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Protein

N-acetylglucosamine-1-phosphotransferase subunits alpha/beta

Gene

Gnptab

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

Functioni

Catalyzes the formation of mannose 6-phosphate (M6P) markers on high mannose type oligosaccharides in the Golgi apparatus. M6P residues are required to bind to the M6P receptors (MPR), which mediate the vesicular transport of lysosomal enzymes to the endosomal/prelysosomal compartment.By similarity

Catalytic activityi

UDP-N-acetyl-D-glucosamine + lysosomal-enzyme D-mannose = UMP + lysosomal-enzyme N-acetyl-D-glucosaminyl-phospho-D-mannose.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi449 – 4491CalciumPROSITE-ProRule annotation
Metal bindingi464 – 4641CalciumPROSITE-ProRule annotation
Metal bindingi467 – 4671CalciumPROSITE-ProRule annotation
Metal bindingi516 – 5161CalciumPROSITE-ProRule annotation
Metal bindingi531 – 5311CalciumPROSITE-ProRule annotation
Metal bindingi534 – 5341CalciumPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi997 – 100812PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

  • carbohydrate phosphorylation Source: MGI
  • lysosome organization Source: UniProtKB
  • N-glycan processing to lysosome Source: UniProtKB
  • protein secretion Source: MGI
  • secretion of lysosomal enzymes Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Ligandi

Calcium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
N-acetylglucosamine-1-phosphotransferase subunits alpha/beta (EC:2.7.8.17By similarity)
Alternative name(s):
GlcNAc-1-phosphotransferase subunits alpha/beta
Stealth protein GNPTAB
UDP-N-acetylglucosamine-1-phosphotransferase subunits alpha/beta
Cleaved into the following 2 chains:
Gene namesi
Name:Gnptab
Synonyms:Gnpta, Kiaa1208
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 10

Organism-specific databases

MGIiMGI:3643902. Gnptab.

Subcellular locationi

N-acetylglucosamine-1-phosphotransferase subunit alpha :
  • Golgi apparatus membrane By similarity; Single-pass type I membrane protein By similarity
N-acetylglucosamine-1-phosphotransferase subunit beta :
  • Golgi apparatus membrane By similarity; Single-pass type II membrane protein By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei22 – 4221HelicalSequence analysisAdd
BLAST
Transmembranei1194 – 121421HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

Pathology & Biotechi

Disruption phenotypei

Severe retinal degeneration, growth retardation and secretory cell lesions. Mice are smaller with a reduced mean body weight and length, along with a reduction in total tissue mass and lean body mass. They show elevated levels of serum lysosomal enzymes, cartilage defects, and display cytoplasmic alterations in secretory cells of several exocrine glands.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 907907N-acetylglucosamine-1-phosphotransferase subunit alphaPRO_0000225010Add
BLAST
Chaini908 – 1235328N-acetylglucosamine-1-phosphotransferase subunit betaPRO_0000225011Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi83 – 831N-linked (GlcNAc...)Sequence analysis
Glycosylationi114 – 1141N-linked (GlcNAc...)Sequence analysis
Glycosylationi148 – 1481N-linked (GlcNAc...)Sequence analysis
Glycosylationi179 – 1791N-linked (GlcNAc...)Sequence analysis
Disulfide bondi438 ↔ 461PROSITE-ProRule annotation
Disulfide bondi452 ↔ 468PROSITE-ProRule annotation
Disulfide bondi505 ↔ 528PROSITE-ProRule annotation
Disulfide bondi519 ↔ 535PROSITE-ProRule annotation
Glycosylationi614 – 6141N-linked (GlcNAc...)Sequence analysis
Glycosylationi729 – 7291N-linked (GlcNAc...)Sequence analysis
Glycosylationi988 – 9881N-linked (GlcNAc...)Sequence analysis
Glycosylationi1108 – 11081N-linked (GlcNAc...)Sequence analysis

Post-translational modificationi

The alpha- and beta-subunits are generated by a proteolytic cleavage by MBTPS1 protease at the Lys-907-Asp-908 bond.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei907 – 9082Cleavage; by MBTPS1By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ69ZN6.
PaxDbiQ69ZN6.
PeptideAtlasiQ69ZN6.
PRIDEiQ69ZN6.

