GDE_HORSE
ID GDE_HORSE Reviewed; 1533 AA.
AC A8BQB4; A8BQB7;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Glycogen debranching enzyme {ECO:0000250|UniProtKB:P35573};
DE AltName: Full=Glycogen debrancher {ECO:0000250|UniProtKB:P35573};
DE Includes:
DE RecName: Full=4-alpha-glucanotransferase {ECO:0000250|UniProtKB:P35573};
DE EC=2.4.1.25;
DE AltName: Full=Oligo-1,4-1,4-glucantransferase {ECO:0000250|UniProtKB:P35573};
DE Includes:
DE RecName: Full=Amylo-alpha-1,6-glucosidase {ECO:0000250|UniProtKB:P35573};
DE Short=Amylo-1,6-glucosidase {ECO:0000250|UniProtKB:P35573};
DE EC=3.2.1.33;
DE AltName: Full=Dextrin 6-alpha-D-glucosidase {ECO:0000250|UniProtKB:P35573};
GN Name=AGL {ECO:0000312|EMBL:ABV45394.1};
OS Equus caballus (Horse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9796;
RN [1] {ECO:0000305, ECO:0000312|EMBL:ABV45394.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), TISSUE
RP SPECIFICITY, AND VARIANTS THR-326 AND LEU-368.
RX PubMed=17905541; DOI=10.1016/j.gene.2007.07.034;
RA Herszberg B., Mata X., Giulotto E., Decaunes P., Piras F.M.,
RA Chowdhary B.P., Chaffaux S., Guerin G.;
RT "Characterization of the equine glycogen debranching enzyme gene (AGL):
RT Genomic and cDNA structure, localization, polymorphism and expression.";
RL Gene 404:1-9(2007).
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. {ECO:0000250|UniProtKB:P35573}.
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; Evidence={ECO:0000250|UniProtKB:P35573};
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 Evidence={ECO:0000250|UniProtKB:P35573};
CC -!- SUBUNIT: Monomer. Interacts with NHLRC1/malin (By similarity).
CC {ECO:0000250|UniProtKB:P35573}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P35573}.
CC Note=Under glycogenolytic conditions localizes to the nucleus.
CC {ECO:0000250|UniProtKB:P35573}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000269|PubMed:17905541};
CC IsoId=A8BQB4-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:17905541};
CC IsoId=A8BQB4-2; Sequence=VSP_040070;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Expressed in striated skeletal muscle,
CC heart, liver, spleen, skin, spinal cord, lung, kidney and testicle.
CC {ECO:0000269|PubMed:17905541}.
CC -!- PTM: Ubiquitinated. {ECO:0000250|UniProtKB:P35573}.
CC -!- SIMILARITY: Belongs to the glycogen debranching enzyme family.
CC {ECO:0000255}.
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DR EMBL; EF660736; ABV45394.1; -; Genomic_DNA.
DR EMBL; EF660736; ABV45395.1; -; Genomic_DNA.
DR EMBL; EF660736; ABV74211.1; -; Genomic_DNA.
DR EMBL; EF660736; ABV74212.1; -; Genomic_DNA.
DR EMBL; EF660736; ABV74213.1; -; Genomic_DNA.
DR EMBL; EF660737; ABV45396.1; -; mRNA.
DR EMBL; EF660738; ABV45397.1; -; mRNA.
DR EMBL; EF660739; ABV45398.1; -; mRNA.
DR EMBL; EF660740; ABV45399.1; -; mRNA.
DR EMBL; EF660741; ABV45400.1; -; mRNA.
DR RefSeq; NP_001103778.1; NM_001110308.1. [A8BQB4-1]
DR AlphaFoldDB; A8BQB4; -.
DR SMR; A8BQB4; -.
DR STRING; 9796.ENSECAP00000009911; -.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR CAZy; GH133; Glycoside Hydrolase Family 133.
DR PaxDb; A8BQB4; -.
DR PeptideAtlas; A8BQB4; -.
DR PRIDE; A8BQB4; -.
DR GeneID; 100050695; -.
DR KEGG; ecb:100050695; -.
DR CTD; 178; -.
DR InParanoid; A8BQB4; -.
DR OrthoDB; 33175at2759; -.
DR BRENDA; 3.2.1.33; 2120.
DR Proteomes; UP000002281; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004134; F:4-alpha-glucanotransferase activity; IBA:GO_Central.
DR GO; GO:0004135; F:amylo-alpha-1,6-glucosidase activity; IBA:GO_Central.
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; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Alternative splicing; Cytoplasm; Glycogen biosynthesis; Glycosidase;
KW Glycosyltransferase; Hydrolase; Multifunctional enzyme; Phosphoprotein;
KW Reference proteome; Transferase; Ubl conjugation.
FT CHAIN 1..1533
FT /note="Glycogen debranching enzyme"
FT /id="PRO_0000401163"
FT REGION 1..?
