ZNT5_MOUSE
ID ZNT5_MOUSE Reviewed; 761 AA.
AC Q8R4H9; Q8BQA0; Q8K315;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Zinc transporter 5;
DE Short=ZnT-5;
DE AltName: Full=Solute carrier family 30 member 5;
GN Name=Slc30a5; Synonyms=Znt5;
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 [MRNA].
RX PubMed=11904301; DOI=10.1074/jbc.m200910200;
RA Kambe T., Narita H., Yamaguchi-Iwai Y., Hirose J., Amano T., Sugiura N.,
RA Sasaki R., Mori K., Iwanaga T., Nagao M.;
RT "Cloning and characterization of a novel mammalian zinc transporter, zinc
RT transporter 5, abundantly expressed in pancreatic beta cells.";
RL J. Biol. Chem. 277:19049-19055(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Lung, and Spinal ganglion;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [4]
RP IDENTIFICATION BY 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).
CC -!- FUNCTION: Functions as a zinc transporter. May be a transporter of zinc
CC into beta cells in order to form insulin crystals. Partly regulates
CC cellular zinc homeostasis. Required with ZNT7 for the activation of
CC zinc-requiring enzymes, alkaline phosphatases (ALPs). Transports zinc
CC into the lumens of the Golgi apparatus and vesicular compartments where
CC ALPs locate, thus, converting apoALPs to holoALPs. Required with ZNT6
CC and ZNT7 for the activation of TNAP (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimerization could enhance the zinc transport efficiency.
CC Forms heterooligomers with ZNT6 (By similarity).
CC {ECO:0000250|UniProtKB:Q8TAD4}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
CC Note=Perimeter of granules, localizes to the brush border membrane of
CC the enterocyte. Concentrated in early compartments of the secretory
CC pathway such as COPII-coated vesicles (By similarity). {ECO:0000250}.
CC -!- MISCELLANEOUS: The histidine-rich loop is essential for ZNT5 and ZNT6
CC heterooligomeric complexes to activate TNAP. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the cation diffusion facilitator (CDF)
CC transporter (TC 2.A.4) family. SLC30A subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC34549.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF461761; AAL96438.1; -; mRNA.
DR EMBL; AK051183; BAC34549.1; ALT_INIT; mRNA.
DR EMBL; AK166006; BAE38515.1; -; mRNA.
DR EMBL; BC029033; AAH29033.3; -; mRNA.
DR EMBL; BC033452; AAH33452.1; -; mRNA.
DR CCDS; CCDS26739.1; -.
DR RefSeq; NP_075023.2; NM_022885.2.
DR AlphaFoldDB; Q8R4H9; -.
DR SMR; Q8R4H9; -.
DR BioGRID; 213194; 2.
DR STRING; 10090.ENSMUSP00000065764; -.
DR iPTMnet; Q8R4H9; -.
DR PhosphoSitePlus; Q8R4H9; -.
DR EPD; Q8R4H9; -.
DR MaxQB; Q8R4H9; -.
DR PaxDb; Q8R4H9; -.
DR PeptideAtlas; Q8R4H9; -.
DR PRIDE; Q8R4H9; -.
DR ProteomicsDB; 275309; -.
DR Antibodypedia; 23894; 48 antibodies from 13 providers.
DR DNASU; 69048; -.
DR Ensembl; ENSMUST00000067246; ENSMUSP00000065764; ENSMUSG00000021629.
DR GeneID; 69048; -.
DR KEGG; mmu:69048; -.
DR UCSC; uc007rrr.1; mouse.
DR CTD; 64924; -.
DR MGI; MGI:1916298; Slc30a5.
DR VEuPathDB; HostDB:ENSMUSG00000021629; -.
DR eggNOG; KOG1484; Eukaryota.
DR GeneTree; ENSGT00940000155754; -.
DR HOGENOM; CLU_013430_11_0_1; -.
DR InParanoid; Q8R4H9; -.
DR OMA; FDPPNIN; -.
DR OrthoDB; 1507860at2759; -.
DR PhylomeDB; Q8R4H9; -.
DR TreeFam; TF315217; -.
DR Reactome; R-MMU-264876; Insulin processing.
DR Reactome; R-MMU-435368; Zinc efflux and compartmentalization by the SLC30 family.
DR BioGRID-ORCS; 69048; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Slc30a5; mouse.
DR PRO; PR:Q8R4H9; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q8R4H9; protein.
DR Bgee; ENSMUSG00000021629; Expressed in choroid plexus epithelium and 260 other tissues.
DR ExpressionAtlas; Q8R4H9; baseline and differential.
DR Genevisible; Q8R4H9; MM.
DR GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
DR GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0030141; C:secretory granule; ISO:MGI.
