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Protein

Zinc transporter 5

Gene

Slc30a5

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Functions as a zinc transporter. May be a transporter of zinc into beta cells in order to form insulin crystals. Partly regulates cellular zinc homeostasis. Required with ZNT7 for the activation of zinc-requiring enzymes, alkaline phosphatases (ALPs). Transports zinc into the lumens of the Golgi apparatus and vesicular compartments where ALPs locate, thus, converting apoALPs to holoALPs. Required with ZNT6 and ZNT7 for the activation of TNAP (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Ion transport, Transport, Zinc transport

Keywords - Ligandi

Zinc

Enzyme and pathway databases

ReactomeiR-MMU-264876. Insulin processing.
R-MMU-435368. Zinc efflux and compartmentalization by the SLC30 family.

Names & Taxonomyi

Protein namesi
Recommended name:
Zinc transporter 5
Short name:
ZnT-5
Alternative name(s):
Solute carrier family 30 member 5
Gene namesi
Name:Slc30a5
Synonyms:Znt5
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 13

Organism-specific databases

MGIiMGI:1916298. Slc30a5.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 2929CytoplasmicSequence analysisAdd
BLAST
Transmembranei30 – 4617HelicalSequence analysisAdd
BLAST
Topological domaini47 – 548Exoplasmic loopSequence analysis
Transmembranei55 – 7521HelicalSequence analysisAdd
BLAST
Topological domaini76 – 9621CytoplasmicSequence analysisAdd
BLAST
Transmembranei97 – 11721HelicalSequence analysisAdd
BLAST
Topological domaini118 – 1181Exoplasmic loopSequence analysis
Transmembranei119 – 13921HelicalSequence analysisAdd
BLAST
Topological domaini140 – 15011CytoplasmicSequence analysisAdd
BLAST
Transmembranei151 – 17121HelicalSequence analysisAdd
BLAST
Topological domaini172 – 19120Exoplasmic loopSequence analysisAdd
BLAST
Transmembranei192 – 21221HelicalSequence analysisAdd
BLAST
Topological domaini213 – 23624CytoplasmicSequence analysisAdd
BLAST
Transmembranei237 – 25721HelicalSequence analysisAdd
BLAST
Topological domaini258 – 2647Exoplasmic loopSequence analysis
Transmembranei265 – 28521HelicalSequence analysisAdd
BLAST
Topological domaini286 – 30116CytoplasmicSequence analysisAdd
BLAST
Transmembranei302 – 32221HelicalSequence analysisAdd
BLAST
Topological domaini323 – 34018Exoplasmic loopSequence analysisAdd
BLAST
Transmembranei341 – 36121HelicalSequence analysisAdd
BLAST
Topological domaini362 – 41655CytoplasmicSequence analysisAdd
BLAST
Transmembranei417 – 43721HelicalSequence analysisAdd
BLAST
Topological domaini438 – 4469Exoplasmic loopSequence analysis
Transmembranei447 – 46721HelicalSequence analysisAdd
BLAST
Topological domaini468 – 48114CytoplasmicSequence analysisAdd
BLAST
Transmembranei482 – 50221HelicalSequence analysisAdd
BLAST
Topological domaini503 – 51816Exoplasmic loopSequence analysisAdd
BLAST
Transmembranei519 – 53921HelicalSequence analysisAdd
BLAST
Topological domaini540 – 58849CytoplasmicSequence analysisAdd
BLAST
Transmembranei589 – 60921HelicalSequence analysisAdd
BLAST
Topological domaini610 – 6134Exoplasmic loopSequence analysis
Transmembranei614 – 63421HelicalSequence analysisAdd
BLAST
Topological domaini635 – 761127CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 761761Zinc transporter 5PRO_0000314294Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ8R4H9.
MaxQBiQ8R4H9.
PaxDbiQ8R4H9.
PRIDEiQ8R4H9.

PTM databases

iPTMnetiQ8R4H9.
PhosphoSiteiQ8R4H9.

Expressioni

Gene expression databases

BgeeiQ8R4H9.
GenevisibleiQ8R4H9. MM.

Interactioni

Subunit structurei

Heterooligomer. Interacts with ZNT6 (By similarity).By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000065764.

Structurei

3D structure databases

ProteinModelPortaliQ8R4H9.
SMRiQ8R4H9. Positions 420-512.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni540 – 57435His-rich loopAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1484. Eukaryota.
COG1230. LUCA.
GeneTreeiENSGT00630000089781.
HOGENOMiHOG000018690.
HOVERGENiHBG056637.
InParanoidiQ8R4H9.
KOiK14692.
OMAiICSVKME.
OrthoDBiEOG7C2R1S.
PhylomeDBiQ8R4H9.
TreeFamiTF315217.

Family and domain databases

Gene3Di1.20.1510.10. 2 hits.
InterProiIPR002524. Cation_efflux.
IPR027469. Cation_efflux_TMD.
[Graphical view]
PANTHERiPTHR11562. PTHR11562. 2 hits.
PfamiPF01545. Cation_efflux. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01297. CDF. 1 hit.

Sequencei

Sequence statusi: Complete.

