ID S39A9_HUMAN Reviewed; 307 AA.
AC Q9NUM3; G3V5J8; Q53HN3; Q5MJQ0; Q6P2Q1; Q86WY2;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 2.
DT 27-MAR-2024, entry version 148.
DE RecName: Full=Zinc transporter ZIP9 {ECO:0000305};
DE AltName: Full=Solute carrier family 39 member 9;
DE AltName: Full=Zrt- and Irt-like protein 9;
DE Short=ZIP-9;
GN Name=SLC39A9 {ECO:0000312|HGNC:HGNC:20182}; Synonyms=ZIP9;
GN ORFNames=UNQ714/PRO1377;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT THR-221.
RA Lin L., Zhong G., Ke R., Li H., Shen C., Nong W., Zhou G., Yang S.;
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORM 3).
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT CYS-285.
RC TISSUE=Duodenum, and Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP FUNCTION, TRANSPORTER ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=19420709; DOI=10.1271/bbb.80910;
RA Matsuura W., Yamazaki T., Yamaguchi-Iwai Y., Masuda S., Nagao M.,
RA Andrews G.K., Kambe T.;
RT "SLC39A9 (ZIP9) regulates zinc homeostasis in the secretory pathway:
RT characterization of the ZIP subfamily I protein in vertebrate cells.";
RL Biosci. Biotechnol. Biochem. 73:1142-1148(2009).
RN [7]
RP FUNCTION.
RX PubMed=23505453; DOI=10.1371/journal.pone.0058022;
RA Taniguchi M., Fukunaka A., Hagihara M., Watanabe K., Kamino S., Kambe T.,
RA Enomoto S., Hiromura M.;
RT "Essential role of the zinc transporter ZIP9/SLC39A9 in regulating the
RT activations of Akt and Erk in B-cell receptor signaling pathway in DT40
RT cells.";
RL PLoS ONE 8:e58022-e58022(2013).
RN [8]
RP FUNCTION, TRANSPORTER ACTIVITY, SUBCELLULAR LOCATION, INDUCTION, AND TISSUE
RP SPECIFICITY.
RX PubMed=25014355; DOI=10.1210/en.2014-1201;
RA Thomas P., Pang Y., Dong J., Berg A.H.;
RT "Identification and characterization of membrane androgen receptors in the
RT ZIP9 zinc transporter subfamily: II. Role of human ZIP9 in testosterone-
RT induced prostate and breast cancer cell apoptosis.";
RL Endocrinology 155:4250-4265(2014).
RN [9]
RP FUNCTION, AND TRANSPORTER ACTIVITY.
RX PubMed=28219737; DOI=10.1016/j.mce.2017.02.025;
RA Thomas P., Pang Y., Dong J.;
RT "Membrane androgen receptor characteristics of human ZIP9 (SLC39A) zinc
RT transporter in prostate cancer cells: Androgen-specific activation and
RT involvement of an inhibitory G protein in zinc and MAP kinase signaling.";
RL Mol. Cell. Endocrinol. 447:23-34(2017).
RN [10]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=34555425; DOI=10.1016/j.mce.2021.111461;
RA Converse A., Thomas P.;
RT "Androgens promote vascular endothelial cell proliferation through
RT activation of a ZIP9-dependent inhibitory G protein/PI3K-Akt/Erk/cyclin D1
RT pathway.";
RL Mol. Cell. Endocrinol. 538:111461-111461(2021).
CC -!- FUNCTION: Transports zinc ions across cell and organelle membranes into
CC the cytoplasm and regulates intracellular zinc homeostasis
CC (PubMed:25014355, PubMed:19420709, PubMed:28219737). Participates in
CC the zinc ions efflux out of the secretory compartments
CC (PubMed:19420709). Regulates intracellular zinc level, resulting in the
CC enhancement of AKT1 and MAPK3/MAPK1 (Erk1/2) phosphorylation in
CC response to the BCR activation (PubMed:23505453). Also functions as a
CC membrane androgen receptor that mediates, through a G protein, the non-
CC classical androgen signaling pathway, characterized by the activation
CC of MAPK3/MAPK1 (Erk1/2) and transcription factors CREB1 or ATF1 (By
CC similarity). This pathway contributes to CLDN1 and CLDN5 expression and
CC tight junction formation between adjacent Sertoli cells (By
CC similarity). Mediates androgen-induced vascular endothelial cell
CC proliferation through activation of an inhibitory G protein leading to
CC the AKT1 and MAPK3/MAPK1 (Erk1/2) activation which in turn modulate
CC inhibition (phosphorylation) of GSK3B and CCND1 transcription
CC (PubMed:34555425). Moreover, has dual functions as a membrane-bound
CC androgen receptor and as an androgen-dependent zinc transporter both of
CC which are mediated through an inhibitory G protein (Gi) that mediates
CC both MAP kinase and zinc signaling leading to the androgen-dependent
CC apoptotic process (PubMed:25014355, PubMed:28219737).
