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Protein

Zinc transporter ZIP6

Gene

Slc39a6

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

Functioni

May act as a zinc-influx transporter.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

ReactomeiREACT_339629. Zinc influx into cells by the SLC39 gene family.

Names & Taxonomyi

Protein namesi
Recommended name:
Zinc transporter ZIP6
Alternative name(s):
Endoplasmic reticulum membrane-linked protein
Short name:
Ermelin
Solute carrier family 39 member 6
Zrt- and Irt-like protein 6
Short name:
ZIP-6
Gene namesi
Name:Slc39a6
Synonyms:Zip6
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 18

Organism-specific databases

MGIiMGI:2147279. Slc39a6.

Subcellular locationi

  • Cell membrane By similarity; Multi-pass membrane protein By similarity

  • Note: Found in the endoplasmic reticulum when overexpressed.1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini21 – 335315ExtracellularSequence AnalysisAdd
BLAST
Transmembranei336 – 35621Helical; Name=1Sequence AnalysisAdd
BLAST
Topological domaini357 – 3659CytoplasmicSequence Analysis
Transmembranei366 – 38621Helical; Name=2Sequence AnalysisAdd
BLAST
Topological domaini387 – 43347ExtracellularSequence AnalysisAdd
BLAST
Transmembranei434 – 45421Helical; Name=3Sequence AnalysisAdd
BLAST
Topological domaini455 – 667213CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei668 – 68821Helical; Name=4Sequence AnalysisAdd
BLAST
Topological domaini689 – 6968ExtracellularSequence Analysis
Transmembranei697 – 71721Helical; Name=5Sequence AnalysisAdd
BLAST
Topological domaini718 – 73417CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei735 – 75521Helical; Name=6Sequence AnalysisAdd
BLAST
Topological domaini756 – 76510ExtracellularSequence Analysis

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Sequence AnalysisAdd
BLAST
Chaini21 – 765745Zinc transporter ZIP6PRO_0000041651Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi68 – 681N-linked (GlcNAc...)1 Publication
Glycosylationi250 – 2501N-linked (GlcNAc...)Sequence Analysis
Glycosylationi275 – 2751N-linked (GlcNAc...)1 Publication
Glycosylationi292 – 2921N-linked (GlcNAc...)Sequence Analysis
Glycosylationi694 – 6941N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiQ8C145.
PaxDbiQ8C145.
PRIDEiQ8C145.

PTM databases

PhosphoSiteiQ8C145.

Expressioni

Tissue specificityi

Highly expressed in the brain and testis. In the brain strongly expressed in the CA1 and CA3 regions, Purkinje cells in cerebellum and dentate gyrus in hippocampus. In testis found in spermatids or mature sperms in the central areas of seminiferous tubules.1 Publication

Inductioni

Induced during neuronal differentiation neuroblastoma cells line but down-regulated during myogenic differentiation of skeletal muscle cells line.1 Publication

Gene expression databases

BgeeiQ8C145.
ExpressionAtlasiQ8C145. baseline and differential.
GenevisibleiQ8C145. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000064667.

Structurei

3D structure databases

ProteinModelPortaliQ8C145.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili475 – 49521Sequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi92 – 14150His-richAdd
BLAST
Compositional biasi458 – 4636Poly-Lys
Compositional biasi523 – 5264Poly-Glu
Compositional biasi551 – 58838His-richAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Coiled coil, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0428.
GeneTreeiENSGT00760000119115.
HOGENOMiHOG000013093.
HOVERGENiHBG055748.
InParanoidiQ8C145.
KOiK14712.
OMAiFNYLCPA.
OrthoDBiEOG7H791W.
PhylomeDBiQ8C145.
TreeFamiTF318470.

