GNPTG_BOVIN
ID GNPTG_BOVIN Reviewed; 306 AA.
AC Q58CS8; A5PJW7;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 4.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=N-acetylglucosamine-1-phosphotransferase subunit gamma;
DE AltName: Full=GlcNAc-1-phosphotransferase subunit gamma;
DE AltName: Full=UDP-N-acetylglucosamine-1-phosphotransferase subunit gamma;
DE Flags: Precursor;
GN Name=GNPTG;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=Hereford; TISSUE=Fetal pons;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 25-28 (ISOFORM 1), AND SUBUNIT.
RX PubMed=8940155; DOI=10.1074/jbc.271.49.31437;
RA Bao M., Booth J.L., Elmendorf B.J., Canfield W.M.;
RT "Bovine UDP-N-acetylglucosamine:lysosomal-enzyme N-acetylglucosamine-1-
RT phosphotransferase. I. Purification and subunit structure.";
RL J. Biol. Chem. 271:31437-31445(1996).
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 (By similarity).
CC {ECO:0000250}.
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. {ECO:0000269|PubMed:8940155}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Golgi apparatus
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q58CS8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q58CS8-2; Sequence=VSP_014757;
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 (By similarity).
CC {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI42267.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BT021869; AAX46716.1; -; mRNA.
DR EMBL; BC142266; AAI42267.1; ALT_INIT; mRNA.
DR RefSeq; NP_001017428.1; NM_001017428.1. [Q58CS8-2]
DR RefSeq; XP_005224468.1; XM_005224411.3. [Q58CS8-1]
DR AlphaFoldDB; Q58CS8; -.
DR CORUM; Q58CS8; -.
DR STRING; 9913.ENSBTAP00000018766; -.
DR PaxDb; Q58CS8; -.
DR PRIDE; Q58CS8; -.
DR GeneID; 508713; -.
DR KEGG; bta:508713; -.
DR CTD; 84572; -.
DR eggNOG; KOG2397; Eukaryota.
DR HOGENOM; CLU_075705_0_0_1; -.
DR InParanoid; Q58CS8; -.
DR OrthoDB; 632472at2759; -.
DR TreeFam; TF329550; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
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; Coiled coil; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Golgi apparatus; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..306
FT /note="N-acetylglucosamine-1-phosphotransferase subunit
FT gamma"
FT /id="PRO_0000019576"
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 REGION 38..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 267..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 239..266
FT /evidence="ECO:0000255"
FT COMPBIAS 38..53
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 88
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT CARBOHYD 115
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
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 /evidence="ECO:0000250"
FT VAR_SEQ 1..26
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16305752"
FT /id="VSP_014757"
SQ SEQUENCE 306 AA; 33783 MW; 8AFBA3BEEF14C2F0 CRC64;
MAARLAGLAV VLGFAARGPA PGGAAKMKVV EEPNTFGLNN PFLPQTSRLQ PKRDPSPVSG
PAHLSRLSGK CFSLVESTYK YELCPFHNVT QHEQTFRWNA YSGILGIWHE WEITNNTFRG
MWMRDGDACQ SRSRQSKVEL TCGKSNRLAH VSEPSTCVYA LTFETPLVCH PHSLLVYPTL
PAALQQRWDQ LEQDLVDELI TAQGYEKSLR AIFEDAGYLK TSEPNEAAQQ EGGTKGLRFE
TLESCQEAHK ALSQEIKRLQ GVLTQHGVPY GKPTETPSSE HWGPQVPTAG MAEPLRGDPG
LRGDTL