CC {ECO:0000250|UniProtKB:Q3KR82, ECO:0000250|UniProtKB:Q8BFU1,
CC ECO:0000269|PubMed:19420709, ECO:0000269|PubMed:23505453,
CC ECO:0000269|PubMed:25014355, ECO:0000269|PubMed:28219737,
CC ECO:0000269|PubMed:34555425}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Zn(2+)(in) = Zn(2+)(out); Xref=Rhea:RHEA:29351,
CC ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:19420709,
CC ECO:0000269|PubMed:25014355, ECO:0000305|PubMed:28219737};
CC -!- INTERACTION:
CC Q9NUM3; Q86W74-2: ANKRD46; NbExp=3; IntAct=EBI-2823239, EBI-12109402;
CC Q9NUM3; Q96BI3: APH1A; NbExp=3; IntAct=EBI-2823239, EBI-2606935;
CC Q9NUM3; Q13520: AQP6; NbExp=3; IntAct=EBI-2823239, EBI-13059134;
CC Q9NUM3; Q12982: BNIP2; NbExp=3; IntAct=EBI-2823239, EBI-752094;
CC Q9NUM3; Q8N350-4: CBARP; NbExp=3; IntAct=EBI-2823239, EBI-19051169;
CC Q9NUM3; P11912: CD79A; NbExp=3; IntAct=EBI-2823239, EBI-7797864;
CC Q9NUM3; Q8IU89: CERS3; NbExp=3; IntAct=EBI-2823239, EBI-18202821;
CC Q9NUM3; Q7Z7G2: CPLX4; NbExp=3; IntAct=EBI-2823239, EBI-18013275;
CC Q9NUM3; Q9BUF7-2: CRB3; NbExp=3; IntAct=EBI-2823239, EBI-17233035;
CC Q9NUM3; Q96BA8: CREB3L1; NbExp=3; IntAct=EBI-2823239, EBI-6942903;
CC Q9NUM3; Q68CJ9: CREB3L3; NbExp=3; IntAct=EBI-2823239, EBI-852194;
CC Q9NUM3; O43169: CYB5B; NbExp=3; IntAct=EBI-2823239, EBI-1058710;
CC Q9NUM3; Q9NYP7: ELOVL5; NbExp=3; IntAct=EBI-2823239, EBI-11037623;
CC Q9NUM3; P34910-2: EVI2B; NbExp=3; IntAct=EBI-2823239, EBI-17640610;
CC Q9NUM3; O15552: FFAR2; NbExp=3; IntAct=EBI-2823239, EBI-2833872;
CC Q9NUM3; P48165: GJA8; NbExp=3; IntAct=EBI-2823239, EBI-17458373;
CC Q9NUM3; Q96P66: GPR101; NbExp=3; IntAct=EBI-2823239, EBI-17935713;
CC Q9NUM3; Q9BSE4: HERPUD2; NbExp=3; IntAct=EBI-2823239, EBI-2868124;
CC Q9NUM3; P28335: HTR2C; NbExp=3; IntAct=EBI-2823239, EBI-994141;
CC Q9NUM3; Q9UIQ6-2: LNPEP; NbExp=3; IntAct=EBI-2823239, EBI-12133176;
CC Q9NUM3; Q9NQG1: MANBAL; NbExp=3; IntAct=EBI-2823239, EBI-3867271;
CC Q9NUM3; Q5SR56: MFSD14B; NbExp=3; IntAct=EBI-2823239, EBI-373355;
CC Q9NUM3; Q6N075: MFSD5; NbExp=3; IntAct=EBI-2823239, EBI-3920969;
CC Q9NUM3; O14880: MGST3; NbExp=3; IntAct=EBI-2823239, EBI-724754;
CC Q9NUM3; Q99519: NEU1; NbExp=3; IntAct=EBI-2823239, EBI-721517;
CC Q9NUM3; Q5QGT7: RTP2; NbExp=3; IntAct=EBI-2823239, EBI-10244780;
CC Q9NUM3; Q3KNW5: SLC10A6; NbExp=3; IntAct=EBI-2823239, EBI-18159983;
CC Q9NUM3; Q9NP94: SLC39A2; NbExp=3; IntAct=EBI-2823239, EBI-12898013;
CC Q9NUM3; Q6ZP29-3: SLC66A1; NbExp=3; IntAct=EBI-2823239, EBI-12889586;
CC Q9NUM3; P30825: SLC7A1; NbExp=3; IntAct=EBI-2823239, EBI-4289564;
CC Q9NUM3; Q8WWF3: SSMEM1; NbExp=3; IntAct=EBI-2823239, EBI-17280858;
CC Q9NUM3; Q96CE8: TM4SF18; NbExp=3; IntAct=EBI-2823239, EBI-13351685;
CC Q9NUM3; Q9NV12: TMEM140; NbExp=3; IntAct=EBI-2823239, EBI-2844246;
CC Q9NUM3; Q96Q45-2: TMEM237; NbExp=3; IntAct=EBI-2823239, EBI-10982110;
CC Q9NUM3; Q8N661: TMEM86B; NbExp=3; IntAct=EBI-2823239, EBI-2548832;
CC Q9NUM3; P34981: TRHR; NbExp=3; IntAct=EBI-2823239, EBI-18055230;
CC Q9NUM3; Q96GC9: VMP1; NbExp=3; IntAct=EBI-2823239, EBI-2800296;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC {ECO:0000269|PubMed:19420709}. Cell membrane
CC {ECO:0000269|PubMed:25014355, ECO:0000269|PubMed:34555425}; Multi-pass
CC membrane protein {ECO:0000305}. Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:25014355, ECO:0000269|PubMed:34555425}.
