ID   GDE_RABIT               Reviewed;        1555 AA.
AC   P35574;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   25-MAY-2022, entry version 116.
DE   RecName: Full=Glycogen debranching enzyme;
DE   AltName: Full=Glycogen debrancher;
DE   Includes:
DE     RecName: Full=4-alpha-glucanotransferase;
DE              EC=2.4.1.25;
DE     AltName: Full=Oligo-1,4-1,4-glucantransferase;
DE   Includes:
DE     RecName: Full=Amylo-alpha-1,6-glucosidase;
DE              Short=Amylo-1,6-glucosidase;
DE              EC=3.2.1.33;
DE     AltName: Full=Dextrin 6-alpha-D-glucosidase;
GN   Name=AGL;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC   TISSUE=Muscle;
RX   PubMed=8215409; DOI=10.1006/abbi.1993.1505;
RA   Liu W., de Castro M.L., Takrama J., Bilous P.T., Vinayagamoorthy T.,
RA   Madsen N.B., Bleackley R.C.;
RT   "Molecular cloning, sequencing, and analysis of the cDNA for rabbit muscle
RT   glycogen debranching enzyme.";
RL   Arch. Biochem. Biophys. 306:232-239(1993).
CC   -!- FUNCTION: Multifunctional enzyme acting as 1,4-alpha-D-glucan:1,4-
CC       alpha-D-glucan 4-alpha-D-glycosyltransferase and amylo-1,6-glucosidase
CC       in glycogen degradation.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Transfers a segment of a (1->4)-alpha-D-glucan to a new
CC         position in an acceptor, which may be glucose or a (1->4)-alpha-D-
CC         glucan.; EC=2.4.1.25;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of (1->6)-alpha-D-glucosidic branch linkages in
CC         glycogen phosphorylase limit dextrin.; EC=3.2.1.33;
CC   -!- SUBUNIT: Monomer. Interacts with NHLRC1/malin (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=Under
CC       glycogenolytic conditions localizes to the nucleus. {ECO:0000250}.
CC   -!- PTM: The N-terminus is blocked.
CC   -!- PTM: Ubiquitinated. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycogen debranching enzyme family.
CC       {ECO:0000305}.
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   EMBL; L10605; AAA16364.1; -; mRNA.
DR   PIR; S38758; S38758.
DR   RefSeq; NP_001075716.1; NM_001082247.1.
DR   AlphaFoldDB; P35574; -.
DR   SMR; P35574; -.
DR   STRING; 9986.ENSOCUP00000019854; -.
DR   BindingDB; P35574; -.
DR   ChEMBL; CHEMBL5273; -.
DR   DrugCentral; P35574; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   CAZy; GH133; Glycoside Hydrolase Family 133.
DR   PRIDE; P35574; -.
DR   GeneID; 100009066; -.
DR   KEGG; ocu:100009066; -.
DR   CTD; 178; -.
DR   eggNOG; KOG3625; Eukaryota.
DR   InParanoid; P35574; -.
DR   OrthoDB; 33175at2759; -.
DR   PRO; PR:P35574; -.
DR   Proteomes; UP000001811; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0004134; F:4-alpha-glucanotransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004135; F:amylo-alpha-1,6-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0102500; F:beta-maltose 4-alpha-glucanotransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005978; P:glycogen biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0005980; P:glycogen catabolic process; IEA:InterPro.
DR   CDD; cd11327; AmyAc_Glg_debranch_2; 1.
DR   InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR   InterPro; IPR010401; AGL/Gdb1.
DR   InterPro; IPR032788; AGL_central.
DR   InterPro; IPR029436; AGL_euk_N.
DR   InterPro; IPR032792; AGL_glucanoTrfase.
DR   InterPro; IPR032790; GDE_C.
DR   InterPro; IPR006421; Glycogen_debranch_met.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR10569; PTHR10569; 1.
DR   Pfam; PF06202; GDE_C; 1.
DR   Pfam; PF14701; hDGE_amylase; 1.
DR   Pfam; PF14702; hGDE_central; 1.
DR   Pfam; PF14699; hGDE_N; 1.
DR   SUPFAM; SSF48208; SSF48208; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   TIGRFAMs; TIGR01531; glyc_debranch; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; Glycogen biosynthesis; Glycosidase;
KW   Glycosyltransferase; Hydrolase; Multifunctional enzyme; Phosphoprotein;
KW   Reference proteome; Transferase; Ubl conjugation.
