S39A5_MOUSE
ID S39A5_MOUSE Reviewed; 535 AA.
AC Q9D856; Q9D909;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Zinc transporter ZIP5;
DE AltName: Full=Solute carrier family 39 member 5;
DE AltName: Full=Zrt- and Irt-like protein 5 {ECO:0000303|PubMed:15322118};
DE Short=ZIP-5 {ECO:0000303|PubMed:15322118};
DE Flags: Precursor;
GN Name=Slc39a5; Synonyms=Zip5 {ECO:0000303|PubMed:15322118};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Pancreas, and Small intestine;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Kidney;
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 [3]
RP FUNCTION, TOPOLOGY, GLYCOSYLATION, AND SUBCELLULAR LOCATION.
RX PubMed=15322118; DOI=10.1074/jbc.m408361200;
RA Wang F., Kim B.-E., Petris M.J., Eide D.J.;
RT "The mammalian Zip5 protein is a zinc transporter that localizes to the
RT basolateral surface of polarized cells.";
RL J. Biol. Chem. 279:51433-51441(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-333, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Pancreas;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RX PubMed=24891338; DOI=10.1136/jmedgenet-2014-102351;
RA Guo H., Jin X., Zhu T., Wang T., Tong P., Tian L., Peng Y., Sun L., Wan A.,
RA Chen J., Liu Y., Li Y., Tian Q., Xia L., Zhang L., Pan Y., Lu L., Liu Q.,
RA Shen L., Li Y., Xiong W., Li J., Tang B., Feng Y., Zhang X., Zhang Z.,
RA Pan Q., Hu Z., Xia K.;
RT "SLC39A5 mutations interfering with the BMP/TGF-beta pathway in non-
RT syndromic high myopia.";
RL J. Med. Genet. 51:518-525(2014).
CC -!- FUNCTION: May play a role in polarized cells by carrying out serosal-
CC to-mucosal zinc transport (PubMed:15322118). Seems to play a central
CC role in controlling organismal zinc status (PubMed:15322118). Could
CC regulate the BMP/TGF-beta (bone morphogenetic protein/transforming
CC growth factor-beta) signaling pathway and modulates extracellular
CC matrix (ECM) proteins of the sclera (By similarity). Plays a role in
CC eye development (By similarity). {ECO:0000250|UniProtKB:Q6ZMH5,
CC ECO:0000269|PubMed:15322118}.
CC -!- SUBCELLULAR LOCATION: Basolateral cell membrane
CC {ECO:0000269|PubMed:15322118}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:15322118}.
CC -!- TISSUE SPECIFICITY: Expressed in all stages of eye development and
CC primarily in the sclera and several layers of the retina, including the
CC inner segment, outer plexiform layer and ganglion cell layer.
CC {ECO:0000269|PubMed:24891338}.
CC -!- DEVELOPMENTAL STAGE: Expressed at 10 dpc, postnatal day P0, P13 and
CC adult. {ECO:0000269|PubMed:24891338}.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:15322118}.
CC -!- PTM: Methylated at His-371 by METTL9. {ECO:0000250|UniProtKB:Q6ZMH5}.
CC -!- SIMILARITY: Belongs to the ZIP transporter (TC 2.A.5) family.
CC {ECO:0000305}.
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DR EMBL; AK007473; BAB25054.1; -; mRNA.
DR EMBL; AK008448; BAB25675.1; -; mRNA.
DR EMBL; BC028990; AAH28990.1; -; mRNA.
DR CCDS; CCDS24275.1; -.
DR RefSeq; NP_001129709.1; NM_001136237.1.
DR RefSeq; NP_082327.2; NM_028051.3.
DR RefSeq; NP_082368.1; NM_028092.3.
DR RefSeq; XP_006514235.1; XM_006514172.3.
DR RefSeq; XP_006514236.1; XM_006514173.3.
DR AlphaFoldDB; Q9D856; -.
DR SMR; Q9D856; -.
DR STRING; 10090.ENSMUSP00000131736; -.
DR GlyGen; Q9D856; 2 sites.
DR iPTMnet; Q9D856; -.
DR PhosphoSitePlus; Q9D856; -.
DR PaxDb; Q9D856; -.
DR PRIDE; Q9D856; -.
DR ProteomicsDB; 256573; -.
DR Antibodypedia; 15788; 99 antibodies from 27 providers.