CC Mitochondrion {ECO:0000269|PubMed:25014355,
CC ECO:0000269|PubMed:34555425}. Nucleus {ECO:0000269|PubMed:25014355}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9NUM3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NUM3-2; Sequence=VSP_027302;
CC Name=3;
CC IsoId=Q9NUM3-3; Sequence=VSP_054057, VSP_054058;
CC -!- TISSUE SPECIFICITY: Highly expressed in pancreas, testis, and pituitary
CC and moderately in the kidney, liver, uterus, heart, prostate, and
CC brain, whereas expression is lower in the ovary and colon.
CC {ECO:0000269|PubMed:25014355}.
CC -!- INDUCTION: Up-regulated by testosterone in cancer cells.
CC {ECO:0000269|PubMed:25014355}.
CC -!- SIMILARITY: Belongs to the ZIP transporter (TC 2.A.5) family.
CC {ECO:0000305}.
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DR EMBL; AY358687; AAQ89050.1; -; mRNA.
DR EMBL; AK002136; BAA92100.1; -; mRNA.
DR EMBL; AK222547; BAD96267.1; -; mRNA.
DR EMBL; AY780789; AAV98359.1; -; mRNA.
DR EMBL; AL157996; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC047682; AAH47682.1; -; mRNA.
DR EMBL; BC064383; AAH64383.1; -; mRNA.
DR CCDS; CCDS58327.1; -. [Q9NUM3-3]
DR CCDS; CCDS58328.1; -. [Q9NUM3-2]
DR CCDS; CCDS9795.1; -. [Q9NUM3-1]
DR RefSeq; NP_001239077.1; NM_001252148.1. [Q9NUM3-2]
DR RefSeq; NP_001239079.1; NM_001252150.1. [Q9NUM3-3]
DR RefSeq; NP_001239080.1; NM_001252151.1.
DR RefSeq; NP_001239081.1; NM_001252152.1.
DR RefSeq; NP_060845.2; NM_018375.4. [Q9NUM3-1]
DR AlphaFoldDB; Q9NUM3; -.
DR SMR; Q9NUM3; -.
DR BioGRID; 120615; 134.
DR IntAct; Q9NUM3; 82.
DR MINT; Q9NUM3; -.
DR STRING; 9606.ENSP00000336887; -.
DR DrugBank; DB14533; Zinc chloride.
DR DrugBank; DB14548; Zinc sulfate, unspecified form.
DR TCDB; 2.A.5.6.1; the zinc (zn(2+))-iron (fe(2+)) permease (zip) family.
DR GlyCosmos; Q9NUM3; 2 sites, No reported glycans.
DR GlyGen; Q9NUM3; 4 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; Q9NUM3; -.
DR PhosphoSitePlus; Q9NUM3; -.
DR BioMuta; SLC39A9; -.
DR DMDM; 156633628; -.
DR EPD; Q9NUM3; -.
DR jPOST; Q9NUM3; -.
DR MassIVE; Q9NUM3; -.
DR MaxQB; Q9NUM3; -.
DR PaxDb; 9606-ENSP00000336887; -.
DR PeptideAtlas; Q9NUM3; -.
DR ProteomicsDB; 33545; -.
DR ProteomicsDB; 82693; -. [Q9NUM3-1]
DR ProteomicsDB; 82694; -. [Q9NUM3-2]
DR Pumba; Q9NUM3; -.
DR TopDownProteomics; Q9NUM3-2; -. [Q9NUM3-2]
DR Antibodypedia; 107; 149 antibodies from 29 providers.
DR DNASU; 55334; -.
