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Database: UniProt
Entry: A0A3B4XPB7_SERLL
LinkDB: A0A3B4XPB7_SERLL
Original site: A0A3B4XPB7_SERLL 
ID   A0A3B4XPB7_SERLL        Unreviewed;       272 AA.
AC   A0A3B4XPB7;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=glycogenin glucosyltransferase {ECO:0000256|ARBA:ARBA00038934};
DE            EC=2.4.1.186 {ECO:0000256|ARBA:ARBA00038934};
OS   Seriola lalandi dorsalis.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Carangaria; Carangiformes; Carangidae; Seriola.
OX   NCBI_TaxID=1841481 {ECO:0000313|Ensembl:ENSSLDP00000018326.1, ECO:0000313|Proteomes:UP000261360};
RN   [1] {ECO:0000313|Ensembl:ENSSLDP00000018326.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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}.
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DR   AlphaFoldDB; A0A3B4XPB7; -.
DR   Ensembl; ENSSLDT00000018952.1; ENSSLDP00000018326.1; ENSSLDG00000014009.1.
DR   GeneTree; ENSGT00940000161628; -.
DR   Proteomes; UP000261360; Unplaced.
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:SF164; GLYCOGENIN-1; 1.
DR   Pfam; PF01501; Glyco_transf_8; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE   3: Inferred from homology;
KW   Glycogen biosynthesis {ECO:0000256|ARBA:ARBA00023056}.
FT   REGION          215..237
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        215..230
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   272 AA;  30661 MW;  A56B5124F030C37E CRC64;
     MSGEAFVTLA TTDSYCMGAT VVARSLRRHG TTRGIVVMVT PNVSQQSRLA LESVFDEVIM
     VDVMDSEDRL HLALLGRPEL GITFTKIHCW TLTQYSKCVF LDADTLVLCN VDELFERDEL
     SAAPDPGWPD CFNSGVFVLR PSLHTHTGLM DHALQHGSFD GNARLHVQTD KLEATIVHFL
     GPVKPWSSSS QRDDGSSHAT EQFATLWWKE YLSHTTPSTP GKQPSQDWKK PQQVPRPIEQ
     LEHRRLWEAG RADYLGRDAF GNIQRKLDRF LD
//
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