PTM databases

iPTMnetiQ69ZN6.
PhosphoSiteiQ69ZN6.
SwissPalmiQ69ZN6.

Expressioni

Gene expression databases

BgeeiENSMUSG00000035311.
ExpressionAtlasiQ69ZN6. baseline and differential.
GenevisibleiQ69ZN6. MM.

Interactioni

Subunit structurei

Hexamer of two alpha, two beta and two gamma (GNPTG) subunits; disulfide-linked. The alpha and/or the beta subunits of the enzyme constitute the catalytic subunits.By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000020251.

Structurei

3D structure databases

ProteinModelPortaliQ69ZN6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati438 – 47336LNR 1Add
BLAST
Repeati505 – 54541LNR 2Add
BLAST
Domaini700 – 810111DMAP-interactionAdd
BLAST
Domaini984 – 101936EF-handPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi480 – 4856Poly-Gly

Domaini

The DMAP-interaction domain mediates substrate recognition. It specifically recognizes a conformation-dependent protein determinant present in acid hydrolases.By similarity

Sequence similaritiesi

Belongs to the stealth family.Curated
Contains 1 DMAP-interaction domain.Curated
Contains 1 EF-hand domain.PROSITE-ProRule annotation
Contains 2 LNR (Lin/Notch) repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IEF9. Eukaryota.
ENOG410XYNB. LUCA.
GeneTreeiENSGT00390000006747.
HOGENOMiHOG000007474.
HOVERGENiHBG057712.
InParanoidiQ69ZN6.
KOiK08239.
OMAiMFPEEFD.
OrthoDBiEOG091G0C78.
PhylomeDBiQ69ZN6.
TreeFamiTF324175.

Family and domain databases

InterProiIPR010506. DMAP1-bd.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR000800. Notch_dom.
IPR031358. Stealth_CR1.
IPR021520. Stealth_CR2.
IPR031357. Stealth_CR3.
IPR031356. Stealth_CR4.
[Graphical view]
PfamiPF06464. DMAP_binding. 1 hit.
PF00066. Notch. 2 hits.
PF17101. Stealth_CR1. 1 hit.
PF11380. Stealth_CR2. 1 hit.
PF17102. Stealth_CR3. 1 hit.
PF17103. Stealth_CR4. 1 hit.
[Graphical view]
SMARTiSM01137. DMAP_binding. 1 hit.
SM00004. NL. 2 hits.
[Graphical view]
SUPFAMiSSF90193. SSF90193. 1 hit.
PROSITEiPS00018. EF_HAND_1. 1 hit.
PS50222. EF_HAND_2. 1 hit.
PS50258. LNR. 2 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q69ZN6-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MLLKLLQRQT YTCLSHRYGL YVCFVGVVVT IVSAFQFGEV VLEWSRDQYH
60 70 80 90 100
VLFDSYRDNI AGKSFQNRLC LPMPIDVVYT WVNGTDLELL KELQQVREHM
110 120 130 140 150
EEEQRAMRET LGKNTTEPTK KSEKQLECLL THCIKVPMLV LDPPLPANCT
160 170 180 190 200
LKDLPTLYPS FHAASDMFNV AKPKNPSTNV SVVVFDTTKD VEDAHAGPFK
210 220 230 240 250
GGSKQMVWRA YLTTDKEAPG LVLMQGLAFL SGFPPTFKET SQLKTKLPEK
260 270 280 290 300
LSSKIKLLRL YSEASVALLK LNNPKGFQEL NKQTKKNMTI DGKELTISPA
310 320 330 340 350
YLLWDLSAIS QSKQDEDVSA SRFEDNEELR YSLRSIERHA PWVRNIFIVT
360 370 380 390 400
NGQIPSWLNL DNPRVTIVTH QDIFQNLSHL PTFSSPAIES HIHRIEGLSQ
410 420 430 440 450
KFIYLNDDVM FGKDVWPDDF YSHSKGQKVY LTWPVPNCAE GCPGSWIKDG
460 470 480 490 500
YCDKACNNSA CDWDGGDCSG NTAGNRFVAG GGGTGNIGAG QHWQFGGGIN
510 520 530 540 550
TISYCNQGCA NSWLADKFCD QACNVLSCGF DAGDCGQDHF HELYKVTLLP
560 570 580 590 600
NQTHYVVPKG EYLSYFSFAN IARRGVEGTY SDNPIIRHAS IANKWKTIHL
610 620 630 640 650
IMHSGMNATT IYFNLTLQNA NDEEFKIQIA VEVDTREAPK LNSTTQKAYE
660 670 680 690 700
SLVSPVTPLP QADVPFEDVP KEKRFPKIRR HDVNATGRFQ EEVKIPRVNI
710 720 730 740 750
SLLPKEAQVR LSNLDLQLER GDITLKGYNL SKSALLRSFL GNSLDTKIKP
760 770 780 790 800
QARTDETKGN LEVPQENPSH RRPHGFAGEH RSERWTAPAE TVTVKGRDHA
810 820 830 840 850
LNPPPVLETN ARLAQPTLGV TVSKENLSPL IVPPESHLPK EEESDRAEGN
860 870 880 890 900
AVPVKELVPG RRLQQNYPGF LPWEKKKYFQ DLLDEEESLK TQLAYFTDSK
910 920 930 940 950
HTGRQLKDTF ADSLRYVNKI LNSKFGFTSR KVPAHMPHMI DRIVMQELQD
960 970 980 990 1000
MFPEEFDKTS FHKVRHSEDM QFAFSYFYYL MSAVQPLNIS QVFHEVDTDQ
1010 1020 1030 1040 1050
SGVLSDREIR TLATRIHDLP LSLQDLTGLE HMLINCSKML PANITQLNNI
1060 1070 1080 1090 1100
PPTQEAYYDP NLPPVTKSLV TNCKPVTDKI HKAYKDKNKY RFEIMGEEEI
1110 1120 1130 1140 1150
AFKMIRTNVS HVVGQLDDIR KNPRKFVCLN DNIDHNHKDA RTVKAVLRDF
1160 1170 1180 1190 1200
YESMFPIPSQ FELPREYRNR FLHMHELQEW RAYRDKLKFW THCVLATLII
1210 1220 1230
FTIFSFFAEQ IIALKRKIFP RRRIHKEASP DRIRV
Length:1,235
Mass (Da):140,984
Last modified:March 7, 2006 - v2
Checksum:i683038D0FDB673FF
GO
Isoform 2 (identifier: Q69ZN6-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-46: Missing.
     47-67: DQYHVLFDSYRDNIAGKSFQN → MGSTSASWASLSPSSRLSSSE

Show »
Length:1,189
Mass (Da):135,245
Checksum:iAE2B3A97DA5EBAA5
GO

Sequence cautioni

The sequence BAD32410 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAE32779 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti444 – 4441G → S in BAE24503 (PubMed:16141072).Curated
Sequence conflicti707 – 7071A → V in BAE32779 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 4646Missing in isoform 2. 1 PublicationVSP_017340Add
BLAST
Alternative sequencei47 – 6721DQYHV…KSFQN → MGSTSASWASLSPSSRLSSS E in isoform 2. 1 PublicationVSP_017341Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK173132 mRNA. Translation: BAD32410.1. Different initiation.
AK140867 mRNA. Translation: BAE24503.1.
AK154710 mRNA. Translation: BAE32779.1. Different initiation.
CCDSiCCDS24110.1. [Q69ZN6-1]
RefSeqiNP_001004164.2. NM_001004164.2. [Q69ZN6-1]
UniGeneiMm.335190.