DR GO; GO:0046873; F:metal ion transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0005385; F:zinc ion transmembrane transporter activity; ISO:MGI.
DR GO; GO:0006882; P:cellular zinc ion homeostasis; ISO:MGI.
DR GO; GO:0006824; P:cobalt ion transport; ISO:MGI.
DR GO; GO:0030001; P:metal ion transport; IBA:GO_Central.
DR GO; GO:0010043; P:response to zinc ion; ISO:MGI.
DR GO; GO:1904257; P:zinc ion import into Golgi apparatus; IBA:GO_Central.
DR GO; GO:0006829; P:zinc ion transport; ISO:MGI.
DR Gene3D; 1.20.1510.10; -; 1.
DR InterPro; IPR002524; Cation_efflux.
DR InterPro; IPR027469; Cation_efflux_TMD_sf.
DR InterPro; IPR045316; Msc2-like.
DR PANTHER; PTHR45755; PTHR45755; 1.
DR Pfam; PF01545; Cation_efflux; 1.
DR SUPFAM; SSF161111; SSF161111; 1.
DR TIGRFAMs; TIGR01297; CDF; 1.
PE 1: Evidence at protein level;
KW Acetylation; Golgi apparatus; Ion transport; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport; Zinc; Zinc transport.
FT CHAIN 1..761
FT /note="Zinc transporter 5"
FT /id="PRO_0000314294"
FT TOPO_DOM 1..29
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 30..46
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 47..54
FT /note="Exoplasmic loop"
FT /evidence="ECO:0000255"
FT TRANSMEM 55..75
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 76..96
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 97..117
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 118
FT /note="Exoplasmic loop"
FT /evidence="ECO:0000255"
FT TRANSMEM 119..139
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 140..150
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 151..171
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 172..191
FT /note="Exoplasmic loop"
FT /evidence="ECO:0000255"
FT TRANSMEM 192..212
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 213..236
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 237..257
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 258..264
FT /note="Exoplasmic loop"
FT /evidence="ECO:0000255"
FT TRANSMEM 265..285
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 286..301
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 302..322
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 323..340
FT /note="Exoplasmic loop"
FT /evidence="ECO:0000255"
FT TRANSMEM 341..361
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 362..416
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 417..437
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 438..446
FT /note="Exoplasmic loop"
FT /evidence="ECO:0000255"
FT TRANSMEM 447..467
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 468..481
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 482..502
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 503..518
FT /note="Exoplasmic loop"
FT /evidence="ECO:0000255"
FT TRANSMEM 519..539
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 540..588
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 589..609
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 610..613
FT /note="Exoplasmic loop"
FT /evidence="ECO:0000255"
FT TRANSMEM 614..634
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 635..761
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 540..574
FT /note="His-rich loop"
FT REGION 549..576
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q8TAD4"
SQ SEQUENCE 761 AA; 83773 MW; 318CBBDEE3D1519B CRC64;
MEEKYGGDAR PGPGGGLGPV DVPSARLTRY ILLLCLTKCL KAVGLFESYD LLKAVHIVQF
IFILKLGTAF FMVLFQKPFS SGKPITKHQW IKIFKHAVAG CIISLLWFFG LTLCGPLRTL
LLFEHSDIVV ISLLSVLFTS SGGGPAKTRG AAFFIIAVIC LLLFDNDDLM AKMAEHPEGH
HDSALTHMLY TAIAFLGVAD HKGGVLLLVL ALCCKVGFHT ASRKLSIDVG GAKRLQALSQ
LVSVFLLCPW VIVLSVTTES KVESWFSLIM PFTTVIFFVM ILDFYMDSVC SVKMDVSKCA
RYGSFPIFIS ALLFGNFWTH PITDQLRAMN RAAHQESTEH VLSGGVVVSA VFFILSANIL
SSPSKRGQKG TLIGYSPEGT PLYHFMGDAF QHSSQSVPRF IKDSLKQVLE ESDSRQIFYF
LCLNLLFTFV ELFYGVLTNS LGLISDGFHM LFDCSALVMG LFAALMSRWK ATRIFSYGYG
RIEILSGFIN GLFLIVIAFF VFMESVARLI DPPELDTNML TPVSVGGLIV NLIGICAFSH
AHSHGHGASQ GNCHSDHGHS HHAHGHGHDH GHSHGFTGGG MNANMRGVFL HVLADTLGSI
GVIVSTVLIE QFGWFIADPL CSLFIAVLIF LSVIPLIKDA CQVLLLRLPP DHEKELHIAL
EKIQKIEGLI SYRDPHFWRH SASIVAGTIH IQVTSEVLEQ RIVQQVTGIL KDAGVNNLTI
QVEKEAYFQH MSGLSTGFHD VLAMTKQMES LKYCKDGTYI M