DR Ensembl; ENST00000336643.10; ENSP00000336887.5; ENSG00000029364.12. [Q9NUM3-1]
DR Ensembl; ENST00000555840.5; ENSP00000450639.1; ENSG00000029364.12. [Q9NUM3-1]
DR Ensembl; ENST00000556605.5; ENSP00000452385.1; ENSG00000029364.12. [Q9NUM3-3]
DR Ensembl; ENST00000557046.1; ENSP00000451833.1; ENSG00000029364.12. [Q9NUM3-2]
DR GeneID; 55334; -.
DR KEGG; hsa:55334; -.
DR MANE-Select; ENST00000336643.10; ENSP00000336887.5; NM_018375.5; NP_060845.2.
DR UCSC; uc001xle.5; human. [Q9NUM3-1]
DR AGR; HGNC:20182; -.
DR CTD; 55334; -.
DR DisGeNET; 55334; -.
DR GeneCards; SLC39A9; -.
DR HGNC; HGNC:20182; SLC39A9.
DR HPA; ENSG00000029364; Low tissue specificity.
DR MIM; 619116; gene.
DR neXtProt; NX_Q9NUM3; -.
DR OpenTargets; ENSG00000029364; -.
DR PharmGKB; PA134889179; -.
DR VEuPathDB; HostDB:ENSG00000029364; -.
DR eggNOG; KOG3907; Eukaryota.
DR GeneTree; ENSGT00390000010094; -.
DR InParanoid; Q9NUM3; -.
DR OMA; DDFPSIC; -.
DR OrthoDB; 1384563at2759; -.
DR PhylomeDB; Q9NUM3; -.
DR TreeFam; TF315051; -.
DR PathwayCommons; Q9NUM3; -.
DR SignaLink; Q9NUM3; -.
DR BioGRID-ORCS; 55334; 56 hits in 1160 CRISPR screens.
DR ChiTaRS; SLC39A9; human.
DR GenomeRNAi; 55334; -.
DR Pharos; Q9NUM3; Tbio.
DR PRO; PR:Q9NUM3; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q9NUM3; Protein.
DR Bgee; ENSG00000029364; Expressed in parotid gland and 186 other cell types or tissues.
DR ExpressionAtlas; Q9NUM3; baseline and differential.
DR Genevisible; Q9NUM3; HS.
DR GO; GO:0031966; C:mitochondrial membrane; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005802; C:trans-Golgi network; IDA:UniProtKB.
DR GO; GO:0005497; F:androgen binding; IDA:UniProtKB.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IDA:UniProtKB.
DR GO; GO:0022883; F:zinc efflux transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0005385; F:zinc ion transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0070830; P:bicellular tight junction assembly; ISS:UniProtKB.
DR GO; GO:0006882; P:intracellular zinc ion homeostasis; IDA:UniProtKB.
DR GO; GO:2000654; P:regulation of cellular response to testosterone stimulus; ISS:UniProtKB.
DR GO; GO:1905562; P:regulation of vascular endothelial cell proliferation; IMP:UniProtKB.
DR GO; GO:0071577; P:zinc ion transmembrane transport; IDA:UniProtKB.
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 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Cytoplasm; Glycoprotein;
KW Golgi apparatus; Ion transport; Membrane; Mitochondrion; Nucleus;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport; Zinc;
KW Zinc transport.
FT CHAIN 1..307
FT /note="Zinc transporter ZIP9"
FT /id="PRO_0000297597"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 35..55
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 106..126
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 146..166
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 176..196
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 210..230
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 244..264
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 286..306
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 29
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 241
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 135..157
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_027302"
FT VAR_SEQ 232
FT /note="S -> D (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12975309"
FT /id="VSP_054057"
FT VAR_SEQ 233..307
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12975309"
FT /id="VSP_054058"
FT VARIANT 64
FT /note="E -> D (in dbSNP:rs2296723)"
FT /id="VAR_034648"
FT VARIANT 221
FT /note="M -> T (in dbSNP:rs2232059)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_034649"
FT VARIANT 285
FT /note="R -> C (in dbSNP:rs17855898)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_034650"
FT CONFLICT 122
FT /note="V -> M (in Ref. 2; BAD96267)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 307 AA; 32251 MW; 3F2CB0ED7B193183 CRC64;
MDDFISISLL SLAMLVGCYV AGIIPLAVNF SEERLKLVTV LGAGLLCGTA LAVIVPEGVH
ALYEDILEGK HHQASETHNV IASDKAAEKS VVHEHEHSHD HTQLHAYIGV SLVLGFVFML
LVDQIGNSHV HSTDDPEAAR SSNSKITTTL GLVVHAAADG VALGAAASTS QTSVQLIVFV
AIMLHKAPAA FGLVSFLMHA GLERNRIRKH LLVFALAAPV MSMVTYLGLS KSSKEALSEV
NATGVAMLFS AGTFLYVATV HVLPEVGGIG HSHKPDATGG RGLSRLEVAA LVLGCLIPLI
LSVGHQH
//
