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Database: UniProt/TrEMBL
Entry: H9G9K0_ANOCA
LinkDB: H9G9K0_ANOCA
Original site: H9G9K0_ANOCA 
ID   H9G9K0_ANOCA            Unreviewed;       732 AA.
AC   H9G9K0;
DT   16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT   16-MAY-2012, sequence version 1.
DT   24-JAN-2024, entry version 63.
DE   RecName: Full=Glycogen [starch] synthase {ECO:0000256|RuleBase:RU363104};
DE            EC=2.4.1.11 {ECO:0000256|RuleBase:RU363104};
GN   Name=gys1 {ECO:0000313|Ensembl:ENSACAP00000004728.2};
OS   Anolis carolinensis (Green anole) (American chameleon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Iguania; Dactyloidae; Anolis.
OX   NCBI_TaxID=28377 {ECO:0000313|Ensembl:ENSACAP00000004728.2, ECO:0000313|Proteomes:UP000001646};
RN   [1] {ECO:0000313|Ensembl:ENSACAP00000004728.2}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JBL SC #1 {ECO:0000313|Ensembl:ENSACAP00000004728.2};
RG   The Genome Sequencing Platform;
RA   Di Palma F., Alfoldi J., Heiman D., Young S., Grabherr M., Johnson J.,
RA   Lander E.S., Lindblad-Toh K.;
RT   "The Genome Sequence of Anolis carolinensis (Green Anole Lizard).";
RL   Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSACAP00000004728.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-2023) to UniProtKB.
CC   -!- FUNCTION: Transfers the glycosyl residue from UDP-Glc to the non-
CC       reducing end of alpha-1,4-glucan. {ECO:0000256|ARBA:ARBA00003605,
CC       ECO:0000256|RuleBase:RU363104}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[(1->4)-alpha-D-glucosyl](n) + UDP-alpha-D-glucose = [(1->4)-
CC         alpha-D-glucosyl](n+1) + H(+) + UDP; Xref=Rhea:RHEA:18549, Rhea:RHEA-
CC         COMP:9584, Rhea:RHEA-COMP:9587, ChEBI:CHEBI:15378, ChEBI:CHEBI:15444,
CC         ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.11;
CC         Evidence={ECO:0000256|ARBA:ARBA00000075,
CC         ECO:0000256|RuleBase:RU363104};
CC   -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004964, ECO:0000256|RuleBase:RU363104}.
CC   -!- SUBUNIT: Interacts with GYG1. {ECO:0000256|ARBA:ARBA00038520}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 3 family.
CC       {ECO:0000256|ARBA:ARBA00010686, ECO:0000256|RuleBase:RU363104}.
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DR   RefSeq; XP_003225280.1; XM_003225232.3.
DR   AlphaFoldDB; H9G9K0; -.
DR   STRING; 28377.ENSACAP00000004728; -.
DR   Ensembl; ENSACAT00000004836.4; ENSACAP00000004728.2; ENSACAG00000004713.4.
DR   GeneID; 100563034; -.
DR   KEGG; acs:100563034; -.
DR   CTD; 2997; -.
DR   eggNOG; KOG3742; Eukaryota.
DR   GeneTree; ENSGT00390000018612; -.
DR   HOGENOM; CLU_015910_1_0_1; -.
DR   InParanoid; H9G9K0; -.
DR   OMA; RDVRNHI; -.
DR   OrthoDB; 9432at2759; -.
DR   TreeFam; TF300306; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000001646; Unplaced.
DR   Bgee; ENSACAG00000004713; Expressed in skeletal muscle tissue and 11 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0004373; F:glycogen (starch) synthase activity; IBA:GO_Central.
DR   GO; GO:0005978; P:glycogen biosynthetic process; IBA:GO_Central.
DR   CDD; cd03793; GT3_GSY2-like; 1.
DR   Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR   InterPro; IPR008631; Glycogen_synth.
DR   PANTHER; PTHR10176:SF2; GLYCOGEN [STARCH] SYNTHASE, MUSCLE; 1.
DR   PANTHER; PTHR10176; GLYCOGEN SYNTHASE; 1.
DR   Pfam; PF05693; Glycogen_syn; 1.
DR   SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 2.
PE   3: Inferred from homology;
KW   Glycogen biosynthesis {ECO:0000256|ARBA:ARBA00023056,
KW   ECO:0000256|RuleBase:RU363104};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW   ECO:0000256|RuleBase:RU363104};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001646};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU363104}.
FT   REGION          628..732
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        700..732
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   732 AA;  83617 MW;  0F1A967544C9D513 CRC64;
     MPLARSLSVT SLTGLEDWDD ELDLDNAVLF EVAWEVANKV GGIYTVIQTK AKITLDEWGE
     NYFLIGPYLE LNVRTQVELI EPPNPAIRRT IDSMNAKGCK VYFGRWLIEG GPYVILIDIG
     ATAWSLDRWK TELWESCSIG IPWYDREAND AVLFGFLTAW FLGEFSAQCE ETPFIIGHFH
     EWLSGVGLFL CRIRKLPVAT IFTTHATLLG RYLCAGSVDF YNNLQTFNLD KEAGDRQIYH
     RYCMERAAVH CTHVFTTVSQ ITAVEAEHLL KRKPDIVTPN GLNVKKFSAM HEFQNLHAQS
     KARIQEFVRG HFYGHLDFNL DKTIFFFIAG RYEYSNKGAD IFLEALARLN YLLRVNGSQT
     TVVAFFIMPA RTNNFNVETL KGQAVRKQLW DTANAVKEKF GKKLYESLLV GNLPDMNKML
     DKEDFTMMKR AIFATQRQSF PPICTHNMLD DSTDPILNSI RRIGLFNSSA DRVKVIFHPE
     FLSSTSPLLP VDYEEFVRGC HLGVFPSYYE PWGYTPAECT VMGIPSVSTN LSGFGCFMEE
     HIADPSAYGI YILDRRFRGL DESCTQLTSF LYSFCQQTRR QRIIQRNRTE RLSDLLDWKY
     LGRYYMYARH MALAKAFPDN FTYEPHEPTA AQGFRYPRPA SVPPSPSVSR HSSPHHSETE
     EDDERYDEEE EAEKDRQNIK PPGMMGPIPE WRKRSKKGSS EASTSSNAST PTIPSSPSDL
     SSPTNSLIEE RN
//
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