DR DNASU; 72002; -.
DR Ensembl; ENSMUST00000042666; ENSMUSP00000037753; ENSMUSG00000039878.
DR Ensembl; ENSMUST00000167859; ENSMUSP00000131736; ENSMUSG00000039878.
DR GeneID; 72002; -.
DR KEGG; mmu:72002; -.
DR UCSC; uc007hmn.3; mouse.
DR CTD; 283375; -.
DR MGI; MGI:1919336; Slc39a5.
DR VEuPathDB; HostDB:ENSMUSG00000039878; -.
DR eggNOG; KOG2693; Eukaryota.
DR GeneTree; ENSGT00940000161155; -.
DR HOGENOM; CLU_015114_13_2_1; -.
DR InParanoid; Q9D856; -.
DR OMA; YMNIVSS; -.
DR OrthoDB; 657777at2759; -.
DR PhylomeDB; Q9D856; -.
DR TreeFam; TF318470; -.
DR BioGRID-ORCS; 72002; 7 hits in 71 CRISPR screens.
DR PRO; PR:Q9D856; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q9D856; protein.
DR Bgee; ENSMUSG00000039878; Expressed in yolk sac and 61 other tissues.
DR ExpressionAtlas; Q9D856; baseline and differential.
DR Genevisible; Q9D856; MM.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0005385; F:zinc ion transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0030509; P:BMP signaling pathway; ISS:UniProtKB.
DR GO; GO:0034224; P:cellular response to zinc ion starvation; IDA:MGI.
DR GO; GO:0006882; P:cellular zinc ion homeostasis; IBA:GO_Central.
DR GO; GO:0001654; P:eye development; ISS:UniProtKB.
DR GO; GO:0048026; P:positive regulation of mRNA splicing, via spliceosome; IMP:MGI.
DR GO; GO:0071578; P:zinc ion import across plasma membrane; IBA:GO_Central.
DR GO; GO:0006829; P:zinc ion transport; TAS:MGI.
DR InterPro; IPR003689; ZIP.
DR Pfam; PF02535; Zip; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Glycoprotein; Ion transport; Membrane; Methylation;
KW Phosphoprotein; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix; Transport; Zinc; Zinc transport.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..535
FT /note="Zinc transporter ZIP5"
FT /id="PRO_0000045796"
FT TOPO_DOM 20..210
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:15322118"
FT TRANSMEM 211..231
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 232..242
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 243..263
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 264..285
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 286..306
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 307..439
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 440..460
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 461..465
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 466..486
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 487..503
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 504..524
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 525..535
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:15322118"
FT REGION 316..373
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..364
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 333
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 371
FT /note="Pros-methylhistidine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZMH5"
FT CARBOHYD 49
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 158
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 137
FT /note="L -> R (in Ref. 1; BAB25054)"
FT /evidence="ECO:0000305"
FT CONFLICT 332
FT /note="G -> V (in Ref. 1; BAB25054)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 535 AA; 56275 MW; 272204D17B2E66CD CRC64;
MGPPVHHLLT GLCVGVALGW VGGSVPNLGP AEQEQNHYLA QLFGLYGENG TLTAGGLARL
LHSLGLGRVQ GLRLGHHEPP TGRAAPTSGD NFTHRLQEPE LSVDIWAGMP LGPSGWGDQE
ESKAPDLHGS GPSSLDLFQR LLLLDHSLAD HLNEDCLNGS QLLVNFGLSP VAPLTPRQFA
LLCPALLYQI DSRVCIKTPA PAPPGDVLSA LLHSGLAVLF LSLPAPLSLL LLRLLGPRLL
RPVLGFLGAL AVGTLCGDAL LHLLPHAQGG RHTGPSEQSE EDLGPGLSVL GGLFLLFMLE
NTLGLVRHRG LRPRCCRNKR DLGEPNPDPE DGSGMVLRPL QAASEPEVQG QRENRQSSPS
LAPPGHQGHS HEHRGGSIAW MVLLGDCLHN LTDGLALGAA FSDGFSSGLS TTLAVFCHEL
PHELGDFAML LQEGLSFRKL LLLSLVSGAL GLGGAALGVG LSLGPVPLTP WVFGTTAGVF
LYVALVDMLP TLLRPPEPLP VFHVLLQGLG LLLGGSLMFT IALLEEQLVP TVPDG
