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ZNT6_CHICK
ID   ZNT6_CHICK              Reviewed;         460 AA.
AC   Q5ZIH3;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Zinc transporter 6;
DE            Short=ZnT-6;
DE   AltName: Full=Solute carrier family 30 member 6;
GN   Name=SLC30A6; Synonyms=ZNT6; ORFNames=RCJMB04_26e2;
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], FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
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).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=CB; TISSUE=Bursa of Fabricius;
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA   Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA   Hayashizaki Y., Buerstedde J.-M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:R6.1-R6.9(2005).
CC   -!- FUNCTION: Zinc-efflux transporter which allocates the cytoplasmic zinc
CC       to the trans-Golgi network (TGN) as well as the vesicular compartment.
CC       {ECO:0000269|PubMed:15994300}.
CC   -!- SUBUNIT: Heterooligomer. Interacts with ZNT5.
CC       {ECO:0000269|PubMed:15994300}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC       {ECO:0000269|PubMed:15994300}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:15994300}. Note=Found in vesicles.
CC   -!- MISCELLANEOUS: Seems to have lost most of the histidine residues in the
CC       loop between the fourth and fifth transmembrane regions and appears to
CC       exert transport function by forming complexes with ZNT5. {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; AJ720811; CAG32470.1; -; mRNA.
DR   EMBL; AY986776; AAY53770.1; -; mRNA.
DR   RefSeq; NP_001006402.1; NM_001006402.1.
DR   AlphaFoldDB; Q5ZIH3; -.
DR   SMR; Q5ZIH3; -.
DR   STRING; 9031.ENSGALP00000017255; -.
DR   PaxDb; Q5ZIH3; -.
DR   GeneID; 421480; -.
DR   KEGG; gga:421480; -.
DR   CTD; 55676; -.
DR   VEuPathDB; HostDB:geneid_421480; -.
DR   eggNOG; KOG1484; Eukaryota.
DR   HOGENOM; CLU_034201_0_0_1; -.
DR   InParanoid; Q5ZIH3; -.
DR   OrthoDB; 969431at2759; -.
DR   PhylomeDB; Q5ZIH3; -.
DR   TreeFam; TF313167; -.
DR   PRO; PR:Q5ZIH3; -.
DR   Proteomes; UP000000539; Unplaced.
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:0005385; F:zinc ion transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0006829; P:zinc ion transport; IBA:GO_Central.
DR   Gene3D; 1.20.1510.10; -; 1.
DR   InterPro; IPR002524; Cation_efflux.
DR   InterPro; IPR027469; Cation_efflux_TMD_sf.
DR   Pfam; PF01545; Cation_efflux; 1.
DR   SUPFAM; SSF161111; SSF161111; 1.
DR   TIGRFAMs; TIGR01297; CDF; 1.
PE   1: Evidence at protein level;
KW   Golgi apparatus; Ion transport; Membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix; Transport; Zinc; Zinc transport.
FT   CHAIN           1..460
FT                   /note="Zinc transporter 6"
FT                   /id="PRO_0000312575"
FT   TOPO_DOM        1..33
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        34..54
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        55..64
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        65..85
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        86..98
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        99..119
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        120..134
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        135..155
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        156..200
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        201..221
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        222..228
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        229..249
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        250..460
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          372..392
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   460 AA;  50936 MW;  6D9EB207DC180E82 CRC64;
     MGTIHLFRKS QRSLVGKLTH EFRLVAADRR SWKILLFGAI NLICIGFLLM WCSSTNSIAL
     TAYTYLTIFD LFSLITCLIS YWVMVKKPSP VYSFGFERFE VLAVFASTVL AQLGALFILK
     ESAERFLEQP EIHTGRLLVG TFVALFFNLF TMLSVRNKPF AYVSEAASTS WLQEHVADLS
     RSICGIIPGL SSIFLPRMNP FVLIDIAGAL ALCITYMLIE INNYYAVDTA SAIAIALMTF
     GTMYPMSVYS GKVLLQTTPP HVFGQLDKLL REVSTLDGVL EVRNEHFWTL GFGTLAGSVH
     VRIRRDANEQ MVLAHVTNRL YTLVSTLTVQ IFKDDWIRPT LSSVPIANNM LNLSDHHVIT
     MPSLKAADNL NPVTSTPAKP SSPPPEFSFN TPGKNVNPVI LLNTQTRPYG LGLNHGSTPY
     SSVLNQGFGI PGMGATQGFR TGFTNVPSRY GTNTRGQSRP
 
 
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