ID F1RIP1_PIG Unreviewed; 744 AA.
AC F1RIP1;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 3.
DT 27-MAR-2024, entry version 76.
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:ENSSSCP00000003419.4,
GN ECO:0000313|VGNC:VGNC:88760};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000003419.4, ECO:0000313|Proteomes:UP000008227};
RN [1] {ECO:0000313|Ensembl:ENSSSCP00000003419.4, ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000003419.4,
RC ECO:0000313|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSSCP00000003419.4}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Glycogen synthase participates in the glycogen biosynthetic
CC process along with glycogenin and glycogen branching enzyme. Extends
CC the primer composed of a few glucose units formed by glycogenin by
CC adding new glucose units to it. In this context, glycogen synthase
CC transfers the glycosyl residue from UDP-Glc to the non-reducing end of
CC alpha-1,4-glucan. {ECO:0000256|ARBA:ARBA00043883}.
CC -!- FUNCTION: Transfers the glycosyl residue from UDP-Glc to the non-
CC reducing end of alpha-1,4-glucan. {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:ARBA00043769};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18550;
CC Evidence={ECO:0000256|ARBA:ARBA00043769};
CC -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004964, ECO:0000256|RuleBase:RU363104}.
CC -!- SUBUNIT: Part of the GYS1-GYG1 complex, a heterooctamer composed of a
CC tetramer of GYS1 and 2 dimers of GYG1, where each GYS1 protomer binds
CC to one GYG1 subunit (via GYG1 C-terminus); the GYS1 tetramer may
CC dissociate from GYG1 dimers to continue glycogen polymerization on its
CC own. {ECO:0000256|ARBA:ARBA00044021}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 3 family.
CC {ECO:0000256|ARBA:ARBA00010686, ECO:0000256|RuleBase:RU363104}.
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DR AlphaFoldDB; F1RIP1; -.
DR SMR; F1RIP1; -.
DR STRING; 9823.ENSSSCP00000003419; -.
DR PaxDb; 9823-ENSSSCP00000003419; -.
DR PeptideAtlas; F1RIP1; -.
DR Ensembl; ENSSSCT00000003502.4; ENSSSCP00000003419.4; ENSSSCG00000003154.5.
DR VGNC; VGNC:88760; GYS1.
DR GeneTree; ENSGT00390000018612; -.
DR HOGENOM; CLU_015910_1_0_1; -.
DR InParanoid; F1RIP1; -.
DR TreeFam; TF300306; -.
DR Reactome; R-SSC-3322077; Glycogen synthesis.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000008227; Chromosome 6.
DR Bgee; ENSSSCG00000003154; Expressed in longissimus thoracis muscle and 43 other cell types or tissues.
DR ExpressionAtlas; F1RIP1; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0016234; C:inclusion body; IEA:Ensembl.
DR GO; GO:0004373; F:glycogen (starch) synthase activity; IBA:GO_Central.
DR GO; GO:0061547; F:glycogen synthase activity, transferring glucose-1-phosphate; IEA:Ensembl.
DR GO; GO:0005978; P:glycogen biosynthetic process; IBA:GO_Central.
DR GO; GO:0007507; P:heart development; IEA:Ensembl.
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 1: Evidence at protein level;
KW Glycogen biosynthesis {ECO:0000256|ARBA:ARBA00023056,
KW ECO:0000256|RuleBase:RU363104};
KW Glycosyltransferase {ECO:0000256|RuleBase:RU363104};
KW Proteomics identification {ECO:0007829|PeptideAtlas:F1RIP1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008227};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU363104}.
FT REGION 637..744
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 670..684
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 685..699
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 703..737
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 744 AA; 84421 MW; 1B5DBE5BA3C672BA CRC64;
MPLNRTLSMS SLPGLEDWED EFDLENTVLF EVAWEVANKV GGIYTVLQTK AKVTGDEWGD
NYYLVGPYTE QGVRTQVELL EPPTPALKRT LDSMNSKGCK VYFGRWLIEG GPLVVLLDVG
ASAWALERWK GELWETCSIG VPWYDREAND AVLFGFLTTW FLGEFLAQSE EKPHVVAHFH
EWLAGIGLCL CRARRLPVAT IFTTHATLLG RYLCAGAVDF YNNLENFNVD KEAGERQIYH
RYCMERAAAH CAHVFTTVSQ ITAIEAQHLL KRKPGPSPPI PDIVTPNGLN VKKFSAMHEF
QNLHAQSKAR IQEFVRGHFY GHLDFNLDKT LYFFIAGRYE FSNKGADVFL EALARLNYLL
RVNGSEQTVV AFFIMPARTN NFNVETLKGQ AVRKQLWDTA NTVKEKFGRK LYESLLVGSL
PDMNKMLDKE DFTMMKRAIF ATQRQSFPPV CTHNMLDDSS DPILTTIRRI GLFNSSADRV
KVIFHPEFLS STSPLLPVDY EEFVRGCHLG VFPSYYEPWG YTPAECTVMG IPSISTNLSG
FGCFMEEHIA DPSAYGIYIL DRRFRSLDDS CSQLTSFLYS FCQQSRRQRI IQRNRTERLS
DLLDWKYLGR YYMSARHMAL AKAFPEHFTY EPHEADATQG YRYPRPASVP PSPSLSRHSS
PHQSEDEEEP RDGPPDEDGE RYDEDEEAAK DRRNIRAPEW PRRASCTSST SGSKRGSVDT
GPSSSLSTPS EPLSPASSLG EERN
//