Genome annotation databases

EnsembliENSMUST00000020251; ENSMUSP00000020251; ENSMUSG00000035311. [Q69ZN6-1]
GeneIDi432486.
KEGGimmu:432486.
UCSCiuc007grk.1. mouse. [Q69ZN6-1]
uc011xlg.1. mouse. [Q69ZN6-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK173132 mRNA. Translation: BAD32410.1. Different initiation.
AK140867 mRNA. Translation: BAE24503.1.
AK154710 mRNA. Translation: BAE32779.1. Different initiation.
CCDSiCCDS24110.1. [Q69ZN6-1]
RefSeqiNP_001004164.2. NM_001004164.2. [Q69ZN6-1]
UniGeneiMm.335190.

3D structure databases

ProteinModelPortaliQ69ZN6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000020251.

PTM databases

iPTMnetiQ69ZN6.
PhosphoSiteiQ69ZN6.
SwissPalmiQ69ZN6.

Proteomic databases

MaxQBiQ69ZN6.
PaxDbiQ69ZN6.
PeptideAtlasiQ69ZN6.
PRIDEiQ69ZN6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000020251; ENSMUSP00000020251; ENSMUSG00000035311. [Q69ZN6-1]
GeneIDi432486.
KEGGimmu:432486.
UCSCiuc007grk.1. mouse. [Q69ZN6-1]
uc011xlg.1. mouse. [Q69ZN6-2]

Organism-specific databases

CTDi79158.
MGIiMGI:3643902. Gnptab.
RougeiSearch...

Phylogenomic databases

eggNOGiENOG410IEF9. Eukaryota.
ENOG410XYNB. LUCA.
GeneTreeiENSGT00390000006747.
HOGENOMiHOG000007474.
HOVERGENiHBG057712.
InParanoidiQ69ZN6.
KOiK08239.
OMAiMFPEEFD.
OrthoDBiEOG091G0C78.
PhylomeDBiQ69ZN6.
TreeFamiTF324175.

Miscellaneous databases

PROiQ69ZN6.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000035311.
ExpressionAtlasiQ69ZN6. baseline and differential.
GenevisibleiQ69ZN6. MM.

Family and domain databases

InterProiIPR010506. DMAP1-bd.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR000800. Notch_dom.
IPR031358. Stealth_CR1.
IPR021520. Stealth_CR2.
IPR031357. Stealth_CR3.
IPR031356. Stealth_CR4.
[Graphical view]
PfamiPF06464. DMAP_binding. 1 hit.
PF00066. Notch. 2 hits.
PF17101. Stealth_CR1. 1 hit.
PF11380. Stealth_CR2. 1 hit.
PF17102. Stealth_CR3. 1 hit.
PF17103. Stealth_CR4. 1 hit.
[Graphical view]
SMARTiSM01137. DMAP_binding. 1 hit.
SM00004. NL. 2 hits.
[Graphical view]
SUPFAMiSSF90193. SSF90193. 1 hit.
PROSITEiPS00018. EF_HAND_1. 1 hit.
PS50222. EF_HAND_2. 1 hit.
PS50258. LNR. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiGNPTA_MOUSE
AccessioniPrimary (citable) accession number: Q69ZN6
Secondary accession number(s): Q3U3K6, Q3US34
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 7, 2006
Last sequence update: March 7, 2006
Last modified: September 7, 2016
This is version 97 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Stealth proteins are part of a protein family that is conserved from bacteria to higher eukaryotes. Family members were first identified in microbes as proteins that help pathogens to elude the host innate immune system. Microbial stealth proteins are most likely involved in the biosynthesis of exopolysaccharides. Stealth proteins are predicted to function as hexose-1-phosphoryltransferases.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.