ID A0A455BHT0_PHYMC Unreviewed; 586 AA.
AC A0A455BHT0;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=glycogenin glucosyltransferase {ECO:0000256|ARBA:ARBA00038934};
DE EC=2.4.1.186 {ECO:0000256|ARBA:ARBA00038934};
GN Name=GYG2 {ECO:0000313|RefSeq:XP_028348297.1};
OS Physeter macrocephalus (Sperm whale) (Physeter catodon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Physeteridae; Physeter.
OX NCBI_TaxID=9755 {ECO:0000313|Proteomes:UP000248484, ECO:0000313|RefSeq:XP_028348297.1};
RN [1] {ECO:0000313|RefSeq:XP_028348297.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_028348297.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Glycogenin participates in the glycogen biosynthetic process
CC along with glycogen synthase and glycogen branching enzyme. It self-
CC glucosylates, via an inter-subunit mechanism, to form an
CC oligosaccharide primer that serves as substrate for glycogen synthase.
CC {ECO:0000256|ARBA:ARBA00043853}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-tyrosyl-[glycogenin] + UDP-alpha-D-glucose = alpha-D-
CC glucosyl-L-tyrosyl-[glycogenin] + H(+) + UDP; Xref=Rhea:RHEA:23360,
CC Rhea:RHEA-COMP:14604, Rhea:RHEA-COMP:14605, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:46858, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885,
CC ChEBI:CHEBI:140573; EC=2.4.1.186;
CC Evidence={ECO:0000256|ARBA:ARBA00043655};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23361;
CC Evidence={ECO:0000256|ARBA:ARBA00043655};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[1,4-alpha-D-glucosyl](n)-L-tyrosyl-[glycogenin] + UDP-alpha-
CC D-glucose = [1,4-alpha-D-glucosyl](n+1)-L-tyrosyl-[glycogenin] + H(+)
CC + UDP; Xref=Rhea:RHEA:56560, Rhea:RHEA-COMP:14606, Rhea:RHEA-
CC COMP:14607, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885,
CC ChEBI:CHEBI:140574; EC=2.4.1.186;
CC Evidence={ECO:0000256|ARBA:ARBA00043795};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56561;
CC Evidence={ECO:0000256|ARBA:ARBA00043795};
CC -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004964}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 8 family. Glycogenin
CC subfamily. {ECO:0000256|ARBA:ARBA00038162}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_028348297.1; XM_028492496.2.
DR AlphaFoldDB; A0A455BHT0; -.
DR STRING; 9755.ENSPCTP00005015440; -.
DR Proteomes; UP000248484; Chromosome 7.
DR GO; GO:0008466; F:glycogenin glucosyltransferase activity; IEA:UniProt.
DR GO; GO:0005978; P:glycogen biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd02537; GT8_Glycogenin; 1.
DR InterPro; IPR002495; Glyco_trans_8.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR11183; GLYCOGENIN SUBFAMILY MEMBER; 1.
DR PANTHER; PTHR11183:SF167; GLYCOGENIN-2; 1.
DR Pfam; PF01501; Glyco_transf_8; 2.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE 3: Inferred from homology;
KW Glycogen biosynthesis {ECO:0000256|ARBA:ARBA00023056};
KW Reference proteome {ECO:0000313|Proteomes:UP000248484}.
FT REGION 390..441
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 479..524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 410..427
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 484..503
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 586 AA; 65065 MW; 42EA0396384D1B89 CRC64;
MHRARLHNPF PSLTERSFSK ITFPGWPLPG QRTGLEPGPG GRPLQTFTLG AGRLKAWSSA
RVAWRRRLRQ ARLEAAPAPR RTWPPGAHGA LGLRPCREAW IIAACFFDAT PKPDSWEFLK
VSDQAFVTLA TNDVYCQGAL VLGQSLRDHR ATRRLVVLVT PQVSNLLRVI LSRVFDEVIE
VNLIDSVDYI HLAFLKRPEL GVTLTKLHCW TLTHYSKCVF LDADTLVLSN IDELFNRREF
SAAPDPGWPD CFNSGVFVFQ PSLETHGLLL QHATDHGSFD GADQGLLNSF FSSWSTADIQ
KHLPFIYNLS SNTAYTYSPA FKQFGSSVKV VHFLGSTKPW NYTYNPQTGS VLEEGSGSVN
QHQTSFLNLW WGIYHRSILP LYENIRHEDE QTSPGHTAHL GGPGVPCSSS APTAEGSCAN
AVPRSTEPCT NWAEGPRQPW PERTMVVVEE TPASPDACPV EDMIGWPEME TSAGVMCDPV
SPPSTQFADF TETQTSSQPV ESAEGGPSEE ALEPSREPPV DVTRDPSLQD ALEVGLALSV
SEISIEEKVK ALSPEEERRK WEEGCIDYLG KDAFVRIQEK LDRFLQ
//
