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Q9JHJ3 (NCUG1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified September 21, 2011. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Lysosomal protein NCU-G1
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length404 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Does not seem to be involved in inflammatory regulation. Ref.1

Subcellular location

Lysosome membrane; Single-pass type I membrane protein Ref.4.

Tissue specificity

Widely expressed. Highly expressed high in kidneys, with highest expression in the cortex. Expressed in liver. Ref.1 Ref.4

Developmental stage

Expressed at all stages of development tested. Ref.1

Post-translational modification

Highly N-glycosylated. Ref.4 Ref.5

Ontologies

Keywords
   Cellular componentLysosome
Membrane
   DomainSignal
Transmembrane
Transmembrane helix
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular componentintegral to membrane

Inferred from direct assay Ref.4. Source: UniProtKB

lysosomal membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3535 Potential
Chain36 – 404369Lysosomal protein NCU-G1
PRO_0000284485

Regions

Topological domain36 – 370335Lumenal Potential
Transmembrane371 – 39121Helical; Potential
Topological domain392 – 40413Cytoplasmic Potential
Motif400 – 4045Lysosomal targeting motif

Amino acid modifications

Glycosylation641N-linked (GlcNAc...) Potential
Glycosylation851N-linked (GlcNAc...) Potential
Glycosylation1331N-linked (GlcNAc...) Ref.5
Glycosylation1571N-linked (GlcNAc...) Potential
Glycosylation1851N-linked (GlcNAc...) Ref.5
Glycosylation2281N-linked (GlcNAc...) Potential

Experimental info

Mutagenesis4001Y → A: Abolishes lysosomal localization. Ref.4
Sequence conflict211L → I in BAC35859. Ref.2
Sequence conflict521P → T in BAE29857. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9JHJ3 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 65D490B53880B8B3

FASTA40443,804
        10         20         30         40         50         60 
MFRCWGPHWG WVPCAPTPWL LLSLLVCSAP FGLQGEETRQ VSMEVISGWP NPQNLLHIRA 

        70         80         90        100        110        120 
VGSNSTLHYV WSSLGPPAVV LVATNTTQSV LSVNWSLLLS PDPAGALMVL PKSSIQFSSA 

       130        140        150        160        170        180 
LVFTRLLEFD STNASEGAQP PGKPYPPYSL AKFSWNNITN SLDLANLSAD FQGRPVDDPT 

       190        200        210        220        230        240 
GAFANGSLTF KVQAFSRSGR PAQPPRLLHT ADVCQLEVAL VGASPRGNHS LFGLEVATLG 

       250        260        270        280        290        300 
QGPDCPSVNE RNSIDDEYAP AVFQLNQLLW GSSPSGFMQW RPVAFSEEER ARESALPCQA 

       310        320        330        340        350        360 
STLHSTLASS LPHSPIVQAF FGSQNNFCAF NLTFGAPTGP GYWDQYYLCW SMLLGMGFPP 

       370        380        390        400 
VDIFSPLVLG IMAVALGAPG LMFLGGGLFL LLRHRRYSEY QSIN

« Hide

References

« Hide 'large scale' references
[1]"cDNA of a novel mRNA expressed predominantly in mouse kidney."
Kawamura T., Kuroda N., Kimura Y., Lazoura E., Okada N., Okada H.
Biochem. Genet. 39:33-42(2001) [PubMed: 11444019] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
Strain: BALB/c.
Tissue: Liver.
[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. 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: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J and NOD.
Tissue: Bone marrow, Dendritic cell, Head, Liver and Spleen.
[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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Eye.
[4]"NCU-G1 is a highly glycosylated integral membrane protein of the lysosome."
Schieweck O., Damme M., Schroeder B., Hasilik A., Schmidt B., Lubke T.
Biochem. J. 422:83-90(2009) [PubMed: 19489740] [Abstract]
Cited for: SUBCELLULAR LOCATION, GLYCOSYLATION, TISSUE SPECIFICITY, MUTAGENESIS OF TYR-400.
[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: 19349973] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-133 AND ASN-185, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AB027141 mRNA. Translation: BAA92527.1.
AB027142 mRNA. Translation: BAA95676.1.
AK075614 mRNA. Translation: BAC35859.1.
AK150794 mRNA. Translation: BAE29857.1.
AK154340 mRNA. Translation: BAE32526.1.
AK160793 mRNA. Translation: BAE36016.1.
AK170696 mRNA. Translation: BAE41960.1.
AK171042 mRNA. Translation: BAE42207.1.
BC021547 mRNA. Translation: AAH21547.1.
IPIIPI00459432.
RefSeqNP_064387.1. NM_020003.1.
UniGeneMm.439922.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ9JHJ3.

Proteomic databases

PRIDEQ9JHJ3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000001454; ENSMUSP00000001454; ENSMUSG00000001418.
GeneID56700.
KEGGmmu:56700.
UCSCuc008pup.1. mouse.

Organism-specific databases

MGIMGI:1913318. 0610031J06Rik.

Phylogenomic databases

eggNOGroNOG08061.
GeneTreeENSGT00390000005131.
InParanoidQ9JHJ3.
OMASTLHYVW.
OrthoDBEOG4B5P60.
PhylomeDBQ9JHJ3.

Gene expression databases

ArrayExpressQ9JHJ3.
BgeeQ9JHJ3.
CleanExMM_0610031J06RIK.
GenevestigatorQ9JHJ3.

Family and domain databases

ProtoNetSearch...

Other

NextBio313143.

Entry information

Entry nameNCUG1_MOUSE
AccessionPrimary (citable) accession number: Q9JHJ3
Secondary accession number(s): Q3TUF5, Q3UBV7, Q8C6H7
Entry history
Integrated into UniProtKB/Swiss-Prot: April 17, 2007
Last sequence update: October 1, 2000
Last modified: September 21, 2011
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents