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Q8BJ48

- NAGPA_MOUSE

UniProt

Q8BJ48 - NAGPA_MOUSE

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Protein

N-acetylglucosamine-1-phosphodiester alpha-N-acetylglucosaminidase

Gene

Nagpa

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli

Functioni

Catalyzes the second step in the formation of the mannose 6-phosphate targeting signal on lysosomal enzyme oligosaccharides by removing GlcNAc residues from GlcNAc-alpha-P-mannose moieties, which are formed in the first step. Also hydrolyzes UDP-GlcNAc, a sugar donor for Golgi N-acetylglucosaminyltransferases.

Catalytic activityi

Glycoprotein N-acetyl-D-glucosaminyl-phospho-D-mannose + H2O = N-acetyl-D-glucosamine + glycoprotein phospho-D-mannose.

Pathwayi

GO - Molecular functioni

  1. N-acetylglucosamine-1-phosphodiester alpha-N-acetylglucosaminidase activity Source: UniProtKB-EC

GO - Biological processi

  1. protein glycosylation Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Enzyme and pathway databases

UniPathwayiUPA00378.

Names & Taxonomyi

Protein namesi
Recommended name:
N-acetylglucosamine-1-phosphodiester alpha-N-acetylglucosaminidase (EC:3.1.4.45)
Alternative name(s):
Mannose 6-phosphate-uncovering enzyme
Phosphodiester alpha-GlcNAcase
Gene namesi
Name:Nagpa
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 16

Organism-specific databases

MGIiMGI:1351598. Nagpa.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini50 – 453404LumenalSequence AnalysisAdd
BLAST
Transmembranei454 – 47421HelicalSequence AnalysisAdd
BLAST
Topological domaini475 – 51743CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. Golgi apparatus Source: UniProtKB-KW
  2. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2525By similarityAdd
BLAST
Propeptidei26 – 4924Removed in mature formBy similarityPRO_0000424660Add
BLAST
Chaini50 – 517468N-acetylglucosamine-1-phosphodiester alpha-N-acetylglucosaminidasePRO_0000021789Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi116 ↔ 149By similarity
Disulfide bondi133 ↔ 324By similarity
Glycosylationi215 – 2151N-linked (GlcNAc...)Sequence Analysis
Glycosylationi297 – 2971N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi308 ↔ 315By similarity
Disulfide bondi363 ↔ 374By similarity
Glycosylationi367 – 3671N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi381 ↔ 390By similarity
Glycosylationi389 – 3891N-linked (GlcNAc...)Sequence Analysis
Glycosylationi421 – 4211N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

The precursor is cleaved and activated in the trans-Golgi network by a furin endopeptidase.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

MaxQBiQ8BJ48.
PaxDbiQ8BJ48.
PRIDEiQ8BJ48.

PTM databases

PhosphoSiteiQ8BJ48.

Expressioni

Gene expression databases

BgeeiQ8BJ48.
ExpressionAtlasiQ8BJ48. baseline and differential.
GenevestigatoriQ8BJ48.

Interactioni

Subunit structurei

Homotetramer arranged as two disulfide-linked homodimers.By similarity

Protein-protein interaction databases

IntActiQ8BJ48. 1 interaction.
MINTiMINT-4103021.

Structurei

3D structure databases

ProteinModelPortaliQ8BJ48.
SMRiQ8BJ48. Positions 335-439.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini359 – 39133EGF-likeAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi488 – 4914Tyrosine-based internalization motif
Motifi511 – 5155NPF internalization motif

Domaini

The tyrosine-based internalization signal may be essential for its retrieval from the plasma membrane to the TGN.
The C-terminal NPFKD sequence is an attractive candidate for either an endocytosis signal acting at the plasma membrane or a retrieval signal acting at the TGN to return the enzyme to the cis/medial-Golgi.

Sequence similaritiesi

Contains 1 EGF-like domain.Curated

Keywords - Domaini

EGF-like domain, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG4632.
GeneTreeiENSGT00730000111213.
HOGENOMiHOG000059612.
HOVERGENiHBG052571.
InParanoidiQ8BJ48.
KOiK01125.
OMAiPSDHCQD.
OrthoDBiEOG7R2BJP.
PhylomeDBiQ8BJ48.
TreeFamiTF331920.