FT   CHAIN           1..1555
FT                   /note="Glycogen debranching enzyme"
FT                   /id="PRO_0000087451"
FT   REGION          1..?
FT                   /note="4-alpha-glucanotransferase"
FT   REGION          ?..1555
FT                   /note="Amylo-1,6-glucosidase"
FT   ACT_SITE        549
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        552
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        650
FT                   /evidence="ECO:0000250"
FT   MOD_RES         87
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P35573"
SQ   SEQUENCE   1555 AA;  177656 MW;  7AD214297CB966E0 CRC64;
     MGNSFDFGVL LILLKYFKSS RSQNGHSKQI RILLLNEMEK LEKTLFRLEQ GFELQFRLGP
     TLQGKPVTVF TNYPFPGETF NREKFRSLEW ENPTEREDDS DKYCKLNLQQ SGSFQYYFLQ
     GNEKSGGGYI VVDPILRVGA DNHMLHLDCV TLQTFLAKCL GPFDEWESRL RVAKESGYNM
     IHFTPLQTLG LSRSCYSLAD QLELNPDFSR PHKKYTWSDV GQLVEKLKRE WNVLCITDVV
     YNHTAANSKW IQEHPECAYN LVNSPHLKPA WVLDRALWHF SCDVAEGKYK NRGVPALIEN
     DHHLNCIRKV IWEDIFPKLH LWEFFQVDVY KAVEKFRGLL TQETWRVIKS DPKQHLKIIQ
     DPEYRRFGCT VDMNIALATF IPHDNGPAAI EECCNWFRKR IEELNSEKHQ LMNYHQEQAV
     NCLLGNVFYE RLAGHGPKLG PVTRKYPLVT RYFTFPFEEM PVSTEETMIH LPNKACFFMA
     HNGWVMGDDP LRNFAEPGSD VYLRRELICW GDSVKLRYGT KPEDCPYLWA HMRKYTEIIA
     TYFQGVRLDN CHSTPLHVAE YMLDAARKLQ PNLYVVAELF TGSEDLDNIF VTRLGISSLI
     REAMSAYNSH EEGRLVYRYG GEPVGSFVQP CLRPLMPAIA HALFMDITHD NECPIVHRSV
     YDALPSTTIV SMACCASGST RGYDELVPHQ ISVVSEERFY TKWNPEALPS NAGEVNFQSG
     IIAARCAINK LHQELGAKGF IQVYVDQVDE DIVAVTRHSP SIHQSFVAVS RTAFRNPKTS
     FYSKDVPQMC IPGKIEEVVL EARTIERNIS PYRKDENSIN GMPNITVEIR EHIQLNESRI
     VKQAGVTTKG PNEYIQEIEF ENLSPGSVII FRVSLDPHAQ VAVGILRNHL TQFSAHFKAG
     SLAVDNSDPI LKIPFASIAS KLTLAEINQI LYRCESEEQE DGGGCYDIPN WSSLKYAGLQ
     GLMSVLAEIR PKNDLGHPFC DNLRSGDWMI DYVSGRLISR SGTIAEVGKW LQAMFFYLKQ
     IPRYLIPCYF DAILIGAYTT LLDIAWKQMS SFVQTGSTFV KHLSLGSVQM CGVGKFPSLP
     LLSPSLTDVP YRLNEITKEK EQCCVSLAAG LPHFSSGIFR CWGRDTFIAL RGLLLITGRY
     LEARNIILAF AGTLRHGLIP NLLGEGTYAR YNCRDAVWWW LQCIQDYCKM VPNGLDILKC
     PVSRMYPTDD SAPLPAGTLD QPLFDVIQEA MQRHMQGIQF RERNAGPQID RNMKDEGFTV
     IAGVNEETGF VYGGNRFNCG TWMDKMGESD RARNRGIPAT PRDGSAVEIV GLCKSTVRWL
     LELSKKNIFP YHEVRVKRHG KVVTVSYEEW NRKIQDNFEK RFHVSEDPSA SNEEHPNLVH
     KRGIYKDSYG ASSPWCDYQL RPNFTIAMVV APELFTAEKA WKALEIAEKK LLGPLGMKTL
     DPDDMVYCGI YDNALDNDNY NLAKGFNYHQ GPEWLWPVGY FLRAKLYFSK LMDRETNART
     IFLVKNVLSR HYVHLERSPW KGLPELTNEN GQYCPFSCET QAWSIATILE TLYDL