHFWT LCTDVYIGTL KLLVAPDADG RWILSQTHNI
FTQAGVRQLY IQIDVAAM