Family and domain databases

InterProiIPR003689. ZIP.
[Graphical view]
PfamiPF02535. Zip. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q8C145-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATDLSVIMI LTFALWVTSP LHELQSTAAF SQTTEKINSN WEPGVNVDLA
60 70 80 90 100
VTMQRHHLQQ LFYRYGENDS LSVEGFRKLL QNIGIDKIKR VHIHHDHEHH
110 120 130 140 150
ADHEHHSDHE HHSDHEHHSD HEHHSDHEHH SDHEHHSHRS HTVAGKNNRK
160 170 180 190 200
AFCPDLDSDN SGKNPRTSLG KGSRPAEHMN GRRNIKESAS SSEVTSAVYN
210 220 230 240 250
AVSEGTRFVE TIETPKPGRR TKDVNPSTPP SITEKSRVGR LSRLARKKSN
260 270 280 290 300
ESVSEPRKSF MYSRNTNDNI QECFNTTKLL TSHGMSIQAL LNATEFNYLC
310 320 330 340 350
PAIINQIDAR ACLIHTASEK KAEIPPKTYS LQIAWLGGFI AISIISFLSL
360 370 380 390 400
LGVILVPLMN RVFFKFLLSF LVALAVGTLS GDALLHLLPH SHASHQHSHS
410 420 430 440 450
HEEPAMEMKR GPLFSHLSAQ NIEESSYFDS TWKGLTALGG LYFMFLVEHV
460 470 480 490 500
LTLIKQFKDK KKKNQKKPEN DEDVESKKQL SKYDSQLSSN EEKVDPGERP
510 520 530 540 550
ESYLRADSQE PSPFDSQQPT MLEEEEVMIA HAHPQEVYNE YVPRGCKNKC
560 570 580 590 600
HSHFHDTLGQ SDDLIHHHHD YHHILHHHHH QNHHPHSHSQ RYSREELKDA
610 620 630 640 650
GIATLAWMVI MGDGLHNFSD GLAIGAAFTE GLSSGLSTSV AVFCHELPHE
660 670 680 690 700
LGDFAVLLKA GMTVKQAVLY NALSAMLAYL GMATGIFIGH YAENVSMWIF
710 720 730 740 750
ALTAGLFMYV ALVDMVPEML HNDASDHGCS RWGYFFLQNA GILLGFGIML
760
LISIFEHKIV FRINF
Length:765
Mass (Da):86,380
Last modified:March 1, 2003 - v1
Checksum:iC8938B9C3371377B
GO

Sequence cautioni

The sequence AAH54780.2 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAB86300.1 differs from that shown. Reason: Frameshift at position 226. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti102 – 1076Missing in BAB86300 (PubMed:11891044).Curated
Sequence conflicti201 – 2011A → V in AAH55012 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK028976 mRNA. Translation: BAC26223.1.
BC054780 mRNA. Translation: AAH54780.2. Different initiation.
BC055012 mRNA. Translation: AAH55012.1.
AB071697 mRNA. Translation: BAB86300.1. Sequence problems.
CCDSiCCDS50239.1.
RefSeqiNP_631882.2. NM_139143.3.
UniGeneiMm.21688.

Genome annotation databases

EnsembliENSMUST00000070726; ENSMUSP00000064667; ENSMUSG00000024270.
GeneIDi106957.
KEGGimmu:106957.
UCSCiuc008egv.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK028976 mRNA. Translation: BAC26223.1.
BC054780 mRNA. Translation: AAH54780.2. Different initiation.
BC055012 mRNA. Translation: AAH55012.1.
AB071697 mRNA. Translation: BAB86300.1. Sequence problems.
CCDSiCCDS50239.1.
RefSeqiNP_631882.2. NM_139143.3.
UniGeneiMm.21688.

3D structure databases

ProteinModelPortaliQ8C145.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000064667.

PTM databases

PhosphoSiteiQ8C145.

Proteomic databases

MaxQBiQ8C145.
PaxDbiQ8C145.
PRIDEiQ8C145.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000070726; ENSMUSP00000064667; ENSMUSG00000024270.
GeneIDi106957.
KEGGimmu:106957.
UCSCiuc008egv.1. mouse.

Organism-specific databases

CTDi25800.
MGIiMGI:2147279. Slc39a6.

Phylogenomic databases

eggNOGiCOG0428.
GeneTreeiENSGT00760000119115.
HOGENOMiHOG000013093.
HOVERGENiHBG055748.
InParanoidiQ8C145.
KOiK14712.
OMAiFNYLCPA.
OrthoDBiEOG7H791W.
PhylomeDBiQ8C145.
TreeFamiTF318470.

Enzyme and pathway databases

ReactomeiREACT_339629. Zinc influx into cells by the SLC39 gene family.

Miscellaneous databases

NextBioi358490.
PROiQ8C145.
SOURCEiSearch...

Gene expression databases

BgeeiQ8C145.
ExpressionAtlasiQ8C145. baseline and differential.
GenevisibleiQ8C145. MM.

Family and domain databases

InterProiIPR003689. ZIP.
[Graphical view]
PfamiPF02535. Zip. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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: Skin.
  2. "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: C57BL/6.
    Tissue: Brain and Olfactory epithelium.
  3. "Ermelin, an endoplasmic reticulum transmembrane protein, contains the novel HELP domain conserved in eukaryotes."
    Suzuki A., Endo T.
    Gene 284:31-40(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 21-765, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION.
  4. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  5. "Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
    Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
    Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-68 AND ASN-275.

Entry informationi

Entry nameiS39A6_MOUSE
AccessioniPrimary (citable) accession number: Q8C145
Secondary accession number(s): Q7TPP9, Q7TQE0, Q8R518
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: March 1, 2003
Last modified: June 24, 2015
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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

External Data

Dasty 3

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 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.