ID S39AE_DANRE Reviewed; 494 AA. AC A0A0G2KQY6; DT 18-JAN-2017, integrated into UniProtKB/Swiss-Prot. DT 22-JUL-2015, sequence version 1. DT 08-MAY-2019, entry version 24. DE RecName: Full=Zinc transporter ZIP14 {ECO:0000305}; DE AltName: Full=Solute carrier family 39 member 14 {ECO:0000305}; DE AltName: Full=Zrt- and Irt-like protein 14 {ECO:0000303|PubMed:27231142}; DE Short=ZIP-14 {ECO:0000303|PubMed:27231142}; DE Flags: Precursor; GN Name=slc39a14 {ECO:0000303|PubMed:27231142}; GN Synonyms=zip14 {ECO:0000303|PubMed:27231142}; OS Danio rerio (Zebrafish) (Brachydanio rerio). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes; OC Cyprinidae; Danio. OX NCBI_TaxID=7955; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Tuebingen; RX PubMed=23594743; DOI=10.1038/nature12111; RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., RA Muffato M., Collins J.E., Humphray S., McLaren K., Matthews L., RA McLaren S., Sealy I., Caccamo M., Churcher C., Scott C., Barrett J.C., RA Koch R., Rauch G.J., White S., Chow W., Kilian B., Quintais L.T., RA Guerra-Assuncao J.A., Zhou Y., Gu Y., Yen J., Vogel J.H., Eyre T., RA Redmond S., Banerjee R., Chi J., Fu B., Langley E., Maguire S.F., RA Laird G.K., Lloyd D., Kenyon E., Donaldson S., Sehra H., RA Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M., RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J., RA Clee C., Oliver K., Clark R., Riddle C., Eliott D., Threadgold G., RA Harden G., Ware D., Mortimer B., Kerry G., Heath P., Phillimore B., RA Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S., Pelan S., RA Griffiths G., Smith M., Glithero R., Howden P., Barker N., Stevens C., RA Harley J., Holt K., Panagiotidis G., Lovell J., Beasley H., RA Henderson C., Gordon D., Auger K., Wright D., Collins J., Raisen C., RA Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D., RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S., RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E., RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., RA Babbage A., Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., RA Wray P., Ellington A., Matthews N., Ellwood M., Woodmansey R., RA Clark G., Cooper J., Tromans A., Grafham D., Skuce C., Pandian R., RA Andrews R., Harrison E., Kimberley A., Garnett J., Fosker N., Hall R., RA Garner P., Kelly D., Bird C., Palmer S., Gehring I., Berger A., RA Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M., RA Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M., RA Rudolph-Geiger S., Teucke M., Osoegawa K., Zhu B., Rapp A., Widaa S., RA Langford C., Yang F., Carter N.P., Harrow J., Ning Z., Herrero J., RA Searle S.M., Enright A., Geisler R., Plasterk R.H., Lee C., RA Westerfield M., de Jong P.J., Zon L.I., Postlethwait J.H., RA Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., Rogers J., RA Stemple D.L.; RT "The zebrafish reference genome sequence and its relationship to the RT human genome."; RL Nature 496:498-503(2013). RN [2] RP FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND RP DEVELOPMENTAL STAGE. RX PubMed=27231142; DOI=10.1038/ncomms11601; RA Tuschl K., Meyer E., Valdivia L.E., Zhao N., Dadswell C., RA Abdul-Sada A., Hung C.Y., Simpson M.A., Chong W.K., Jacques T.S., RA Woltjer R.L., Eaton S., Gregory A., Sanford L., Kara E., Houlden H., RA Cuno S.M., Prokisch H., Valletta L., Tiranti V., Younis R., RA Maher E.R., Spencer J., Straatman-Iwanowska A., Gissen P., Selim L.A., RA Pintos-Morell G., Coroleu-Lletget W., Mohammad S.S., Yoganathan S., RA Dale R.C., Thomas M., Rihel J., Bodamer O.A., Enns C.A., RA Hayflick S.J., Clayton P.T., Mills P.B., Kurian M.A., Wilson S.W.; RT "Mutations in SLC39A14 disrupt manganese homeostasis and cause RT childhood-onset parkinsonism-dystonia."; RL Nat. Commun. 7:11601-11601(2016). CC -!- FUNCTION: Broad-scope metal ion transporter with a preference for CC zinc uptake. Also mediates cellular uptake of nontransferrin-bound CC iron. {ECO:0000269|PubMed:27231142}. CC -!