FT /note="4-alpha-glucanotransferase"
FT /evidence="ECO:0000250|UniProtKB:P35573"
FT REGION ?..1533
FT /note="Amylo-1,6-glucosidase"
FT /evidence="ECO:0000250|UniProtKB:P35573"
FT ACT_SITE 527
FT /evidence="ECO:0000250|UniProtKB:P35573"
FT ACT_SITE 530
FT /evidence="ECO:0000250|UniProtKB:P35573"
FT ACT_SITE 628
FT /evidence="ECO:0000250|UniProtKB:P35573"
FT MOD_RES 64
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35573"
FT VAR_SEQ 1..156
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17905541"
FT /id="VSP_040070"
FT VARIANT 326
FT /note="S -> T"
FT /evidence="ECO:0000269|PubMed:17905541"
FT VARIANT 368
FT /note="I -> L"
FT /evidence="ECO:0000269|PubMed:17905541"
SQ SEQUENCE 1533 AA; 174666 MW; C19B5C7C192302F3 CRC64;
MGHSKQIRTL LLNEMEKLEK TLFRLEQGFE LQFRLGPTLQ GKAVTVYTNY PFPGETFNRE
KFHSLQWENP TEREDDSDKY CKLNLQQAGS FQYYFLQGNE KSGGGYIVVD PILRVGADNH
VLPLDCVTLQ TFLTKCLGPF DEWESRLRVA KESGYNMIHF TPLQTLGLSR SSYSLADQLE
LNPDFSRPNK KYTWHDVGQL VEKLKKEWDI LCITDVVYNH TAANSKWIHE HPESAYNLVN
SPHLKPAWVL DRALWHLSCD VAEGKYREKG VPALIENDHQ MNCIRKIIWE DIYPKIHLWE
FFQVDVHKAV EQFRGLLTQE NRKIISQPDP KQHLKIIQDP EYRRLGCTVD MNIALATFIP
HDNGPAAIDE CCNWFRKRIE ELNAEKHQLV NYHQEQAVNC LLGNVFYERL AGHGPKLGPV
TRKHPLVTRY FTFPFEEMTP STEESMIHLP NKACFLMAHN GWVMGDDPLR NFAEPGSDVY
LRRELICWGD SVKLRYGNKP EDCPYLWAHM KKYTEITATH FQGVRLDNCH STPIHVAEYM
LDAARKLQPN LYVVAELFTG SEDLDNIFVT RLGISSLIRE AMSAADSHEE GRLVYRYGGE
PVGSFVQPCL RPLMPAIAHA LFMDITHDNE CPIVHRSAYD ALPSSTIVSM ASCASGSTKG
YDELVPHQIS VVSEERFYTK WNPEALPSNT GEVNFQSGII AARRAINKLH QELGAKGFIQ
VYVDQVDQDI VAVTRHSPSI HQSVVSVSRT AFRNPKTSFY SKEVPHMYIP GKIEEVVLEA
RTIERHTIPY KKDENSINGM PDITVEIREH IQLNESKIVK HAGIVTKGPN EFVQEIEFEN
LTPGSVIIFR VSLDPHAQVA VGILRNHLTQ FSPHFKSGSL AVDNADPILK IPFASIASKL
TLAELNQVLY RCESEEQEDG GGCYNIPNWS SLKYAGLQGL MSILAEIRPR NDLGHPFCDN
LRSGDWMIDY VSSRLISRSG TIAEVGKWLQ AMFLYLKQIP RYLIPCYFDA ILIGAYTTLL
DIAWKQMSSF VQNGSTFVKH LSLGSVQMCG VGKFPSLPLL SPSLTDLPYR VNEITKEKEQ
CCGSLAAGLP HFSAGIFRCW GRDTFIALRG LLLVTGRYLE ARNIILAFAG TLRHGLIPNL
LGEGTHARYN CRDAVWWWLQ CIQDYCKIVP NGLDILRCPV SRMYPTDDSV PLSAGTVDQP
LFEVIQEAMQ RHVQGIQFRE RNAGPQIDRN MKDEGFNITA GVDEETGFVY GGNRFNCGTW
MDKMGESDRA RNRGIPATPR DGSAVEIVGL SKSAVRWLLE LSRKNIFPYH EVRVKRHGKF
VTVSYDEWNR KIQDNFEKLF HVSEDPSDFN EKHPELVHKR GIYKDSYGAS SPWCDYQLRP
NFTIAMVVAP ELFTPEKAWK ALEIAEKKLL GPLGMKTLDP DDMVYCGIYD NALDNDNYNL
AKGFNYHQGP EWLWPTGYFL RAKLYFSKLM GPETNAKTMF LVKNVLSRHY VHLERSPWKG
LPELTNENGQ YCPFSCETQA WSIATVLETL YDL
