GNPTG_MOUSE
ID GNPTG_MOUSE Reviewed; 307 AA.
AC Q6S5C2; Q7TNE0; Q8C5J3;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=N-acetylglucosamine-1-phosphotransferase subunit gamma;
DE AltName: Full=GlcNAc-1-phosphotransferase subunit gamma;
DE AltName: Full=M6PR domain-containing protein 1;
DE AltName: Full=UDP-N-acetylglucosamine-1-phosphotransferase subunit gamma;
DE Flags: Precursor;
GN Name=Gnptg; Synonyms=Mdcp1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RX PubMed=15716021; DOI=10.1016/j.gene.2004.10.029;
RA Sun Q., Li J., Wang C., Huang X., Huang H., Du D., Liang Y., Han H.;
RT "Overexpression of mouse GlcNAc-1-phosphotransferase-gamma subunit in cells
RT induced an I-cell-like phenotype of mucolipidosis.";
RL Gene 347:55-64(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Olfactory bulb;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Salivary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP SUBCELLULAR LOCATION, GLYCOSYLATION AT ASN-88 AND ASN-115, AND MUTAGENESIS
RP OF CYS-84; ASN-88; ASN-115; CYS-142; CYS-157; CYS-169 AND CYS-245.
RX PubMed=21173149; DOI=10.1074/jbc.m110.202382;
RA Encarnacao M., Kollmann K., Trusch M., Braulke T., Pohl S.;
RT "Post-translational modifications of the gamma-subunit affect intracellular
RT trafficking and complex assembly of GlcNAc-1-phosphotransferase.";
RL J. Biol. Chem. 286:5311-5318(2011).
CC -!- FUNCTION: Non-catalytic subunit of the N-acetylglucosamine-1-
CC phosphotransferase complex, an enzyme that catalyzes the formation of
CC mannose 6-phosphate (M6P) markers on high mannose type oligosaccharides
CC in the Golgi apparatus. Binds and presents the high mannose glycans of
CC the acceptor to the catalytic alpha and beta subunits (GNPTAB).
CC Enhances the rate of N-acetylglucosamine-1-phosphate transfer to the
CC oligosaccharides of acid hydrolase acceptors.
CC {ECO:0000269|PubMed:15716021}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. Hexamer of two alpha (GNPTAB),
CC two beta (GNPTAB) and two gamma (GNPTG) subunits; disulfide-linked. The
CC alpha and/or the beta subunits of the enzyme constitute the catalytic
CC subunits (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted. Golgi apparatus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6S5C2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6S5C2-2; Sequence=VSP_014758;
CC -!- TISSUE SPECIFICITY: Widely expressed. Highly expressed in the liver,
CC intestine, brain, thymus, testis and ovary.
CC {ECO:0000269|PubMed:15716021}.
CC -!- PTM: Cys-245 mediates the formation of the interchain disulfide bond
CC for formation of the homodimer. Cys-142, Cys-157 and Cys-169 are
CC involved in intramolecular disulfide bonds formation (PubMed:21173149).
CC {ECO:0000269|PubMed:21173149}.
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DR EMBL; AY465529; AAR19081.1; -; mRNA.
DR EMBL; AK078230; BAC37183.1; -; mRNA.
DR EMBL; BC055872; AAH55872.1; -; mRNA.
DR CCDS; CCDS28511.1; -. [Q6S5C2-1]
DR CCDS; CCDS89019.1; -. [Q6S5C2-2]
DR RefSeq; NP_001333666.1; NM_001346737.1.
DR RefSeq; NP_766117.2; NM_172529.3.
DR AlphaFoldDB; Q6S5C2; -.
DR BioGRID; 229533; 1.
DR STRING; 10090.ENSMUSP00000110807; -.
DR GlyConnect; 2526; 2 N-Linked glycans (1 site).
DR GlyGen; Q6S5C2; 2 sites, 2 N-linked glycans (1 site).
DR iPTMnet; Q6S5C2; -.
DR PhosphoSitePlus; Q6S5C2; -.
DR CPTAC; non-CPTAC-3984; -.
DR EPD; Q6S5C2; -.
DR MaxQB; Q6S5C2; -.
DR PaxDb; Q6S5C2; -.
DR PeptideAtlas; Q6S5C2; -.
DR PRIDE; Q6S5C2; -.
DR ProteomicsDB; 267644; -. [Q6S5C2-1]
DR ProteomicsDB; 267645; -. [Q6S5C2-2]
DR DNASU; 214505; -.
DR GeneID; 214505; -.
DR KEGG; mmu:214505; -.
