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Database: UniProt
Entry: A0A1S3AIA1_ERIEU
LinkDB: A0A1S3AIA1_ERIEU
Original site: A0A1S3AIA1_ERIEU 
ID   A0A1S3AIA1_ERIEU        Unreviewed;       307 AA.
AC   A0A1S3AIA1;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=Zinc transporter ZIP9 {ECO:0000256|ARBA:ARBA00026135, ECO:0000256|RuleBase:RU369011};
DE            Short=ZIP-9 {ECO:0000256|RuleBase:RU369011};
DE   AltName: Full=Solute carrier family 39 member 9 {ECO:0000256|ARBA:ARBA00031674, ECO:0000256|RuleBase:RU369011};
DE   AltName: Full=Zrt- and Irt-like protein 9 {ECO:0000256|ARBA:ARBA00031377, ECO:0000256|RuleBase:RU369011};
GN   Name=SLC39A9 {ECO:0000313|RefSeq:XP_007535381.1};
OS   Erinaceus europaeus (Western European hedgehog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Eulipotyphla; Erinaceidae; Erinaceinae;
OC   Erinaceus.
OX   NCBI_TaxID=9365 {ECO:0000313|Proteomes:UP000079721, ECO:0000313|RefSeq:XP_007535381.1};
RN   [1] {ECO:0000313|RefSeq:XP_007535381.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: Transports zinc ions across cell and organelle membranes into
CC       the cytoplasm and regulates intracellular zinc homeostasis.
CC       Participates in the zinc ions efflux out of the secretory compartments.
CC       Also functions as membrane androgen receptor that mediates, through a G
CC       protein, the non-classical androgen signaling pathway, characterized by
CC       the activation of MAPK3/MAPK1 (Erk1/2) and transcription factors CREB1
CC       or ATF1. Moreover, has dual functions as membrane-bound androgen
CC       receptor and as an androgen-dependent zinc transporter both of which
CC       are mediated through an inhibitory G protein (Gi) that mediates both
CC       MAP kinase and zinc signaling leading to the androgen-dependent
CC       apoptotic process. {ECO:0000256|RuleBase:RU369011}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Zn(2+)(in) = Zn(2+)(out); Xref=Rhea:RHEA:29351,
CC         ChEBI:CHEBI:29105; Evidence={ECO:0000256|ARBA:ARBA00034634};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU369011};
CC       Multi-pass membrane protein {ECO:0000256|RuleBase:RU369011}. Cytoplasm,
CC       perinuclear region {ECO:0000256|ARBA:ARBA00004556,
CC       ECO:0000256|RuleBase:RU369011}. Golgi apparatus, trans-Golgi network
CC       membrane {ECO:0000256|ARBA:ARBA00004198,
CC       ECO:0000256|RuleBase:RU369011}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}. Mitochondrion
CC       {ECO:0000256|ARBA:ARBA00004173, ECO:0000256|RuleBase:RU369011}. Nucleus
CC       {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU369011}.
CC   -!- SIMILARITY: Belongs to the ZIP transporter (TC 2.A.5) family.
CC       {ECO:0000256|RuleBase:RU369011}.
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DR   RefSeq; XP_007535381.1; XM_007535319.2.
DR   AlphaFoldDB; A0A1S3AIA1; -.
DR   GeneID; 103124589; -.
DR   CTD; 55334; -.
DR   eggNOG; KOG3907; Eukaryota.
DR   InParanoid; A0A1S3AIA1; -.
DR   OrthoDB; 1384563at2759; -.
DR   Proteomes; UP000079721; Unplaced.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005385; F:zinc ion transmembrane transporter activity; IEA:UniProtKB-UniRule.
DR   InterPro; IPR003689; ZIP.
DR   InterPro; IPR045891; ZIP9.
DR   PANTHER; PTHR16133; SOLUTE CARRIER FAMILY 39 ZINC TRANSPORTER , MEMBER 9-RELATED; 1.
DR   PANTHER; PTHR16133:SF5; ZINC TRANSPORTER ZIP9; 1.
DR   Pfam; PF02535; Zip; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Glycoprotein {ECO:0000256|RuleBase:RU369011};
KW   Ion transport {ECO:0000256|RuleBase:RU369011};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU369011};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000079721};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU369011};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU369011}; Transport {ECO:0000256|RuleBase:RU369011};
KW   Zinc {ECO:0000256|RuleBase:RU369011};
KW   Zinc transport {ECO:0000256|RuleBase:RU369011}.
FT   TRANSMEM        6..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU369011"
FT   TRANSMEM        35..55
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU369011"
FT   TRANSMEM        104..122
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU369011"
FT   TRANSMEM        176..198
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU369011"
FT   TRANSMEM        210..229
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU369011"
FT   TRANSMEM        241..263
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU369011"
FT   TRANSMEM        283..304
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU369011"
SQ   SEQUENCE   307 AA;  32252 MW;  7D109EA96BD4EFAA CRC64;
     MDDFFSISLL SLAMLVGCYV AGIIPLAVNF SEERLKLVTV LGAGLLCGTA LAVIVPEGVH
     ALYEDILEGN HHQPSETQNV IASAKETDAR VAHEHEHSHE HTQLHAYIGV SLVLGFVFML
     LVDQIGSSHV HSTDDPEAAR SSTSKITTTL GLVVHAAADG VALGAAASTS QTSVQLIVFV
     AIMLHKAPAA FGLVSFLMHA GLERNRIRKH LLVFALAAPA MSMMTYLGLS KSSKEALSEV
     NATGVAMLFS AGTFLYVATV HVLPEVGGIG HSHKTDPAGG KGLSRLEVAA LVLGCLIPLI
     LSVGHQH
//
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