Q8R4H9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEEKYGGDAR PGPGGGLGPV DVPSARLTRY ILLLCLTKCL KAVGLFESYD
60 70 80 90 100
LLKAVHIVQF IFILKLGTAF FMVLFQKPFS SGKPITKHQW IKIFKHAVAG
110 120 130 140 150
CIISLLWFFG LTLCGPLRTL LLFEHSDIVV ISLLSVLFTS SGGGPAKTRG
160 170 180 190 200
AAFFIIAVIC LLLFDNDDLM AKMAEHPEGH HDSALTHMLY TAIAFLGVAD
210 220 230 240 250
HKGGVLLLVL ALCCKVGFHT ASRKLSIDVG GAKRLQALSQ LVSVFLLCPW
260 270 280 290 300
VIVLSVTTES KVESWFSLIM PFTTVIFFVM ILDFYMDSVC SVKMDVSKCA
310 320 330 340 350
RYGSFPIFIS ALLFGNFWTH PITDQLRAMN RAAHQESTEH VLSGGVVVSA
360 370 380 390 400
VFFILSANIL SSPSKRGQKG TLIGYSPEGT PLYHFMGDAF QHSSQSVPRF
410 420 430 440 450
IKDSLKQVLE ESDSRQIFYF LCLNLLFTFV ELFYGVLTNS LGLISDGFHM
460 470 480 490 500
LFDCSALVMG LFAALMSRWK ATRIFSYGYG RIEILSGFIN GLFLIVIAFF
510 520 530 540 550
VFMESVARLI DPPELDTNML TPVSVGGLIV NLIGICAFSH AHSHGHGASQ
560 570 580 590 600
GNCHSDHGHS HHAHGHGHDH GHSHGFTGGG MNANMRGVFL HVLADTLGSI
610 620 630 640 650
GVIVSTVLIE QFGWFIADPL CSLFIAVLIF LSVIPLIKDA CQVLLLRLPP
660 670 680 690 700
DHEKELHIAL EKIQKIEGLI SYRDPHFWRH SASIVAGTIH IQVTSEVLEQ
710 720 730 740 750
RIVQQVTGIL KDAGVNNLTI QVEKEAYFQH MSGLSTGFHD VLAMTKQMES
760
LKYCKDGTYI M
Length:761
Mass (Da):83,773
Last modified:June 1, 2002 - v1
Checksum:i318CBBDEE3D1519B
GO

Sequence cautioni

The sequence BAC34549.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF461761 mRNA. Translation: AAL96438.1.
AK051183 mRNA. Translation: BAC34549.1. Different initiation.
AK166006 mRNA. Translation: BAE38515.1.
BC029033 mRNA. Translation: AAH29033.3.
BC033452 mRNA. Translation: AAH33452.1.
CCDSiCCDS26739.1.
RefSeqiNP_075023.2. NM_022885.2.
UniGeneiMm.402215.

Genome annotation databases

EnsembliENSMUST00000067246; ENSMUSP00000065764; ENSMUSG00000021629.
GeneIDi69048.
KEGGimmu:69048.
UCSCiuc007rrr.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF461761 mRNA. Translation: AAL96438.1.
AK051183 mRNA. Translation: BAC34549.1. Different initiation.
AK166006 mRNA. Translation: BAE38515.1.
BC029033 mRNA. Translation: AAH29033.3.
BC033452 mRNA. Translation: AAH33452.1.
CCDSiCCDS26739.1.
RefSeqiNP_075023.2. NM_022885.2.
UniGeneiMm.402215.

3D structure databases

ProteinModelPortaliQ8R4H9.
SMRiQ8R4H9. Positions 420-512.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000065764.

PTM databases

iPTMnetiQ8R4H9.
PhosphoSiteiQ8R4H9.

Proteomic databases

EPDiQ8R4H9.
MaxQBiQ8R4H9.
PaxDbiQ8R4H9.
PRIDEiQ8R4H9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000067246; ENSMUSP00000065764; ENSMUSG00000021629.
GeneIDi69048.
KEGGimmu:69048.
UCSCiuc007rrr.1. mouse.

Organism-specific databases

CTDi64924.
MGIiMGI:1916298. Slc30a5.

Phylogenomic databases

eggNOGiKOG1484. Eukaryota.
COG1230. LUCA.
GeneTreeiENSGT00630000089781.
HOGENOMiHOG000018690.
HOVERGENiHBG056637.
InParanoidiQ8R4H9.
KOiK14692.
OMAiICSVKME.
OrthoDBiEOG7C2R1S.
PhylomeDBiQ8R4H9.
TreeFamiTF315217.

Enzyme and pathway databases

ReactomeiR-MMU-264876. Insulin processing.
R-MMU-435368. Zinc efflux and compartmentalization by the SLC30 family.

Miscellaneous databases

ChiTaRSiSlc30a5. mouse.
PROiQ8R4H9.
SOURCEiSearch...

Gene expression databases

BgeeiQ8R4H9.
GenevisibleiQ8R4H9. MM.

Family and domain databases

Gene3Di1.20.1510.10. 2 hits.
InterProiIPR002524. Cation_efflux.
IPR027469. Cation_efflux_TMD.
[Graphical view]
PANTHERiPTHR11562. PTHR11562. 2 hits.
PfamiPF01545. Cation_efflux. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01297. CDF. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of a novel mammalian zinc transporter, zinc transporter 5, abundantly expressed in pancreatic beta cells."
    Kambe T., Narita H., Yamaguchi-Iwai Y., Hirose J., Amano T., Sugiura N., Sasaki R., Mori K., Iwanaga T., Nagao M.
    J. Biol. Chem. 277:19049-19055(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Lung and Spinal ganglion.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Mammary tumor.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Pancreas.

Entry informationi

Entry nameiZNT5_MOUSE
AccessioniPrimary (citable) accession number: Q8R4H9
Secondary accession number(s): Q8BQA0, Q8K315
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: June 1, 2002
Last modified: June 8, 2016
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

The histidine-rich loop is essential for ZNT5 and ZNT6 heterooligomeric complexes to activate TNAP.By similarity

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.