Family and domain databases

InterProiIPR018711. DUF2233.
IPR000742. EG-like_dom.
IPR013032. EGF-like_CS.
[Graphical view]
PfamiPF09992. DUF2233. 1 hit.
[Graphical view]
SMARTiSM00181. EGF. 1 hit.
[Graphical view]
PROSITEiPS00022. EGF_1. 1 hit.
PS01186. EGF_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q8BJ48-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAAPRGPGLF LIPALLGLLG VAWCSLSFGV SRDDDLLLPY PLARRRPSRD
60 70 80 90 100
CARVRSGSPE QESWPPPPTN PGASHHAAVR TFVSHFEGRA VAGHLTRVAD
110 120 130 140 150
PLRTFSVLEP GGAGGCAQKR RATVEDTAVP AGCRIAQNGG FFRMSTGECL
160 170 180 190 200
GNVVSDGRLV SSSGGLQNAQ FGIRRDGTIV TGYLSEEEVL DPVNPFVQLL
210 220 230 240 250
SGVVWLIRNG NIYINESQAI ECDETQETGS FSKFVNVMSA RTAVGHDREG
260 270 280 290 300
QLILFHADGQ TEQRGLNLWE MAEFLRQQDV VNAINLDGGG SATFVLNGTL
310 320 330 340 350
ASYPSDHCQD NMWRCPRQVS TVVCVHEPRC QPPDCSGHGT CVDGHCECTS
360 370 380 390 400
HFWRGEACSE LDCGPSNCSQ HGLCTETGCH CDAGWTGSNC SEECPLGWYG
410 420 430 440 450
PGCQRPCQCE HQCSCDPQTG NCSISQVRQC LQPTEATPRA GELASFTRTT
460 470 480 490 500
WLALTLTLIF LLLISTGVNV SLFLGSRAER NRHLDGDYVY HPLQEVNGEA
510
LTAEKEHMEE TSNPFKD
Length:517
Mass (Da):56,044
Last modified:December 21, 2004 - v2
Checksum:i80E9D4AFB3873177
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti69 – 735TNPGA → LATHEPRAP in AAF08274. (PubMed:10551838)Curated
Sequence conflicti117 – 1215AQKRR → GGRSAA in AAF08274. (PubMed:10551838)Curated
Sequence conflicti130 – 1301P → R in AAF08274. (PubMed:10551838)Curated
Sequence conflicti183 – 1853YLS → SCL in AAF08274. (PubMed:10551838)Curated
Sequence conflicti265 – 2651G → GD in AAF08274. (PubMed:10551838)Curated
Sequence conflicti349 – 3491T → N in BAC27731. (PubMed:16141072)Curated
Sequence conflicti414 – 4141S → F in AAF08274. (PubMed:10551838)Curated
Sequence conflicti508 – 5081M → T in AAH39790. (PubMed:15489334)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK032158 mRNA. Translation: BAC27731.1.
AK138035 mRNA. Translation: BAE23539.1.
BC039790 mRNA. Translation: AAH39790.1.
AF187073 Genomic DNA. Translation: AAF08274.1.
CCDSiCCDS27933.1.
RefSeqiNP_038824.2. NM_013796.3.
UniGeneiMm.215641.

Genome annotation databases

EnsembliENSMUST00000023911; ENSMUSP00000023911; ENSMUSG00000023143.
GeneIDi27426.
KEGGimmu:27426.
UCSCiuc007ybv.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK032158 mRNA. Translation: BAC27731.1 .
AK138035 mRNA. Translation: BAE23539.1 .
BC039790 mRNA. Translation: AAH39790.1 .
AF187073 Genomic DNA. Translation: AAF08274.1 .
CCDSi CCDS27933.1.
RefSeqi NP_038824.2. NM_013796.3.
UniGenei Mm.215641.

3D structure databases

ProteinModelPortali Q8BJ48.
SMRi Q8BJ48. Positions 335-439.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q8BJ48. 1 interaction.
MINTi MINT-4103021.

PTM databases

PhosphoSitei Q8BJ48.

Proteomic databases

MaxQBi Q8BJ48.
PaxDbi Q8BJ48.
PRIDEi Q8BJ48.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000023911 ; ENSMUSP00000023911 ; ENSMUSG00000023143 .
GeneIDi 27426.
KEGGi mmu:27426.
UCSCi uc007ybv.2. mouse.

Organism-specific databases

CTDi 51172.
MGIi MGI:1351598. Nagpa.

Phylogenomic databases

eggNOGi COG4632.
GeneTreei ENSGT00730000111213.
HOGENOMi HOG000059612.
HOVERGENi HBG052571.
InParanoidi Q8BJ48.
KOi K01125.
OMAi PSDHCQD.
OrthoDBi EOG7R2BJP.
PhylomeDBi Q8BJ48.
TreeFami TF331920.

Enzyme and pathway databases

UniPathwayi UPA00378 .

Miscellaneous databases

NextBioi 305480.
PROi Q8BJ48.
SOURCEi Search...

Gene expression databases

Bgeei Q8BJ48.
ExpressionAtlasi Q8BJ48. baseline and differential.
Genevestigatori Q8BJ48.

Family and domain databases

InterProi IPR018711. DUF2233.
IPR000742. EG-like_dom.
IPR013032. EGF-like_CS.
[Graphical view ]
Pfami PF09992. DUF2233. 1 hit.
[Graphical view ]
SMARTi SM00181. EGF. 1 hit.
[Graphical view ]
PROSITEi PS00022. EGF_1. 1 hit.
PS01186. EGF_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: Brain and Thymus.
  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: FVB/N.
    Tissue: Mammary gland.
  3. "Molecular cloning and functional expression of two splice forms of human N-acetylglucosamine-1-phosphodiester alpha-N-acetylglucosaminidase."
    Kornfeld R.H., Bao M., Brewer K., Noll C., Canfield W.M.
    J. Biol. Chem. 274:32778-32785(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 30-517.

Entry informationi

Entry nameiNAGPA_MOUSE
AccessioniPrimary (citable) accession number: Q8BJ48
Secondary accession number(s): Q3UUT5, Q8CHQ8, Q9QZE6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 21, 2004
Last sequence update: December 21, 2004
Last modified: October 29, 2014
This is version 111 of the entry and version 2 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3