GDE_CANLF
ID GDE_CANLF Reviewed; 1533 AA.
AC Q2PQH8;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 02-DEC-2020, entry version 89.
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 Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=17338148; DOI=10.1892/0891-6640(2007)21[40:gsdtii]2.0.co;2;
RA Gregory B.L., Shelton G.D., Bali D.S., Chen Y.T., Fyfe J.C.;
RT "Glycogen storage disease type IIIa in curly-coated retrievers.";
RL J. Vet. Intern. Med. 21:40-46(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}.
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: 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; DQ307574; ABC25005.1; -; mRNA.
DR RefSeq; NP_001041561.1; NM_001048096.1.
DR STRING; 9612.ENSCAFP00000039212; -.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR CAZy; GH133; Glycoside Hydrolase Family 133.
DR PaxDb; Q2PQH8; -.
DR GeneID; 479931; -.
DR KEGG; cfa:479931; -.
DR CTD; 178; -.
DR eggNOG; KOG3625; Eukaryota.
DR InParanoid; Q2PQH8; -.
DR OrthoDB; 33175at2759; -.
DR Proteomes; UP000002254; 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 2: Evidence at transcript level;
KW Cytoplasm; Glycogen biosynthesis; Glycogen storage disease; 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_0000232710"
FT REGION 1..?
FT /note="4-alpha-glucanotransferase"
FT REGION ?..1533
FT /note="Amylo-1,6-glucosidase"
FT ACT_SITE 527
FT /evidence="ECO:0000250"
FT ACT_SITE 530
FT /evidence="ECO:0000250"
FT ACT_SITE 628
FT /evidence="ECO:0000250"
FT MOD_RES 64
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35573"
SQ SEQUENCE 1533 AA; 174828 MW; 8A6E8A11F2252087 CRC64;
MGHSKQIRIL LLNEMEKLEK TLFRLEQGFE LQFRLGPTLQ GKAVTVYTNY PFPGETFNRE
KFRSLEWENP TEREDDSDKY CKLNLQQAGS FQYYFLQGNE KSGGGYIVVD PILYVGADNH
VLPLDCVTLQ TFLAKCLGPF DEWESRLRVA KESGYNMIHF TPLQTLGLSR SCYSLANQLE
LNPDFSRPNK KYTWSDVGQL VEKMKKEWNV LCITDVVYNH TAANSKWIQE HPESAYNLVN
SPHLKPAWVL DRALWHLSCD VAEGKYKEKG VPALIENDHQ MNCIRKIIWE DIFPKIQLWE
FFQVDVYKAV EQFRRLLTQE NRKITTKPDP KEHLKIIQDP EYRRLGCTVD MNIALATFIP
HDKGPAAIDE CCNWFRKRIE ELNSEKHQLV NYHQEQAVNC LLGNVFYERM AGHGPKLGPV
TRKHPLVTRY FTFPFEEMTV STEESMIHNP NKACFLMAHN GWVMGDDPLR NFAEPGSEVY
LRRELICWGD SVKLRYGNKP EDCPYLWAHM KKYTEITATY FQGVRLDNCH STPLHVAEYM
LDAARKLQPN LYVVAELFTG SEDLDNIFVT RLGISSLIRE AMSAYNSHEE GRLVYRYGGE
PVGSFVQPCL RPLMPAIAHA LFMDITHDNE CPIVHRSEYD ALPSTTIVSM ACCASGSTKG
YDELVPHQIS VVSEERFYTK WNPGASPSNT GEVNFQSGII AARCAINKLH QELGAQGFIQ
VYVDQVDEDI VAVTRHSPSI HQSVVSVSRT AFRNPKTSFY SKEVPQMCIP GKIEEVVLEA
RTIERNTKPY QKDKNSINGM PNITVEIREH IQLSESKIVK QAGVATKGPN EYIQEIEFEN
LSPGSVIIFR VSLDPHAQVA VGILRNHLTQ FSPHFKSGSL AVENSDPILK IPFAFIASKL
TLAELNQVLY RCEAEEQEDG GGCYDIPNWS SLKYAGLQGL MSVLAEIRPK NDLGHPFCDN
LRSGDWMIDY VSNRLISRSG TIAEVGKWFQ AMFFYLKQIP RYLIPCYFDA ILIGAYTTLL
DIAWKQMSSF VQNGSTFVKH LSLGSVQMCG VGKCPSLPLL SPSLMDVPYR LNEITKEKEQ
CCVSLAAGLP HFSSGIFRCW GRDTFIALRG LLLITGRYLE ARNIILAFAG TLRHGLIPNL
LGEGTYARYN CRDAVWWWLQ CIQDYCKMVP NGLDILKCPV SRMYPTDDSV PLSAGTLDQP
LFEVIQEVMQ RHIQGIQFRE RNAGPQIDRN MKDEGFNITA GVDEETGFVY GGNRLNCGTW
MDKMGESDRA RNRGIPATPR DGSAVEIVGL SKSTVRWLLE LSKKRIFPYH EVRVKRHGKV
VTISYDEWNK KIQDNFEKLF HVSEDPXDFN EKHPNLVHKR GIYKDSYGAS SPWCDYQLRP
NFTIAMVVAP ELFTAEKAWK ALEIAEKKLL GPLGMKTLDP DDMVYCGIYD NALDNDNYNL
AKGFNYHQGP EWLWPVGYFL RAKLYFSKLM GPEANAKTVF LVKNILSRHY VHLERSPWKG
LPELTNENGQ YCPFSCETQA WSIATVLETL YDL