- SUBUNIT: Homotrimer. {ECO:0000250|UniProtKB:Q15043}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:27231142}; CC Multi-pass membrane protein {ECO:0000255}. Cytoplasm CC {ECO:0000250|UniProtKB:Q15043}. Cell projection, lamellipodium CC {ECO:0000250|UniProtKB:Q15043}. CC -!- DEVELOPMENTAL STAGE: Expressed at all stages of embryonic and CC early larval development. {ECO:0000269|PubMed:27231142}. CC -!- DISRUPTION PHENOTYPE: Embryos with CRISPR-induced slc39a14 null CC mutations display altered manganese homeostasis. This is CC associated with manganese deposition in the brain and altered CC locomotor activity. Mutants survived into adulthood without any CC obvious morphological or developmental defects. CC {ECO:0000269|PubMed:27231142}. CC -!- SIMILARITY: Belongs to the ZIP transporter (TC 2.A.5) family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CABZ01088693; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CABZ01088694; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CABZ01088695; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CABZ01088696; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CABZ01088697; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CABZ01088698; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; NP_001313628.1; NM_001326699.1. DR SMR; A0A0G2KQY6; -. DR Ensembl; ENSDART00000163942; ENSDARP00000134809; ENSDARG00000102387. DR Ensembl; ENSDART00000185624; ENSDARP00000156772; ENSDARG00000102387. DR GeneID; 799782; -. DR KEGG; dre:799782; -. DR CTD; 23516; -. DR ZFIN; ZDB-GENE-060315-2; slc39a14. DR GeneTree; ENSGT00940000157986; -. DR KO; K14720; -. DR OMA; GCYWLKG; -. DR OrthoDB; 657777at2759; -. DR Reactome; R-DRE-442380; Zinc influx into cells by the SLC39 gene family. DR PRO; PR:A0A0G2KQY6; -. DR Proteomes; UP000000437; Chromosome 5. DR Bgee; ENSDARG00000102387; Expressed in 22 organ(s), highest expression level in female gonad. DR ExpressionAtlas; A0A0G2KQY6; baseline and differential. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central. DR GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0005384; F:manganese ion transmembrane transporter activity; ISS:UniProtKB. DR GO; GO:0005385; F:zinc ion transmembrane transporter activity; ISS:ZFIN. DR GO; GO:0006882; P:cellular zinc ion homeostasis; IBA:GO_Central. DR GO; GO:0055071; P:manganese ion homeostasis; IMP:ZFIN. DR GO; GO:0071578; P:zinc ion import across plasma membrane; ISS:UniProtKB. DR GO; GO:0006829; P:zinc ion transport; ISS:ZFIN. DR InterPro; IPR003689; ZIP. DR Pfam; PF02535; Zip; 1. PE 2: Evidence at transcript level; KW Cell membrane; Cell projection; Complete proteome; Cytoplasm; KW Ion transport; Membrane; Reference proteome; Signal; Transmembrane; KW Transmembrane helix; Transport; Zinc; Zinc transport. FT SIGNAL 1 34 {ECO:0000255}. FT CHAIN 35 494 Zinc transporter ZIP14. {ECO:0000255}. FT /FTId=PRO_5002547407. FT TOPO_DOM 35 152 Extracellular. {ECO:0000305}. FT TRANSMEM 153 173 Helical. {ECO:0000255}. FT TOPO_DOM 174 181 Cytoplasmic. {ECO:0000305}. FT TRANSMEM 182 202 Helical. {ECO:0000255}. FT TOPO_DOM 203 219 Extracellular. {ECO:0000305}. FT TRANSMEM 220 240 Helical. {ECO:0000255}. FT TOPO_DOM 241 397 Cytoplasmic. {ECO:0000305}. FT TRANSMEM 398 418 Helical. {ECO:0000255}. FT TOPO_DOM 419 426 Extracellular. {ECO:0000305}. FT TRANSMEM 427 447 Helical. {ECO:0000255}. FT TOPO_DOM 448 462 Cytoplasmic. {ECO:0000305}. FT TRANSMEM 463 483 Helical. {ECO:0000255}. FT TOPO_DOM 484 494 Extracellular. {ECO:0000305}. FT MOTIF 248 255 HHHGHXHX-motif. {ECO:0000305}. FT MOTIF 376 381 XEXPHE-motif. {ECO:0000305}. SQ SEQUENCE 494 AA; 53266 MW; 313E3DD0E8213C08 CRC64; MTLRRASGCR QLTLTIGLAL TLGLLQWPIG DVRGQDGASP AQVLQELLTR YGDNASISVP QLRSLLVRLN GGQSEDHDSK TQPTRTNASK CLAADTLAVY GMSEQSRIDE RGLQQICPTM IQQLDSQACK TQPNQESESS PRPTEAEVWG YGLLCVTVIS LCSLVGASVV PFMRKTFYKR LLLYFIALAI GTLYSNALFQ LIPEAFGFDP MEDYYVPKSA VVFGGFYLFF FTEKILKMIL KPKDTGGHGH GHSHFPAERY ANSNGDLEDG VMEKLQNGEA GGAALPRAEA DGRGVGEDDK MLSTGQTVQD TQSSGGGGTG GCYWLKGRAY SDIGTLAWMI TLSDGLHNFI DGLAIGASFT ASVFQGISTS VAILCEEFPH ELGDFVILLN AGMSIQQALF FNFLSACCCY LGMGFGILAG NNFSPNWIFA LAGGMFLYIA LADMFPEMNE VSREEEEAGG SGFLLTFALQ NAGLLTGFAI MLVLTIYSGQ IQLG //