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Q6P5F6 (S39AA_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 82. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Zinc transporter ZIP10
Alternative name(s):
Solute carrier family 39 member 10
Zrt- and Irt-like protein 10
Short name=ZIP-10
Gene names
Name:Slc39a10
Synonyms:Kiaa1265, Zip10
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length833 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May act as a zinc-influx transporter By similarity.

Subcellular location

Membrane; Multi-pass membrane protein Potential.

Sequence similarities

Belongs to the ZIP transporter (TC 2.A.5) family. [View classification]

Sequence caution

The sequence AAH59214.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAC33542.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processIon transport
Transport
Zinc transport
   Cellular componentMembrane
   DomainSignal
Transmembrane
Transmembrane helix
   LigandZinc
   PTMGlycoprotein
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processzinc ion transport

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentintegral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionmetal ion transmembrane transporter activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525 Potential
Chain26 – 833808Zinc transporter ZIP10
PRO_0000297633

Regions

Transmembrane413 – 43321Helical; Potential
Transmembrane440 – 46021Helical; Potential
Transmembrane497 – 51721Helical; Potential
Transmembrane689 – 70921Helical; Potential
Transmembrane734 – 75421Helical; Potential
Transmembrane761 – 78121Helical; Potential
Transmembrane803 – 82321Helical; Potential
Compositional bias26 – 4015His-rich
Compositional bias101 – 294194His-rich
Compositional bias460 – 48526His-rich
Compositional bias609 – 65850His-rich

Amino acid modifications

Modified residue5381Phosphothreonine By similarity
Modified residue5551Phosphothreonine By similarity
Modified residue5931Phosphoserine By similarity
Glycosylation1911N-linked (GlcNAc...) Potential
Glycosylation1981N-linked (GlcNAc...) Ref.5 Ref.6
Glycosylation2181N-linked (GlcNAc...) Ref.5 Ref.6
Glycosylation3411N-linked (GlcNAc...) Ref.6

Experimental info

Sequence conflict3461L → S in BAC65765. Ref.2
Sequence conflict6761I → F in BAC27077. Ref.3
Sequence conflict8291F → Y in BAC65765. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q6P5F6 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: BA51B66A2296AFC2

FASTA83394,394
        10         20         30         40         50         60 
MKVHIHTKFC LICLLTFIFH HCNHCHEDHD HGPEELHRHH RGMTESESSK FSVQDAENEK 

        70         80         90        100        110        120 
KYYIEKLFDR YGENGRLSFF GLEKLLTNLG LGEIKVVEIN HEDLGHDHVS HLDILAVQEG 

       130        140        150        160        170        180 
KHFHSHTHQH FHNHLNAENH TTTSVTSKRN HKCDPEKEAA ELPIKADDKH LHDRNHRFHH 

       190        200        210        220        230        240 
RHRLHHHLDH NTTRHVHNDS VAHSEHGEPG HSPSPETNKT QEQSEVKSVK VRRKEKGKRK 

       250        260        270        280        290        300 
KENSEVNTPG FLPNHDHSEQ YEHNRVHKLD RVHSPGHPHA HLPEHSGHEL GHGHQELDPD 

       310        320        330        340        350        360 
NEGELRHTRK REAPHVRKSA IYSTPSHKDQ SEDDRQHECL NVTQLLKHFG LGPNSPISPD 

       370        380        390        400        410        420 
LFTYLCPALL YQIDSRLCIE HFDKLLVEDL NKDKTLVPED KTNIGASAWI CGIISITVIS 

       430        440        450        460        470        480 
LLSLLGVILV PIINQGCFKF LLTFLVALAV GTMSGDALLH LLPHSQGGHD HSHQHTHGHG 

       490        500        510        520        530        540 
HSHGHESKEF LEEYDAVLKG LVALGGIYLL FIIEHCIRMF KHYKQQRGKQ KWFMKQSTEE 

       550        560        570        580        590        600 
STIGRKLSDH KLNSTPDADW LQLKPLAGTD DSVVSEDRLN ETELTDLEAQ QESPPKNYLG 

       610        620        630        640        650        660 
VEEEKIMDHS HSDGLHTIHE HEVHVTSHNH HDEDKAVLRK HSHQWHHRHA HHSHGPCHSG 

       670        680        690        700        710        720 
SDLKETGIAN IAWMVIMGDG IHNFSDGLAI GAAFSAGLTG GISTSIAVFC HELPHELGDF 

       730        740        750        760        770        780 
AVLLKAGMTV KQAIVYNLLS AMMAYIGMLI GTAVGQYANN ITLWIFAITA GMFLYVALVD 

       790        800        810        820        830 
MLPEMLHGDG DHEEHGFCPV GQFILQNLGL LFGFAIMLVI ALYEDKIVFD IQF 

« Hide

References

[1]"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 Egg.
[2]"Prediction of the coding sequences of mouse homologues of KIAA gene: II. The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S., Nakajima D., Nagase T., Ohara O., Koga H.
DNA Res. 10:35-48(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 173-833.
Tissue: Brain.
[3]"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. expand/collapse author list , 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] OF 403-833.
Strain: C57BL/6J.
Tissue: Cerebellum and Head.
[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]"The mouse C2C12 myoblast cell surface N-linked glycoproteome: identification, glycosite occupancy, and membrane orientation."
Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E., Wollscheid B.
Mol. Cell. Proteomics 8:2555-2569(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-198 AND ASN-218.
Tissue: Myoblast.
[6]"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-198; ASN-218 AND ASN-341.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC052880 mRNA. Translation: AAH52880.1.
BC059214 mRNA. Translation: AAH59214.1. Different initiation.
BC062918 mRNA. Translation: AAH62918.1.
AK122483 mRNA. Translation: BAC65765.1.
AK030685 mRNA. Translation: BAC27077.1.
AK049099 mRNA. Translation: BAC33542.1. Different initiation.
CCDSCCDS14936.1.
RefSeqNP_766241.2. NM_172653.2.
XP_006495996.1. XM_006495933.1.
XP_006495997.1. XM_006495934.1.
XP_006495998.1. XM_006495935.1.
UniGeneMm.233889.
Mm.475398.

3D structure databases

ProteinModelPortalQ6P5F6.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ6P5F6.

Proteomic databases

MaxQBQ6P5F6.
PaxDbQ6P5F6.
PRIDEQ6P5F6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000027131; ENSMUSP00000027131; ENSMUSG00000025986.
GeneID227059.
KEGGmmu:227059.
UCSCuc007axc.1. mouse.

Organism-specific databases

CTD57181.
MGIMGI:1914515. Slc39a10.
RougeSearch...

Phylogenomic databases

eggNOGCOG0428.
GeneTreeENSGT00750000117560.
HOGENOMHOG000013093.
HOVERGENHBG055748.
InParanoidQ6P5F6.
KOK14716.
OMADPGHGHQ.
OrthoDBEOG7H791W.
PhylomeDBQ6P5F6.
TreeFamTF318470.

Gene expression databases

BgeeQ6P5F6.
GenevestigatorQ6P5F6.

Family and domain databases

InterProIPR003689. ZIP.
[Graphical view]
PfamPF02535. Zip. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSLC39A10. mouse.
NextBio378450.
PROQ6P5F6.
SOURCESearch...

Entry information

Entry nameS39AA_MOUSE
AccessionPrimary (citable) accession number: Q6P5F6
Secondary accession number(s): Q80TG2, Q8BX42, Q8C0L2
Entry history
Integrated into UniProtKB/Swiss-Prot: August 21, 2007
Last sequence update: July 5, 2004
Last modified: July 9, 2014
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

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