ID A0A091FKV1_9AVES Unreviewed; 305 AA.
AC A0A091FKV1;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Zinc transporter ZIP9 {ECO:0000256|RuleBase:RU369011};
DE Short=ZIP-9 {ECO:0000256|RuleBase:RU369011};
DE AltName: Full=Solute carrier family 39 member 9 {ECO:0000256|RuleBase:RU369011};
DE AltName: Full=Zrt- and Irt-like protein 9 {ECO:0000256|RuleBase:RU369011};
GN ORFNames=N303_07136 {ECO:0000313|EMBL:KFO70228.1};
OS Cuculus canorus (common cuckoo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Cuculiformes; Cuculidae; Cuculus.
OX NCBI_TaxID=55661 {ECO:0000313|EMBL:KFO70228.1, ECO:0000313|Proteomes:UP000053760};
RN [1] {ECO:0000313|EMBL:KFO70228.1, ECO:0000313|Proteomes:UP000053760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N303 {ECO:0000313|EMBL:KFO70228.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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 EMBL; KL447134; KFO70228.1; -; Genomic_DNA.
DR RefSeq; XP_009563235.1; XM_009564940.1.
DR AlphaFoldDB; A0A091FKV1; -.
DR STRING; 55661.A0A091FKV1; -.
DR GeneID; 104062819; -.
DR KEGG; cuca:104062819; -.
DR CTD; 55334; -.
DR OrthoDB; 1384563at2759; -.
DR Proteomes; UP000053760; Unassembled WGS sequence.
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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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:UP000053760};
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 102..120
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU369011"
FT TRANSMEM 174..196
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU369011"
FT TRANSMEM 208..227
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU369011"
FT TRANSMEM 239..261
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU369011"
FT TRANSMEM 281..302
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU369011"
SQ SEQUENCE 305 AA; 32164 MW; 1CB1FBE950E45E72 CRC64;
MDDFRSICLL SLAMLVACYV AGIIPLAVNF SEERLKLVTV LGAGLLCGTA LAVIVPEGVH
ALYEDILEGK HHPASEMQRV IESEKVAEIP VVHEYGHDHS RLHAYIGVSL VLGFVFMLLV
DQIGSSHVHS TDDPEAARSG NSKITTTLGL VVHAAADGVA LGAAASTSQT SVQLIVFVAI
MLHKAPAAFG LVSFLMHAGL ERNRIRKHLL VFALAAPVMS MVTYLGLSKS SKEALSEVNA
TGVAMLFSAG TFLYVATVHV LPEVGGIAHS HKPESTGGKG LSRLEVAALV LGCLIPLVLS
IGHHH
//