DR UCSC; uc008bab.2; mouse. [Q6S5C2-1]
DR UCSC; uc008bac.2; mouse. [Q6S5C2-2]
DR CTD; 84572; -.
DR MGI; MGI:2147006; Gnptg.
DR eggNOG; KOG2397; Eukaryota.
DR InParanoid; Q6S5C2; -.
DR OrthoDB; 632472at2759; -.
DR PhylomeDB; Q6S5C2; -.
DR TreeFam; TF329550; -.
DR BRENDA; 2.7.8.17; 3474.
DR BioGRID-ORCS; 214505; 4 hits in 72 CRISPR screens.
DR ChiTaRS; Gnptg; mouse.
DR PRO; PR:Q6S5C2; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q6S5C2; protein.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0070622; C:UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase complex; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0003976; F:UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity; ISO:MGI.
DR GO; GO:0046835; P:carbohydrate phosphorylation; ISS:UniProtKB.
DR Gene3D; 2.70.130.10; -; 1.
DR InterPro; IPR010506; DMAP1-bd.
DR InterPro; IPR039792; GNPTG.
DR InterPro; IPR039794; Gtb1-like.
DR InterPro; IPR009011; Man6P_isomerase_rcpt-bd_dom_sf.
DR InterPro; IPR044865; MRH_dom.
DR InterPro; IPR036607; PRKCSH.
DR PANTHER; PTHR12630; PTHR12630; 1.
DR PANTHER; PTHR12630:SF6; PTHR12630:SF6; 1.
DR Pfam; PF13015; PRKCSH_1; 1.
DR SMART; SM01137; DMAP_binding; 1.
DR SUPFAM; SSF50911; SSF50911; 1.
DR PROSITE; PS51912; DMAP1_BIND; 1.
DR PROSITE; PS51914; MRH; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Disulfide bond; Glycoprotein; Golgi apparatus;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..307
FT /note="N-acetylglucosamine-1-phosphotransferase subunit
FT gamma"
FT /id="PRO_0000019578"
FT DOMAIN 69..171
FT /note="MRH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DOMAIN 176..279
FT /note="DMAP1-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01260"
FT CARBOHYD 88
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:21173149"
FT CARBOHYD 115
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:21173149"
FT DISULFID 71..84
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 129..157
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 142..169
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 245
FT /note="Interchain"
FT VAR_SEQ 137
FT /note="K -> KPLRLSSQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_014758"
FT MUTAGEN 84
FT /note="C->S: Abolishes homodimerization; when associated
FT with S-157 and S-245. Does not affect homodimerization;
FT when associated with S-157."
FT /evidence="ECO:0000269|PubMed:21173149"
FT MUTAGEN 88
FT /note="N->Q: Abolishes localization to the Golgi apparatus;
FT when associated with Q-115."
FT /evidence="ECO:0000269|PubMed:21173149"
FT MUTAGEN 115
FT /note="N->Q: Abolishes localization to the Golgi apparatus;
FT when associated with Q-88."
FT /evidence="ECO:0000269|PubMed:21173149"
FT MUTAGEN 142
FT /note="C->S: Does not affect homodimerization."
FT /evidence="ECO:0000269|PubMed:21173149"
FT MUTAGEN 157
FT /note="C->S: Abolishes homodimerization; when associated
FT with S-84 S-245."
FT /evidence="ECO:0000269|PubMed:21173149"
FT MUTAGEN 169
FT /note="C->S: Does not affect homodimerization."
FT /evidence="ECO:0000269|PubMed:21173149"
FT MUTAGEN 245
FT /note="C->S: Abolishes homodimerization. Abolishes
FT homodimerization; when associated with S-84 and S-157."
FT /evidence="ECO:0000269|PubMed:21173149"
SQ SEQUENCE 307 AA; 34169 MW; 8E9111D62E159C84 CRC64;
MAGRLAGFLM LLGLASQGPA PAYAGKMKVV EEPNTFGLNN PFLPQASRLQ PKREPSAVSG
PLHLFRLAGK CFSLVESTYK YEFCPFHNVT QHEQTFRWNA YSGILGIWHE WEIINNTFKG
MWMTDGDSCH SRSRQSKVEL TCGKINRLAH VSEPSTCVYA LTFETPLVCH PHSLLVYPTL
SEALQQRWDQ VEQDLADELI TPQGYEKLLR VLFEDAGYLK VPGETHPTQL AGGSKGLGLE
TLDNCRKAHA ELSQEVQRLT SLLQQHGIPH TQPTETTHSQ HLGQQLPIGA IAAEHLRSDP
GLRGNIL
