Zinc transporter ZIP6 precursor - Mus musculus (Mouse)

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Q8C145 (S39A6_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 86. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

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 names

Name:	Slc39a6
Synonyms:	Zip6

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	765 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	May act as a zinc-influx transporter By similarity.
Subcellular location	Cell membrane; Multi-pass membrane protein By similarity. Note: Found in the endoplasmic reticulum when overexpressed. Ref.3
Tissue specificity	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. Ref.3
Induction	Induced during neuronal differentiation neuroblastoma cells line but down-regulated during myogenic differentiation of skeletal muscle cells line. Ref.3
Sequence similarities	Belongs to the ZIP transporter (TC 2.A.5) family. [View classification]
Sequence caution	The sequence AAH54780.2 differs from that shown. Reason: Erroneous initiation. The sequence BAB86300.1 differs from that shown. Reason: Frameshift at position 226.

Ontologies

Keywords
Biological process	Ion transport Transport Zinc transport
Cellular component	Cell membrane Membrane
Domain	Coiled coil Signal Transmembrane Transmembrane helix
Ligand	Zinc
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cellular zinc ion homeostasis Inferred from electronic annotation. Source: Compara zinc ion transmembrane import Inferred from electronic annotation. Source: Compara zinc ion transmembrane transport Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	endoplasmic reticulum Inferred from direct assay Ref.3. Source: MGI integral to plasma membrane Inferred from electronic annotation. Source: Compara lamellipodium membrane Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	zinc ion transmembrane transporter activity Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 20

Potential

Chain

21 – 765

745

Zinc transporter ZIP6

PRO_0000041651

Regions

Topological domain

21 – 335

315

Extracellular Potential

Transmembrane

336 – 356

Helical; Name=1; Potential

Topological domain

357 – 365

Cytoplasmic Potential

Transmembrane

366 – 386

Helical; Name=2; Potential

Topological domain

387 – 433

Extracellular Potential

Transmembrane

434 – 454

Helical; Name=3; Potential

Topological domain

455 – 667

213

Cytoplasmic Potential

Transmembrane

668 – 688

Helical; Name=4; Potential

Topological domain

689 – 696

Extracellular Potential

Transmembrane

697 – 717

Helical; Name=5; Potential

Topological domain

718 – 734

Cytoplasmic Potential

Transmembrane

735 – 755

Helical; Name=6; Potential

Topological domain

756 – 765

Extracellular Potential

Coiled coil

475 – 495

Potential

Compositional bias

92 – 141

His-rich

Compositional bias

458 – 463

Poly-Lys

Compositional bias

523 – 526

Poly-Glu

Compositional bias

551 – 588

His-rich

Amino acid modifications

Glycosylation

N-linked (GlcNAc...) Ref.4

Glycosylation

250

N-linked (GlcNAc...) Potential

Glycosylation

275

N-linked (GlcNAc...) Ref.4

Glycosylation

292

N-linked (GlcNAc...) Potential

Glycosylation

694

N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict

102 – 107

Missing in BAB86300. Ref.3

Sequence conflict

201

A → V in AAH55012. Ref.2

Sequences

Sequence

Length

Mass (Da)

Tools

Q8C145 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: C8938B9C3371377B
Show »

FASTA

765

86,380

        10         20         30         40         50         60 
MATDLSVIMI LTFALWVTSP LHELQSTAAF SQTTEKINSN WEPGVNVDLA VTMQRHHLQQ 

        70         80         90        100        110        120 
LFYRYGENDS LSVEGFRKLL QNIGIDKIKR VHIHHDHEHH ADHEHHSDHE HHSDHEHHSD 

       130        140        150        160        170        180 
HEHHSDHEHH SDHEHHSHRS HTVAGKNNRK AFCPDLDSDN SGKNPRTSLG KGSRPAEHMN 

       190        200        210        220        230        240 
GRRNIKESAS SSEVTSAVYN AVSEGTRFVE TIETPKPGRR TKDVNPSTPP SITEKSRVGR 

       250        260        270        280        290        300 
LSRLARKKSN ESVSEPRKSF MYSRNTNDNI QECFNTTKLL TSHGMSIQAL LNATEFNYLC 

       310        320        330        340        350        360 
PAIINQIDAR ACLIHTASEK KAEIPPKTYS LQIAWLGGFI AISIISFLSL LGVILVPLMN 

       370        380        390        400        410        420 
RVFFKFLLSF LVALAVGTLS GDALLHLLPH SHASHQHSHS HEEPAMEMKR GPLFSHLSAQ 

       430        440        450        460        470        480 
NIEESSYFDS TWKGLTALGG LYFMFLVEHV LTLIKQFKDK KKKNQKKPEN DEDVESKKQL 

       490        500        510        520        530        540 
SKYDSQLSSN EEKVDPGERP ESYLRADSQE PSPFDSQQPT MLEEEEVMIA HAHPQEVYNE 

       550        560        570        580        590        600 
YVPRGCKNKC HSHFHDTLGQ SDDLIHHHHD YHHILHHHHH QNHHPHSHSQ RYSREELKDA 

       610        620        630        640        650        660 
GIATLAWMVI MGDGLHNFSD GLAIGAAFTE GLSSGLSTSV AVFCHELPHE LGDFAVLLKA 

       670        680        690        700        710        720 
GMTVKQAVLY NALSAMLAYL GMATGIFIGH YAENVSMWIF ALTAGLFMYV ALVDMVPEML 

       730        740        750        760 
HNDASDHGCS RWGYFFLQNA GILLGFGIML LISIFEHKIV FRINF

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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. 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]	"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, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK028976 mRNA. Translation: BAC26223.1. BC054780 mRNA. Translation: AAH54780.2. Different initiation. BC055012 mRNA. Translation: AAH55012.1. AB071697 mRNA. Translation: BAB86300.1. Sequence problems.
IPI	IPI00469000.
RefSeq	NP_631882.2. NM_139143.3.
UniGene	Mm.21688.
3D structure databases
ProteinModelPortal	Q8C145.
ModBase	Search...
Protein-protein interaction databases
STRING	10090.ENSMUSP00000064667.
PTM databases
PhosphoSite	Q8C145.
Proteomic databases
PaxDb	Q8C145.
PRIDE	Q8C145.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000070726; ENSMUSP00000064667; ENSMUSG00000024270.
GeneID	106957.
KEGG	mmu:106957.
UCSC	uc008egv.1. mouse.
Organism-specific databases
CTD	25800.
MGI	MGI:2147279. Slc39a6.
Phylogenomic databases
eggNOG	COG0428.
GeneTree	ENSGT00680000099672.
HOGENOM	HOG000013093.
HOVERGEN	HBG055748.
InParanoid	Q8C145.
KO	K14712.
OMA	FNYLCPA.
OrthoDB	EOG4WDDBC.
Gene expression databases
ArrayExpress	Q8C145.
Bgee	Q8C145.
Genevestigator	Q8C145.
GermOnline	ENSMUSG00000024270. Mus musculus.
Family and domain databases
InterPro	IPR003689. ZIP. [Graphical view]
Pfam	PF02535. Zip. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	358490.
SOURCE	Search...

Entry information

Entry name

S39A6_MOUSE

Accession

Primary (citable) accession number: Q8C145
Secondary accession number(s): Q7TPP9, Q7TQE0, Q8R518

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 5, 2005
Last sequence update:	March 1, 2003
Last modified:	April 3, 2013
This is version 86 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents