Wolframin - Mus musculus (Mouse)

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P56695 (WFS1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 80. History...

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

Documents (1) |

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:
Wolframin

Gene names

Name:

Wfs1

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	890 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Participates in the regulation of cellular Ca²⁺ homeostasis, at least partly, by modulating the filling state of the endoplasmic reticulum Ca²⁺ store By similarity.
Subcellular location	Endoplasmic reticulum membrane; Multi-pass membrane protein.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane
Domain	Transmembrane Transmembrane helix
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	ER-associated protein catabolic process Inferred from direct assay PubMed 20160352. Source: BHF-UCL endoplasmic reticulum calcium ion homeostasis Inferred from sequence or structural similarity. Source: BHF-UCL endoplasmic reticulum unfolded protein response Inferred from direct assay PubMed 20160352. Source: BHF-UCL glucose homeostasis Inferred from sequence or structural similarity. Source: BHF-UCL kidney development Inferred from sequence or structural similarity. Source: BHF-UCL negative regulation of neuron apoptotic process Inferred from sequence or structural similarity. Source: BHF-UCL negative regulation of sequence-specific DNA binding transcription factor activity Inferred from direct assay PubMed 20160352. Source: BHF-UCL negative regulation of type B pancreatic cell apoptotic process Inferred from mutant phenotype PubMed 16087305. Source: BHF-UCL polyubiquitinated misfolded protein transport Inferred from direct assay PubMed 20160352. Source: BHF-UCL positive regulation of calcium ion transport Inferred from sequence or structural similarity. Source: BHF-UCL positive regulation of growth Inferred from mutant phenotype PubMed 19293327. Source: BHF-UCL positive regulation of protein ubiquitination Inferred from direct assay PubMed 20160352. Source: BHF-UCL positive regulation of proteolysis Inferred from direct assay PubMed 20160352. Source: BHF-UCL protein stabilization Inferred from mutant phenotype PubMed 20160352. Source: BHF-UCL regulation of cell cycle Non-traceable author statement PubMed 16571599. Source: BHF-UCL renal water homeostasis Inferred from sequence or structural similarity. Source: BHF-UCL sensory perception of sound Inferred from sequence or structural similarity. Source: BHF-UCL visual perception Inferred from sequence or structural similarity. Source: BHF-UCL
Cellular_component	dendrite Inferred from sequence or structural similarity. Source: BHF-UCL integral to endoplasmic reticulum membrane Inferred from sequence or structural similarity. Source: BHF-UCL
Molecular_function	ATPase binding Inferred from direct assay PubMed 17947299. Source: BHF-UCL activating transcription factor binding Inferred from direct assay PubMed 20160352. Source: BHF-UCL transporter activity Inferred from direct assay PubMed 20160352. Source: BHF-UCL ubiquitin protein ligase binding Inferred from direct assay PubMed 20160352. Source: BHF-UCL
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 890

890

Wolframin

PRO_0000065964

Regions

Transmembrane

314 – 334

Helical; Potential

Transmembrane

340 – 360

Helical; Potential

Transmembrane

402 – 422

Helical; Potential

Transmembrane

427 – 447

Helical; Potential

Transmembrane

465 – 485

Helical; Potential

Transmembrane

496 – 516

Helical; Potential

Transmembrane

529 – 549

Helical; Potential

Transmembrane

563 – 583

Helical; Potential

Transmembrane

589 – 609

Helical; Potential

Transmembrane

632 – 652

Helical; Potential

Transmembrane

870 – 890

Helical; Potential

Compositional bias

13 – 21

Poly-Pro

Compositional bias

191 – 194

Poly-Lys

Compositional bias

877 – 886

Poly-Phe

Amino acid modifications

Modified residue

Phosphoserine Ref.3

Experimental info

Sequence conflict

215

A → V in AAC64944. Ref.2

Sequences

Sequence

Length

Mass (Da)

Tools

P56695 [UniParc].

Last modified July 15, 1999. Version 1.
Checksum: CB6C6CA16171A942
Show »

FASTA

890

100,579

        10         20         30         40         50         60 
MNSGTPPPSP SGPPPPPAPQ PQARARLNAT ASLEQDKIEP PRAPRPQADP SAGRSAGEAA 

        70         80         90        100        110        120 
APEPRAPQTG SREETDRAGP MKADVEIPFE EVLEKAKAGD PKAQTEVGKH YLRLANDADE 

       130        140        150        160        170        180 
ELNSCSAVAW LILAAKQGRR EAVKLLRRCL ADRKGITSEN EAEVKQLSSE TDLERAVRKA 

       190        200        210        220        230        240 
ALVMYWKLNP KKKKQVAVSE LLENVGQVNE QDGGAQPGPV PKSLQKQRRM LERLVSSESK 

       250        260        270        280        290        300 
NYIALDDFVE LTKKYAKGII PTNLFLQDED EDEDELAGKS PEDLPLRQKV VKYPLHAIME 

       310        320        330        340        350        360 
IKEYLIDVAS KAGMHWLSTI VPTHHINALI FFFIISNLTI DFFAFFIPLV VFYLSFVSMV 

       370        380        390        400        410        420 
ICTLKVFQDS KAWENFRTLT DLLLRFEPNL DVEQAEVNFG WNHLEPYIHF LLSVVFVIFS 

       430        440        450        460        470        480 
FPLASKDCIP CSELAVISTF FTVTSYMSLS SSAEPYTRRA LVTEVAAGLL SLLPTVPVDW 

       490        500        510        520        530        540 
RFLKVLGQTF FTVPVGHFII LNVSLPCLLY VYLFYLFFRM AQLRNFKGTY CYLVPYLVCF 

       550        560        570        580        590        600 
MWCELSVVIL LQSTGLGLVR ASIGYFLFLF ALPILVAGLA LMGTVQFARW FLSLDLTKIM 

       610        620        630        640        650        660 
VTTVICGVPL LFRWWTKANF SVMGMVKSLT KSSMVKLILV WLTAILLFCW FYVYRSEGMK 

       670        680        690        700        710        720 
VYNSTLTWQQ YGFLCGPRAW KETNMARTQI LCSHLEGHRV TWTGRFKYVR VTEIDNSAES 

       730        740        750        760        770        780 
AINMLPFFLG DWMRCLYGEA YPSCSSGNTS TAEEELCRLK QLAKHPCHIK KFDRYKFEIT 

       790        800        810        820        830        840 
VGMPFGTNGN RGHEEDDITK DIVLRASSEF KDVLLNLRQG SLIEFSTILE GRLGSKWPVF 

       850        860        870        880        890 
ELKAISCLNC MTQLSPARRH VKIEQDWRST VHGALKFAFD FFFFPFLSAA

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Diabetes insipidus, diabetes mellitus, optic atrophy and deafness (DIDMOAD) caused by mutations in a novel gene (wolframin) coding for a predicted transmembrane protein." Strom T.M., Hoertnagel K., Hofmann S., Gekeler F., Scharfe C., Rabl W., Gerbitz K.-D., Meitinger T. Hum. Mol. Genet. 7:2021-2028(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"A gene encoding a transmembrane protein is mutated in patients with diabetes mellitus and optic atrophy (Wolfram Syndrome)." Inoue H., Tanizawa Y., Wasson J., Behn P., Kalidas K., Bernal-Mizrachi E., Mueckler M., Marshall H., Donis-Keller H., Crock P., Rogers D., Mikuni M., Kumashiro H., Higashi K., Sobue G., Oka Y., Permutt M.A. Nat. Genet. 20:143-148(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Insulinoma.
[3]	"Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations." Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M. Mol. Cell. Proteomics 6:283-293(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32, MASS SPECTROMETRY. Tissue: Brain cortex.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ011971 mRNA. Translation: CAA09892.1. AF084482 mRNA. Translation: AAC64944.1.
IPI	IPI00114833.
RefSeq	NP_035846.1. NM_011716.2.
UniGene	Mm.20916.
3D structure databases
ProteinModelPortal	P56695.
SMR	P56695. Positions 87-163.
ModBase	Search...
PTM databases
PhosphoSite	P56695.
Proteomic databases
PaxDb	P56695.
PRIDE	P56695.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000043964; ENSMUSP00000048053; ENSMUSG00000039474.
GeneID	22393.
KEGG	mmu:22393.
Organism-specific databases
CTD	7466.
MGI	MGI:1328355. Wfs1.
Phylogenomic databases
eggNOG	NOG82472.
HOGENOM	HOG000132944.
HOVERGEN	HBG014957.
InParanoid	P56695.
KO	K14020.
OMA	TIDFFAF.
OrthoDB	EOG44BB1V.
Gene expression databases
ArrayExpress	P56695.
Bgee	P56695.
CleanEx	MM_WFS1.
Genevestigator	P56695.
GermOnline	ENSMUSG00000039474. Mus musculus.
Family and domain databases
InterPro	IPR026208. Wolframin. IPR026209. Wolframin_fam. [Graphical view]
PANTHER	PTHR13098. PTHR13098. 1 hit.
PRINTS	PR02060. WOLFFAMILY. PR02061. WOLFRAMIN.
ProtoNet	Search...
Other
ChiTaRS	WFS1. mouse.
NextBio	302771.
SOURCE	Search...

Entry information

Entry name

WFS1_MOUSE

Accession

Primary (citable) accession number: P56695
Secondary accession number(s): Q9Z276

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1999
Last sequence update:	July 15, 1999
Last modified:	April 3, 2013
This is version 80 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

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

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